Zhu, W., Bhinderwala, F., Rambo, S., & Gronenborn, A.M. (2025). Quantifying protein-drug lifetimes in human cells by 19F NMR spectroscopy. J Biomol NMR, 1-11.Springer Nature. doi: 10.1007/s10858-025-00466-x.
Bai, X.C., Gonen, T., Gronenborn, A.M., Perrakis, A., Thorn, A., & Yang, J. (2024). Challenges and opportunities in macromolecular structure determination. Nat Rev Mol Cell Biol, 25(1), 7-12.Springer Nature. doi: 10.1038/s41580-023-00659-y.
Zadorozhnyi, R., Gronenborn, A.M., & Polenova, T. (2024). Integrative approaches for characterizing protein dynamics: NMR, CryoEM, and computer simulations. Curr Opin Struct Biol, 84, 102736.Elsevier. doi: 10.1016/j.sbi.2023.102736.
Sarkar, S., Zadrozny, K.K., Zadorozhnyi, R., Russell, R.W., Quinn, C.M., Kleinpeter, A., Ablan, S., Meshkin, H., Perilla, J.R., Freed, E.O., Ganser-Pornillos, B.K., Pornillos, O., Gronenborn, A.M., & Polenova, T. (2023). Structural basis of HIV-1 maturation inhibitor binding and activity. Nat Commun, 14(1), 1237.Springer Nature. doi: 10.1038/s41467-023-36569-y.
Gronenborn, A.M. (2022). Small, but powerful and attractive: 19F in biomolecular NMR. Structure, 30(1), 6-14.Elsevier. doi: 10.1016/j.str.2021.09.009.
Zhang, C., Guo, C., Russell, R.W., Quinn, C.M., Li, M., Williams, J.C., Gronenborn, A.M., & Polenova, T. (2022). Magic-angle-spinning NMR structure of the kinesin-1 motor domain assembled with microtubules reveals the elusive neck linker orientation. Nat Commun, 13(1), 6795.Springer Nature. doi: 10.1038/s41467-022-34026-w.
Byeon, I.J.L., Calero, G., Wu, Y., Byeon, C.H., Jung, J., DeLucia, M., Zhou, X., Weiss, S., Ahn, J., Hao, C., Skowronski, J., & Gronenborn, A.M. (2021). Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A. Nat Commun, 12(1), 6864.Springer Nature. doi: 10.1038/s41467-021-27009-w.
FEBS Journal Editorial Team, & Gronenborn, A.M. (2021). Editor Profile: Angela Gronenborn. FEBS J, 288(15), 4432-4434.Wiley. doi: 10.1111/febs.15889.
Gronenborn, A.M. (2021). Meet the IUPAB councilor - Angela M. Gronenborn. Biophys Rev, 13(6), 835-838.Springer Nature. doi: 10.1007/s12551-021-00886-7.
Guo, C., Fritz, M.P., Struppe, J., Wegner, S., Stringer, J., Sergeyev, I.V., Quinn, C.M., Gronenborn, A.M., & Polenova, T. (2021). Fast 19F Magic Angle Spinning NMR Crystallography for Structural Characterization of Fluorine-Containing Pharmaceutical Compounds. Anal Chem, 93(23), 8210-8218.American Chemical Society (ACS). doi: 10.1021/acs.analchem.1c00784.
Guseman, A.J., Whitley, M.J., González, J.J., Rathi, N., Ambarian, M., & Gronenborn, A.M. (2021). Assessing the Structures and Interactions of γD-Crystallin Deamidation Variants. Structure, 29(3), 284-291.e3.Elsevier. doi: 10.1016/j.str.2020.11.006.
Nestor, G., Ruda, A., Anderson, T., Oscarson, S., Widmalm, G., & Gronenborn, A.M. (2021). A detailed picture of a protein-carbohydrate hydrogen-bonding network revealed by NMR and MD simulations. Glycobiology, 31(4), 508-518.Oxford University Press (OUP). doi: 10.1093/glycob/cwaa081.
Perilla, J.R., Hadden-Perilla, J.A., Gronenborn, A.M., & Polenova, T. (2021). Integrative structural biology of HIV-1 capsid protein assemblies: combining experiment and computation. Curr Opin Virol, 48, 57-64.Elsevier. doi: 10.1016/j.coviro.2021.03.005.
Quinn, C.M., Zadorozhnyi, R., Struppe, J., Sergeyev, I.V., Gronenborn, A.M., & Polenova, T. (2021). Fast 19F Magic-Angle Spinning Nuclear Magnetic Resonance for the Structural Characterization of Active Pharmaceutical Ingredients in Blockbuster Drugs. Anal Chem, 93(38), 13029-13037.American Chemical Society (ACS). doi: 10.1021/acs.analchem.1c02917.
Byeon, I.J.L., Jung, J., Byeon, C.H., DeLucia, M., Ahn, J., & Gronenborn, A.M. (2020). Complete 1H, 13C, 15N resonance assignments and secondary structure of the Vpr binding region of hHR23A (residues 223-363). Biomol NMR Assign, 14(1), 13-17.Springer Nature. doi: 10.1007/s12104-019-09913-x.
Hassan, A., Quinn, C.M., Struppe, J., Sergeyev, I.V., Zhang, C., Guo, C., Runge, B., Theint, T., Dao, H.H., Jaroniec, C.P., Berbon, M., Lends, A., Habenstein, B., Loquet, A., Kuemmerle, R., Perrone, B., Gronenborn, A.M., & Polenova, T. (2020). Sensitivity boosts by the CPMAS CryoProbe for challenging biological assemblies. J Magn Reson, 311, 106680.Elsevier. doi: 10.1016/j.jmr.2019.106680.
Kraus, J., Gupta, R., Lu, M., Gronenborn, A.M., Akke, M., & Polenova, T. (2020). Accurate Backbone 13 C and 15 N Chemical Shift Tensors in Galectin-3 Determined by MAS NMR and QM/MM: Details of Structure and Environment Matter. Chemphyschem, 21(13), 1436-1443.Wiley. doi: 10.1002/cphc.202000249.
Lu, M., Russell, R.W., Bryer, A.J., Quinn, C.M., Hou, G., Zhang, H., Schwieters, C.D., Perilla, J.R., Gronenborn, A.M., & Polenova, T. (2020). Atomic-resolution structure of HIV-1 capsid tubes by magic-angle spinning NMR. Nat Struct Mol Biol, 27(9), 863-869.Springer Nature. doi: 10.1038/s41594-020-0489-2.
Struppe, J., Quinn, C.M., Sarkar, S., Gronenborn, A.M., & Polenova, T. (2020). Ultrafast 1H MAS NMR Crystallography for Natural Abundance Pharmaceutical Compounds. Mol Pharm, 17(2), 674-682.American Chemical Society (ACS). doi: 10.1021/acs.molpharmaceut.9b01157.
Bozkurt, E., & Gronenborn, A.M. (2019). Diversifying Constrained Peptide Scaffolds: How To Truss Up a Bundle Really Tight. Biochemistry, 58(9), 1179-1180.American Chemical Society (ACS). doi: 10.1021/acs.biochem.9b00065.
Carlon, A., Gigli, L., Ravera, E., Parigi, G., Gronenborn, A.M., & Luchinat, C. (2019). Assessing Structural Preferences of Unstructured Protein Regions by NMR. Biophys J, 117(10), 1948-1953.Elsevier. doi: 10.1016/j.bpj.2019.10.008.
Debiec, K.T., Gronenborn, A.M., & Chong, L.T. (2019). Correction to "Evaluating the Strength of Salt Bridges: A Comparison of Current Biomolecular Force Fields". J Phys Chem B, 123(19), 4346.American Chemical Society (ACS). doi: 10.1021/acs.jpcb.9b03732.
Fritz, M., Kraus, J., Quinn, C.M., Yap, G.P.A., Struppe, J., Sergeyev, I.V., Gronenborn, A.M., & Polenova, T. (2019). Measurement of Accurate Interfluorine Distances in Crystalline Organic Solids: A High-Frequency Magic Angle Spinning NMR Approach. J Phys Chem B, 123(50), 10680-10690.American Chemical Society (ACS). doi: 10.1021/acs.jpcb.9b08919.
Gronenborn, A.M. (2019). Integrated BioNMR - "getting by with a little help from my friends". J Magn Reson, 306, 192-194.Elsevier. doi: 10.1016/j.jmr.2019.07.040.
Gronenborn, A.M. (2019). Integrated multidisciplinarity in the natural sciences. J Biol Chem, 294(48), 18162-18167.Elsevier. doi: 10.1074/jbc.AW119.008142.
Gupta, R., Zhang, H., Lu, M., Hou, G., Caporini, M., Rosay, M., Maas, W., Struppe, J., Ahn, J., Byeon, I.J.L., Oschkinat, H., Jaudzems, K., Barbet-Massin, E., Emsley, L., Pintacuda, G., Lesage, A., Gronenborn, A.M., & Polenova, T. (2019). Dynamic Nuclear Polarization Magic-Angle Spinning Nuclear Magnetic Resonance Combined with Molecular Dynamics Simulations Permits Detection of Order and Disorder in Viral Assemblies. J Phys Chem B, 123(24), 5048-5058.American Chemical Society (ACS). doi: 10.1021/acs.jpcb.9b02293.
Guseman, A.J., & Gronenborn, A.M. (2019). Isomerization as the secret Achilles' heel of long-lived proteins. J Biol Chem, 294(19), 7556-7557.Elsevier. doi: 10.1074/jbc.H119.008716.
Lu, M., Ishima, R., Polenova, T., & Gronenborn, A.M. (2019). 19F NMR relaxation studies of fluorosubstituted tryptophans. J Biomol NMR, 73(8-9), 401-409.Springer Nature. doi: 10.1007/s10858-019-00268-y.
Lu, M., Wang, M., Sergeyev, I.V., Quinn, C.M., Struppe, J., Rosay, M., Maas, W., Gronenborn, A.M., & Polenova, T. (2019). 19F Dynamic Nuclear Polarization at Fast Magic Angle Spinning for NMR of HIV-1 Capsid Protein Assemblies. J Am Chem Soc, 141(14), 5681-5691.American Chemical Society (ACS). doi: 10.1021/jacs.8b09216.
Russell, R.W., Fritz, M.P., Kraus, J., Quinn, C.M., Polenova, T., & Gronenborn, A.M. (2019). Accuracy and precision of protein structures determined by magic angle spinning NMR spectroscopy: for some 'with a little help from a friend'. J Biomol NMR, 73(6-7), 333-346.Springer Nature. doi: 10.1007/s10858-019-00233-9.
Debiec, K.T., Whitley, M.J., Koharudin, L.M.I., Chong, L.T., & Gronenborn, A.M. (2018). Integrating NMR, SAXS, and Atomistic Simulations: Structure and Dynamics of a Two-Domain Protein. Biophys J, 114(4), 839-855.Elsevier. doi: 10.1016/j.bpj.2018.01.001.
Fritz, M., Quinn, C.M., Wang, M., Hou, G., Lu, X., Koharudin, L.M.I., Struppe, J., Case, D.A., Polenova, T., & Gronenborn, A.M. (2018). Determination of accurate backbone chemical shift tensors in microcrystalline proteins by integrating MAS NMR and QM/MM. Phys Chem Chem Phys, 20(14), 9543-9553.Royal Society of Chemistry (RSC). doi: 10.1039/c8cp00647d.
Gronenborn, A.M. (2018). Harnessing the Combined Power of SAXS and NMR. Adv Exp Med Biol, 1105, 171-180.Springer Nature. doi: 10.1007/978-981-13-2200-6_11.
Kraus, J., Gupta, R., Yehl, J., Lu, M., Case, D.A., Gronenborn, A.M., Akke, M., & Polenova, T. (2018). Chemical Shifts of the Carbohydrate Binding Domain of Galectin-3 from Magic Angle Spinning NMR and Hybrid Quantum Mechanics/Molecular Mechanics Calculations. J Phys Chem B, 122(11), 2931-2939.American Chemical Society (ACS). doi: 10.1021/acs.jpcb.8b00853.
Krzysiak, T.C., Thomas, L., Choi, Y.J., Auclair, S., Qian, Y., Luan, S., Krasnow, S.M., Thomas, L.L., Koharudin, L.M.I., Benos, P.V., Marks, D.L., Gronenborn, A.M., & Thomas, G. (2018). An Insulin-Responsive Sensor in the SIRT1 Disordered Region Binds DBC1 and PACS-2 to Control Enzyme Activity. Mol Cell, 72(6), 985-998.e7.Elsevier. doi: 10.1016/j.molcel.2018.10.007.
Lu, M., Sarkar, S., Wang, M., Kraus, J., Fritz, M., Quinn, C.M., Bai, S., Holmes, S.T., Dybowski, C., Yap, G.P.A., Struppe, J., Sergeyev, I.V., Maas, W., Gronenborn, A.M., & Polenova, T. (2018). 19F Magic Angle Spinning NMR Spectroscopy and Density Functional Theory Calculations of Fluorosubstituted Tryptophans: Integrating Experiment and Theory for Accurate Determination of Chemical Shift Tensors. J Phys Chem B, 122(23), 6148-6155.American Chemical Society (ACS). doi: 10.1021/acs.jpcb.8b00377.
Nestor, G., Anderson, T., Oscarson, S., & Gronenborn, A.M. (2018). Direct Observation of Carbohydrate Hydroxyl Protons in Hydrogen Bonds with a Protein. J Am Chem Soc, 140(1), 339-345.American Chemical Society (ACS). doi: 10.1021/jacs.7b10595.
Paramasivam, S., Gronenborn, A.M., & Polenova, T. (2018). Backbone amide 15N chemical shift tensors report on hydrogen bonding interactions in proteins: A magic angle spinning NMR study. Solid State Nucl Magn Reson, 92, 1-6.Elsevier. doi: 10.1016/j.ssnmr.2018.03.002.
Quinn, C.M., Wang, M., Fritz, M.P., Runge, B., Ahn, J., Xu, C., Perilla, J.R., Gronenborn, A.M., & Polenova, T. (2018). Dynamic regulation of HIV-1 capsid interaction with the restriction factor TRIM5α identified by magic-angle spinning NMR and molecular dynamics simulations. Proc Natl Acad Sci U S A, 115(45), 11519-11524.Proceedings of the National Academy of Sciences. doi: 10.1073/pnas.1800796115.
Wang, M., Lu, M., Fritz, M.P., Quinn, C.M., Byeon, I.J.L., Byeon, C.H., Struppe, J., Maas, W., Gronenborn, A.M., & Polenova, T. (2018). Fast Magic-Angle Spinning 19 F NMR Spectroscopy of HIV-1 Capsid Protein Assemblies. Angew Chem Int Ed Engl, 57(50), 16375-16379.Wiley. doi: 10.1002/anie.201809060.
Boatz, J.C., Whitley, M.J., Li, M., Gronenborn, A.M., & van der Wel, P.C.A. (2017). Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH. Nat Commun, 8(1), 15137.Springer Nature. doi: 10.1038/ncomms15137.
Fritz, M., Quinn, C.M., Wang, M., Hou, G., Lu, X., Koharudin, L.M.I., Polenova, T., & Gronenborn, A.M. (2017). Toward Closing the Gap: Quantum Mechanical Calculations and Experimentally Measured Chemical Shifts of a Microcrystalline Lectin. J Phys Chem B, 121(15), 3574-3585.American Chemical Society (ACS). doi: 10.1021/acs.jpcb.6b09479.
Mitchell, S.D., & Gronenborn, A.M. (2017). After Fifty Years, Why Are Protein X-ray Crystallographers Still in Business?. BRITISH JOURNAL FOR THE PHILOSOPHY OF SCIENCE, 68(3), 703-723.University of Chicago Press. doi: 10.1093/bjps/axv051.
Nestor, G., Anderson, T., Oscarson, S., & Gronenborn, A.M. (2017). Exploiting Uniformly 13C-Labeled Carbohydrates for Probing Carbohydrate-Protein Interactions by NMR Spectroscopy. J Am Chem Soc, 139(17), 6210-6216.American Chemical Society (ACS). doi: 10.1021/jacs.7b01929.
Perilla, J.R., Zhao, G., Lu, M., Ning, J., Hou, G., Byeon, I.J.L., Gronenborn, A.M., Polenova, T., & Zhang, P. (2017). CryoEM Structure Refinement by Integrating NMR Chemical Shifts with Molecular Dynamics Simulations. J Phys Chem B, 121(15), 3853-3863.American Chemical Society (ACS). doi: 10.1021/acs.jpcb.6b13105.
Sharaf, N.G., Brereton, A.E., Byeon, I.J.L., Karplus, P.A., & Gronenborn, A.M. (2017). Correction to: NMR structure of the HIV-1 reverse transcriptase thumb subdomain. J Biomol NMR, 69(4), 247.Springer Nature. doi: 10.1007/s10858-017-0139-0.
Sharaf, N.G., Xi, Z., Ishima, R., & Gronenborn, A.M. (2017). The HIV-1 p66 homodimeric RT exhibits different conformations in the binding-competent and -incompetent NNRTI site. Proteins, 85(12), 2191-2197.Wiley. doi: 10.1002/prot.25383.
Struppe, J., Quinn, C.M., Lu, M., Wang, M., Hou, G., Lu, X., Kraus, J., Andreas, L.B., Stanek, J., Lalli, D., Lesage, A., Pintacuda, G., Maas, W., Gronenborn, A.M., & Polenova, T. (2017). Expanding the horizons for structural analysis of fully protonated protein assemblies by NMR spectroscopy at MAS frequencies above 100 kHz. Solid State Nucl Magn Reson, 87, 117-125.Elsevier. doi: 10.1016/j.ssnmr.2017.07.001.
Wang, M., Quinn, C.M., Perilla, J.R., Zhang, H., Shirra, R., Hou, G., Byeon, I.J., Suiter, C.L., Ablan, S., Urano, E., Nitz, T.J., Aiken, C., Freed, E.O., Zhang, P., Schulten, K., Gronenborn, A.M., & Polenova, T. (2017). Quenching protein dynamics interferes with HIV capsid maturation. Nat Commun, 8(1), 1779.Springer Nature. doi: 10.1038/s41467-017-01856-y.
Whitley, M.J., Xi, Z., Bartko, J.C., Jensen, M.R., Blackledge, M., & Gronenborn, A.M. (2017). A Combined NMR and SAXS Analysis of the Partially Folded Cataract-Associated V75D γD-Crystallin. Biophys J, 112(6), 1135-1146.Elsevier. doi: 10.1016/j.bpj.2017.02.010.
Xi, Z., Whitley, M.J., & Gronenborn, A.M. (2017). Human βB2-Crystallin Forms a Face-en-Face Dimer in Solution: An Integrated NMR and SAXS Study. Structure, 25(3), 496-505.Elsevier. doi: 10.1016/j.str.2017.02.001.
Byeon, I.J.L., Byeon, C.H., Wu, T., Mitra, M., Singer, D., Levin, J.G., & Gronenborn, A.M. (2016). Nuclear Magnetic Resonance Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity. Biochemistry, 55(21), 2944-2959.American Chemical Society (ACS). doi: 10.1021/acs.biochem.6b00382.
Debiec, K.T., Cerutti, D.S., Baker, L.R., Gronenborn, A.M., Case, D.A., & Chong, L.T. (2016). Further along the Road Less Traveled: AMBER ff15ipq, an Original Protein Force Field Built on a Self-Consistent Physical Model. J Chem Theory Comput, 12(8), 3926-3947.American Chemical Society (ACS). doi: 10.1021/acs.jctc.6b00567.
Gupta, R., Lu, M., Hou, G., Caporini, M.A., Rosay, M., Maas, W., Struppe, J., Suiter, C., Ahn, J., Byeon, I.J.L., Franks, W.T., Orwick-Rydmark, M., Bertarello, A., Oschkinat, H., Lesage, A., Pintacuda, G., Gronenborn, A.M., & Polenova, T. (2016). Dynamic Nuclear Polarization Enhanced MAS NMR Spectroscopy for Structural Analysis of HIV-1 Protein Assemblies. J Phys Chem B, 120(2), 329-339.American Chemical Society (ACS). doi: 10.1021/acs.jpcb.5b12134.
Krzysiak, T.C., Chen, B.B., Lear, T., Mallampalli, R.K., & Gronenborn, A.M. (2016). Crystal structure and interaction studies of the human FBxo3 ApaG domain. FEBS J, 283(11), 2091-2101.Wiley. doi: 10.1111/febs.13721.
Liu, C., Perilla, J.R., Ning, J., Lu, M., Hou, G., Ramalho, R., Himes, B.A., Zhao, G., Bedwell, G.J., Byeon, I.J., Ahn, J., Gronenborn, A.M., Prevelige, P.E., Rousso, I., Aiken, C., Polenova, T., Schulten, K., & Zhang, P. (2016). Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site. Nat Commun, 7(1), 10714.Springer Nature. doi: 10.1038/ncomms10714.
Liu, X., Hillwig, M.L., Koharudin, L.M.I., & Gronenborn, A.M. (2016). Unified biogenesis of ambiguine, fischerindole, hapalindole and welwitindolinone: identification of a monogeranylated indolenine as a cryptic common biosynthetic intermediate by an unusual magnesium-dependent aromatic prenyltransferase. Chem Commun (Camb), 52(8), 1737-1740.Royal Society of Chemistry (RSC). doi: 10.1039/c5cc10060g.
Matei, E., & Gronenborn, A.M. (2016). (19)F Paramagnetic Relaxation Enhancement: A Valuable Tool for Distance Measurements in Proteins. Angew Chem Int Ed Engl, 55(1), 150-154.Wiley. doi: 10.1002/anie.201508464.
Matei, E., Basu, R., Furey, W., Shi, J., Calnan, C., Aiken, C., & Gronenborn, A.M. (2016). Structure and Glycan Binding of a New Cyanovirin-N Homolog. J Biol Chem, 291(36), 18967-18976.Elsevier. doi: 10.1074/jbc.M116.740415.
Perilla, J.R., & Gronenborn, A.M. (2016). Molecular Architecture of the Retroviral Capsid. Trends Biochem Sci, 41(5), 410-420.Elsevier. doi: 10.1016/j.tibs.2016.02.009.
Sharaf, N.G., Brereton, A.E., Byeon, I.J.L., Karplus, P.A., & Gronenborn, A.M. (2016). NMR structure of the HIV-1 reverse transcriptase thumb subdomain. J Biomol NMR, 66(4), 273-280.Springer Nature. doi: 10.1007/s10858-016-0077-2.
Sharaf, N.G., Ishima, R., & Gronenborn, A.M. (2016). Conformational Plasticity of the NNRTI-Binding Pocket in HIV-1 Reverse Transcriptase: A Fluorine Nuclear Magnetic Resonance Study. Biochemistry, 55(28), 3864-3873.American Chemical Society (ACS). doi: 10.1021/acs.biochem.6b00113.
