| Year |
Citation |
Score |
| 2023 |
Sarkar S, Zadrozny KK, Zadorozhnyi R, Russell RW, Quinn CM, Kleinpeter A, Ablan S, Meshkin H, Perilla JR, Freed EO, Ganser-Pornillos BK, Pornillos O, Gronenborn AM, Polenova T. Structural basis of HIV-1 maturation inhibitor binding and activity. Nature Communications. 14: 1237. PMID 36871077 DOI: 10.1038/s41467-023-36569-y |
0.653 |
|
| 2022 |
Sarkar S, Runge B, Russell RW, Movellan KT, Calero D, Zeinalilathori S, Quinn CM, Lu M, Calero G, Gronenborn AM, Polenova T. Atomic-Resolution Structure of SARS-CoV-2 Nucleocapsid Protein N-Terminal Domain. Journal of the American Chemical Society. 144: 10543-10555. PMID 35638584 DOI: 10.1021/jacs.2c03320 |
0.31 |
|
| 2021 |
Byeon IL, Calero G, Wu Y, Byeon CH, Jung J, DeLucia M, Zhou X, Weiss S, Ahn J, Hao C, Skowronski J, Gronenborn AM. Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A. Nature Communications. 12: 6864. PMID 34824204 DOI: 10.1038/s41467-021-27009-w |
0.346 |
|
| 2021 |
Perilla JR, Hadden-Perilla JA, Gronenborn AM, Polenova T. Integrative structural biology of HIV-1 capsid protein assemblies: combining experiment and computation. Current Opinion in Virology. 48: 57-64. PMID 33901736 DOI: 10.1016/j.coviro.2021.03.005 |
0.63 |
|
| 2020 |
Nestor G, Ruda A, Anderson T, Oscarson S, Widmalm G, Gronenborn AM. A detailed picture of a protein-carbohydrate hydrogen-bonding network revealed by NMR and MD simulations. Glycobiology. PMID 32902635 DOI: 10.1093/Glycob/Cwaa081 |
0.354 |
|
| 2020 |
Lu M, Russell RW, Bryer AJ, Quinn CM, Hou G, Zhang H, Schwieters CD, Perilla JR, Gronenborn AM, Polenova T. Atomic-resolution structure of HIV-1 capsid tubes by magic-angle spinning NMR. Nature Structural & Molecular Biology. 27: 863-869. PMID 32901160 DOI: 10.1038/S41594-020-0489-2 |
0.691 |
|
| 2020 |
Kraus J, Gupta R, Lu M, Gronenborn A, Akke M, Polenova T. Accurate Backbone 13C and 15N Chemical Shift Tensors in Galectin-3 by MAS NMR and QM/MM: Details of Structure and Environment Matter. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 32363727 DOI: 10.1002/Cphc.202000249 |
0.41 |
|
| 2020 |
Lu M, Polenova TE, Gronenborn AM. 19F NMR Studies of Cyclophilin a and its Interaction with HIV-1 Capsid Biophysical Journal. 118. DOI: 10.1016/J.Bpj.2019.11.2776 |
0.311 |
|
| 2020 |
Guseman AJ, Whitley MJ, Gonzalez J, Gronenborn AM. Deamidation of yD-Crystallin - Effects on Structure and Interaction Properties Biophysical Journal. 118: 336a. DOI: 10.1016/J.Bpj.2019.11.1875 |
0.303 |
|
| 2019 |
Hassan A, Quinn CM, Struppe J, Sergeyev IV, Zhang C, Guo C, Runge B, Theint T, Dao HH, Jaroniec CP, Berbon M, Lends A, Habenstein B, Loquet A, Kuemmerle R, ... ... Gronenborn AM, et al. Sensitivity boosts by the CPMAS CryoProbe for challenging biological assemblies. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 311: 106680. PMID 31951864 DOI: 10.1016/J.Jmr.2019.106680 |
0.342 |
|
| 2019 |
Struppe J, Quinn CM, Sarkar S, Gronenborn AM, Polenova T. Ultrafast H MAS NMR Crystallography For Natural Abundance Pharmaceutical Compounds. Molecular Pharmaceutics. PMID 31891271 DOI: 10.1021/Acs.Molpharmaceut.9B01157 |
0.327 |
|
| 2019 |