Stevenson, H.P., Lin, G., Barnes, C.O., Sutkeviciute, I., Krzysiak, T., Weiss, S.C., Reynolds, S., Wu, Y., Nagarajan, V., Makhov, A.M., Lawrence, R., Lamm, E., Clark, L., Gardella, T.J., Hogue, B.G., Ogata, C.M., Ahn, J., Gronenborn, A.M., Conway, J.F., Vilardaga, J.P., Cohen, A.E., & Calero, G. (2016). Transmission electron microscopy for the evaluation and optimization of crystal growth. Acta Crystallogr D Struct Biol, 72(Pt 5), 603-615.International Union of Crystallography (IUCr). doi: 10.1107/S2059798316001546.
Wu, Y., Zhou, X., Barnes, C.O., DeLucia, M., Cohen, A.E., Gronenborn, A.M., Ahn, J., & Calero, G. (2016). The DDB1-DCAF1-Vpr-UNG2 crystal structure reveals how HIV-1 Vpr steers human UNG2 toward destruction. Nat Struct Mol Biol, 23(10), 933-940.Springer Nature. doi: 10.1038/nsmb.3284.
Zhang, H., Hou, G., Lu, M., Ahn, J., Byeon, I.J.L., Langmead, C.J., Perilla, J.R., Hung, I., Gor'kov, P.L., Gan, Z., Brey, W.W., Case, D.A., Schulten, K., Gronenborn, A.M., & Polenova, T. (2016). HIV-1 Capsid Function Is Regulated by Dynamics: Quantitative Atomic-Resolution Insights by Integrating Magic-Angle-Spinning NMR, QM/MM, and MD. J Am Chem Soc, 138(42), 14066-14075.American Chemical Society (ACS). doi: 10.1021/jacs.6b08744.
Carneiro, M.G., Koharudin, L.M.I., Ban, D., Sabo, T.M., Trigo-Mourino, P., Mazur, A., Griesinger, C., Gronenborn, A.M., & Lee, D. (2015). Sampling of Glycan-Bound Conformers by the Anti-HIV Lectin Oscillatoria agardhii agglutinin in the Absence of Sugar. Angew Chem Int Ed Engl, 54(22), 6462-6465.Wiley. doi: 10.1002/anie.201500213.
Carneiro, M.G., Koharudin, L.M.I., Griesinger, C., Gronenborn, A.M., & Lee, D. (2015). (1)H, (13)C and (15)N resonance assignment of the anti-HIV lectin from Oscillatoria agardhii. Biomol NMR Assign, 9(2), 317-319.Springer Nature. doi: 10.1007/s12104-015-9600-8.
Koharudin, L.M.I., Debiec, K.T., & Gronenborn, A.M. (2015). Structural Insight into Fungal Cell Wall Recognition by a CVNH Protein with a Single LysM Domain. Structure, 23(11), 2143-2154.Elsevier. doi: 10.1016/j.str.2015.07.023.
Lu, M., Hou, G., Zhang, H., Suiter, C.L., Ahn, J., Byeon, I.J.L., Perilla, J.R., Langmead, C.J., Hung, I., Gor'kov, P.L., Gan, Z., Brey, W., Aiken, C., Zhang, P., Schulten, K., Gronenborn, A.M., & Polenova, T. (2015). Dynamic allostery governs cyclophilin A-HIV capsid interplay. Proc Natl Acad Sci U S A, 112(47), 14617-14622.Proceedings of the National Academy of Sciences. doi: 10.1073/pnas.1516920112.
Mitra, M., Singer, D., Mano, Y., Hritz, J., Nam, G., Gorelick, R.J., Byeon, I.J.L., Gronenborn, A.M., Iwatani, Y., & Levin, J.G. (2015). Sequence and structural determinants of human APOBEC3H deaminase and anti-HIV-1 activities. Retrovirology, 12(1), 3.Springer Nature. doi: 10.1186/s12977-014-0130-8.
Sharaf, N.G., & Gronenborn, A.M. (2015). (19)F-modified proteins and (19)F-containing ligands as tools in solution NMR studies of protein interactions. Methods Enzymol, 565, 67-95.Elsevier. doi: 10.1016/bs.mie.2015.05.014.
Wu, Y., Koharudin, L.M.I., Mehrens, J., DeLucia, M., Byeon, C.H., Byeon, I.J.L., Calero, G., Ahn, J., & Gronenborn, A.M. (2015). Structural Basis of Clade-specific Engagement of SAMHD1 (Sterile α Motif and Histidine/Aspartate-containing Protein 1) Restriction Factors by Lentiviral Viral Protein X (Vpx) Virulence Factors. J Biol Chem, 290(29), 17935-17945.Elsevier. doi: 10.1074/jbc.M115.665513.
Debiec, K.T., Gronenborn, A.M., & Chong, L.T. (2014). Evaluating the strength of salt bridges: a comparison of current biomolecular force fields. J Phys Chem B, 118(24), 6561-6569.American Chemical Society (ACS). doi: 10.1021/jp500958r.
Férir, G., Huskens, D., Noppen, S., Koharudin, L.M.I., Gronenborn, A.M., & Schols, D. (2014). Broad anti-HIV activity of the Oscillatoria agardhii agglutinin homologue lectin family. J Antimicrob Chemother, 69(10), 2746-2758.Oxford University Press (OUP). doi: 10.1093/jac/dku220.
Hritz, J., Byeon, I.J.L., Krzysiak, T., Martinez, A., Sklenar, V., & Gronenborn, A.M. (2014). Dissection of binding between a phosphorylated tyrosine hydroxylase peptide and 14-3-3zeta: A complex story elucidated by NMR. Biophys J, 107(9), 2185-2194.Elsevier. doi: 10.1016/j.bpj.2014.08.039.
Jung, J., Byeon, I.J.L., DeLucia, M., Koharudin, L.M.I., Ahn, J., & Gronenborn, A.M. (2014). Binding of HIV-1 Vpr protein to the human homolog of the yeast DNA repair protein RAD23 (hHR23A) requires its xeroderma pigmentosum complementation group C binding (XPCB) domain as well as the ubiquitin-associated 2 (UBA2) domain. J Biol Chem, 289(5), 2577-2588.Elsevier. doi: 10.1074/jbc.M113.534453.
Koharudin, L.M.I., & Gronenborn, A.M. (2014). Antiviral lectins as potential HIV microbicides. Curr Opin Virol, 7(1), 95-100.Elsevier. doi: 10.1016/j.coviro.2014.05.006.
Koharudin, L.M.I., & Gronenborn, A.M. (2014). Lectins as HIV Microbicides. In HIV glycans in infection and immunity. 9781461488729, (pp. 177-211).Springer Nature. doi: 10.1007/978-1-4614-8872-9_7.
Koharudin, L.M.I., Wu, Y., DeLucia, M., Mehrens, J., Gronenborn, A.M., & Ahn, J. (2014). Structural basis of allosteric activation of sterile α motif and histidine-aspartate domain-containing protein 1 (SAMHD1) by nucleoside triphosphates. J Biol Chem, 289(47), 32617-32627.Elsevier. doi: 10.1074/jbc.M114.591958.
Mitra, M., Hercík, K., Byeon, I.J.L., Ahn, J., Hill, S., Hinchee-Rodriguez, K., Singer, D., Byeon, C.H., Charlton, L.M., Nam, G., Heidecker, G., Gronenborn, A.M., & Levin, J.G. (2014). Structural determinants of human APOBEC3A enzymatic and nucleic acid binding properties. Nucleic Acids Res, 42(2), 1095-1110.Oxford University Press (OUP). doi: 10.1093/nar/gkt945.
Qin, J., & Gronenborn, A.M. (2014). Weak protein complexes: challenging to study but essential for life. FEBS J, 281(8), 1948-1949.Wiley. doi: 10.1111/febs.12744.
Sharaf, N.G., Poliner, E., Slack, R.L., Christen, M.T., Byeon, I.J.L., Parniak, M.A., Gronenborn, A.M., & Ishima, R. (2014). The p66 immature precursor of HIV-1 reverse transcriptase. Proteins, 82(10), 2343-2352.Wiley. doi: 10.1002/prot.24594.
Ban, D., Mazur, A., Carneiro, M.G., Sabo, T.M., Giller, K., Koharudin, L.M.I., Becker, S., Gronenborn, A.M., Griesinger, C., & Lee, D. (2013). Enhanced accuracy of kinetic information from CT-CPMG experiments by transverse rotating-frame spectroscopy. J Biomol NMR, 57(1), 73-82.Springer Nature. doi: 10.1007/s10858-013-9769-z.
Byeon, I.J.L., Ahn, J., Mitra, M., Byeon, C.H., Hercík, K., Hritz, J., Charlton, L.M., Levin, J.G., & Gronenborn, A.M. (2013). NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity. Nat Commun, 4(1), 1890.Springer Nature. doi: 10.1038/ncomms2883.
Han, Y., Hou, G., Suiter, C.L., Ahn, J., Byeon, I.J.L., Lipton, A.S., Burton, S., Hung, I., Gor'kov, P.L., Gan, Z., Brey, W., Rice, D., Gronenborn, A.M., & Polenova, T. (2013). Magic angle spinning NMR reveals sequence-dependent structural plasticity, dynamics, and the spacer peptide 1 conformation in HIV-1 capsid protein assemblies. J Am Chem Soc, 135(47), 17793-17803.American Chemical Society (ACS). doi: 10.1021/ja406907h.
Ji, F., Jung, J., Koharudin, L.M.I., & Gronenborn, A.M. (2013). The human W42R γD-crystallin mutant structure provides a link between congenital and age-related cataracts. J Biol Chem, 288(1), 99-109.Elsevier. doi: 10.1074/jbc.M112.416354.
Ji, F., Koharudin, L.M.I., Jung, J., & Gronenborn, A.M. (2013). Crystal structure of the cataract-causing P23T γD-crystallin mutant. Proteins, 81(9), 1493-1498.Wiley. doi: 10.1002/prot.24321.
Ji, X., Wu, Y., Yan, J., Mehrens, J., Yang, H., DeLucia, M., Hao, C., Gronenborn, A.M., Skowronski, J., Ahn, J., & Xiong, Y. (2013). Mechanism of allosteric activation of SAMHD1 by dGTP. Nat Struct Mol Biol, 20(11), 1304-1309.Springer Nature. doi: 10.1038/nsmb.2692.
Koharudin, L.M.I., & Gronenborn, A.M. (2013). Sweet entanglements--protein:glycan interactions in two HIV-inactivating lectin families. Biopolymers, 99(3), 196-202.Wiley. doi: 10.1002/bip.22106.
Koharudin, L.M.I., & Gronenborn, A.M. (2013). Structures of novel HIV-Inactivating lectins. NATO Science for Peace and Security Series B: Physics and Biophysics, 59-67. doi: 10.1007/978-94-007-4923-8-4.
Koharudin, L.M.I., Boelens, R., Kaptein, R., & Gronenborn, A.M. (2013). A NMR guided approach for CsrA-RNA crystallization. J Biomol NMR, 56(1), 31-39.Springer Nature. doi: 10.1007/s10858-013-9712-3.
Koharudin, L.M.I., Liu, L., & Gronenborn, A.M. (2013). Different 3D domain-swapped oligomeric cyanovirin-N structures suggest trapped folding intermediates. Proc Natl Acad Sci U S A, 110(19), 7702-7707.Proceedings of the National Academy of Sciences. doi: 10.1073/pnas.1300327110.
Matei, E., André, S., Glinschert, A., Infantino, A.S., Oscarson, S., Gabius, H.J., & Gronenborn, A.M. (2013). Fluorinated carbohydrates as lectin ligands: dissecting glycan-cyanovirin interactions by using 19F NMR spectroscopy. Chemistry, 19(17), 5364-5374.Wiley. doi: 10.1002/chem.201204070.
Wang, X., Matei, E., Deng, L., Koharudin, L., Gronenborn, A.M., Ramström, O., & Yan, M. (2013). Sensing lectin-glycan interactions using lectin super-microarrays and glycans labeled with dye-doped silica nanoparticles. Biosens Bioelectron, 47, 258-264.Elsevier. doi: 10.1016/j.bios.2013.03.014.
Whitley, M.J., Furey, W., Kollipara, S., & Gronenborn, A.M. (2013). Burkholderia oklahomensis agglutinin is a canonical two-domain OAA-family lectin: structures, carbohydrate binding and anti-HIV activity. FEBS J, 280(9), 2056-2067.Wiley. doi: 10.1111/febs.12229.
Yan, J., Kaur, S., DeLucia, M., Hao, C., Mehrens, J., Wang, C., Golczak, M., Palczewski, K., Gronenborn, A.M., Ahn, J., & Skowronski, J. (2013). Tetramerization of SAMHD1 is required for biological activity and inhibition of HIV infection. J Biol Chem, 288(15), 10406-10417.Elsevier. doi: 10.1074/jbc.M112.443796.
Zhao, G., Perilla, J.R., Yufenyuy, E.L., Meng, X., Chen, B., Ning, J., Ahn, J., Gronenborn, A.M., Schulten, K., Aiken, C., & Zhang, P. (2013). Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics. Nature, 497(7451), 643-646.Springer Nature. doi: 10.1038/nature12162.
Ahn, J., Hao, C., Yan, J., DeLucia, M., Mehrens, J., Wang, C., Gronenborn, A.M., & Skowronski, J. (2012). HIV/simian immunodeficiency virus (SIV) accessory virulence factor Vpx loads the host cell restriction factor SAMHD1 onto the E3 ubiquitin ligase complex CRL4DCAF1. J Biol Chem, 287(15), 12550-12558.Elsevier. doi: 10.1074/jbc.M112.340711.
Byeon, I.J.L., Hou, G., Han, Y., Suiter, C.L., Ahn, J., Jung, J., Byeon, C.H., Gronenborn, A.M., & Polenova, T. (2012). Motions on the millisecond time scale and multiple conformations of HIV-1 capsid protein: implications for structural polymorphism of CA assemblies. J Am Chem Soc, 134(14), 6455-6466.American Chemical Society (ACS). doi: 10.1021/ja300937v.
Hou, G., Byeon, I.J.L., Ahn, J., Gronenborn, A.M., & Polenova, T. (2012). Recoupling of chemical shift anisotropy by R-symmetry sequences in magic angle spinning NMR spectroscopy. J Chem Phys, 137(13), 134201.AIP Publishing. doi: 10.1063/1.4754149.
Jayaraman, M., Mishra, R., Kodali, R., Thakur, A.K., Koharudin, L.M.I., Gronenborn, A.M., & Wetzel, R. (2012). Kinetically competing huntingtin aggregation pathways control amyloid polymorphism and properties. Biochemistry, 51(13), 2706-2716.American Chemical Society (ACS). doi: 10.1021/bi3000929.
Ji, F., Jung, J., & Gronenborn, A.M. (2012). Structural and biochemical characterization of the childhood cataract-associated R76S mutant of human γD-crystallin. Biochemistry, 51(12), 2588-2596.American Chemical Society (ACS). doi: 10.1021/bi300199d.
Kilpatrick, A.M., Koharudin, L.M.I., Calero, G.A., & Gronenborn, A.M. (2012). Structural and binding studies of the C-terminal domains of yeast TFIIF subunits Tfg1 and Tfg2. Proteins, 80(2), 519-529.Wiley. doi: 10.1002/prot.23217.
Koharudin, L.M.I., & Gronenborn, A.M. (2012). Structural Glycobiology. In Structural Glycobiology, Yuriev, E., & Ramsland, P.A. (Eds.). (pp. 29-45).CRC Press. doi: 10.1201/b12965.
Koharudin, L.M.I., Kollipara, S., Aiken, C., & Gronenborn, A.M. (2012). Structural insights into the anti-HIV activity of the Oscillatoria agardhii agglutinin homolog lectin family. J Biol Chem, 287(40), 33796-33811.Elsevier. doi: 10.1074/jbc.M112.388579.
Krzysiak, T.C., Jung, J., Thompson, J., Baker, D., & Gronenborn, A.M. (2012). APOBEC2 is a monomer in solution: implications for APOBEC3G models. Biochemistry, 51(9), 2008-2017.American Chemical Society (ACS). doi: 10.1021/bi300021s.
Liu, L., & Gronenborn, A.M. (2012). 3.8 Protein and Nucleic Acid Folding: Domain Swapping in Proteins. In Comprehensive Biophysics. 3, (pp. 148-169).Elsevier. doi: 10.1016/b978-0-12-374920-8.00309-x.
Liu, L., Byeon, I.J.L., Bahar, I., & Gronenborn, A.M. (2012). Domain swapping proceeds via complete unfolding: a 19F- and 1H-NMR study of the Cyanovirin-N protein. J Am Chem Soc, 134(9), 4229-4235.American Chemical Society (ACS). doi: 10.1021/ja210118w.
Liu, L., Gronenborn, A.M., & Bahar, I. (2012). Longer simulations sample larger subspaces of conformations while maintaining robust mechanisms of motion. Proteins, 80(2), 616-625.Wiley. doi: 10.1002/prot.23225.
Markley, J.L., Akutsu, H., Asakura, T., Baldus, M., Boelens, R., Bonvin, A., Kaptein, R., Bax, A., Bezsonova, I., Gryk, M.R., Hoch, J.C., Korzhnev, D.M., Maciejewski, M.W., Case, D., Chazin, W.J., Cross, T.A., Dames, S., Kessler, H., Lange, O., Madl, T., Reif, B., Sattler, M., Eliezer, D., Fersht, A., Forman-Kay, J., Kay, L.E., Fraser, J., Gross, J., Kortemme, T., Sali, A., Fujiwara, T., Gardner, K., Luo, X., Rizo-Rey, J., Rosen, M., Gil, R.R., Ho, C., Rule, G., Gronenborn, A.M., Ishima, R., Klein-Seetharaman, J., Tang, P., van der Wel, P., Xu, Y., Grzesiek, S., Hiller, S., Seelig, J., Laue, E.D., Mott, H., Nietlispach, D., Barsukov, I., Lian, L.Y., Middleton, D., Blumenschein, T., Moore, G., Campbell, I., Schnell, J., Vakonakis, I.J., Watts, A., Conte, M.R., Mason, J., Pfuhl, M., Sanderson, M.R., Craven, J., Williamson, M., Dominguez, C., Roberts, G., Günther, U., Overduin, M., Werner, J., Williamson, P., Blindauer, C., Crump, M., Driscoll, P., Frenkiel, T., Golovanov, A., Matthews, S., Parkinson, J., Uhrin, D., Williams, M., Neuhaus, D., Oschkinat, H., Ramos, A., Shaw, D.E., Steinbeck, C., Vendruscolo, M., Vuister, G.W., Walters, K.J., Weinstein, H., Wüthrich, K., & Yokoyama, S. (2012). In support of the BMRB. Nat Struct Mol Biol, 19(9), 854-860.Springer Nature. doi: 10.1038/nsmb.2371.
Meng, X., Zhao, G., Yufenyuy, E., Ke, D., Ning, J., Delucia, M., Ahn, J., Gronenborn, A.M., Aiken, C., & Zhang, P. (2012). Protease cleavage leads to formation of mature trimer interface in HIV-1 capsid. In Young, J.A.T. (Ed.). PLoS Pathog, 8(8), e1002886.Public Library of Science (PLoS). doi: 10.1371/journal.ppat.1002886.
Sun, S., Han, Y., Paramasivam, S., Yan, S., Siglin, A.E., Williams, J.C., Byeon, I.J.L., Ahn, J., Gronenborn, A.M., & Polenova, T. (2012). Solid-state NMR spectroscopy of protein complexes. Methods Mol Biol, 831, 303-331.Springer Nature. doi: 10.1007/978-1-61779-480-3_17.
Wang, X., Matei, E., Gronenborn, A.M., Ramström, O., & Yan, M. (2012). Direct measurement of glyconanoparticles and lectin interactions by isothermal titration calorimetry. Anal Chem, 84(10), 4248-4252.American Chemical Society (ACS). doi: 10.1021/ac3006632.
Yang, H., Ji, X., Zhao, G., Ning, J., Zhao, Q., Aiken, C., Gronenborn, A.M., Zhang, P., & Xiong, Y. (2012). Structural insight into HIV-1 capsid recognition by rhesus TRIM5α. Proc Natl Acad Sci U S A, 109(45), 18372-18377.Proceedings of the National Academy of Sciences. doi: 10.1073/pnas.1210903109.
Yang, R., Shi, J., Byeon, I.J.L., Ahn, J., Sheehan, J.H., Meiler, J., Gronenborn, A.M., & Aiken, C. (2012). Second-site suppressors of HIV-1 capsid mutations: restoration of intracellular activities without correction of intrinsic capsid stability defects. Retrovirology, 9(1), 30.Springer Nature. doi: 10.1186/1742-4690-9-30.
Ahn, J., Novince, Z., Concel, J., Byeon, C.H., Makhov, A.M., Byeon, I.J.L., Zhang, P., & Gronenborn, A.M. (2011). The Cullin-RING E3 ubiquitin ligase CRL4-DCAF1 complex dimerizes via a short helical region in DCAF1. Biochemistry, 50(8), 1359-1367.American Chemical Society (ACS). doi: 10.1021/bi101749s.
Dao, K.K., Pey, A.L., Gjerde, A.U., Teigen, K., Byeon, I.J.L., Døskeland, S.O., Gronenborn, A.M., & Martinez, A. (2011). The regulatory subunit of PKA-I remains partially structured and undergoes β-aggregation upon thermal denaturation. In Mayer, C. (Ed.). PLoS One, 6(3), e17602.Public Library of Science (PLoS). doi: 10.1371/journal.pone.0017602.
Garrett, D.S., Gronenborn, A.M., & Clore, G.M. (2011). A short recollection on the paper entitled "A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams" by D.S. Garrett, R. Powers, A.M. Gronenborn, and G.M. Clore [J. Magn. Reson. 95 (1991) 214-220]. J Magn Reson, 213(2), 364-365.Elsevier. doi: 10.1016/j.jmr.2011.08.009.
Garrett, D.S., Powers, R., Gronenborn, A.M., & Clore, G.M. (2011). A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams. 1991. J Magn Reson, 213(2), 357-363.Elsevier. doi: 10.1016/j.jmr.2011.09.007.
Hou, G., Byeon, I.J.L., Ahn, J., Gronenborn, A.M., & Polenova, T. (2011). 1H-13C/1H-15N heteronuclear dipolar recoupling by R-symmetry sequences under fast magic angle spinning for dynamics analysis of biological and organic solids. J Am Chem Soc, 133(46), 18646-18655.American Chemical Society (ACS). doi: 10.1021/ja203771a.
Hou, G., Yan, S., Sun, S., Han, Y., Byeon, I.J.L., Ahn, J., Concel, J., Samoson, A., Gronenborn, A.M., & Polenova, T. (2011). Spin diffusion driven by R-symmetry sequences: applications to homonuclear correlation spectroscopy in MAS NMR of biological and organic solids. J Am Chem Soc, 133(11), 3943-3953.American Chemical Society (ACS). doi: 10.1021/ja108650x.