Fritz M, Kraus J, Quinn CM, Yap GPA, Struppe J, Sergeyev IV, Gronenborn AM, Polenova T. Measurement of Accurate Interfluorine Distances in Crystalline Organic Solids: A High-Spinning MAS NMR Approach. The Journal of Physical Chemistry. B. PMID 31682453 DOI: 10.1021/Acs.Jpcb.9B08919 |
0.341 |
|
| 2019 |
Carlon A, Gigli L, Ravera E, Parigi G, Gronenborn AM, Luchinat C. Assessing Structural Preferences of Unstructured Protein Regions by NMR. Biophysical Journal. 117: 1948-1953. PMID 31676138 DOI: 10.1016/J.Bpj.2019.10.008 |
0.42 |
|
| 2019 |
Gronenborn AM. Integrated multidisciplinarity in the natural sciences. The Journal of Biological Chemistry. PMID 31636121 DOI: 10.1074/Jbc.Aw119.008142 |
0.316 |
|
| 2019 |
Byeon IL, Jung J, Byeon CH, DeLucia M, Ahn J, Gronenborn AM. Complete H, C, N resonance assignments and secondary structure of the Vpr binding region of hHR23A (residues 223-363). Biomolecular Nmr Assignments. PMID 31463759 DOI: 10.1007/S12104-019-09913-X |
0.431 |
|
| 2019 |
Gronenborn AM. Integrated BioNMR - "getting by with a little help from my friends". Journal of Magnetic Resonance (San Diego, Calif. : 1997). 306: 192-194. PMID 31320228 DOI: 10.1016/J.Jmr.2019.07.040 |
0.335 |
|
| 2019 |
Gupta R, Zhang H, Lu M, Hou G, Caporini M, Rosay M, Maas W, Struppe J, Ahn J, Byeon IL, Oschkinat H, Jaudzems K, Barbet-Massin E, Emsley L, Pintacuda G, ... ... Gronenborn AM, et al. Dynamic Nuclear Polarization Magic Angle Spinning NMR Combined with MD Simulations Permits Detection of Order and Disorder in Viral Assemblies. The Journal of Physical Chemistry. B. PMID 31125232 DOI: 10.1021/Acs.Jpcb.9B02293 |
0.403 |
|
| 2019 |
Guseman AJ, Gronenborn AM. Isomerization as the secret Achilles' heel of long-lived proteins. The Journal of Biological Chemistry. 294: 7556-7557. PMID 31076522 DOI: 10.1074/Jbc.H119.008716 |
0.353 |
|
| 2019 |
Lu M, Wang M, Sergeyev IV, Quinn CM, Struppe J, Rosay M, Maas W, Gronenborn AM, Polenova T. F Dynamic Nuclear Polarization at Fast Magic Angle Spinning for NMR of HIV-1 Capsid Protein Assemblies. Journal of the American Chemical Society. PMID 30871317 DOI: 10.1021/Jacs.8B09216 |
0.387 |
|
| 2019 |
Russell RW, Fritz MP, Kraus J, Quinn CM, Polenova T, Gronenborn AM. Accuracy and precision of protein structures determined by magic angle spinning NMR spectroscopy: for some 'with a little help from a friend'. Journal of Biomolecular Nmr. PMID 30847635 DOI: 10.1007/S10858-019-00233-9 |
0.456 |
|
| 2019 |
Gronenborn AM. Harnessing the Combined Power of SAXS and NMR. Advances in Experimental Medicine and Biology. 1105: 171-180. PMID 30617829 DOI: 10.1007/978-981-13-2200-6_11 |
0.372 |
|
| 2019 |
Russell RW, Fritz M, Kraus J, Quinn CM, Gronenborn AM, Polenova T. Computational Assessment of Distance Restraint Requirements for Accurate Protein Structure Determination by MAS NMR Biophysical Journal. 116: 160a. DOI: 10.1016/J.Bpj.2018.11.889 |
0.38 |
|
| 2019 |
Lu M, Wang M, Struppe J, Maas W, Gronenborn A, Polenova T. Towards Atomic-Resolution Structure Determination of HIV-1 Capsid Assemblies using Magic Angle Spinning NMR Biophysical Journal. 116: 310a. DOI: 10.1016/J.Bpj.2018.11.1682 |
0.352 |
|
| 2018 |
Krzysiak TC, Thomas L, Choi YJ, Auclair S, Qian Y, Luan S, Krasnow SM, Thomas LL, Koharudin LMI, Benos PV, Marks DL, Gronenborn AM, Thomas G. An Insulin-Responsive Sensor in the SIRT1 Disordered Region Binds DBC1 and PACS-2 to Control Enzyme Activity. Molecular Cell. PMID 30415949 DOI: 10.1016/J.Molcel.2018.10.007 |