Jung, J., Byeon, I.J.L., Ahn, J., & Gronenborn, A.M. (2011). Structure, dynamics, and Hck interaction of full-length HIV-1 Nef. Proteins, 79(5), 1609-1622.Wiley. doi: 10.1002/prot.22986.
Koharudin, L.M.I., & Gronenborn, A.M. (2011). Structural basis of the anti-HIV activity of the cyanobacterial Oscillatoria Agardhii agglutinin. Structure, 19(8), 1170-1181.Elsevier. doi: 10.1016/j.str.2011.05.010.
Koharudin, L.M.I., Furey, W., & Gronenborn, A.M. (2011). Novel fold and carbohydrate specificity of the potent anti-HIV cyanobacterial lectin from Oscillatoria agardhii. J Biol Chem, 286(2), 1588-1597.Elsevier. doi: 10.1074/jbc.M110.173278.
Koharudin, L.M.I., Viscomi, A.R., Montanini, B., Kershaw, M.J., Talbot, N.J., Ottonello, S., & Gronenborn, A.M. (2011). Structure-function analysis of a CVNH-LysM lectin expressed during plant infection by the rice blast fungus Magnaporthe oryzae. Structure, 19(5), 662-674.Elsevier. doi: 10.1016/j.str.2011.03.004.
Matei, E., Louis, J.M., Jee, J., & Gronenborn, A.M. (2011). NMR solution structure of a cyanovirin homolog from wheat head blight fungus. Proteins, 79(5), 1538-1549.Wiley. doi: 10.1002/prot.22981.
Wang, X., Matei, E., Deng, L., Ramström, O., Gronenborn, A.M., & Yan, M. (2011). Multivalent glyconanoparticles with enhanced affinity to the anti-viral lectin Cyanovirin-N. Chem Commun (Camb), 47(30), 8620-8622.Royal Society of Chemistry (RSC). doi: 10.1039/c1cc12981c.
Zhao, G., Ke, D., Vu, T., Ahn, J., Shah, V.B., Yang, R., Aiken, C., Charlton, L.M., Gronenborn, A.M., & Zhang, P. (2011). Rhesus TRIM5α disrupts the HIV-1 capsid at the inter-hexamer interfaces. In Luban, J. (Ed.). PLoS Pathog, 7(3), e1002009.Public Library of Science (PLoS). doi: 10.1371/journal.ppat.1002009.
Ahn, J., Byeon, I.J.L., Dharmasena, S., Huber, K., Concel, J., Gronenborn, A.M., & Sluis-Cremer, N. (2010). The RNA binding protein HuR does not interact directly with HIV-1 reverse transcriptase and does not affect reverse transcription in vitro. Retrovirology, 7(1), 40.Springer Nature. doi: 10.1186/1742-4690-7-40.
Ahn, J., Vu, T., Novince, Z., Guerrero-Santoro, J., Rapic-Otrin, V., & Gronenborn, A.M. (2010). HIV-1 Vpr loads uracil DNA glycosylase-2 onto DCAF1, a substrate recognition subunit of a cullin 4A-ring E3 ubiquitin ligase for proteasome-dependent degradation. J Biol Chem, 285(48), 37333-37341.Elsevier. doi: 10.1074/jbc.M110.133181.
Byeon, I.J.L., Dao, K.K., Jung, J., Keen, J., Leiros, I., Døskeland, S.O., Martinez, A., & Gronenborn, A.M. (2010). Allosteric communication between cAMP binding sites in the RI subunit of protein kinase A revealed by NMR. J Biol Chem, 285(18), 14062-14070.Elsevier. doi: 10.1074/jbc.M110.106666.
Dikeakos, J.D., Atkins, K.M., Thomas, L., Emert-Sedlak, L., Byeon, I.J.L., Jung, J., Ahn, J., Wortman, M.D., Kukull, B., Saito, M., Koizumi, H., Williamson, D.M., Hiyoshi, M., Barklis, E., Takiguchi, M., Suzu, S., Gronenborn, A.M., Smithgall, T.E., & Thomas, G. (2010). Small molecule inhibition of HIV-1-induced MHC-I down-regulation identifies a temporally regulated switch in Nef action. In Riezman, H. (Ed.). Mol Biol Cell, 21(19), 3279-3292.American Society for Cell Biology (ASCB). doi: 10.1091/mbc.E10-05-0470.
Han, Y., Ahn, J., Concel, J., Byeon, I.J.L., Gronenborn, A.M., Yang, J., & Polenova, T. (2010). Solid-state NMR studies of HIV-1 capsid protein assemblies. J Am Chem Soc, 132(6), 1976-1987.American Chemical Society (ACS). doi: 10.1021/ja908687k.
Hou, G., Paramasivam, S., Byeon, I.J.L., Gronenborn, A.M., & Polenova, T. (2010). Determination of relative tensor orientations by γ-encoded chemical shift anisotropy/heteronuclear dipolar coupling 3D NMR spectroscopy in biological solids. Phys Chem Chem Phys, 12(45), 14873-14883.Royal Society of Chemistry (RSC). doi: 10.1039/c0cp00795a.
Jung, J., Byeon, I.J.L., Ahn, J., Concel, J., & Gronenborn, A.M. (2010). 1H, 15N and 13C assignments of the dimeric C-terminal domain of HIV-1 capsid protein. Biomol NMR Assign, 4(1), 21-23.Springer Nature. doi: 10.1007/s12104-009-9198-9.
Koharudin, L.M.I., Liu, H., Di Maio, R., Kodali, R.B., Graham, S.H., & Gronenborn, A.M. (2010). Cyclopentenone prostaglandin-induced unfolding and aggregation of the Parkinson disease-associated UCH-L1. Proc Natl Acad Sci U S A, 107(15), 6835-6840.Proceedings of the National Academy of Sciences. doi: 10.1073/pnas.1002295107.
Matei, E., Zheng, A., Furey, W., Rose, J., Aiken, C., & Gronenborn, A.M. (2010). Anti-HIV activity of defective cyanovirin-N mutants is restored by dimerization. J Biol Chem, 285(17), 13057-13065.Elsevier. doi: 10.1074/jbc.M109.094938.
Walsh, J.D., Meier, K., Ishima, R., & Gronenborn, A.M. (2010). NMR studies on domain diffusion and alignment in modular GB1 repeats. Biophys J, 99(8), 2636-2646.Elsevier. doi: 10.1016/j.bpj.2010.08.036.
Ahn, J., Byeon, I.J.L., Byeon, C.H., & Gronenborn, A.M. (2009). Insight into the structural basis of pro- and antiapoptotic p53 modulation by ASPP proteins. J Biol Chem, 284(20), 13812-13822.Elsevier. doi: 10.1074/jbc.M808821200.
Byeon, I.J.L., Meng, X., Jung, J., Zhao, G., Yang, R., Ahn, J., Shi, J., Concel, J., Aiken, C., Zhang, P., & Gronenborn, A.M. (2009). Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function. Cell, 139(4), 780-790.Elsevier. doi: 10.1016/j.cell.2009.10.010.
Gronenborn, A.M. (2009). Protein acrobatics in pairs--dimerization via domain swapping. Curr Opin Struct Biol, 19(1), 39-49.Elsevier. doi: 10.1016/j.sbi.2008.12.002.
Iwatani, Y., Chan, D.S.B., Liu, L., Yoshii, H., Shibata, J., Yamamoto, N., Levin, J.G., Gronenborn, A.M., & Sugiura, W. (2009). HIV-1 Vif-mediated ubiquitination/degradation of APOBEC3G involves four critical lysine residues in its C-terminal domain. Proc Natl Acad Sci U S A, 106(46), 19539-19544.Proceedings of the National Academy of Sciences. doi: 10.1073/pnas.0906652106.
Jung, J., Byeon, I.J.L., Wang, Y., King, J., & Gronenborn, A.M. (2009). The structure of the cataract-causing P23T mutant of human gammaD-crystallin exhibits distinctive local conformational and dynamic changes. Biochemistry, 48(12), 2597-2609.American Chemical Society (ACS). doi: 10.1021/bi802292q.
Koharudin, L.M.I., Furey, W., & Gronenborn, A.M. (2009). A designed chimeric cyanovirin-N homolog lectin: structure and molecular basis of sucrose binding. Proteins, 77(4), 904-915.Wiley. doi: 10.1002/prot.22514.
Koharudin, L.M.I., Furey, W., Liu, H., Liu, Y.J., & Gronenborn, A.M. (2009). The phox domain of sorting nexin 5 lacks phosphatidylinositol 3-phosphate (PtdIns(3)P) specificity and preferentially binds to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). J Biol Chem, 284(35), 23697-23707.Elsevier. doi: 10.1074/jbc.M109.008995.
Liu, L., Koharudin, L.M.I., Gronenborn, A.M., & Bahar, I. (2009). A comparative analysis of the equilibrium dynamics of a designed protein inferred from NMR, X-ray, and computations. Proteins, 77(4), 927-939.Wiley. doi: 10.1002/prot.22518.
Thakur, A.K., Jayaraman, M., Mishra, R., Thakur, M., Chellgren, V.M., Byeon, I.J.L., Anjum, D.H., Kodali, R., Creamer, T.P., Conway, J.F., Gronenborn, A.M., & Wetzel, R. (2009). Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism. Nat Struct Mol Biol, 16(4), 380-389.Springer Nature. doi: 10.1038/nsmb.1570.
Wang, J., Zuo, X., Yu, P., Byeon, I.J.L., Jung, J., Wang, X., Dyba, M., Seifert, S., Schwieters, C.D., Qin, J., Gronenborn, A.M., & Wang, Y.X. (2009). Determination of multicomponent protein structures in solution using global orientation and shape restraints. J Am Chem Soc, 131(30), 10507-10515.American Chemical Society (ACS). doi: 10.1021/ja902528f.
Jee, J., Byeon, I.J.L., Louis, J.M., & Gronenborn, A.M. (2008). The point mutation A34F causes dimerization of GB1. Proteins, 71(3), 1420-1431.Wiley. doi: 10.1002/prot.21831.
Jee, J., Ishima, R., & Gronenborn, A.M. (2008). Characterization of specific protein association by 15N CPMG relaxation dispersion NMR: the GB1(A34F) monomer-dimer equilibrium. J Phys Chem B, 112(19), 6008-6012.American Chemical Society (ACS). doi: 10.1021/jp076094h.
Koharudin, L.M.I., Viscomi, A.R., Jee, J.G., Ottonello, S., & Gronenborn, A.M. (2008). The evolutionarily conserved family of cyanovirin-N homologs: structures and carbohydrate specificity. Structure, 16(4), 570-584.Elsevier. doi: 10.1016/j.str.2008.01.015.
Matei, E., Furey, W., & Gronenborn, A.M. (2008). Solution and crystal structures of a sugar binding site mutant of cyanovirin-N: no evidence of domain swapping. Structure, 16(8), 1183-1194.Elsevier. doi: 10.1016/j.str.2008.05.011.
Sandström, C., Hakkarainen, B., Matei, E., Glinchert, A., Lahmann, M., Oscarson, S., Kenne, L., & Gronenborn, A.M. (2008). Atomic mapping of the sugar interactions in one-site and two-site mutants of cyanovirin-N by NMR spectroscopy. Biochemistry, 47(12), 3625-3635.American Chemical Society (ACS). doi: 10.1021/bi702200m.
Wang, X., Fukuda, K., Byeon, I.J., Velyvis, A., Wu, C., Gronenborn, A., & Qin, J. (2008). The structure of alpha-parvin CH2-paxillin LD1 complex reveals a novel modular recognition for focal adhesion assembly. J Biol Chem, 283(30), 21113-21119.Elsevier. doi: 10.1074/jbc.M801270200.
Ermolenko, D.N., Dangi, B., Gvritishvili, A., Gronenborn, A.M., & Makhatadze, G.I. (2007). Elimination of the C-cap in ubiquitin - structure, dynamics and thermodynamic consequences. Biophys Chem, 126(1-3), 25-35.Elsevier. doi: 10.1016/j.bpc.2006.03.017.
Gronenborn, A.M. (2007). Some Basic Biomolecular NMR for Protein Structure Determination. In Supramolecular Structure and Function 9. (pp. 33-44).Springer Nature. doi: 10.1007/978-1-4020-6466-1_3.
Iwatani, Y., Chan, D.S.B., Wang, F., Stewart-Maynard, K., Sugiura, W., Gronenborn, A.M., Rouzina, I., Williams, M.C., Musier-Forsyth, K., & Levin, J.G. (2007). Deaminase-independent inhibition of HIV-1 reverse transcription by APOBEC3G. Nucleic Acids Res, 35(21), 7096-7108.Oxford University Press (OUP). doi: 10.1093/nar/gkm750.
Shahkhatuni, A.A., Shahkhatuni, A.G., Panosyan, H.A., Sahakyan, A.B., Byeon, I.J.L., & Gronenborn, A.M. (2007). Assessment of solvent effects: do weak alignment media affect the structure of the solute?. Magn Reson Chem, 45(7), 557-563.Wiley. doi: 10.1002/mrc.2004.
Vega-Rocha, S., Byeon, I.J.L., Gronenborn, B., Gronenborn, A.M., & Campos-Olivas, R. (2007). Solution structure, divalent metal and DNA binding of the endonuclease domain from the replication initiation protein from porcine circovirus 2. J Mol Biol, 367(2), 473-487.Elsevier. doi: 10.1016/j.jmb.2007.01.002.
Vega-Rocha, S., Gronenborn, A.M., Gronenborn, B., & Campos-Olivas, R. (2007). 1H, 13C, and 15N NMR assignment of the master Rep protein nuclease domain from the nanovirus FBNYV. J Biomol NMR, 38(2), 169.Springer Nature. doi: 10.1007/s10858-006-9085-y.
Vega-Rocha, S., Gronenborn, B., Gronenborn, A.M., & Campos-Olivas, R. (2007). Solution structure of the endonuclease domain from the master replication initiator protein of the nanovirus faba bean necrotic yellows virus and comparison with the corresponding geminivirus and circovirus structures. Biochemistry, 46(21), 6201-6212.American Chemical Society (ACS). doi: 10.1021/bi700159q.
Yang, L.W., Eyal, E., Chennubhotla, C., Jee, J., Gronenborn, A.M., & Bahar, I. (2007). Insights into equilibrium dynamics of proteins from comparison of NMR and X-ray data with computational predictions. Structure, 15(6), 741-749.Elsevier. doi: 10.1016/j.str.2007.04.014.
Barrientos, L.G., Matei, E., Lasala, F., Delgado, R., & Gronenborn, A.M. (2006). Dissecting carbohydrate-Cyanovirin-N binding by structure-guided mutagenesis: functional implications for viral entry inhibition. Protein Eng Des Sel, 19(12), 525-535.Oxford University Press (OUP). doi: 10.1093/protein/gzl040.
Toptygin, D., Gronenborn, A.M., & Brand, L. (2006). Nanosecond relaxation dynamics of protein GB1 identified by the time-dependent red shift in the fluorescence of tryptophan and 5-fluorotryptophan. J Phys Chem B, 110(51), 26292-26302.American Chemical Society (ACS). doi: 10.1021/jp064528n.
Barrientos, L.G., & Gronenborn, A.M. (2005). The highly specific carbohydrate-binding protein cyanovirin-N: structure, anti-HIV/Ebola activity and possibilities for therapy. Mini Rev Med Chem, 5(1), 21-31.Bentham Science Publishers. doi: 10.2174/1389557053402783.
Byeon, I.J.L., Li, H., Song, H., Gronenborn, A.M., & Tsai, M.D. (2005). Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67. Nat Struct Mol Biol, 12(11), 987-993.Springer Nature. doi: 10.1038/nsmb1008.
Louis, J.M., Byeon, I.J.L., Baxa, U., & Gronenborn, A.M. (2005). The GB1 amyloid fibril: recruitment of the peripheral beta-strands of the domain swapped dimer into the polymeric interface. J Mol Biol, 348(3), 687-698.Elsevier. doi: 10.1016/j.jmb.2005.02.071.
Mangold, S.L., Morgan, J.R., Strohmeyer, G.C., Gronenborn, A.M., & Cloninger, M.J. (2005). Cyanovirin-N binding to Manalpha1-2Man functionalized dendrimers. Org Biomol Chem, 3(12), 2354-2358.Royal Society of Chemistry (RSC). doi: 10.1039/b417789d.
Zubkov, S., Gronenborn, A.M., Byeon, I.J.L., & Mohanty, S. (2005). Structural consequences of the pH-induced conformational switch in A.polyphemus pheromone-binding protein: mechanisms of ligand release. J Mol Biol, 354(5), 1081-1090.Elsevier. doi: 10.1016/j.jmb.2005.10.015.
Barrientos, L.G., Lasala, F., Delgado, R., Sanchez, A., & Gronenborn, A.M. (2004). Flipping the switch from monomeric to dimeric CV-N has little effect on antiviral activity. Structure, 12(10), 1799-1807.Elsevier. doi: 10.1016/j.str.2004.07.019.
Byeon, I.J.L., Louis, J.M., & Gronenborn, A.M. (2004). A captured folding intermediate involved in dimerization and domain-swapping of GB1. J Mol Biol, 340(3), 615-625.Elsevier. doi: 10.1016/j.jmb.2004.04.069.
Dangi, B., Gronenborn, A.M., Rosner, J.L., & Martin, R.G. (2004). Versatility of the carboxy-terminal domain of the alpha subunit of RNA polymerase in transcriptional activation: use of the DNA contact site as a protein contact site for MarA. Mol Microbiol, 54(1), 45-59.Wiley. doi: 10.1111/j.1365-2958.2004.04250.x.
Ding, K., & Gronenborn, A.M. (2004). Protein Backbone 1H(N)-13Calpha and 15N-13Calpha residual dipolar and J couplings: new constraints for NMR structure determination. J Am Chem Soc, 126(20), 6232-6233.American Chemical Society (ACS). doi: 10.1021/ja049049l.
Ding, K., & Gronenborn, A.M. (2004). Sensitivity-enhanced IPAP experiments for measuring one-bond 13C'-13Calpha and 13Calpha-1Halpha residual dipolar couplings in proteins. J Magn Reson, 167(2), 253-258.Elsevier. doi: 10.1016/j.jmr.2003.12.016.
Ding, K., Louis, J.M., & Gronenborn, A.M. (2004). Insights into conformation and dynamics of protein GB1 during folding and unfolding by NMR. J Mol Biol, 335(5), 1299-1307.Elsevier. doi: 10.1016/j.jmb.2003.11.042.
Gronenborn, A.M. (2004). MRC abstracted in Medline. Magnetic Resonance in Chemistry, 42(5), 419.Wiley. doi: 10.1002/mrc.1390.
McKinney, J., Knappskog, P.M., Pereira, J., Ekern, T., Toska, K., Kuitert, B.B., Levine, D., Gronenborn, A.M., Martinez, A., & Haavik, J. (2004). Expression and purification of human tryptophan hydroxylase from Escherichia coli and Pichia pastoris. Protein Expr Purif, 33(2), 185-194.Elsevier. doi: 10.1016/j.pep.2003.09.014.
Mohanty, S., Zubkov, S., & Gronenborn, A.M. (2004). The solution NMR structure of Antheraea polyphemus PBP provides new insight into pheromone recognition by pheromone-binding proteins. J Mol Biol, 337(2), 443-451.Elsevier. doi: 10.1016/j.jmb.2004.01.009.
Mohanty, S., Zubkov, S., & Gronenborn, A.M. (2004). The solution NMR structure of Antheraea polyphemus PBP provides new insight into pheromone recognition by pheromone-binding proteins (vol 337, pg 443, 2004). JOURNAL OF MOLECULAR BIOLOGY, 338(5), 1037.Elsevier. doi: 10.1016/j.jmb.2004.03.052.
Sandström, C., Berteau, O., Gemma, E., Oscarson, S., Kenne, L., & Gronenborn, A.M. (2004). Atomic mapping of the interactions between the antiviral agent cyanovirin-N and oligomannosides by saturation-transfer difference NMR. Biochemistry, 43(44), 13926-13931.American Chemical Society (ACS). doi: 10.1021/bi048676k.
Winkler, G.S., Albert, T.K., Dominguez, C., Legtenberg, Y.I.A., Boelens, R., & Timmers, H.T.M. (2004). An Altered-specificity Ubiquitin-conjugating Enzyme/Ubiquitin–Protein Ligase Pair. Journal of Molecular Biology, 337(1), 157-165.Elsevier BV. doi: 10.1016/j.jmb.2004.01.031.
Barrientos, L.G., Louis, J.M., Ratner, D.M., Seeberger, P.H., & Gronenborn, A.M. (2003). Solution structure of a circular-permuted variant of the potent HIV-inactivating protein cyanovirin-N: structural basis for protein stability and oligosaccharide interaction. J Mol Biol, 325(1), 211-223.Elsevier. doi: 10.1016/s0022-2836(02)01205-6.
Barrientos, L.G., O'Keefe, B.R., Bray, M., Sanchez, A., Gronenborn, A.M., & Boyd, M.R. (2003). Cyanovirin-N binds to the viral surface glycoprotein, GP1,2 and inhibits infectivity of Ebola virus. Antiviral Res, 58(1), 47-56.Elsevier. doi: 10.1016/s0166-3542(02)00183-3.
Byeon, I.J.L., Louis, J.M., & Gronenborn, A.M. (2003). A protein contortionist: core mutations of GB1 that induce dimerization and domain swapping. J Mol Biol, 333(1), 141-152.Elsevier. doi: 10.1016/s0022-2836(03)00928-8.
Byeon, I.J.L., Louis, J.M., & Gronenborn, A.M. (2003). A protein contortionist: Core mutations of GBI that induce dimerization and domain swapping (vol 333, pg 141, 2003). JOURNAL OF MOLECULAR BIOLOGY, 334(3), 605.Elsevier. doi: 10.1016/j.jmb.2003.10.001.
Ding, K., & Gronenborn, A.M. (2003). Simultaneous and accurate determination of one-bond (15)N-(13)C' and two-bond (1)H(N)--(13)C' dipolar couplings. J Am Chem Soc, 125(38), 11504-11505.American Chemical Society (ACS). doi: 10.1021/ja035954e.
Ding, K., & Gronenborn, A.M. (2003). Sensitivity-enhanced 2D IPAP, TROSY-anti-TROSY, and E.COSY experiments: alternatives for measuring dipolar 15N-1HN couplings. J Magn Reson, 163(2), 208-214.Elsevier. doi: 10.1016/s1090-7807(03)00081-8.
Dobrodumov, A., & Gronenborn, A.M. (2003). Filtering and selection of structural models: combining docking and NMR. Proteins, 53(1), 18-32.Wiley. doi: 10.1002/prot.10439.
Gronenborn, A.M. (2003). Rapid screening of E. coli extracts by heteronuclear NMR. Curr Protoc Protein Sci, Chapter 7(1), Unit-7.11.Wiley. doi: 10.1002/0471140864.ps0711s31.
Ishima, R., Torchia, D.A., Lynch, S.M., Gronenborn, A.M., & Louis, J.M. (2003). Solution structure of the mature HIV-1 protease monomer: insight into the tertiary fold and stability of a precursor. J Biol Chem, 278(44), 43311-43319.Elsevier. doi: 10.1074/jbc.M307549200.
Katoh, E., Louis, J.M., Yamazaki, T., Gronenborn, A.M., Torchia, D.A., & Ishima, R. (2003). A solution NMR study of the binding kinetics and the internal dynamics of an HIV-1 protease-substrate complex. Protein Sci, 12(7), 1376-1385.Wiley. doi: 10.1110/ps.0300703.
Louis, J.M., Ishima, R., Nesheiwat, I., Pannell, L.K., Lynch, S.M., Torchia, D.A., & Gronenborn, A.M. (2003). Revisiting monomeric HIV-1 protease. Characterization and redesign for improved properties. J Biol Chem, 278(8), 6085-6092.Elsevier. doi: 10.1074/jbc.M209726200.
Mesleh, M.F., Valentine, K.G., Opella, S.J., Louis, J.M., & Gronenborn, A.M. (2003). Myristoylation as a general method for immobilization and alignment of soluble proteins for solid-state NMR structural studies. J Biomol NMR, 25(1), 55-61.Springer Nature. doi: 10.1023/a:1021964314987.
Barrientos, L.G., & Gronenborn, A.M. (2002). The domain-swapped dimer of cyanovirin-N contains two sets of oligosaccharide binding sites in solution. Biochem Biophys Res Commun, 298(4), 598-602.Elsevier. doi: 10.1016/s0006-291x(02)02489-0.
Barrientos, L.G., Gawrisch, K., Cheng, N., Steven, A.C., & Gronenborn, A.M. (2002). Structural characterization of the dilute aqueous surfactant solution of cetylpyridinium bromide/hexanol/sodium bromide. LANGMUIR, 18(10), 3773-3779.American Chemical Society (ACS). doi: 10.1021/la011448w.
Barrientos, L.G., Louis, J.M., Botos, I., Mori, T., Han, Z., O'Keefe, B.R., Boyd, M.R., Wlodawer, A., & Gronenborn, A.M. (2002). The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliation of X-ray and NMR structures. Structure, 10(5), 673-686.Elsevier. doi: 10.1016/s0969-2126(02)00758-x.
Barrientos, L.G., Louis, J.M., Hung, J., Smith, T.H., O'Keefe, B.R., Gardella, R.S., Mori, T., Boyd, M.R., & Gronenborn, A.M. (2002). Design and initial characterization of a circular permuted variant of the potent HIV-inactivating protein cyanovirin-N. Proteins, 46(2), 153-160.Wiley. doi: 10.1002/prot.10024.
Campos-Olivas, R., Aziz, R., Helms, G.L., Evans, J.N.S., & Gronenborn, A.M. (2002). Placement of 19F into the center of GB1: effects on structure and stability. FEBS Lett, 517(1-3), 55-60.Wiley. doi: 10.1016/s0014-5793(02)02577-2.
Campos-Olivas, R., Louis, J.M., Clerot, D., Gronenborn, B., & Gronenborn, A.M. (2002). The structure of a replication initiator unites diverse aspects of nucleic acid metabolism. Proc Natl Acad Sci U S A, 99(16), 10310-10315.Proceedings of the National Academy of Sciences. doi: 10.1073/pnas.152342699.
Campos-Olivas, R., Louis, J.M., Clérot, D., Gronenborn, B., & Gronenborn, A.M. (2002). 1H, 13C, and 15N assignment of the N-terminal, catalytic domain of the replication initiation protein from the geminivirus TYLCV. J Biomol NMR, 24(1), 73-74.Springer Nature. doi: 10.1023/a:1020664809314.
Dangi, B., Dobrodumov, A.V., Louis, J.M., & Gronenborn, A.M. (2002). Solution structure and dynamics of the human-Escherichia coli thioredoxin chimera: insights into thermodynamic stability. Biochemistry, 41(30), 9376-9388.American Chemical Society (ACS). doi: 10.1021/bi0258501.
Ding, K., & Gronenborn, A.M. (2002). Sensitivity-enhanced E.COSY-type HSQC experiments for accurate measurements of one-bond 15N-1H(N) and 15N-13C' and two-bond 13C'-1H(N) residual dipolar couplings in proteins. J Magn Reson, 158(1-2), 173-177.Elsevier. doi: 10.1016/s1090-7807(02)00024-1.
Ding, K., & Gronenborn, A.M. (2002). Novel 2D triple-resonance NMR experiments for sequential resonance assignments of proteins. J Magn Reson, 156(2), 262-268.Elsevier. doi: 10.1006/jmre.2002.2537.
Ermolenko, D.N., Thomas, S.T., Aurora, R., Gronenborn, A.M., & Makhatadze, G.I. (2002). Hydrophobic interactions at the Ccap position of the C-capping motif of alpha-helices. J Mol Biol, 322(1), 123-135.Elsevier. doi: 10.1016/s0022-2836(02)00734-9.
Gronenborn, A.M. (2002). The importance of being ordered: improving NMR structures using residual dipolar couplings. C R Biol, 325(9), 957-966.Cellule MathDoc/Centre Mersenne. doi: 10.1016/s1631-0691(02)01512-3.
Kirsten Frank, M., Dyda, F., Dobrodumov, A., & Gronenborn, A.M. (2002). Core mutations switch monomeric protein GB1 into an intertwined tetramer. Nat Struct Biol, 9(11), 877-885.Springer Nature. doi: 10.1038/nsb854.
Mori, T., Barrientos, L.G., Han, Z., Gronenborn, A.M., Turpin, J.A., & Boyd, M.R. (2002). Functional homologs of cyanovirin-N amenable to mass production in prokaryotic and eukaryotic hosts. Protein Expr Purif, 26(1), 42-49.Elsevier. doi: 10.1016/s1046-5928(02)00513-2.
Rosner, J.L., Dangi, B., Gronenborn, A.M., & Martin, R.G. (2002). Posttranscriptional activation of the transcriptional activator Rob by dipyridyl in Escherichia coli. J Bacteriol, 184(5), 1407-1416.American Society for Microbiology. doi: 10.1128/JB.184.5.1407-1416.2002.
Shenoy, S.R., Barrientos, L.G., Ratner, D.M., O'Keefe, B.R., Seeberger, P.H., Gronenborn, A.M., & Boyd, M.R. (2002). Multisite and multivalent binding between cyanovirin-N and branched oligomannosides: calorimetric and NMR characterization. Chem Biol, 9(10), 1109-1118.Elsevier. doi: 10.1016/s1074-5521(02)00237-5.
Tcherkasskaya, O., Gronenborn, A.M., & Klushin, L. (2002). Excluded volume effect within the continuous model for the fluorescence energy transfer. Biophys J, 83(5), 2826-2834.Elsevier. doi: 10.1016/S0006-3495(02)75291-0.
Tcherkasskaya, O., Klushin, L., & Gronenborn, A.M. (2002). Effective lattice behavior of fluorescence energy transfer at lamellar macromolecular interfaces. Biophys J, 82(2), 988-995.Elsevier. doi: 10.1016/S0006-3495(02)75458-1.
Barrientos, L.G., Campos-Olivas, R., Louis, J.M., Fiser, A., Sali, A., & Gronenborn, A.M. (2001). 1H, 13C, 15N resonance assignments and fold verification of a circular permuted variant of the potent HIV-inactivating protein cyanovirin-N. J Biomol NMR, 19(3), 289-290.Springer Nature. doi: 10.1023/a:1011292919947.
Barrientos, L.G., Louis, J.M., & Gronenborn, A.M. (2001). Characterization of the cholesteric phase of filamentous bacteriophage fd for molecular alignment. J Magn Reson, 149(1), 154-158.Elsevier. doi: 10.1006/jmre.2000.2276.
Campos-Olivas, R., Hörr, I., Bormann, C., Jung, G., & Gronenborn, A.M. (2001). Solution structure, backbone dynamics and chitin binding of the anti-fungal protein from Streptomyces tendae TU901. J Mol Biol, 308(4), 765-782.Elsevier. doi: 10.1006/jmbi.2001.4622.
Dangi, B., Pelupessey, P., Martin, R.G., Rosner, J.L., Louis, J.M., & Gronenborn, A.M. (2001). Structure and dynamics of MarA-DNA complexes: an NMR investigation. J Mol Biol, 314(1), 113-127.Elsevier. doi: 10.1006/jmbi.2001.5106.
Ishima, R., Ghirlando, R., Tözsér, J., Gronenborn, A.M., Torchia, D.A., & Louis, J.M. (2001). Folded monomer of HIV-1 protease. J Biol Chem, 276(52), 49110-49116.Elsevier. doi: 10.1074/jbc.M108136200.
Louis, J.M., Georgescu, R.E., Tasayco, M.L., Tcherkasskaya, O., & Gronenborn, A.M. (2001). Probing the structure and stability of a hybrid protein: the human-E. coli thioredoxin chimera. Biochemistry, 40(37), 11184-11192.American Chemical Society (ACS). doi: 10.1021/bi010745x.
Qin, J., Vinogradova, O., & Gronenborn, A.M. (2001). Protein-protein interactions probed by nuclear magnetic resonance spectroscopy. Methods Enzymol, 339, 377-389.Elsevier. doi: 10.1016/s0076-6879(01)39323-0.
Barrientos, L.G., Dolan, C., & Gronenborn, A.M. (2000). Characterization of surfactant liquid crystal phases suitable for molecular alignment and measurement of dipolar couplings. J Biomol NMR, 16(4), 329-337.Springer Nature. doi: 10.1023/a:1008356618658.
Castagné, C., Murphy, E.C., Gronenborn, A.M., & Delepierre, M. (2000). 31P NMR analysis of the DNA conformation induced by protein binding SRY/DNA complexes. Eur J Biochem, 267(4), 1223-1229.Wiley. doi: 10.1046/j.1432-1327.2000.01124.x.
Gakh, Y.G., Gakh, A.A., & Gronenborn, A.M. (2000). Fluorine as an NMR probe for structural studies of chemical and biological systems. MAGNETIC RESONANCE IN CHEMISTRY, 38(7), 551-558.Wiley. doi: 10.1002/1097-458X(200007)38:7<551::AID-MRC686>3.0.CO;2-Q.
Li, H., Yamada, H., Akasaka, K., & Gronenborn, A.M. (2000). Pressure alters electronic orbital overlap in hydrogen bonds. J Biomol NMR, 18(3), 207-216.Springer Nature. doi: 10.1023/a:1026537609584.
Louis, J.M., Weber, I.T., Tözsér, J., Clore, G.M., & Gronenborn, A.M. (2000). HIV-1 protease: maturation, enzyme specificity, and drug resistance. Adv Pharmacol, 49, 111-146.Elsevier. doi: 10.1016/s1054-3589(00)49025-3.
Qin, J., Yang, Y., Velyvis, A., & Gronenborn, A. (2000). Molecular views of redox regulation: three-dimensional structures of redox regulatory proteins and protein complexes. Antioxid Redox Signal, 2(4), 827-840.Mary Ann Liebert. doi: 10.1089/ars.2000.2.4-827.
Tcherkasskaya, O., Bychkova, V.E., Uversky, V.N., & Gronenborn, A.M. (2000). Multisite fluorescence in proteins with multiple tryptophan residues. Apomyoglobin natural variants and site-directed mutants. J Biol Chem, 275(46), 36285-36294.Elsevier. doi: 10.1074/jbc.M003008200.
Tcherkasskaya, O., Knutson, J.R., Bowley, S.A., Frank, M.K., & Gronenborn, A.M. (2000). Nanosecond dynamics of the single tryptophan reveals multi-state equilibrium unfolding of protein GB1. Biochemistry, 39(37), 11216-11226.American Chemical Society (ACS). doi: 10.1021/bi000345u.
Caffrey, M., Kaufman, J., Stahl, S., Wingfield, P., Gronenborn, A.M., & Clore, G.M. (1999). Monomer-trimer equilibrium of the ectodomain of SIV gp41: insight into the mechanism of peptide inhibition of HIV infection. Protein Sci, 8(9), 1904-1907.Wiley. doi: 10.1110/ps.8.9.1904.
Cornilescu, G., Ramirez, B.E., Frank, M.K., Clore, G.M., Gronenborn, A.M., & Bax, A. (1999). Correlation between 3hJNC′ and hydrogen bond length in proteins. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 121(26), 6275-6279.American Chemical Society (ACS). doi: 10.1021/ja9909024.
Garrett, D.S., Seok, Y.J., Peterkofsky, A., Gronenborn, A.M., & Clore, G.M. (1999). Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr. Nat Struct Biol, 6(2), 166-173.Springer Nature. doi: 10.1038/5854.
Gronenborn, A.M., Clore, G.M., Louis, J.M., & Wingfield, P.T. (1999). Is human thioredoxin monomeric or dimeric?. Protein Sci, 8(2), 426-429.Wiley. doi: 10.1110/ps.8.2.426.
Kuszewski, J., Gronenborn, A.M., & Clore, G.M. (1999). Improving the packing and accuracy of NMR structures with a pseudopotential for the radius of gyration. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 121(10), 2337-2338.American Chemical Society (ACS). doi: 10.1021/ja9843730.
Louis, J.M., Clore, G.M., & Gronenborn, A.M. (1999). Autoprocessing of HIV-1 protease is tightly coupled to protein folding. Nat Struct Biol, 6(9), 868-875.Springer Nature. doi: 10.1038/12327.
Yang, F., Bewley, C.A., Louis, J.M., Gustafson, K.R., Boyd, M.R., Gronenborn, A.M., Clore, G.M., & Wlodawer, A. (1999). Crystal structure of cyanovirin-N, a potent HIV-inactivating protein, shows unexpected domain swapping. J Mol Biol, 288(3), 403-412.Elsevier. doi: 10.1006/jmbi.1999.2693.
Yu, B., Blaber, M., Gronenborn, A.M., Clore, G.M., & Caspar, D.L. (1999). Disordered water within a hydrophobic protein cavity visualized by x-ray crystallography. Proc Natl Acad Sci U S A, 96(1), 103-108.Proceedings of the National Academy of Sciences. doi: 10.1073/pnas.96.1.103.
Bewley, C.A., Gronenborn, A.M., & Clore, G.M. (1998). Minor groove-binding architectural proteins: structure, function, and DNA recognition. Annu Rev Biophys Biomol Struct, 27(1), 105-131.Annual Reviews. doi: 10.1146/annurev.biophys.27.1.105.
Bewley, C.A., Gustafson, K.R., Boyd, M.R., Covell, D.G., Bax, A., Clore, G.M., & Gronenborn, A.M. (1998). Solution structure of cyanovirin-N, a potent HIV-inactivating protein. Nat Struct Biol, 5(7), 571-578.Springer Nature. doi: 10.1038/828.
Caffrey, M., Cai, M., Kaufman, J., Stahl, S.J., Wingfield, P.T., Covell, D.G., Gronenborn, A.M., & Clore, G.M. (1998). Three-dimensional solution structure of the 44 kDa ectodomain of SIV gp41. EMBO J, 17(16), 4572-4584.Springer Nature. doi: 10.1093/emboj/17.16.4572.
Caffrey, M., Kaufman, J., Stahl, S.J., Wingfield, P.T., Gronenborn, A.M., & Clore, G.M. (1998). 3D NMR experiments for measuring 15N relaxation data of large proteins: application to the 44 kDa ectodomain of SIV gp41. J Magn Reson, 135(2), 368-372.Elsevier. doi: 10.1006/jmre.1998.1583.
Cai, M., Huang, Y., Caffrey, M., Zheng, R., Craigie, R., Clore, G.M., & Gronenborn, A.M. (1998). Solution structure of the His12 --> Cys mutant of the N-terminal zinc binding domain of HIV-1 integrase complexed to cadmium. Protein Sci, 7(12), 2669-2674.Wiley. doi: 10.1002/pro.5560071221.
Cai, M., Huang, Y., Sakaguchi, K., Clore, G.M., Gronenborn, A.M., & Craigie, R. (1998). An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli. J Biomol NMR, 11(1), 97-102.Springer Nature. doi: 10.1023/a:1008222131470.
Cai, M., Huang, Y., Zheng, R., Wei, S.Q., Ghirlando, R., Lee, M.S., Craigie, R., Gronenborn, A.M., & Clore, G.M. (1998). Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration. Nat Struct Biol, 5(10), 903-909.Springer Nature. doi: 10.1038/2345.
Clore, G.M., & Gronenborn, A.M. (1998). NMR structure determination of proteins and protein complexes larger than 20 kDa. Curr Opin Chem Biol, 2(5), 564-570.Elsevier. doi: 10.1016/s1367-5931(98)80084-7.
Clore, G.M., & Gronenborn, A.M. (1998). New methods of structure refinement for macromolecular structure determination by NMR. Proc Natl Acad Sci U S A, 95(11), 5891-5898.Proceedings of the National Academy of Sciences. doi: 10.1073/pnas.95.11.5891.
Clore, G.M., & Gronenborn, A.M. (1998). Determining the structures of large proteins and protein complexes by NMR. Trends Biotechnol, 16(1), 22-34.Elsevier. doi: 10.1016/S0167-7799(97)01135-9.
Clore, G.M., Gronenborn, A.M., & Bax, A. (1998). A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information. J Magn Reson, 133(1), 216-221.Elsevier. doi: 10.1006/jmre.1998.1419.
Clore, G.M., Gronenborn, A.M., & Tjandra, N. (1998). Direct structure refinement against residual dipolar couplings in the presence of rhombicity of unknown magnitude. J Magn Reson, 131(1), 159-162.Elsevier. doi: 10.1006/jmre.1997.1345.
Clore, G.M., Gronenborn, A.M., Szabo, A., & Tjandra, N. (1998). Determining the magnitude of the fully asymmetric diffusion tensor from heteronuclear relaxation data in the absence of structural information. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 120(19), 4889-4890.American Chemical Society (ACS). doi: 10.1021/ja980192m.
Clore, G.M., Murphy, E.C., Gronenborn, A.M., & Bax, A. (1998). Determination of three-bond 1H3'-31P couplings in nucleic acids and protein-nucleic acid complexes by quantitative J correlation spectroscopy. J Magn Reson, 134(1), 164-167.Elsevier. doi: 10.1006/jmre.1998.1513.
Clore, G.M., Starich, M.R., & Gronenborn, A.M. (1998). Measurement of residual dipolar couplings of macromolecules aligned in the nematic phase of a colloidal suspension of rod-shaped viruses. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 120(40), 10571-10572.American Chemical Society (ACS). doi: 10.1021/ja982592f.
Garrett, D.S., Seok, Y.J., Peterkofsky, A., Clore, G.M., & Gronenborn, A.M. (1998). Tautomeric state and pKa of the phosphorylated active site histidine in the N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system. Protein Sci, 7(3), 789-793.Wiley. doi: 10.1002/pro.5560070329.
Louis, J.M., Martin, R.G., Clore, G.M., & Gronenborn, A.M. (1998). Preparation of uniformly isotope-labeled DNA oligonucleotides for NMR spectroscopy. J Biol Chem, 273(4), 2374-2378.Elsevier. doi: 10.1074/jbc.273.4.2374.
Starich, M.R., Wikström, M., Arst, H.N., Clore, G.M., & Gronenborn, A.M. (1998). The solution structure of a fungal AREA protein-DNA complex: an alternative binding mode for the basic carboxyl tail of GATA factors. J Mol Biol, 277(3), 605-620.Elsevier. doi: 10.1006/jmbi.1998.1625.
Starich, M.R., Wikström, M., Schumacher, S., Arst, H.N., Gronenborn, A.M., & Clore, G.M. (1998). The solution structure of the Leu22-->Val mutant AREA DNA binding domain complexed with a TGATAG core element defines a role for hydrophobic packing in the determination of specificity. J Mol Biol, 277(3), 621-634.Elsevier. doi: 10.1006/jmbi.1997.1626.
Caffrey, M., Cai, M., Kaufman, J., Stahl, S.J., Wingfield, P.T., Gronenborn, A.M., & Clore, G.M. (1997). Determination of the secondary structure and global topology of the 44 kDa ectodomain of gp41 of the simian immunodeficiency virus by multidimensional nuclear magnetic resonance spectroscopy. J Mol Biol, 271(5), 819-826.Elsevier. doi: 10.1006/jmbi.1997.1217.
Cai, M., Zheng, R., Caffrey, M., Craigie, R., Clore, G.M., & Gronenborn, A.M. (1997). Solution structure of the N-terminal zinc binding domain of HIV-1 integrase. Nat Struct Biol, 4(7), 567-577.Springer Nature. doi: 10.1038/nsb0797-567.
Cai, M., Zheng, R., Caffrey, M., Craigie, R., Clore, G.M., & Gronenborn, A.M. (1997). Solution structure of the N-terminal zinc binding domain of HIV-1 integrase. Nature Structural & Molecular Biology, 4(10), 839-840.Springer Nature. doi: 10.1038/nsb1097-839.
Clore, G.M., & Gronenborn, A.M. (1997). NMR structures of proteins and protein complexes beyond 20,000 M(r). Nat Struct Biol, 4 Suppl(SUPPL.), 849-853.
Clore, G.M., & Gronenborn, A.M. (1997). Dissecting intrinsic chaperonin activity. Proc Natl Acad Sci U S A, 94(1), 7-8.Proceedings of the National Academy of Sciences. doi: 10.1073/pnas.94.1.7.
Clubb, R.T., Schumacher, S., Mizuuchi, K., Gronenborn, A.M., & Clore, G.M. (1997). Solution structure of the I gamma subdomain of the Mu end DNA-binding domain of phage Mu transposase. J Mol Biol, 273(1), 19-25.Elsevier. doi: 10.1006/jmbi.1997.1312.
Garrett, D.S., Seok, Y.J., Liao, D.I., Peterkofsky, A., Gronenborn, A.M., & Clore, G.M. (1997). Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR. Biochemistry, 36(9), 2517-2530.American Chemical Society (ACS). doi: 10.1021/bi962924y.
Garrett, D.S., Seok, Y.J., Peterkofsky, A., Clore, G.M., & Gronenborn, A.M. (1997). Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system. Biochemistry, 36(15), 4393-4398.American Chemical Society (ACS). doi: 10.1021/bi970221q.
Huth, J.R., Bewley, C.A., Jackson, B.M., Hinnebusch, A.G., Clore, G.M., & Gronenborn, A.M. (1997). Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR. Protein Sci, 6(11), 2359-2364.Wiley. doi: 10.1002/pro.5560061109.
Huth, J.R., Bewley, C.A., Nissen, M.S., Evans, J.N., Reeves, R., Gronenborn, A.M., & Clore, G.M. (1997). The solution structure of an HMG-I(Y)-DNA complex defines a new architectural minor groove binding motif. Nat Struct Biol, 4(8), 657-665.Springer Nature. doi: 10.1038/nsb0897-657.
Kuszewski, J., Gronenborn, A.M., & Clore, G.M. (1997). Improvements and extensions in the conformational database potential for the refinement of NMR and X-ray structures of proteins and nucleic acids. J Magn Reson, 125(1), 171-177.Elsevier. doi: 10.1006/jmre.1997.1116.