0.309 |
|
| 2018 |
Quinn CM, Wang M, Fritz MP, Runge B, Ahn J, Xu C, Perilla JR, Gronenborn AM, Polenova T. Dynamic regulation of HIV-1 capsid interaction with the restriction factor TRIM5α identified by magic-angle spinning NMR and molecular dynamics simulations. Proceedings of the National Academy of Sciences of the United States of America. PMID 30333189 DOI: 10.1073/Pnas.1800796115 |
0.678 |
|
| 2018 |
Wang M, Lu M, Fritz M, Quinn C, Byeon IJ, Byeon CH, Struppe J, Maas W, Gronenborn A, Polenova T. Fast Magic Angle Spinning ¹⁹F NMR of HIV-1 Capsid Protein Assemblies. Angewandte Chemie (International Ed. in English). PMID 30225969 DOI: 10.1002/Anie.201809060 |
0.382 |
|
| 2018 |
Paramasivam S, Gronenborn AM, Polenova T. Backbone amideN chemical shift tensors report on hydrogen bonding interactions in proteins: A magic angle spinning NMR study. Solid State Nuclear Magnetic Resonance. 92: 1-6. PMID 29579703 DOI: 10.1016/J.Ssnmr.2018.03.002 |
0.368 |
|
| 2018 |
Fritz M, Quinn CM, Wang M, Hou G, Lu X, Koharudin LMI, Struppe J, Case DA, Polenova T, Gronenborn AM. Determination of accurate backbone chemical shift tensors in microcrystalline proteins by integrating MAS NMR and QM/MM. Physical Chemistry Chemical Physics : Pccp. PMID 29577158 DOI: 10.1039/C8Cp00647D |
0.377 |
|
| 2018 |
Kraus J, Gupta R, Lu M, Yehl JB, Case DA, Gronenborn AM, Akke M, Polenova T. Chemical Shifts of the Carbohydrate Binding Domain of Galectin-3 from Magic Angle Spinning NMR and Hybrid Quantum Mechanics/Molecular Mechanics Calculations. The Journal of Physical Chemistry. B. PMID 29498857 DOI: 10.1021/Acs.Jpcb.8B00853 |
0.4 |
|
| 2018 |
Debiec KT, Whitley MJ, Koharudin LMI, Chong LT, Gronenborn AM. Integrating NMR, SAXS, and Atomistic Simulations: Structure and Dynamics of a Two-Domain Protein. Biophysical Journal. 114: 839-855. PMID 29490245 DOI: 10.1016/J.Bpj.2018.01.001 |
0.4 |
|
| 2017 |
Nestor G, Anderson T, Oscarson S, Gronenborn AM. Direct Observation of Carbohydrate Hydroxyl Protons in Hydrogen Bonds with a Protein. Journal of the American Chemical Society. PMID 29227646 DOI: 10.1021/Jacs.7B10595 |
0.347 |
|
| 2017 |
Wang M, Quinn CM, Perilla JR, Zhang H, Shirra R, Hou G, Byeon IJ, Suiter CL, Ablan S, Urano E, Nitz TJ, Aiken C, Freed EO, Zhang P, Schulten K, ... Gronenborn AM, et al. Quenching protein dynamics interferes with HIV capsid maturation. Nature Communications. 8: 1779. PMID 29176596 DOI: 10.1038/S41467-017-01856-Y |
0.626 |
|
| 2017 |
Wang M, Quinn CM, Perilla JR, Zhang H, Shirra R, Hou G, Byeon IJ, Suiter CL, Ablan S, Urano E, Nitz TJ, Aiken C, Freed EO, Zhang P, Schulten K, ... Gronenborn AM, et al. Quenching protein dynamics interferes with HIV capsid maturation. Nature Communications. 8: 1779. PMID 29176596 DOI: 10.1038/S41467-017-01856-Y |
0.626 |
|
| 2017 |
Struppe J, Quinn CM, Lu M, Wang M, Hou G, Lu X, Kraus J, Andreas LB, Stanek J, Lalli D, Lesage A, Pintacuda G, Maas W, Gronenborn AM, Polenova T. Expanding the horizons for structural analysis of fully protonated protein assemblies by NMR spectroscopy at MAS frequencies above 100 kHz. Solid State Nuclear Magnetic Resonance. PMID 28732673 DOI: 10.1016/J.Ssnmr.2017.07.001 |