Nagaich, A.K., Zhurkin, V.B., Sakamoto, H., Gorin, A.A., Clore, G.M., Gronenborn, A.M., Appella, E., & Harrington, R.E. (1997). Architectural accommodation in the complex of four p53 DNA binding domain peptides with the p21/waf1/cip1 DNA response element. J Biol Chem, 272(23), 14830-14841.Elsevier. doi: 10.1074/jbc.272.23.14830.
Omichinski, J.G., Pedone, P.V., Felsenfeld, G., Gronenborn, A.M., & Clore, G.M. (1997). The solution structure of a specific GAGA factor-DNA complex reveals a modular binding mode. Nat Struct Biol, 4(2), 122-132.Springer Nature. doi: 10.1038/nsb0297-122.
Pedone, P.V., Omichinski, J.G., Nony, P., Trainor, C., Gronenborn, A.M., Clore, G.M., & Felsenfeld, G. (1997). The N-terminal fingers of chicken GATA-2 and GATA-3 are independent sequence-specific DNA binding domains. EMBO J, 16(10), 2874-2882.Springer Nature. doi: 10.1093/emboj/16.10.2874.
Schumacher, S., Clubb, R.T., Cai, M., Mizuuchi, K., Clore, G.M., & Gronenborn, A.M. (1997). Solution structure of the Mu end DNA-binding ibeta subdomain of phage Mu transposase: modular DNA recognition by two tethered domains. EMBO J, 16(24), 7532-7541.Springer Nature. doi: 10.1093/emboj/16.24.7532.
Tjandra, N., Garrett, D.S., Gronenborn, A.M., Bax, A., & Clore, G.M. (1997). Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy. Nat Struct Biol, 4(6), 443-449.Springer Nature. doi: 10.1038/nsb0697-443.
Tjandra, N., Omichinski, J.G., Gronenborn, A.M., Clore, G.M., & Bax, A. (1997). Use of dipolar 1H-15N and 1H-13C couplings in the structure determination of magnetically oriented macromolecules in solution. Nat Struct Biol, 4(9), 732-738.Springer Nature. doi: 10.1038/nsb0997-732.
Werner, M.H., Clore, G.M., Fisher, C.L., Fisher, R.J., Trinh, L., Shiloach, J., & Gronenborn, A.M. (1997). Correction of the NMR structure of the ETS1/DNA complex. J Biomol NMR, 10(4), 317-328.Springer Nature. doi: 10.1023/a:1018399711996.
Werner, M.H., Gronenborn, A.M., & Clore, G.M. (1997). ETS1-DNA binding and intercalation: correction. Science, 276(5321), 1957.American Association for the Advancement of Science (AAAS). doi: 10.1126/science.276.5321.1953d.
Wingfield, P.T., Stahl, S.J., Kaufman, J., Zlotnick, A., Hyde, C.C., Gronenborn, A.M., & Clore, G.M. (1997). The extracellular domain of immunodeficiency virus gp41 protein: expression in Escherichia coli, purification, and crystallization. Protein Sci, 6(8), 1653-1660.Wiley. doi: 10.1002/pro.5560060806.
Clubb, R.T., Mizuuchi, M., Huth, J.R., Omichinski, J.G., Savilahti, H., Mizuuchi, K., Clore, G.M., & Gronenborn, A.M. (1996). The wing of the enhancer-binding domain of Mu phage transposase is flexible and is essential for efficient transposition. Proc Natl Acad Sci U S A, 93(3), 1146-1150.Proceedings of the National Academy of Sciences. doi: 10.1073/pnas.93.3.1146.
Gronenborn, A.M., & Clore, G.M. (1996). Rapid screening for structural integrity of expressed proteins by heteronuclear NMR spectroscopy. Protein Sci, 5(1), 174-177.Wiley. doi: 10.1002/pro.5560050123.
Gronenborn, A.M., & Clore, G.M. (1996). Rapid screening for structural integrity of expressed proteins by heteronuclear NMR spectroscopy. Protein Science, 5(5), 981.Wiley. doi: 10.1002/pro.5560050522.
Gronenborn, A.M., Frank, M.K., & Clore, G.M. (1996). Core mutants of the immunoglobulin binding domain of streptococcal protein G: stability and structural integrity. FEBS Lett, 398(2-3), 312-316.Wiley. doi: 10.1016/s0014-5793(96)01262-8.
Grzesiek, S., Bax, A., Clore, G.M., Gronenborn, A.M., Hu, J.S., Kaufman, J., Palmer, I., Stahl, S.J., & Wingfield, P.T. (1996). The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase. Nat Struct Biol, 3(4), 340-345.Springer Nature. doi: 10.1038/nsb0496-340.
Kuszewski, J., Gronenborn, A.M., & Clore, G.M. (1996). A potential involving multiple proton chemical-shift restraints for nonstereospecifically assigned methyl and methylene protons. J Magn Reson B, 112(1), 79-81.Elsevier. doi: 10.1006/jmrb.1996.0113.
Kuszewski, J., Gronenborn, A.M., & Clore, G.M. (1996). Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases. Protein Sci, 5(6), 1067-1080.Wiley. doi: 10.1002/pro.5560050609.
Miller, M., Lubkowski, J., Rao, J.K., Danishefsky, A.T., Omichinski, J.G., Sakaguchi, K., Sakamoto, H., Appella, E., Gronenborn, A.M., & Clore, G.M. (1996). The oligomerization domain of p53: crystal structure of the trigonal form. FEBS Lett, 399(1-2), 166-170.Wiley. doi: 10.1016/s0014-5793(96)01231-8.
Pedone, P.V., Ghirlando, R., Clore, G.M., Gronenborn, A.M., Felsenfeld, G., & Omichinski, J.G. (1996). The single Cys2-His2 zinc finger domain of the GAGA protein flanked by basic residues is sufficient for high-affinity specific DNA binding. Proc Natl Acad Sci U S A, 93(7), 2822-2826.Proceedings of the National Academy of Sciences. doi: 10.1073/pnas.93.7.2822.
Pedone, P.V., Ghirlando, R., Clore, G.M., Gronenborn, A.M., Felsenfeld, G., & Omichinski, J.G. (1996). Erratum: The single Cys
Qin, J., Clore, G.M., & Gronenborn, A.M. (1996). Ionization equilibria for side-chain carboxyl groups in oxidized and reduced human thioredoxin and in the complex with its target peptide from the transcription factor NF kappa B. Biochemistry, 35(1), 7-13.American Chemical Society (ACS). doi: 10.1021/bi952299h.
Qin, J., Clore, G.M., Kennedy, W.P., Kuszewski, J., & Gronenborn, A.M. (1996). The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal. Structure, 4(5), 613-620.Elsevier. doi: 10.1016/s0969-2126(96)00065-2.
Trainor, C.D., Omichinski, J.G., Vandergon, T.L., Gronenborn, A.M., Clore, G.M., & Felsenfeld, G. (1996). A palindromic regulatory site within vertebrate GATA-1 promoters requires both zinc fingers of the GATA-1 DNA-binding domain for high-affinity interaction. Mol Cell Biol, 16(5), 2238-2247.Taylor & Francis. doi: 10.1128/MCB.16.5.2238.
Werner, M.H., Clore, G.M., Fisher, C.L., Fisher, R.J., Trinh, L., Shiloach, J., & Gronenborn, A.M. (1996). Erratum. Cell, 87(2), 356.Elsevier. doi: 10.1016/s0092-8674(00)81352-5.
Werner, M.H., Gronenborn, A.M., & Clore, G.M. (1996). Intercalation, DNA kinking, and the control of transcription. Science, 271(5250), 778-784.American Association for the Advancement of Science (AAAS). doi: 10.1126/science.271.5250.778.
Werner, M.H., Huth, J.R., Gronenborn, A.M., & Clore, G.M. (1996). Molecular determinants of mammmalian sex. Trends Biochem Sci, 21(8), 302-308.Elsevier. doi: 10.1016/S0968-0004(96)10032-3.
Balagurumoorthy, P., Sakamoto, H., Lewis, M.S., Zambrano, N., Clore, G.M., Gronenborn, A.M., Appella, E., & Harrington, R.E. (1995). Four p53 DNA-binding domain peptides bind natural p53-response elements and bend the DNA. Proc Natl Acad Sci U S A, 92(19), 8591-8595.Proceedings of the National Academy of Sciences. doi: 10.1073/pnas.92.19.8591.
Clore, G.M., & Gronenborn, A.M. (1995). Three-dimensional structures of alpha and beta chemokines. FASEB J, 9(1), 57-62.Wiley. doi: 10.1096/fasebj.9.1.7821760.
Clore, G.M., Ernst, J., Clubb, R., Omichinski, J.G., Kennedy, W.M., Sakaguchi, K., Appella, E., & Gronenborn, A.M. (1995). Refined solution structure of the oligomerization domain of the tumour suppressor p53. Nat Struct Biol, 2(4), 321-333.Springer Nature. doi: 10.1038/nsb0495-321.
Clore, G.M., Omichinski, J.G., Sakaguchi, K., Zambrano, N., Sakamoto, H., Appella, E., & Gronenborn, A.M. (1995). Interhelical angles in the solution structure of the oligomerization domain of p53: correction. Science, 267(5203), 1515-1516.American Association for the Advancement of Science (AAAS). doi: 10.1126/science.7878474.
Clubb, R.T., Omichinski, J.G., Sakaguchi, K., Appella, E., Gronenborn, A.M., & Clore, G.M. (1995). Backbone dynamics of the oligomerization domain of p53 determined from 15N NMR relaxation measurements. Protein Sci, 4(5), 855-862.Wiley. doi: 10.1002/pro.5560040505.
Ernst, J.A., Clubb, R.T., Zhou, H.X., Gronenborn, A.M., & Clore, G.M. (1995). Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR. Science, 267(5205), 1813-1817.American Association for the Advancement of Science (AAAS). doi: 10.1126/science.7892604.
Frank, M.K., Clore, G.M., & Gronenborn, A.M. (1995). Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal protein G by multidimensional heteronuclear NMR spectroscopy. Protein Sci, 4(12), 2605-2615.Wiley. doi: 10.1002/pro.5560041218.
Gronenborn, A.M., & Clore, G.M. (1995). Structures of protein complexes by multidimensional heteronuclear magnetic resonance spectroscopy. Crit Rev Biochem Mol Biol, 30(5), 351-385.Taylor & Francis. doi: 10.3109/10409239509083489.
Kuszewski, J., Gronenborn, A.M., & Clore, G.M. (1995). The impact of direct refinement against proton chemical shifts on protein structure determination by NMR. J Magn Reson B, 107(3), 293-297.Elsevier. doi: 10.1006/jmrb.1995.1093.
Kuszewski, J., Qin, J., Gronenborn, A.M., & Clore, G.M. (1995). The impact of direct refinement against 13C alpha and 13C beta chemical shifts on protein structure determination by NMR. J Magn Reson B, 106(1), 92-96.Elsevier. doi: 10.1006/jmrb.1995.1017.
Lodi, P.J., Ernst, J.A., Kuszewski, J., Hickman, A.B., Engelman, A., Craigie, R., Clore, G.M., & Gronenborn, A.M. (1995). Solution structure of the DNA binding domain of HIV-1 integrase. Biochemistry, 34(31), 9826-9833.American Chemical Society (ACS). doi: 10.1021/bi00031a002.
Makhatadze, G.I., Clore, G.M., & Gronenborn, A.M. (1995). Solvent isotope effect and protein stability. Nat Struct Biol, 2(10), 852-855.Springer Nature. doi: 10.1038/nsb1095-852.
Qin, J., Clore, G.M., Kennedy, W.M., Huth, J.R., & Gronenborn, A.M. (1995). Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B. Structure, 3(3), 289-297.Elsevier. doi: 10.1016/s0969-2126(01)00159-9.
Strzelecka, T.E., Clore, G.M., & Gronenborn, A.M. (1995). The solution structure of the Mu Ner protein reveals a helix-turn-helix DNA recognition motif. Structure, 3(10), 1087-1095.Elsevier. doi: 10.1016/s0969-2126(01)00244-1.
Strzelecka, T.E., Hayes, J.J., Clore, G.M., & Gronenborn, A.M. (1995). DNA binding specificity of the Mu Ner protein. Biochemistry, 34(9), 2946-2955.American Chemical Society (ACS). doi: 10.1021/bi00009a026.
Werner, M.H., Bianchi, M.E., Gronenborn, A.M., & Clore, G.M. (1995). NMR spectroscopic analysis of the DNA conformation induced by the human testis determining factor SRY. Biochemistry, 34(37), 11998-12004.American Chemical Society (ACS). doi: 10.1021/bi00037a042.
Werner, M.H., Clore, M., Fisher, C.L., Fisher, R.J., Trinh, L., Shiloach, J., & Gronenborn, A.M. (1995). The solution structure of the human ETS1-DNA complex reveals a novel mode of binding and true side chain intercalation. Cell, 83(5), 761-771.Elsevier. doi: 10.1016/0092-8674(95)90189-2.
Werner, M.H., Huth, J.R., Gronenborn, A.M., & Clore, G.M. (1995). Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex. Cell, 81(5), 705-714.Elsevier. doi: 10.1016/0092-8674(95)90532-4.
Barchi, J.J., Grasberger, B., Gronenborn, A.M., & Clore, G.M. (1994). Investigation of the backbone dynamics of the IgG-binding domain of streptococcal protein G by heteronuclear two-dimensional 1H-15N nuclear magnetic resonance spectroscopy. Protein Sci, 3(1), 15-21.Wiley. doi: 10.1002/pro.5560030103.
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BAX, A., GRZESIEK, S., GRONENBORN, A.M., & CLORE, G.M. (1994). ISOTOPE-FILTERED 2D HOHAHA SPECTROSCOPY OF A PEPTIDE-PROTEIN COMPLEX USING HETERONUCLEAR HARTMANN-HAHN DEPHASING. JOURNAL OF MAGNETIC RESONANCE SERIES A, 106(2), 269-273.Elsevier. doi: 10.1006/jmra.1994.1038.
Clore, G.M., & Gronenborn, A.M. (1994). Structures of larger proteins, protein-ligand and protein-DNA complexes by multi-dimensional heteronuclear NMR. Prog Biophys Mol Biol, 62(2), 153-184.Elsevier. doi: 10.1016/0079-6107(94)90010-8.
Clore, G.M., & Gronenborn, A.M. (1994). Multidimensional heteronuclear nuclear magnetic resonance of proteins. Methods Enzymol, 239, 349-363.Elsevier. doi: 10.1016/s0076-6879(94)39013-4.
Clore, G.M., & Gronenborn, A.M. (1994). Erratum: Structures of larger proteins, protein-ligand and protein-DNA complexes by multidimensional heteronuclear NMR (Protein Science (March 1994)). Protein Science, 3(4), 713.
Clore, G.M., Bax, A., Omichinski, J.G., & Gronenborn, A.M. (1994). Localization of bound water in the solution structure of a complex of the erythroid transcription factor GATA-1 with DNA. Structure, 2(2), 89-94.Elsevier. doi: 10.1016/s0969-2126(00)00011-3.
Clore, G.M., Omichinski, J.G., Sakaguchi, K., Zambrano, N., Sakamoto, H., Appella, E., & Gronenborn, A.M. (1994). High-resolution structure of the oligomerization domain of p53 by multidimensional NMR. Science, 265(5170), 386-391.American Association for the Advancement of Science (AAAS). doi: 10.1126/science.8023159.
Clore, G.M., Robien, M.A., & Gronenborn, A.M. (1994). Erratum: Exploring the limits of precision and accuracy of protein structures determined by nuclear magnetic resonance spectroscopy (J. Mol. Biol. (1993) 231, 82-102). Journal of Molecular Biology, 237(2), 243.
Clore, G.M., Robien, M.A., & Gronenborn, A.M. (1994). Corrigendum. Journal of Molecular Biology, 237(2), 243.Elsevier. doi: 10.1006/jmbi.1994.1226.
Clubb, R.T., Omichinski, J.G., Clore, G.M., & Gronenborn, A.M. (1994). Mapping the binding surface of interleukin-8 complexed with an N-terminal fragment of the type 1 human interleukin-8 receptor. FEBS Lett, 338(1), 93-97.Wiley. doi: 10.1016/0014-5793(94)80123-1.
Clubb, R.T., Omichinski, J.G., Savilahti, H., Mizuuchi, K., Gronenborn, A.M., & Clore, G.M. (1994). A novel class of winged helix-turn-helix protein: the DNA-binding domain of Mu transposase. Structure, 2(11), 1041-1048.Elsevier. doi: 10.1016/s0969-2126(94)00107-3.
Covell, D.G., Smythers, G.W., Gronenborn, A.M., & Clore, G.M. (1994). Analysis of hydrophobicity in the alpha and beta chemokine families and its relevance to dimerization. Protein Sci, 3(11), 2064-2072.Wiley. doi: 10.1002/pro.5560031119.
Garrett, D.S., Kuszewski, J., Hancock, T.J., Lodi, P.J., Vuister, G.W., Gronenborn, A.M., & Clore, G.M. (1994). The impact of direct refinement against three-bond HN-C alpha H coupling constants on protein structure determination by NMR. J Magn Reson B, 104(1), 99-103.Elsevier. doi: 10.1006/jmrb.1994.1061.
Garrett, D.S., Lodi, P.J., Shamoo, Y., Williams, K.R., Clore, G.M., & Gronenborn, A.M. (1994). Determination of the secondary structure and folding topology of an RNA binding domain of mammalian hnRNP A1 protein using three-dimensional heteronuclear magnetic resonance spectroscopy. Biochemistry, 33(10), 2852-2858.American Chemical Society (ACS). doi: 10.1021/bi00176a015.
Grasberger, B.L., Clore, G.M., & Gronenborn, A.M. (1994). High-resolution structure of Ascaris trypsin inhibitor in solution: direct evidence for a pH-induced conformational transition in the reactive site. Structure, 2(7), 669-678.Elsevier. doi: 10.1016/s0969-2126(00)00067-8.
Gronenborn, A.M., & Clore, G.M. (1994). Where is NMR taking us?. Proteins, 19(4), 273-276.Wiley. doi: 10.1002/prot.340190402.
Gronenborn, A.M., & Clore, G.M. (1994). Identification of N-terminal helix capping boxes by means of 13C chemical shifts. J Biomol NMR, 4(3), 455-458.Springer Nature. doi: 10.1007/BF00179351.
Gronenborn, A.M., & Clore, G.M. (1994). Experimental support for the "hydrophobic zipper" hypothesis. Science, 263(5146), 536.American Association for the Advancement of Science (AAAS). doi: 10.1126/science.8290964.
Kuszewski, J., Clore, G.M., & Gronenborn, A.M. (1994). Fast folding of a prototypic polypeptide: the immunoglobulin binding domain of streptococcal protein G. Protein Sci, 3(11), 1945-1952.Wiley. doi: 10.1002/pro.5560031106.
Lodi, P.J., Garrett, D.S., Kuszewski, J., Tsang, M.L., Weatherbee, J.A., Leonard, W.J., Gronenborn, A.M., & Clore, G.M. (1994). High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR. Science, 263(5154), 1762-1767.American Association for the Advancement of Science (AAAS). doi: 10.1126/science.8134838.
Makhatadze, G.I., Clore, G.M., Gronenborn, A.M., & Privalov, P.L. (1994). Thermodynamics of unfolding of the all beta-sheet protein interleukin-1 beta. Biochemistry, 33(31), 9327-9332.American Chemical Society (ACS). doi: 10.1021/bi00197a037.
Qin, J., Clore, G.M., & Gronenborn, A.M. (1994). The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin. Structure, 2(6), 503-522.Elsevier. doi: 10.1016/s0969-2126(00)00051-4.
Rozwarski, D.A., Gronenborn, A.M., Clore, G.M., Bazan, J.F., Bohm, A., Wlodawer, A., Hatada, M., & Karplus, P.A. (1994). Structural comparisons among the short-chain helical cytokines. Structure, 2(3), 159-173.Elsevier. doi: 10.1016/s0969-2126(00)00018-6.
Smith, L.J., Redfield, C., Smith, R.A., Dobson, C.M., Clore, G.M., Gronenborn, A.M., Walter, M.R., Naganbushan, T.L., & Wlodawer, A. (1994). Comparison of four independently determined structures of human recombinant interleukin-4. Nat Struct Biol, 1(5), 301-310.Springer Nature. doi: 10.1038/nsb0594-301.
Wang, A.C., Lodi, P.J., Qin, J., Vuister, G.W., Gronenborn, A.M., & Clore, G.M. (1994). An efficient triple-resonance experiment for proton-directed sequential backbone assignment of medium-sized proteins. J Magn Reson B, 105(2), 196-198.Elsevier. doi: 10.1006/jmrb.1994.1123.
Werner, M.H., Clore, G.M., Gronenborn, A.M., & Nash, H.A. (1994). Symmetry and asymmetry in the function of Escherichia coli integration host factor: implications for target identification by DNA-binding proteins. Curr Biol, 4(6), 477-487.Elsevier. doi: 10.1016/s0960-9822(00)00108-1.
Werner, M.H., Clore, G.M., Gronenborn, A.M., Kondoh, A., & Fisher, R.J. (1994). Refolding proteins by gel filtration chromatography. FEBS Lett, 345(2-3), 125-130.Wiley. doi: 10.1016/0014-5793(94)00401-3.
Brünger, A.T., Clore, G.M., Gronenborn, A.M., Saffrich, R., & Nilges, M. (1993). Assessing the quality of solution nuclear magnetic resonance structures by complete cross-validation. Science, 261(5119), 328-331.American Association for the Advancement of Science (AAAS). doi: 10.1126/science.8332897.
Clore, G.M., & Gronenborn, A.M. (1993). Structural Studies of InterIeukin-1β, Interleukin-4, and lnterleukin-8. Methods, 3(1), 56-81.Elsevier. doi: 10.1006/immu.1993.1040.
CLORE, G.M., BAX, A., IKURA, M., & GRONENBORN, A.M. (1993). STRUCTURE OF CALMODULIN TARGET PEPTIDE COMPLEXES. CURRENT OPINION IN STRUCTURAL BIOLOGY, 3(6), 838-845.Elsevier. doi: 10.1016/0959-440X(93)90146-C.
Clore, G.M., Robien, M.A., & Gronenborn, A.M. (1993). Exploring the limits of precision and accuracy of protein structures determined by nuclear magnetic resonance spectroscopy. J Mol Biol, 231(1), 82-102.Elsevier. doi: 10.1006/jmbi.1993.1259.
Grasberger, B.L., Gronenborn, A.M., & Clore, G.M. (1993). Analysis of the backbone dynamics of interleukin-8 by 15N relaxation measurements. J Mol Biol, 230(2), 364-372.Elsevier. doi: 10.1006/jmbi.1993.1152.