0.42 |
|
| 2017 |
Boatz JC, Whitley MJ, Li M, Gronenborn AM, van der Wel PCA. Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH. Nature Communications. 8: 15137. PMID 28474685 DOI: 10.1038/Ncomms15137 |
0.314 |
|
| 2017 |
Nestor G, Anderson T, Oscarson S, Gronenborn AM. Exploiting Uniformly (13)C-Labeled Carbohydrates for Probing Carbohydrate-Protein Interactions by NMR Spectroscopy. Journal of the American Chemical Society. PMID 28406013 DOI: 10.1021/Jacs.7B01929 |
0.402 |
|
| 2017 |
Whitley MJ, Xi Z, Bartko JC, Jensen MR, Blackledge M, Gronenborn AM. A Combined NMR and SAXS Analysis of the Partially Folded Cataract-Associated V75D γD-Crystallin. Biophysical Journal. 112: 1135-1146. PMID 28355541 DOI: 10.1016/J.Bpj.2017.02.010 |
0.408 |
|
| 2017 |
Xi Z, Whitley MJ, Gronenborn AM. Human βB2-Crystallin Forms a Face-en-Face Dimer in Solution: An Integrated NMR and SAXS Study. Structure (London, England : 1993). PMID 28238532 DOI: 10.1016/J.Str.2017.02.001 |
0.369 |
|
| 2017 |
Perilla JR, Zhao G, Lu M, Ning J, Hou G, Byeon IL, Gronenborn AM, Polenova T, Zhang P. CryoEM Structure Refinement by Integrating NMR Chemical Shifts with Molecular Dynamics Simulations. The Journal of Physical Chemistry. B. PMID 28181439 DOI: 10.1021/Acs.Jpcb.6B13105 |
0.696 |
|
| 2017 |
Slack RL, Sharaf NG, Gronenborn AM, Ishima R. Structural Characteristics of the RNAse H Domain in HIV-1 Reverse Transcriptase Biophysical Journal. 112: 487a. DOI: 10.1016/J.Bpj.2016.11.2635 |
0.344 |
|
| 2016 |
Fritz M, Quinn CM, Wang M, Hou G, Lu X, Koharudin LM, Polenova T, Gronenborn AM. Toward Closing the Gap: Quantum Mechanical Calculations and Experimentally Measured Chemical Shifts of a Microcrystalline Lectin. The Journal of Physical Chemistry. B. PMID 28001418 DOI: 10.1021/Acs.Jpcb.6B09479 |
0.381 |
|
| 2016 |
Sharaf NG, Brereton AE, Byeon IL, Andrew Karplus P, Gronenborn AM. NMR structure of the HIV-1 reverse transcriptase thumb subdomain. Journal of Biomolecular Nmr. PMID 27858311 DOI: 10.1007/S10858-016-0077-2 |
0.431 |
|
| 2016 |
Zhang H, Hou G, Lu M, Ahn J, Byeon IL, Langmead CJ, Perilla JR, Hung I, Gor'kov PL, Gan Z, Brey WW, Case DA, Schulten K, Gronenborn AM, Polenova T. HIV-1 Capsid Function is Regulated by Dynamics: Quantitative Atomic-Resolution Insights by Integrating Magic-Angle-Spinning NMR, QM/MM, and MD. Journal of the American Chemical Society. PMID 27701859 DOI: 10.1021/Jacs.6B08744 |
0.674 |
|
| 2016 |
Wu Y, Zhou X, Barnes CO, DeLucia M, Cohen AE, Gronenborn AM, Ahn J, Calero G. The DDB1-DCAF1-Vpr-UNG2 crystal structure reveals how HIV-1 Vpr steers human UNG2 toward destruction. Nature Structural & Molecular Biology. PMID 27571178 DOI: 10.1038/Nsmb.3284 |
0.426 |
|
| 2016 |
Matei E, Basu R, Furey W, Shi J, Calnan C, Aiken C, Gronenborn AM. Structure and Glycan Binding of a New Cyanovirin-N Homolog. The Journal of Biological Chemistry. PMID 27402833 DOI: 10.1074/Jbc.M116.740415 |
0.416 |
|
| 2016 |
Byeon IL, Byeon CH, Wu T, Mitra M, Singer D, Levin JG, Gronenborn AM. NMR Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity. Biochemistry. PMID 27163633 DOI: 10.1021/Acs.Biochem.6B00382 |
0.401 |
|
| 2016 |
Sharaf NG, Ishima R, Gronenborn AM. Conformational plasticity of the NNRTI-binding pocket in HIV-1 reverse transcriptase - A fluorine NMR study. Biochemistry. PMID 27163463 DOI: 10.1021/Acs.Biochem.6B00113 |
0.359 |
|
| 2016 |
Perilla JR, Gronenborn AM. Molecular Architecture of the Retroviral Capsid. Trends in Biochemical Sciences. PMID 27039020 DOI: 10.1016/J.Tibs.2016.02.009 |
0.634 |
|
| 2016 |
Krzysiak TC, Chen BB, Lear T, Mallampalli RK, Gronenborn AM. Crystal Structure and Interaction Studies of the Human FBxo3 ApaG Domain. The Febs Journal. PMID 27010866 DOI: 10.1111/Febs.13721 |
0.384 |
|
| 2016 |
Liu C, Perilla JR, Ning J, Lu M, Hou G, Ramalho R, Himes BA, Zhao G, Bedwell GJ, Byeon IJ, Ahn J, Gronenborn AM, Prevelige PE, Rousso I, Aiken C, et al. Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site. Nature Communications. 7: 10714. PMID 26940118 DOI: 10.1038/Ncomms10714 |
0.676 |
|
| 2016 |
Byeon I, Byeon C, Gronenborn A. NMR Structure of the C-Terminal Domain of human APOBEC3B Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2Nbq/Pdb |
0.369 |
|
| 2016 |
Boatz JC, Whitley MJ, Hoop CL, Zeng X, Yates N, Gronenborn AM, van der Wel PC. An Investigation of the Atomic Structure of Cataract-Forming Mutant Gamma-D-Crystallin Aggregates Formed under Distinct Environmental Conditions Biophysical Journal. 110: 27a. DOI: 10.1016/J.Bpj.2015.11.210 |
0.346 |
|
| 2015 |
Gupta R, Lu M, Hou G, Caporini MA, Rosay M, Maas WE, Struppe JO, Suiter CL, Ahn J, Byeon IL, Franks WT, Orwick-Rydmark M, Bertarello A, Oschkinat H, Lesage A, ... ... Gronenborn AM, et al. Dynamic Nuclear Polarization Enhanced MAS NMR for Structural Analysis of HIV-1 Protein Assemblies. The Journal of Physical Chemistry. B. PMID 26709853 DOI: 10.1021/Acs.Jpcb.5B12134 |
0.388 |
|
| 2015 |
Sharaf NG, Gronenborn AM. (19)F-Modified Proteins and (19)F-Containing Ligands as Tools in Solution NMR Studies of Protein Interactions. Methods in Enzymology. 565: 67-95. PMID 26577728 DOI: 10.1016/Bs.Mie.2015.05.014 |
0.304 |
|
| 2015 |
Lu M, Hou G, Zhang H, Suiter CL, Ahn J, Byeon IL, Perilla JR, Langmead CJ, Hung I, Gor'kov PL, Gan Z, Brey W, Aiken C, Zhang P, Schulten K, ... Gronenborn AM, et al. Dynamic allostery governs cyclophilin A-HIV capsid interplay. Proceedings of the National Academy of Sciences of the United States of America. PMID 26553990 DOI: 10.1073/Pnas.1516920112 |
0.666 |
|
| 2015 |
Koharudin LM, Debiec KT, Gronenborn AM. Structural Insight into Fungal Cell Wall Recognition by a CVNH Protein with a Single LysM Domain. Structure (London, England : 1993). 23: 2143-54. PMID 26455798 DOI: 10.1016/J.Str.2015.07.023 |
0.407 |
|
| 2015 |
Wu Y, Koharudin LM, Mehrens J, DeLucia M, Byeon CH, Byeon IJ, Calero G, Ahn J, Gronenborn AM. 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. The Journal of Biological Chemistry. 290: 17935-45. PMID 26045556 DOI: 10.1074/Jbc.M115.665513 |
0.397 |
|
| 2015 |
Carneiro MG, Koharudin LM, Ban D, Sabo TM, Trigo-Mourino P, Mazur A, Griesinger C, Gronenborn AM, Lee D. Sampling of Glycan-Bound Conformers by the Anti-HIV Lectin Oscillatoria agardhii agglutinin in the Absence of Sugar. Angewandte Chemie (International Ed. in English). 54: 6462-5. PMID 25873445 DOI: 10.1002/Anie.201500213 |
0.391 |
|
| 2015 |