Gronenborn, A.M., & Clore, G.M. (1993). Identification of the contact surface of a streptococcal protein G domain complexed with a human Fc fragment. J Mol Biol, 233(3), 331-335.Elsevier. doi: 10.1006/jmbi.1993.1514.
Gronenborn, A.M., & Clore, G.M. (1993). Structural Studies of Immunoglobulin-Binding Domains of Streptococcal Protein G. Methods, 2(1), 3-8.Elsevier. doi: 10.1006/immu.1993.1002.
Omichinski, J.G., Clore, G.M., Schaad, O., Felsenfeld, G., Trainor, C., Appella, E., Stahl, S.J., & Gronenborn, A.M. (1993). NMR structure of a specific DNA complex of Zn-containing DNA binding domain of GATA-1. Science, 261(5120), 438-446.American Association for the Advancement of Science (AAAS). doi: 10.1126/science.8332909.
Omichinski, J.G., Trainor, C., Evans, T., Gronenborn, A.M., Clore, G.M., & Felsenfeld, G. (1993). A small single-"finger" peptide from the erythroid transcription factor GATA-1 binds specifically to DNA as a zinc or iron complex. Proc Natl Acad Sci U S A, 90(5), 1676-1680.Proceedings of the National Academy of Sciences. doi: 10.1073/pnas.90.5.1676.
POWERS, R., CLORE, G.M., GARRETT, D.S., & GRONENBORN, A.M. (1993). RELATIONSHIPS BETWEEN THE PRECISION OF HIGH-RESOLUTION PROTEIN NMR STRUCTURES, SOLUTION-ORDER PARAMETERS, AND CRYSTALLOGRAPHIC B-FACTORS. JOURNAL OF MAGNETIC RESONANCE SERIES B, 101(3), 325-327.Elsevier. doi: 10.1006/jmrb.1993.1051.
Powers, R., Garrett, D.S., March, C.J., Frieden, E.A., Gronenborn, A.M., & Clore, G.M. (1993). The high-resolution, three-dimensional solution structure of human interleukin-4 determined by multidimensional heteronuclear magnetic resonance spectroscopy. Biochemistry, 32(26), 6744-6762.American Chemical Society (ACS). doi: 10.1021/bi00077a030.
Sakaguchi, K., Zambrano, N., Baldwin, E.T., Shapiro, B.A., Erickson, J.W., Omichinski, J.G., Clore, G.M., Gronenborn, A.M., & Appella, E. (1993). Identification of a binding site for the human immunodeficiency virus type 1 nucleocapsid protein. Proc Natl Acad Sci U S A, 90(11), 5219-5223.Proceedings of the National Academy of Sciences. doi: 10.1073/pnas.90.11.5219.
Varley, P., Gronenborn, A.M., Christensen, H., Wingfield, P.T., Pain, R.H., & Clore, G.M. (1993). Kinetics of folding of the all-beta sheet protein interleukin-1 beta. Science, 260(5111), 1110-1113.American Association for the Advancement of Science (AAAS). doi: 10.1126/science.8493553.
VUISTER, G.W., CLORE, G.M., GRONENBORN, A.M., POWERS, R., GARRETT, D.S., TSCHUDIN, R., & BAX, A. (1993). INCREASED RESOLUTION AND IMPROVED SPECTRAL QUALITY IN 4-DIMENSIONAL C-13/C-13-SEPARATED HMQC-NOESY-HMQC SPECTRA USING PULSED-FIELD GRADIENTS. JOURNAL OF MAGNETIC RESONANCE SERIES B, 101(2), 210-213.Elsevier. doi: 10.1006/jmrb.1993.1035.
Achari, A., Hale, S.P., Howard, A.J., Clore, G.M., Gronenborn, A.M., Hardman, K.D., & Whitlow, M. (1992). 1.67-A X-ray structure of the B2 immunoglobulin-binding domain of streptococcal protein G and comparison to the NMR structure of the B1 domain. Biochemistry, 31(43), 10449-10457.American Chemical Society (ACS). doi: 10.1021/bi00158a006.
Chandrasekhar, I., Clore, G.M., Szabo, A., Gronenborn, A.M., & Brooks, B.R. (1992). A 500 ps molecular dynamics simulation study of interleukin-1 beta in water. Correlation with nuclear magnetic resonance spectroscopy and crystallography. J Mol Biol, 226(1), 239-250.Elsevier. doi: 10.1016/0022-2836(92)90136-8.
Clore, G.M., & Gronenborn, A.M. (1992). NMR and X-ray analysis of the three-dimensional structure of interleukin-8. Cytokines, 4, 18-40.
Clore, G.M., & Gronenborn, A.M. (1992). Localization of bound water in the solution structure of the immunoglobulin binding domain of streptococcal protein G. Evidence for solvent-induced helical distortion in solution. J Mol Biol, 223(4), 853-856.Elsevier. doi: 10.1016/0022-2836(92)90247-h.
Forman-Kay, J.D., Clore, G.M., & Gronenborn, A.M. (1992). Relationship between electrostatics and redox function in human thioredoxin: characterization of pH titration shifts using two-dimensional homo- and heteronuclear NMR. Biochemistry, 31(13), 3442-3452.American Chemical Society (ACS). doi: 10.1021/bi00128a019.
Forman-Kay, J.D., Clore, G.M., Stahl, S.J., & Gronenborn, A.M. (1992). 1H and 15N resonance assignments and secondary structure of the human thioredoxin C62A, C69A, C73A mutant. J Biomol NMR, 2(5), 431-445.Springer Nature. doi: 10.1007/BF02192807.
Garrett, D.S., Powers, R., March, C.J., Frieden, E.A., Clore, G.M., & Gronenborn, A.M. (1992). Determination of the secondary structure and folding topology of human interleukin-4 using three-dimensional heteronuclear magnetic resonance spectroscopy. Biochemistry, 31(17), 4347-4353.American Chemical Society (ACS). doi: 10.1021/bi00132a027.
GRZESIEK, S., IKURA, M., CLORE, G.M., GRONENBORN, A.M., & BAX, A. (1992). A 3D TRIPLE-RESONANCE NMR TECHNIQUE FOR QUALITATIVE MEASUREMENT OF CARBONYL-H-BETA J COUPLINGS IN ISOTOPICALLY ENRICHED PROTEINS. JOURNAL OF MAGNETIC RESONANCE, 96(1), 215-221.Elsevier. doi: 10.1016/0022-2364(92)90307-S.
Ikura, M., Clore, G.M., Gronenborn, A.M., Zhu, G., Klee, C.B., & Bax, A. (1992). Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science, 256(5057), 632-638.American Association for the Advancement of Science (AAAS). doi: 10.1126/science.1585175.
Omichinski, J.G., Clore, G.M., Robien, M., Sakaguchi, K., Appella, E., & Gronenborn, A.M. (1992). High-resolution solution structure of the double Cys2His2 zinc finger from the human enhancer binding protein MBP-1. Biochemistry, 31(16), 3907-3917.American Chemical Society (ACS). doi: 10.1021/bi00131a004.
Omichinski, J.G., Sakaguchi, K., Clore, G.M., Gronenborn, A.M., & Appella, E. (1992). High-resolution structure of a double zinc finger from the human enhancer binding protein MPB-1 in solution. The Protein Journal, 11(4), 408-409.Springer Nature. doi: 10.1007/bf01673767.
Powers, R., Clore, G.M., Stahl, S.J., Wingfield, P.T., & Gronenborn, A. (1992). Analysis of the backbone dynamics of the ribonuclease H domain of the human immunodeficiency virus reverse transcriptase using 15N relaxation measurements. Biochemistry, 31(38), 9150-9157.American Chemical Society (ACS). doi: 10.1021/bi00153a006.
Powers, R., Garrett, D.S., March, C.J., Frieden, E.A., Gronenborn, A.M., & Clore, G.M. (1992). Three-dimensional solution structure of human interleukin-4 by multidimensional heteronuclear magnetic resonance spectroscopy. Science, 256(5064), 1673-1677.American Association for the Advancement of Science (AAAS). doi: 10.1126/science.256.5064.1673.
Powers, R., Garrett, D.S., March, C.J., Frieden, E.A., Gronenborn, A.M., & Clore, G.M. (1992). 1H, 15N, 13C, and 13CO assignments of human interleukin-4 using three-dimensional double- and triple-resonance heteronuclear magnetic resonance spectroscopy. Biochemistry, 31(17), 4334-4346.American Chemical Society (ACS). doi: 10.1021/bi00132a026.
Robien, M.A., Clore, G.M., Omichinski, J.G., Perham, R.N., Appella, E., Sakaguchi, K., & Gronenborn, A.M. (1992). Three-dimensional solution structure of the E3-binding domain of the dihydrolipoamide succinyltransferase core from the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli. Biochemistry, 31(13), 3463-3471.American Chemical Society (ACS). doi: 10.1021/bi00128a021.
Rose, K., Simona, M.G., Savoy, L.A., Regamey, P.O., Green, B.N., Clore, G.M., Gronenborn, A.M., & Wingfield, P.T. (1992). Pyruvic acid is attached through its central carbon atom to the amino terminus of the recombinant DNA-derived DNA-binding protein Ner of bacteriophage Mu. J Biol Chem, 267(27), 19101-19106.Elsevier. doi: 10.1016/s0021-9258(18)41747-4.
Shaanan, B., Gronenborn, A.M., Cohen, G.H., Gilliland, G.L., Veerapandian, B., Davies, D.R., & Clore, G.M. (1992). Combining experimental information from crystal and solution studies: joint X-ray and NMR refinement. Science, 257(5072), 961-964.American Association for the Advancement of Science (AAAS). doi: 10.1126/science.1502561.
Baldwin, E.T., Weber, I.T., St Charles, R., Xuan, J.C., Appella, E., Yamada, M., Matsushima, K., Edwards, B.F., Clore, G.M., & Gronenborn, A.M. (1991). Crystal structure of interleukin 8: symbiosis of NMR and crystallography. Proc Natl Acad Sci U S A, 88(2), 502-506.Proceedings of the National Academy of Sciences. doi: 10.1073/pnas.88.2.502.
Clore, G.M., & Gronenborn, A.M. (1991). Comparison of the solution nuclear magnetic resonance and X-ray crystal structures of human recombinant interleukin-1 beta. J Mol Biol, 221(1), 47-53.Elsevier. doi: 10.1016/0022-2836(91)80202-6.
Clore, G.M., & Gronenborn, A.M. (1991). Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy. Science, 252(5011), 1390-1399.American Association for the Advancement of Science (AAAS). doi: 10.1126/science.2047852.
Clore, G.M., & Gronenborn, A.M. (1991). Comparison of the solution nuclear magnetic resonance and crystal structures of interleukin-8. Possible implications for the mechanism of receptor binding. J Mol Biol, 217(4), 611-620.Elsevier. doi: 10.1016/0022-2836(91)90518-b.
Clore, G.M., & Gronenborn, A.M. (1991). Two-, three-, and four-dimensional NMR methods for obtaining larger and more precise three-dimensional structures of proteins in solution. Annu Rev Biophys Biophys Chem, 20(1), 29-63.Annual Reviews. doi: 10.1146/annurev.bb.20.060191.000333.
CLORE, G.M., & GRONENBORN, A.M. (1991). APPLICATIONS OF 3-DIMENSIONAL AND 4-DIMENSIONAL HETERONUCLEAR NMR-SPECTROSCOPY TO PROTEIN-STRUCTURE DETERMINATION. PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY, 23(1), 43-92.Elsevier. doi: 10.1016/0079-6565(91)80002-J.
Clore, G.M., Bax, A., & Gronenborn, A.M. (1991). Stereospecific assignment of beta-methylene protons in larger proteins using 3D 15N-separated Hartmann-Hahn and 13C-separated rotating frame Overhauser spectroscopy. J Biomol NMR, 1(1), 13-22.Springer Nature. doi: 10.1007/BF01874566.
Clore, G.M., Driscoll, P.C., Wingfield, P.T., & Gronenborn, A.M. (1991). Analysis of the backbone dynamics of interleukin-1 .beta. using two-dimensional inverse detected heteronuclear nitrogen-15-proton NMR spectroscopy [Erratum to document cited in CA113(9):76266p]. Biochemistry, 30(1), 312.American Chemical Society (ACS). doi: 10.1021/bi00215a043.
Clore, G.M., Kay, L.E., Bax, A., & Gronenborn, A.M. (1991). Four-dimensional 13C/13C-edited nuclear Overhauser enhancement spectroscopy of a protein in solution: application to interleukin 1 beta. Biochemistry, 30(1), 12-18.American Chemical Society (ACS). doi: 10.1021/bi00215a002.
CLORE, G.M., OMICHINSKI, J.G., & GRONENBORN, A.M. (1991). SLOW CONFORMATIONAL DYNAMICS AT THE METAL COORDINATION SITE OF A ZINC FINGER. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 113(11), 4350-4351.American Chemical Society (ACS). doi: 10.1021/ja00011a059.
Clore, G.M., Wingfield, P.T., & Gronenborn, A.M. (1991). High-resolution three-dimensional structure of interleukin 1 beta in solution by three- and four-dimensional nuclear magnetic resonance spectroscopy. Biochemistry, 30(9), 2315-2323.American Chemical Society (ACS). doi: 10.1021/bi00223a005.
Forman-Kay, J.D., Clore, G.M., Wingfield, P.T., & Gronenborn, A.M. (1991). High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution. Biochemistry, 30(10), 2685-2698.American Chemical Society (ACS). doi: 10.1021/bi00224a017.
Forman-Kay, J.D., Gronenborn, A.M., Wingfield, P.T., & Clore, G.M. (1991). Determination of the positions of bound water molecules in the solution structure of reduced human thioredoxin by heteronuclear three-dimensional nuclear magnetic resonance spectroscopy. J Mol Biol, 220(2), 209-216.Elsevier. doi: 10.1016/0022-2836(91)90004-p.
GARRETT, D.S., POWERS, R., GRONENBORN, A.M., & CLORE, G.M. (1991). A COMMON-SENSE APPROACH TO PEAK PICKING IN 2-DIMENSIONAL, 3-DIMENSIONAL, AND 4-DIMENSIONAL SPECTRA USING AUTOMATIC COMPUTER-ANALYSIS OF CONTOUR DIAGRAMS. JOURNAL OF MAGNETIC RESONANCE, 95(1), 214-220.Elsevier. doi: 10.1016/0022-2364(91)90341-P.
Gronenborn, A.M., & Clore, G.M. (1991). Modeling the three-dimensional structure of the monocyte chemo-attractant and activating protein MCAF/MCP-1 on the basis of the solution structure of interleukin-8. Protein Eng, 4(3), 263-269.Oxford University Press (OUP). doi: 10.1093/protein/4.3.263.
Gronenborn, A.M., & Clore, G.M. (1991). Protein structure determination in solution using nuclear magnetic resonance spectroscopy. NIDA Res Monogr, 112(112), 78-105.
Gronenborn, A.M., Filpula, D.R., Essig, N.Z., Achari, A., Whitlow, M., Wingfield, P.T., & Clore, G.M. (1991). A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G. Science, 253(5020), 657-661.American Association for the Advancement of Science (AAAS). doi: 10.1126/science.1871600.
Kraulis, P.J. (1991). Similarity of protein G and ubiquitin. Science, 254(5031), 581-582.American Association for the Advancement of Science (AAAS). doi: 10.1126/science.1658931.
Marius Clore, G., Driscoll, P.G., Wingfield, P.T., & Gronenborn, A.M. (1991). Erratum: Analysis of the backbone dynamics of interleukin-1β using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy (Biochemistry® (1990) 29(32) (7387-7401)). Biochemistry®, 30(1), 312.
Omichinski, J.G., Clore, G.M., Sakaguchi, K., Appella, E., & Gronenborn, A.M. (1991). Structural characterization of a 39-residue synthetic peptide containing the two zinc binding domains from the HIV-1 p7 nucleocapsid protein by CD and NMR spectroscopy. FEBS Lett, 292(1-2), 25-30.Wiley. doi: 10.1016/0014-5793(91)80825-n.
Powers, R., Clore, G.M., Bax, A., Garrett, D.S., Stahl, S.J., Wingfield, P.T., & Gronenborn, A.M. (1991). Secondary structure of the ribonuclease H domain of the human immunodeficiency virus reverse transcriptase in solution using three-dimensional double and triple resonance heteronuclear magnetic resonance spectroscopy. J Mol Biol, 221(4), 1081-1090.Elsevier. doi: 10.1016/0022-2836(91)90920-2.
POWERS, R., GRONENBORN, A.M., CLORE, G.M., & BAX, A. (1991). 3-DIMENSIONAL TRIPLE-RESONANCE NMR OF C-13/N-15-ENRICHED PROTEINS USING CONSTANT-TIME EVOLUTION. JOURNAL OF MAGNETIC RESONANCE, 94(1), 209-213.Elsevier. doi: 10.1016/0022-2364(91)90312-H.
Sakaguchi, K., Appella, E., Omichinski, J.G., Clore, G.M., & Gronenborn, A.M. (1991). Specific DNA binding to a major histocompatibility complex enhancer sequence by a synthetic 57-residue double zinc finger peptide from a human enhancer binding protein. J Biol Chem, 266(11), 7306-7311.Elsevier. doi: 10.1016/s0021-9258(20)89645-8.
Appella, E., Matsushima, K., Oppenheim, J.J., Yoshimura, T., Leonard, E.J., Clore, G.M., & Gronenborn, A.M. (1990). Determination of the primary and secondary structure of NAP-1/IL-8 and a monocyte chemoattractant protein, MCP-1/MCAF. Prog Clin Biol Res, 349, 405-417.
BAX, A., CLORE, G.M., & GRONENBORN, A.M. (1990). H-1-H-1 CORRELATION VIA ISOTROPIC MIXING OF C-13 MAGNETIZATION, A NEW 3-DIMENSIONAL APPROACH FOR ASSIGNING H-1 AND C-13 SPECTRA OF C-13-ENRICHED PROTEINS. JOURNAL OF MAGNETIC RESONANCE, 88(2), 425-431.Elsevier. doi: 10.1016/0022-2364(90)90202-K.
BAX, A., CLORE, G.M., DRISCOLL, P.C., GRONENBORN, A.M., IKURA, M., & KAY, L.E. (1990). PRACTICAL ASPECTS OF PROTON CARBON CARBON PROTON 3-DIMENSIONAL CORRELATION SPECTROSCOPY OF C-13-LABELED PROTEINS. JOURNAL OF MAGNETIC RESONANCE, 87(3), 620-627.Elsevier. doi: 10.1016/0022-2364(90)90320-9.
Becerra, S.P., Clore, G.M., Gronenborn, A.M., Karlström, A.R., Stahl, S.J., Wilson, S.H., & Wingfield, P.T. (1990). Purification and characterization of the RNase H domain of HIV-1 reverse transcriptase expressed in recombinant Escherichia coli. FEBS Lett, 270(1-2), 76-80.Wiley. doi: 10.1016/0014-5793(90)81238-j.
Clore, G.M., Appella, E., Yamada, M., Matsushima, K., & Gronenborn, A.M. (1990). Three-dimensional structure of interleukin 8 in solution. Biochemistry, 29(7), 1689-1696.American Chemical Society (ACS). doi: 10.1021/bi00459a004.
Clore, G.M., Bax, A., Driscoll, P.C., Wingfield, P.T., & Gronenborn, A.M. (1990). Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy. Biochemistry, 29(35), 8172-8184.American Chemical Society (ACS). doi: 10.1021/bi00487a027.
Clore, G.M., Bax, A., Wingfield, P.T., & Gronenborn, A.M. (1990). Identification and localization of bound internal water in the solution structure of interleukin 1 beta by heteronuclear three-dimensional 1H rotating-frame Overhauser 15N-1H multiple quantum coherence NMR spectroscopy. Biochemistry, 29(24), 5671-5676.American Chemical Society (ACS). doi: 10.1021/bi00476a004.
Clore, G.M., Driscoll, P.C., Wingfield, P.T., & Gronenborn, A.M. (1990). Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy. Biochemistry, 29(32), 7387-7401.American Chemical Society (ACS). doi: 10.1021/bi00484a006.
Clore, G.M., Driscoll, P.C., Wingfield, P.T., & Gronenborn, A.M. (1990). Low resolution structure of interleukin-1 beta in solution derived from 1H-15N heteronuclear three-dimensional nuclear magnetic resonance spectroscopy. J Mol Biol, 214(4), 811-817.Elsevier. doi: 10.1016/0022-2836(90)90336-k.
CLORE, G.M., SZABO, A., BAX, A., KAY, L.E., DRISCOLL, P.C., & GRONENBORN, A.M. (1990). DEVIATIONS FROM THE SIMPLE 2-PARAMETER MODEL-FREE APPROACH TO THE INTERPRETATION OF N-15 NUCLEAR MAGNETIC-RELAXATION OF PROTEINS. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 112(12), 4989-4991.American Chemical Society (ACS). doi: 10.1021/ja00168a070.
Driscoll, P.C., Clore, G.M., Marion, D., Wingfield, P.T., & Gronenborn, A.M. (1990). Complete resonance assignment for the polypeptide backbone of interleukin 1 beta using three-dimensional heteronuclear NMR spectroscopy. Biochemistry, 29(14), 3542-3556.American Chemical Society (ACS). doi: 10.1021/bi00466a018.
Driscoll, P.C., Gronenborn, A.M., Wingfield, P.T., & Clore, G.M. (1990). Determination of the secondary structure and molecular topology of interleukin-1 beta by use of two- and three-dimensional heteronuclear 15N-1H NMR spectroscopy. Biochemistry, 29(19), 4668-4682.American Chemical Society (ACS). doi: 10.1021/bi00471a023.
Forman-Kay, J.E., Gronenborn, A.M., Kay, L.E., Wingfield, P.T., & Clore, G.M. (1990). Studies on the solution conformation of human thioredoxin using heteronuclear 15N-1H nuclear magnetic resonance spectroscopy. Biochemistry, 29(6), 1566-1572.American Chemical Society (ACS). doi: 10.1021/bi00458a030.
Gronenborn, A.M., & Clore, G.M. (1990). Determination of ligand conformation in macromolecular complexes using the transferred nuclear Overhauser effect. Biochem Pharmacol, 40(1), 115-119.Elsevier. doi: 10.1016/0006-2952(90)90185-n.
Gronenborn, A.M., & Clore, G.M. (1990). Protein structure determination in solution by two-dimensional and three-dimensional nuclear magnetic resonance spectroscopy. Anal Chem, 62(1), 2-15.American Chemical Society (ACS). doi: 10.1021/ac00200a003.
Gronenborn, A.M., Nilges, M., Peanasky, R.J., & Clore, G.M. (1990). Sequential resonance assignment and secondary structure determination of the Ascaris trypsin inhibitor, a member of a novel class of proteinase inhibitors. Biochemistry, 29(1), 183-189.American Chemical Society (ACS). doi: 10.1021/bi00453a025.
IKURA, M., BAX, A., CLORE, G.M., & GRONENBORN, A.M. (1990). DETECTION OF NUCLEAR OVERHAUSER EFFECTS BETWEEN DEGENERATE AMIDE PROTON RESONANCES BY HETERONUCLEAR 3-DIMENSIONAL NUCLEAR-MAGNETIC-RESONANCE SPECTROSCOPY. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 112(24), 9020-9022.American Chemical Society (ACS). doi: 10.1021/ja00180a080.
Kay, L.E., Clore, G.M., Bax, A., & Gronenborn, A.M. (1990). Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 beta in solution. Science, 249(4967), 411-414.American Association for the Advancement of Science (AAAS). doi: 10.1126/science.2377896.
Nilges, M., Clore, G.M., & Gronenborn, A.M. (1990). 1H-NMR stereospecific assignments by conformational data-base searches. Biopolymers, 29(4-5), 813-822.Wiley. doi: 10.1002/bip.360290415.
Omichinski, J.G., Clore, G.M., Appella, E., Sakaguchi, K., & Gronenborn, A.M. (1990). High-resolution three-dimensional structure of a single zinc finger from a human enhancer binding protein in solution. Biochemistry, 29(40), 9324-9334.American Chemical Society (ACS). doi: 10.1021/bi00492a004.
Allet, B., Payton, M., Mattaliano, R.J., Gronenborn, A.M., Clore, G.M., & Wingfield, P.T. (1989). Commentary on the article: Purification and Characterization of the Ner Repressor of Bacteriophage Mu (1989) FEBS Lett. 244, 369-375 by G. Kukolj, P.P. Tolias and M.S. DuBow. FEBS Lett, 251(1-2), 282.Wiley. doi: 10.1016/0014-5793(89)81471-1.
Clore, G.M., & Gronenborn, A.M. (1989). Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy. Crit Rev Biochem Mol Biol, 24(5), 479-564.Taylor & Francis. doi: 10.3109/10409238909086962.
CLORE, G.M., & GRONENBORN, A.M. (1989). HOW ACCURATELY CAN INTERPROTON DISTANCES IN MACROMOLECULES REALLY BE DETERMINED BY FULL RELAXATION MATRIX ANALYSIS OF NUCLEAR OVERHAUSER ENHANCEMENT DATA. JOURNAL OF MAGNETIC RESONANCE, 84(2), 398-409.Elsevier. doi: 10.1016/0022-2364(89)90388-0.
Clore, G.M., Appella, E., Yamada, M., Matsushima, K., & Gronenborn, A.M. (1989). Determination of the secondary structure of interleukin-8 by nuclear magnetic resonance spectroscopy. J Biol Chem, 264(32), 18907-18911.Elsevier. doi: 10.1016/s0021-9258(19)47243-8.
Driscoll, P.C., Clore, G.M., Beress, L., & Gronenborn, A.M. (1989). A proton nuclear magnetic resonance study of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: sequential and stereospecific resonance assignment and secondary structure. Biochemistry, 28(5), 2178-2187.American Chemical Society (ACS). doi: 10.1021/bi00431a032.
Driscoll, P.C., Gronenborn, A.M., & Clore, G.M. (1989). The influence of stereospecific assignments on the determination of three-dimensional structures of proteins by nuclear magnetic resonance spectroscopy. Application to the sea anemone protein BDS-I. FEBS Lett, 243(2), 223-233.Wiley. doi: 10.1016/0014-5793(89)80134-6.
Driscoll, P.C., Gronenborn, A.M., Beress, L., & Clore, G.M. (1989). Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing. Biochemistry, 28(5), 2188-2198.American Chemical Society (ACS). doi: 10.1021/bi00431a033.
Folkers, P.J., Clore, G.M., Driscoll, P.C., Dodt, J., Köhler, S., & Gronenborn, A.M. (1989). Solution structure of recombinant hirudin and the Lys-47----Glu mutant: a nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study. Biochemistry, 28(6), 2601-2617.American Chemical Society (ACS). doi: 10.1021/bi00432a038.
Forman-Kay, J.D., Clore, G.M., Driscoll, P.C., Wingfield, P., Richards, F.M., & Gronenborn, A.M. (1989). A proton nuclear magnetic resonance assignment and secondary structure determination of recombinant human thioredoxin. Biochemistry, 28(17), 7088-7097.American Chemical Society (ACS). doi: 10.1021/bi00443a045.
Gronenborn, A.M., & Clore, G.M. (1989). Analysis of the relative contributions of the nuclear Overhauser interproton distance restraints and the empirical energy function in the calculation of oligonucleotide structures using restrained molecular dynamics. Biochemistry, 28(14), 5978-5984.American Chemical Society (ACS). doi: 10.1021/bi00440a039.
Gronenborn, A.M., & Clore, G.M. (1989). Three-dimensional structures of proteins in solution by nuclear magnetic resonance spectroscopy. Protein Seq Data Anal, 2(1), 1-8.
Gronenborn, A.M., Bax, A., Wingfield, P.T., & Clore, G.M. (1989). A powerful method of sequential proton resonance assignment in proteins using relayed 15N-1H multiple quantum coherence spectroscopy. FEBS Lett, 243(1), 93-98.Wiley. doi: 10.1016/0014-5793(89)81224-4.
Gronenborn, A.M., Wingfield, P.T., & Clore, G.M. (1989). Determination of the secondary structure of the DNA binding protein Ner from phage Mu using 1H homonuclear and 15N-1H heteronuclear NMR spectroscopy. Biochemistry, 28(12), 5081-5089.American Chemical Society (ACS). doi: 10.1021/bi00438a027.
Kraulis, J., Clore, G.M., Nilges, M., Jones, T.A., Pettersson, G., Knowles, J., & Gronenborn, A.M. (1989). Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing. Biochemistry, 28(18), 7241-7257.American Chemical Society (ACS). doi: 10.1021/bi00444a016.
Marion, D., Driscoll, P.C., Kay, L.E., Wingfield, P.T., Bax, A., Gronenborn, A.M., & Clore, G.M. (1989). Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1 beta. Biochemistry, 28(15), 6150-6156.American Chemical Society (ACS). doi: 10.1021/bi00441a004.
OSCHKINAT, H., CIESLAR, C., GRONENBORN, A.M., & CLORE, G.M. (1989). 3-DIMENSIONAL HOMONUCLEAR HARTMANN-HAHN-NUCLEAR OVERHAUSER ENHANCEMENT SPECTROSCOPY IN H2O AND ITS APPLICATION TO PROTEINS. JOURNAL OF MAGNETIC RESONANCE, 81(1), 212-216.Elsevier. doi: 10.1016/0022-2364(89)90283-7.
OSCHKINAT, H., CIESLAR, C., HOLAK, T.A., CLORE, G.M., & GRONENBORN, A.M. (1989). PRACTICAL AND THEORETICAL ASPECTS OF 3-DIMENSIONAL HOMONUCLEAR HARTMANN-HAHN-NUCLEAR OVERHAUSER ENHANCEMENT SPECTROSCOPY OF PROTEINS. JOURNAL OF MAGNETIC RESONANCE, 83(3), 450-472.Elsevier. doi: 10.1016/0022-2364(89)90342-9.
Wingfield, P., Graber, P., Shaw, A.R., Gronenborn, A.M., Clore, G.M., & MacDonald, H.R. (1989). Preparation, characterization and application of interleukin-1 beta mutant proteins with surface-accessible cysteine residues. Eur J Biochem, 179(3), 565-571.Wiley. doi: 10.1111/j.1432-1033.1989.tb14584.x.
Allet, B., Payton, M., Mattaliano, R.J., Gronenborn, A.M., Clore, G.M., & Wingfield, P.T. (1988). Purification and characterization of the DNA-binding protein Ner of bacteriophage Mu. Gene, 65(2), 259-268.Elsevier. doi: 10.1016/0378-1119(88)90462-3.
CIESLAR, C., CLORE, G.M., & GRONENBORN, A.M. (1988). COMPUTER-AIDED SEQUENTIAL ASSIGNMENT OF PROTEIN H-1-NMR SPECTRA. JOURNAL OF MAGNETIC RESONANCE, 80(1), 119-127.Elsevier. doi: 10.1016/0022-2364(88)90063-7.
CIESLAR, C., CLORE, G.M., & GRONENBORN, A.M. (1988). AUTOMATIC PHASING OF PURE PHASE ABSORPTION TWO-DIMENSIONAL NMR-SPECTRA. JOURNAL OF MAGNETIC RESONANCE, 79(1), 154-157.Elsevier. doi: 10.1016/0022-2364(88)90332-0.
Clore, G.M., Bax, A., Wingfield, P., & Gronenborn, A.M. (1988). Long-range 15N-1H correlation as an aid to sequential proton resonance assignment of proteins. Application to the DNA-binding protein ner from phage Mu. FEBS Lett, 238(1), 17-21.Wiley. doi: 10.1016/0014-5793(88)80216-3.
Clore, G.M., Nilges, M., Brünger, A., & Gronenborn, A.M. (1988). Determination of the backbone conformation of secretin by restrained molecular dynamics on the basis of interproton distance data. Eur J Biochem, 171(3), 479-484.Wiley. doi: 10.1111/j.1432-1033.1988.tb13814.x.
Clore, G.M., Oschkinat, H., McLaughlin, L.W., Benseler, F., Happ, C.S., Happ, E., & Gronenborn, A.M. (1988). Refinement of the solution structure of the DNA dodecamer 5'd(CGCGPATTCGCG)2 containing a stable purine-thymine base pair: combined use of nuclear magnetic resonance and restrained molecular dynamics. Biochemistry, 27(11), 4185-4197.American Chemical Society (ACS). doi: 10.1021/bi00411a042.
Garin, J., Vignais, P.V., Gronenborn, A.M., Clore, G.M., Gao, Z., & Baeuerlein, E. (1988). 1H-NMR studies on nucleotide binding to the catalytic sites of bovine mitochondrial F1-ATPase. FEBS Lett, 242(1), 178-182.Wiley. doi: 10.1016/0014-5793(88)81011-1.
Gronenborn, A.M., Sandulache, R., Gärtner, S., & Clore, G.M. (1988). Mutations in the cyclic AMP binding site of the cyclic AMP receptor protein of Escherichia coli. Biochem J, 253(3), 801-807.Portland Press. doi: 10.1042/bj2530801.
Gronenborn, A.M., Wingfield, P.T., McDonald, H.R., Schmeissner, U., & Clore, G.M. (1988). Site directed mutants of human interleukin-1 alpha: a 1H-NMR and receptor binding study. FEBS Lett, 231(1), 135-138.Wiley. doi: 10.1016/0014-5793(88)80717-8.
Happ, C.S., Happ, E., Clore, G.M., & Gronenborn, A.M. (1988). Refinement of the solution structure of the RNA-DNA hybrid 5'-[r(GCA)d(TGC)]2. Combined use of nuclear magnetic resonance and restrained molecular dynamics. FEBS Lett, 236(1), 62-70.Wiley. doi: 10.1016/0014-5793(88)80286-2.
HAPP, C.S., HAPP, E., GRONENBORN, A.M., & CLORE, G.M. (1988). SYNTHESIS AND H-1-NMR STUDIES OF DNA-RNA HYBRIDS FOR STRUCTURAL-ANALYSIS. NUCLEOSIDES & NUCLEOTIDES, 7(5-6), 733-736.Taylor & Francis. doi: 10.1080/07328318808056320.
Happ, C.S., Happ, E., Nilges, M., Gronenborn, A.M., & Clore, G.M. (1988). Refinement of the solution structure of the ribonucleotide 5'r(GCAUGC)2: combined use of nuclear magnetic resonance and restrained molecular dynamics. Biochemistry, 27(5), 1735-1743.American Chemical Society (ACS). doi: 10.1021/bi00405a053.
Holak, T.A., Engström, A., Kraulis, P.J., Lindeberg, G., Bennich, H., Jones, T.A., Gronenborn, A.M., & Clore, G.M. (1988). The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study. Biochemistry, 27(20), 7620-7629.American Chemical Society (ACS). doi: 10.1021/bi00420a008.
Holak, T.A., Nilges, M., Prestegard, J.H., Gronenborn, A.M., & Clore, G.M. (1988). Three-dimensional structure of acyl carrier protein in solution determined by nuclear magnetic resonance and the combined use of dynamical simulated annealing and distance geometry. Eur J Biochem, 175(1), 9-15.Wiley. doi: 10.1111/j.1432-1033.1988.tb14159.x.
Meyer, E.F., Clore, G.M., Gronenborn, A.M., & Hansen, H.A. (1988). Analysis of an enzyme-substrate complex by X-ray crystallography and transferred nuclear Overhauser enhancement measurements: porcine pancreatic elastase and a hexapeptide. Biochemistry, 27(2), 725-730.American Chemical Society (ACS). doi: 10.1021/bi00402a035.
Nilges, M., Clore, G.M., & Gronenborn, A.M. (1988). Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding. FEBS Lett, 239(1), 129-136.Wiley. doi: 10.1016/0014-5793(88)80559-3.
Nilges, M., Clore, G.M., & Gronenborn, A.M. (1988). Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations. FEBS Lett, 229(2), 317-324.Wiley. doi: 10.1016/0014-5793(88)81148-7.
Nilges, M., Gronenborn, A.M., Brünger, A.T., & Clore, G.M. (1988). Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints. Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2. Protein Eng, 2(1), 27-38.Oxford University Press (OUP). doi: 10.1093/protein/2.1.27.
OSCHKINAT, H., CLORE, G.M., & GRONENBORN, A.M. (1988). A TWO-DIMENSIONAL NUCLEAR OVERHAUSER ENHANCEMENT EXPERIMENT USING SEMISELECTIVE SOFT PULSES, AND ITS APPLICATIONS TO PROTEINS. JOURNAL OF MAGNETIC RESONANCE, 78(2), 371-375.Elsevier. doi: 10.1016/0022-2364(88)90285-5.
Oschkinat, H., Griesinger, C., Kraulis, P.J., Sørensen, O.W., Ernst, R.R., Gronenborn, A.M., & Clore, G.M. (1988). Three-dimensional NMR spectroscopy of a protein in solution. Nature, 332(6162), 374-376.Springer Nature. doi: 10.1038/332374a0.
Zarbock, J., Gennaro, R., Romeo, D., Clore, G.M., & Gronenborn, A.M. (1988). A proton nuclear magnetic resonance study of the conformation of bovine anaphylatoxin C5a in solution. FEBS Lett, 238(2), 289-294.Wiley. doi: 10.1016/0014-5793(88)80499-x.
BAX, A., SKLENAR, V., CLORE, G.M., & GRONENBORN, A.M. (1987). WATER SUPPRESSION IN TWO-DIMENSIONAL SPIN-LOCKED NUCLEAR-MAGNETIC-RESONANCE EXPERIMENTS USING A NOVEL PHASE-CYCLING PROCEDURE. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 109(21), 6511-6513.American Chemical Society (ACS). doi: 10.1021/ja00255a047.
Brünger, A.T., Campbell, R.L., Clore, G.M., Gronenborn, A.M., Karplus, M., Petsko, G.A., & Teeter, M.M. (1987). Solution of a protein crystal structure with a model obtained from NMR interproton distance restraints. Science, 235(4792), 1049-1053.American Association for the Advancement of Science (AAAS). doi: 10.1126/science.235.4792.1049.
Brünger, A.T., Clore, G.M., Gronenborn, A.M., & Karplus, M. (1987). Solution conformations of human growth hormone releasing factor: comparison of the restrained molecular dynamics and distance geometry methods for a system without long-range distance data. Protein Eng, 1(5), 399-406.Oxford University Press (OUP). doi: 10.1093/protein/1.5.399.
Clore, G.M., & Gronenborn, A.M. (1987). Determination of three-dimensional structures of proteins in solution by nuclear magnetic resonance spectroscopy. Protein Eng, 1(4), 275-288.Oxford University Press (OUP). doi: 10.1093/protein/1.4.275.
Clore, G.M., Gronenborn, A.M., James, M.N., Kjaer, M., McPhalen, C.A., & Poulsen, F.M. (1987). Comparison of the solution and X-ray structures of barley serine proteinase inhibitor 2. Protein Eng, 1(4), 313-318.Oxford University Press (OUP). doi: 10.1093/protein/1.4.313.
Clore, G.M., Gronenborn, A.M., Kjaer, M., & Poulsen, F.M. (1987). The determination of the three-dimensional structure of barley serine proteinase inhibitor 2 by nuclear magnetic resonance, distance geometry and restrained molecular dynamics. Protein Eng, 1(4), 305-311.Oxford University Press (OUP). doi: 10.1093/protein/1.4.305.
Clore, G.M., Gronenborn, A.M., Nilges, M., & Ryan, C.A. (1987). Three-dimensional structure of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics. Biochemistry, 26(24), 8012-8023.American Chemical Society (ACS). doi: 10.1021/bi00398a069.
Clore, G.M., Gronenborn, A.M., Nilges, M., Sukumaran, D.K., & Zarbock, J. (1987). The polypeptide fold of the globular domain of histone H5 in solution. A study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics. EMBO J, 6(6), 1833-1842.Springer Nature. doi: 10.1002/j.1460-2075.1987.tb02438.x.
Clore, G.M., Nilges, M., Brünger, A.T., Karplus, M., & Gronenborn, A.M. (1987). A comparison of the restrained molecular dynamics and distance geometry methods for determining three-dimensional structures of proteins on the basis of interproton distances. FEBS Lett, 213(2), 269-277.Wiley. doi: 10.1016/0014-5793(87)81504-1.
Clore, G.M., Sukumaran, D.K., Gronenborn, A.M., Teeter, M.M., Whitlow, M., & Jones, B.L. (1987). Nuclear magnetic resonance study of the solution structure of alpha 1-purothionin. Sequential resonance assignment, secondary structure and low resolution tertiary structure. J Mol Biol, 193(3), 571-578.Elsevier. doi: 10.1016/0022-2836(87)90267-1.
CLORE, G.M., SUKUMARAN, D.K., NILGES, M., & GRONENBORN, A.M. (1987). 3-DIMENSIONAL STRUCTURE OF PHORATOXIN IN SOLUTION - COMBINED USE OF NUCLEAR-MAGNETIC-RESONANCE, DISTANCE GEOMETRY, AND RESTRAINED MOLECULAR-DYNAMICS. BIOCHEMISTRY, 26(6), 1732-1745.American Chemical Society (ACS). doi: 10.1021/bi00380a037.
Clore, G.M., Sukumaran, D.K., Nilges, M., Zarbock, J., & Gronenborn, A.M. (1987). The conformations of hirudin in solution: a study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics. EMBO J, 6(2), 529-537.Springer Nature. doi: 10.1002/j.1460-2075.1987.tb04785.x.
Gent, M.E., Gärtner, S., Gronenborn, A.M., Sandulache, R., & Clore, G.M. (1987). Site-directed mutants of the cAMP receptor protein--DNA binding of five mutant proteins. Protein Eng, 1(3), 201-203.Oxford University Press (OUP). doi: 10.1093/protein/1.3.201.
Gent, M.E., Gronenborn, A.M., Davies, R.W., & Clore, G.M. (1987). Probing the sequence-specific interaction of the cyclic AMP receptor protein with DNA by site-directed mutagenesis. Biochem J, 242(3), 645-653.Portland Press. doi: 10.1042/bj2420645.
Gronenborn, A.M., Bovermann, G., & Clore, G.M. (1987). A 1H-NMR study of the solution conformation of secretin. Resonance assignment and secondary structure. FEBS Lett, 215(1), 88-94.Wiley. doi: 10.1016/0014-5793(87)80119-9.
Happ, E., Scalfi-Happ, C., Clore, G.M., & Gronenborn, A.M. (1987). Chemical synthesis of r(GCAUGC) for high-resolution 1H-NMR studies. Nucleic Acids Symp Ser, (18), 265-268.
Jansen, C., Gronenborn, A.M., & Clore, G.M. (1987). The binding of the cyclic AMP receptor protein to synthetic DNA sites containing permutations in the consensus sequence TGTGA. Biochem J, 246(1), 227-232.Portland Press. doi: 10.1042/bj2460227.
NILGES, M., CLORE, G.M., & GRONENBORN, A.M. (1987). A SIMPLE METHOD FOR DELINEATING WELL-DEFINED AND VARIABLE REGIONS IN PROTEIN STRUCTURES DETERMINED FROM INTERPROTON DISTANCE DATA. FEBS LETTERS, 219(1), 11-16.Wiley. doi: 10.1016/0014-5793(87)81181-X.
Nilges, M., Clore, G.M., Gronenborn, A.M., Brunger, A.T., Karplus, M., & Nilsson, L. (1987). Refinement of the solution structure of the DNA hexamer 5'd(GCATGC)2: combined use of nuclear magnetic resonance and restrained molecular dynamics. Biochemistry, 26(12), 3718-3733.American Chemical Society (ACS). doi: 10.1021/bi00386a068.
Nilges, M., Clore, G.M., Gronenborn, A.M., Piel, N., & McLaughlin, L.W. (1987). Refinement of the solution structure of the DNA decamer 5'd(CTGGATCCAG)2: combined use of nuclear magnetic resonance and restrained molecular dynamics. Biochemistry, 26(12), 3734-3744.American Chemical Society (ACS). doi: 10.1021/bi00386a069.
OSCHKINAT, H., CLORE, G.M., NILGES, M., & GRONENBORN, A.M. (1987). APPLICATION OF THE Z-COSY TECHNIQUE WITH A MODIFIED PULSE SEQUENCE TO MEASUREMENT OF COUPLING-CONSTANTS IN MACROMOLECULES. JOURNAL OF MAGNETIC RESONANCE, 75(3), 534-539.Elsevier. doi: 10.1016/0022-2364(87)90111-9.
Shih, D.T., Peratz, M.F., Gronenborn, A.M., & Clore, G.M. (1987). Histidine proton resonances of carbonmonoxyhaemoglobins A and Cowtown in chloride-free buffer. J Mol Biol, 195(2), 453-455.Elsevier. doi: 10.1016/0022-2836(87)90666-8.
Sukumaran, D.K., Clore, G.M., Preuss, A., Zarbock, J., & Gronenborn, A.M. (1987). Proton nuclear magnetic resonance study of hirudin: resonance assignment and secondary structure. Biochemistry, 26(2), 333-338.American Chemical Society (ACS). doi: 10.1021/bi00376a001.
Wingfield, P., Graber, P., Movva, N.R., Gronenborn, A.M., Clore, G.M., & MacDonald, H.R. (1987). N-terminal-methionylated interleukin-1 beta has reduced receptor-binding affinity. FEBS Lett, 215(1), 160-164.Wiley. doi: 10.1016/0014-5793(87)80133-3.
Wingfield, P.T., Mattaliano, R.J., MacDonald, H.R., Craig, S., Clore, G.M., Gronenborn, A.M., & Schmeissner, U. (1987). Recombinant-derived interleukin-1 alpha stabilized against specific deamidation. Protein Eng, 1(5), 413-417.Oxford University Press (OUP). doi: 10.1093/protein/1.5.413.
Brünger, A.T., Clore, G.M., Gronenborn, A.M., & Karplus, M. (1986). Three-dimensional structure of proteins determined by molecular dynamics with interproton distance restraints: application to crambin. Proc Natl Acad Sci U S A, 83(11), 3801-3805.Proceedings of the National Academy of Sciences. doi: 10.1073/pnas.83.11.3801.
Clore, G.M., Brünger, A.T., Karplus, M., & Gronenborn, A.M. (1986). Application of molecular dynamics with interproton distance restraints to three-dimensional protein structure determination. A model study of crambin. J Mol Biol, 191(3), 523-551.Elsevier. doi: 10.1016/0022-2836(86)90146-4.
Clore, G.M., Gronenborn, A.M., Carlson, G., & Meyer, E.F. (1986). Stereochemistry of binding of the tetrapeptide acetyl-Pro-Ala-Pro-Tyr-NH2 to porcine pancreatic elastase. Combined use of two-dimensional transferred nuclear Overhauser enhancement measurements, restrained molecular dynamics, X-ray crystallography and molecular modelling. J Mol Biol, 190(2), 259-267.Elsevier. doi: 10.1016/0022-2836(86)90297-4.
Clore, G.M., Gronenborn, A.M., Greipel, J., & Maass, G. (1986). Conformation of the DNA undecamer 5'd(A-A-G-T-G-T-G-A-T-A-T) bound to the single-stranded DNA binding protein of Escherichia coli. A time-dependent transferred nuclear Overhauser enhancement study. J Mol Biol, 187(1), 119-124.Elsevier. doi: 10.1016/0022-2836(86)90411-0.
Clore, G.M., Martin, S.R., & Gronenborn, A.M. (1986). Solution structure of human growth hormone releasing factor. Combined use of circular dichroism and nuclear magnetic resonance spectroscopy. J Mol Biol, 191(3), 553-561.Elsevier. doi: 10.1016/0022-2836(86)90147-6.
Gronenborn, A.M., & Clore, G.M. (1986). Overproduction of the cyclic AMP receptor protein of Escherichia coli and expression of the engineered C-terminal DNA-binding domain. Biochem J, 236(3), 643-649.Portland Press. doi: 10.1042/bj2360643.
Gronenborn, A.M., Clore, G.M., Schmeissner, U., & Wingfield, P. (1986). A 1H-NMR study of human interleukin-1 beta. Sequence-specific assignment of aromatic residues using site-directed mutant proteins. Eur J Biochem, 161(1), 37-43.Wiley. doi: 10.1111/j.1432-1033.1986.tb10121.x.
MacDonald, H.R., Wingfield, P., Schmeissner, U., Shaw, A., Clore, G.M., & Gronenborn, A.M. (1986). Point mutations of human interleukin-1 with decreased receptor binding affinity. FEBS Lett, 209(2), 295-298.Wiley. doi: 10.1016/0014-5793(86)81130-9.
Minter, S.J., Clore, G.M., Gronenborn, A.M., & Davies, R.W. (1986). Cooperative DNA binding by lambda integration protein--a key component of specificity. Eur J Biochem, 161(3), 727-731.Wiley. doi: 10.1111/j.1432-1033.1986.tb10500.x.
Nilsson, L., Clore, G.M., Gronenborn, A.M., Brünger, A.T., & Karplus, M. (1986). Structure refinement of oligonucleotides by molecular dynamics with nuclear Overhauser effect interproton distance restraints: application to 5' d(C-G-T-A-C-G)2. J Mol Biol, 188(3), 455-475.Elsevier. doi: 10.1016/0022-2836(86)90168-3.
Zarbock, J., Clore, G.M., & Gronenborn, A.M. (1986). Nuclear magnetic resonance study of the globular domain of chicken histone H5: resonance assignment and secondary structure. Proc Natl Acad Sci U S A, 83(20), 7628-7632.Proceedings of the National Academy of Sciences. doi: 10.1073/pnas.83.20.7628.
Andrews, J., Clore, G.M., Davies, R.W., Gronenborn, A.M., Gronenborn, B., Kalderon, D., Papadopoulos, P.C., Schäfer, S., Sims, P.F., & Stancombe, R. (1985). Nucleotide sequence of the dihydrofolate reductase gene of methotrexate-resistant Lactobacillus casei. Gene, 35(1-2), 217-222.Elsevier. doi: 10.1016/0378-1119(85)90174-x.
Clore, G.M., & Gronenborn, A.M. (1985). The solution structure of a B-DNA undecamer comprising a portion of the specific target site for the cAMP receptor protein in the gal operon. Refinement on the basis of interproton distance data. EMBO J, 4(3), 829-835.Springer Nature. doi: 10.1002/j.1460-2075.1985.tb03705.x.
Clore, G.M., & Gronenborn, A.M. (1985). Probing the three-dimensional structures of DNA and RNA oligonucleotides in solution by nuclear Overhauser enhancement measurements. FEBS Lett, 179(2), 187-198.Wiley. doi: 10.1016/0014-5793(85)80516-0.
CLORE, G.M., & GRONENBORN, A.M. (1985). ASSESSMENT OF ERRORS INVOLVED IN THE DETERMINATION OF INTERPROTON DISTANCE RATIOS AND DISTANCES BY MEANS OF ONE-DIMENSIONAL AND 2-DIMENSIONAL NOE MEASUREMENTS. JOURNAL OF MAGNETIC RESONANCE, 61(1), 158-164.Elsevier. doi: 10.1016/0022-2364(85)90279-3.
Clore, G.M., Gronenborn, A.M., & McLaughlin, L.W. (1985). The structure of the double-stranded RNA pentamer 5'(CACAG) . 5'(CUGUG) determined by nuclear Overhauser enhancement measurements: interproton distance determination and structure refinement on the basis of X-ray coordinates. Eur J Biochem, 151(1), 153-165.Wiley. doi: 10.1111/j.1432-1033.1985.tb09080.x.
Clore, G.M., Gronenborn, A.M., Brünger, A.T., & Karplus, M. (1985). Solution conformation of a heptadecapeptide comprising the DNA binding helix F of the cyclic AMP receptor protein of Escherichia coli. Combined use of 1H nuclear magnetic resonance and restrained molecular dynamics. J Mol Biol, 186(2), 435-455.Elsevier. doi: 10.1016/0022-2836(85)90116-0.
Clore, G.M., Gronenborn, A.M., Moss, D.S., & Tickle, I.J. (1985). Refinement of the solution structure of the B DNA hexamer 5'd(C-G-T-A-C-G)2 on the basis of inter-proton distance data. J Mol Biol, 185(1), 219-226.Elsevier. doi: 10.1016/0022-2836(85)90195-0.
GRONENBORN, A.M., & CLORE, G.M. (1985). INVESTIGATION OF THE SOLUTION STRUCTURES OF SHORT NUCLEIC-ACID FRAGMENTS BY MEANS OF NUCLEAR OVERHAUSER ENHANCEMENT MEASUREMENTS. PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY, 17(C), 1-32.Elsevier. doi: 10.1016/0079-6565(85)80004-2.
Perutz, M.F., Gronenborn, A.M., Clore, G.M., Fogg, J.H., & Shih, D.T. (1985). The pKa values of two histidine residues in human haemoglobin, the Bohr effect, and the dipole moments of alpha-helices. J Mol Biol, 183(3), 491-498.Elsevier. doi: 10.1016/0022-2836(85)90016-6.
Perutz, M.F., Gronenborn, A.M., Clore, G.M., Shib, D.T., & Craescu, C.T. (1985). Comparison of histidine proton magnetic resonances of human carbonmonoxyhaemoglobin in different buffers. J Mol Biol, 186(2), 471-473.Elsevier. doi: 10.1016/0022-2836(85)90119-6.
Antonjuk, D.J., Birdsall, B., Cheung, H.T., Clore, G.M., Feeney, J., Gronenborn, A., Roberts, G.C., & Tran, T.Q. (1984). A 1H n.m.r. study of the role of the glutamate moiety in the binding of methotrexate to Lactobacillus casei dihydrofolate reductase. Br J Pharmacol, 81(2), 309-315.Wiley. doi: 10.1111/j.1476-5381.1984.tb10080.x.
Birdsall, B., Bevan, A.W., Pascual, C., Roberts, G.C., Feeney, J., Gronenborn, A., & Clore, G.M. (1984). Multinuclear NMR characterization of two coexisting conformational states of the Lactobacillus casei dihydrofolate reductase-trimethoprim-NADP+ complex. Biochemistry, 23(20), 4733-4742.American Chemical Society (ACS). doi: 10.1021/bi00315a032.
Chung, S.H., Johnson, M.S., & Gronenborn, A.M. (1984). L-cycloserine: a potent anticonvulsant. Epilepsia, 25(3), 353-362.Wiley. doi: 10.1111/j.1528-1157.1984.tb04200.x.
Clore, G.M., & Gronenborn, A.M. (1984). Interproton distance measurements in solution for a double-stranded DNA undecamer comprising a portion of the specific target site for the cycliC AMP receptor protein in the gal operon. A nuclear Overhauser enhancement study. FEBS Lett, 175(1), 117-123.Wiley. doi: 10.1016/0014-5793(84)80582-7.
Clore, G.M., & Gronenborn, A.M. (1984). Internal mobility in a double-stranded B DNA hexamer and undecamer. A time-dependent proton-proton nuclear Overhauser enhancement study. FEBS Lett, 172(2), 219-225.Wiley. doi: 10.1016/0014-5793(84)81129-1.
Clore, G.M., & Gronenborn, A.M. (1984). A nuclear-Overhauser-enhancement study of the solution structure of a double-stranded DNA undecamer comprising a portion of the specific target site for the cyclic-AMP-receptor protein in the gal operon. Sequential resonance assignment. Eur J Biochem, 141(1), 119-129.Wiley. doi: 10.1111/j.1432-1033.1984.tb08166.x.
Clore, G.M., & Gronenborn, A.M. (1984). An investigation into the solution structure of the single-stranded DNA undecamer 5'd AAGTGTGATAT by means of nuclear Overhauser enhancement measurements. Eur Biophys J, 11(2), 95-102.Springer Nature. doi: 10.1007/BF00276624.
Clore, G.M., Gronenborn, A.M., & McLaughlin, L.W. (1984). Structure of the ribotrinucleoside diphosphate codon UpUpC bound to tRNAPhe from yeast. A time-dependent transferred nuclear Overhauser enhancement study. J Mol Biol, 174(1), 163-173.Elsevier. doi: 10.1016/0022-2836(84)90370-x.
Clore, G.M., Gronenborn, A.M., Birdsall, B., Feeney, J., & Roberts, G.C. (1984). 19F-n.m.r. studies of 3',5'-difluoromethotrexate binding to Lactobacillus casei dihydrofolate reductase. Molecular motion and coenzyme-induced conformational changes. Biochem J, 217(3), 659-666.Portland Press. doi: 10.1042/bj2170659.
Clore, G.M., Gronenborn, A.M., Piper, E.A., McLaughlin, L.W., Graeser, E., & van Boom, J.H. (1984). The solution structure of a RNA pentadecamer comprising the anticodon loop and stem of yeast tRNAPhe. A 500 MHz 1H-n.m.r. study. Biochem J, 221(3), 737-751.Portland Press. doi: 10.1042/bj2210737.
Clore, G.M., Lauble, H., Frenkiel, T.A., & Gronenborn, A.M. (1984). A two-dimensional NMR study of the solution structure of a DNA dodecamer comprising the concensus sequence for the specific DNA-binding sites of the glucocorticoid receptor protein. Eur J Biochem, 145(3), 629-636.Wiley. doi: 10.1111/j.1432-1033.1984.tb08603.x.
Gronenborn, A.M., Clore, G.M., & Jeffery, J. (1984). An unusual conformation of NAD+ bound to sorbitol dehydrogenase? A time-dependent transferred nuclear Overhauser effect study. J Mol Biol, 172(4), 559-572.Elsevier. doi: 10.1016/s0022-2836(84)80023-6.
Gronenborn, A.M., Clore, G.M., & Kimber, B.J. (1984). An investigation into the solution structures of two self-complementary DNA oligomers, 5'-d(C-G-T-A-C-G) and 5'-d(A-C-G-C-G-C-G-T), by means of nuclear-Overhauser-enhancement measurements. Biochem J, 221(3), 723-736.Portland Press. doi: 10.1042/bj2210723.
Gronenborn, A.M., Clore, G.M., Brunori, M., Giardina, B., Falcioni, G., & Perutz, M.F. (1984). Stereochemistry of ATP and GTP bound to fish haemoglobins. A transferred nuclear overhauser enhancement, 31P-nuclear magnetic resonance, oxygen equilibrium and molecular modelling study. J Mol Biol, 178(3), 731-742.Elsevier. doi: 10.1016/0022-2836(84)90249-3.
Gronenborn, A.M., Clore, G.M., Brunori, M., Giardina, B., Falcioni, G., & Perutz, M.F. (1984). Stereochemistry of ATP and GTP bound to fish haemoglobins. A transferred nuclear overhauser enhancement, 31P-nuclear magnetic resonance, oxygen equilibrium and molecular modelling study. Journal of Molecular Biology, 178(3), 731-742. doi: 10.1016/0022-2836(84)90249-3.
Gronenborn, A.M., Clore, G.M., Jones, M.B., & Jiricny, J. (1984). A nuclear Overhauser enhancement study on the imino proton resonances of a DNA pentadecamer comprising the specific target site of the cyclic AMP receptor protein in the ara BAD operon. FEBS Lett, 165(2), 216-222.Wiley. doi: 10.1016/0014-5793(84)80172-6.
Gronenborn, A.M., Clore, G.M., McLaughlin, L.W., Graeser, E., Lorber, B., & Giegé, R. (1984). Yeast tRNAAsp: codon and wobble codon-anticodon interactions. A transferred nuclear Overhauser enhancement study. Eur J Biochem, 145(2), 359-364.Wiley. doi: 10.1111/j.1432-1033.1984.tb08562.x.
Gronenborn, A.M., Nermut, M.V., Eason, P., & Clore, G.M. (1984). Visualization of cAMP receptor protein-induced DNA kinking by electron microscopy. J Mol Biol, 179(4), 751-757.Elsevier. doi: 10.1016/0022-2836(84)90166-9.
Gronenborn, A.M., Papadopoulos, P., & Clore, G.M. (1984). Immunochemical evidence for extensive ligand-induced conformational changes in Lactobacillus casei dihydrofolate reductase. J Biol Chem, 259(2), 1082-1085.Elsevier. doi: 10.1016/s0021-9258(17)43568-x.
Clore, G.M., & Gronenborn, A.M. (1983). Sequence-dependent structural variations in two right-handed alternating pyrimidine-purine DNA oligomers in solution determined by nuclear Overhauser enhancement measurements. EMBO J, 2(12), 2109-2115.Springer Nature. doi: 10.1002/j.1460-2075.1983.tb01710.x.
CLORE, G.M., & GRONENBORN, A.M. (1983). THEORY OF THE TIME-DEPENDENT TRANSFERRED NUCLEAR OVERHAUSER EFFECT - APPLICATIONS TO STRUCTURAL-ANALYSIS OF LIGAND PROTEIN COMPLEXES IN SOLUTION. JOURNAL OF MAGNETIC RESONANCE, 53(3), 423-442.Elsevier. doi: 10.1016/0022-2364(83)90215-9.
Clore, G.M., Gronenborn, A.M., & Davies, R.W. (1983). Cooperative non-specific DNA binding of the N-terminal core of the cyclic AMP receptor protein of Escherichia coli and its modulation by cyclic AMP. FEBS Lett, 164(1), 57-62.Wiley. doi: 10.1016/0014-5793(83)80018-0.
CLORE, G.M., KIMBER, B.J., & GRONENBORN, A.M. (1983). THE 1-1 HARD PULSE - A SIMPLE AND EFFECTIVE METHOD OF WATER RESONANCE SUPPRESSION IN FT H-1-NMR. JOURNAL OF MAGNETIC RESONANCE, 54(1), 170-173.Elsevier. doi: 10.1016/0022-2364(83)90160-9.
Gronenborn, A.M., & Clore, G.M. (1983). Characterization of the DNA binding region recognized by dihydrofolate reductase from lactobacillus casei. J Biol Chem, 258(18), 11256-11259.Elsevier. doi: 10.1016/s0021-9258(17)44411-5.
Gronenborn, A.M., Clore, G.M., & Gronenborn, B. (1983). Protection against nuclease cleavage of pBR322 DNA by the cAMP receptor protein of Escherichia coli. J Mol Biol, 166(1), 93-98.Elsevier. doi: 10.1016/s0022-2836(83)80053-9.
Gronenborn, A.M., Kimber, B.J., Clore, G.M., & McLaughlin, L.W. (1983). A nuclear magnetic resonance study of the ribotrinucleoside diphophate UpUpC. Nucleic Acids Res, 11(16), 5691-5699.Oxford University Press (OUP). doi: 10.1093/nar/11.16.5691.
Martin, S.R., Gronenborn, A.M., & Clore, G.M. (1983). Specific DNA binding of the cyclic AMP receptor protein to a synthetic oligodeoxyribonucleotide. A circular dichroism study. FEBS Lett, 159(1-2), 102-106.Wiley. doi: 10.1016/0014-5793(83)80425-6.
Unger, B., Clore, G.M., Gronenborn, A.M., & Hillen, W. (1983). Specific DNA binding of the cAMP receptor protein within the lac operon stabilizes double-stranded DNA in the presence of cAMP. EMBO J, 2(2), 289-293.Springer Nature. doi: 10.1002/j.1460-2075.1983.tb01419.x.
Birdsall, B., Gronenborn, A., Hyde, E.I., Clore, G.M., Roberts, G.C., Feeney, J., & Burgen, A.S. (1982). Hydrogen-1, carbon-13, and phosphorus-31 nuclear magnetic resonance studies of the dihydrofolate reductase-nicotinamide adenine dinucleotide phosphate-folate complex: characterization of three coexisting conformational states. Biochemistry, 21(23), 5831-5838.American Chemical Society (ACS). doi: 10.1021/bi00266a017.
Clore, G.M., & Gronenborn, A.M. (1982). Determination of the conformations of cyclic nucleotides bound to the N-terminal core of the cyclic AMP receptor protein of Escherichia coli by 1H-NMR. FEBS Lett, 145(2), 197-202.Wiley. doi: 10.1016/0014-5793(82)80167-1.
Clore, G.M., & Gronenborn, A.M. (1982). Proton nuclear magnetic resonance study of the histidine residues of the Escherichia coli adenosine cyclic 3',5'-phosphate receptor protein. pH titration behavior, deuterium exchange, and partial assignments. Biochemistry, 21(17), 4048-4053.American Chemical Society (ACS). doi: 10.1021/bi00260a021.
CLORE, G.M., & GRONENBORN, A.M. (1982). KINETIC AND STRUCTURAL STUDIES ON THE INTERMEDIATES FORMED IN THE REACTIONS OF 5'-ADENOSINE MONOPHOSPHATE AND 5'-GUANOSINE MONOPHOSPHATE WITH CIS-DICHLORODIAMMINEPLATINUM(II) USING H-1 AND PT-195 MAGNETIC-RESONANCE SPECTROSCOPY. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 104(5), 1369-1375.American Chemical Society (ACS). doi: 10.1021/ja00369a037.
CLORE, G.M., & GRONENBORN, A.M. (1982). THEORY AND APPLICATIONS OF THE TRANSFERRED NUCLEAR OVERHAUSER EFFECT TO THE STUDY OF THE CONFORMATIONS OF SMALL LIGANDS BOUND TO PROTEINS. JOURNAL OF MAGNETIC RESONANCE, 48(3), 402-417.Elsevier. doi: 10.1016/0022-2364(82)90073-7.
Clore, G.M., Gronenborn, A.M., & Davies, R.W. (1982). Theoretical aspects of specific and non-specific equilibrium binding of proteins to DNA as studied by the nitrocellulose filter binding assay. Co-operative and non-co-operative binding to a one-dimensional lattice. J Mol Biol, 155(4), 447-466.Elsevier. doi: 10.1016/0022-2836(82)90481-8.
Clore, G.M., Gronenborn, A.M., Mitchinson, C., & Green, N.M. (1982). 1H-NMR studies on nucleotide binding to the sarcoplasmic reticulum Ca2+ ATPase. Determination of the conformations of bound nucleotides by the measurement of proton-proton transferred nuclear Overhauser enhancements. Eur J Biochem, 128(1), 113-117.Wiley. doi: 10.1111/j.1432-1033.1982.tb06940.x.
Gronenborn, A.M., & Clore, G.M. (1982). Proton nuclear magnetic resonance studies on cyclic nucleotide binding to the Escherichia coli adenosine cyclic 3',5'-phosphate receptor protein. Biochemistry, 21(17), 4040-4048.American Chemical Society (ACS). doi: 10.1021/bi00260a020.
Gronenborn, A.M., & Clore, G.M. (1982). Conformation of NAD+ bound to yeast and horse liver alcohol dehydrogenase in solution. The use of the proton-proton transferred nuclear Overhauser enhancement. J Mol Biol, 157(1), 155-160.Elsevier. doi: 10.1016/0022-2836(82)90518-6.
GRONENBORN, A.M., & ROTH, K. (1982). NMR-SPECTROSCOPY INVIVO. CHEMIE IN UNSERER ZEIT, 16(1), 1-31.Wiley. doi: 10.1002/ciuz.19820160103.
ROTH, K., & GRONENBORN, A.M. (1982). NMR TOMOGRAPHY. CHEMIE IN UNSERER ZEIT, 16(2), 35-45.Wiley. doi: 10.1002/ciuz.19820160203.
TAKAHASHI, M., GRONENBORN, A.M., CLORE, G.M., BLAZY, B., & BAUDRAS, A. (1982). DNA-BINDING OF CAMP RECEPTOR PROTEIN AND ITS N-TERMINAL CORE STABILIZES THE DOUBLE HELIX AND IS MODULATED BY THE ALLOSTERIC EFFECTOR CAMP. FEBS LETTERS, 139(1), 37-40.Wiley. doi: 10.1016/0014-5793(82)80481-X.
Birdsall, B., Gronenborn, A., Clore, G.M., Roberts, G.C., Feeney, J., & Burgen, A.S. (1981). 13C NMR evidence for three slowly interconverting conformations of the dihydrofolate reductase-NADP+-folate complex. Biochem Biophys Res Commun, 101(4), 1139-1144.Elsevier. doi: 10.1016/0006-291x(81)91566-7.
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Gronenborn, A.M., Clore, G.M., & Davies, R.W. (1981). Modulation of specific binding of Lactobacillus casei dihydrofolate reductase to DNA by folinic acid. FEBS Lett, 133(1), 92-94.Wiley. doi: 10.1016/0014-5793(81)80478-4.
Gronenborn, A.M., Clore, G.M., Blazy, B., & Baudras, A. (1981). Conformational selection of syn-cAMP upon binding to the cAMP: receptor protein. FEBS Lett, 136(1), 160-164.Wiley. doi: 10.1016/0014-5793(81)81237-9.
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