Carneiro MG, Koharudin LM, Griesinger C, Gronenborn AM, Lee D. (1)H, (13)C and (15)N resonance assignment of the anti-HIV lectin from Oscillatoria agardhii. Biomolecular Nmr Assignments. PMID 25680849 DOI: 10.1007/S12104-015-9600-8 |
0.355 |
|
| 2015 |
Mitra M, Singer D, Mano Y, Hritz J, Nam G, Gorelick RJ, Byeon IJ, Gronenborn AM, Iwatani Y, Levin JG. Sequence and structural determinants of human APOBEC3H deaminase and anti-HIV-1 activities. Retrovirology. 12: 3. PMID 25614027 DOI: 10.1186/S12977-014-0130-8 |
0.701 |
|
| 2015 |
Mitra M, Singer D, Mano Y, Hritz J, Nam G, Gorelick RJ, Byeon IJL, Gronenborn AM, Iwatani Y, Levin JG. Sequence and structural determinants of human APOBEC3H deaminase and anti-HIV-1 activities Retrovirology. 12. DOI: 10.1186/s12977-014-0130-8 |
0.655 |
|
| 2015 |
Zhang P, Liu C, Perilla JR, Byeon I, Ning J, Ahn J, Aiken C, Gronenborn AM, Polenova T, Schulten K. Cyclophilin a Stabilizes the Mature HIV-1 Capsid through a Novel Non-Canonical Binding Site Biophysical Journal. 108: 190a. DOI: 10.1016/J.Bpj.2014.11.1051 |
0.697 |
|
| 2014 |
Hritz J, Byeon IJ, Krzysiak T, Martinez A, Sklenar V, Gronenborn AM. Dissection of binding between a phosphorylated tyrosine hydroxylase peptide and 14-3-3?: A complex story elucidated by NMR. Biophysical Journal. 107: 2185-94. PMID 25418103 DOI: 10.1016/J.Bpj.2014.08.039 |
0.678 |
|
| 2014 |
Koharudin LMI, Wu Y, DeLucia M, Mehrens J, Gronenborn AM, Ahn J. Structural basis of allosteric activation of sterile α motif and histidine-aspartate domain-containing protein 1 (SAMHD1) by nucleoside triphosphates Journal of Biological Chemistry. 289: 32617-32627. PMID 25288794 DOI: 10.1074/Jbc.M114.591958 |
0.42 |
|
| 2014 |
Koharudin LM, Gronenborn AM. Antiviral lectins as potential HIV microbicides Current Opinion in Virology. 7: 95-100. PMID 25010042 DOI: 10.1016/J.Coviro.2014.05.006 |
0.345 |
|
| 2014 |
Férir G, Huskens D, Noppen S, Koharudin LMI, Gronenborn AM, Schols D. Broad anti-HIV activity of the Oscillatoria agardhii agglutinin homologue lectin family The Journal of Antimicrobial Chemotherapy. 69: 2746-2758. PMID 24970741 DOI: 10.1093/Jac/Dku220 |
0.342 |
|
| 2014 |
Sharaf NG, Poliner E, Slack RL, Christen MT, Byeon IJ, Parniak MA, Gronenborn AM, Ishima R. The p66 immature precursor of HIV-1 reverse transcriptase. Proteins. 82: 2343-52. PMID 24771554 DOI: 10.1002/Prot.24594 |
0.367 |
|
| 2014 |
Jung J, Byeon IJL, De Lucia M, Koharudin LMI, Ahn J, Gronenborn AM. 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 Journal of Biological Chemistry. 289: 2577-2588. PMID 24318982 DOI: 10.1074/Jbc.M113.534453 |
0.414 |
|
| 2014 |
Mitra M, Hercík K, Byeon IJL, Ahn J, Hill S, Hinchee-Rodriguez K, Singer D, Byeon CH, Charlton LM, Nam G, Heidecker G, Gronenborn AM, Levin JG. Structural determinants of human APOBEC3A enzymatic and nucleic acid binding properties Nucleic Acids Research. 42: 1095-1110. PMID 24163103 DOI: 10.1093/Nar/Gkt945 |
0.38 |
|
| 2014 |
Ji X, Wu Y, Yan J, Mehrens J, DeLucia M, Hao C, Gronenborn A, Skowronski J, Anh J, Xiong Y. Kill HIV by Starvation–Mechanism of Allosteric Activation of SAMHD1 Acta Crystallographica Section a Foundations and Advances. 70: C121-C121. DOI: 10.1107/S2053273314098787 |
0.359 |
|
| 2013 |
Han Y, Hou G, Suiter CL, Ahn J, Byeon IJ, Lipton AS, Burton S, Hung I, Gor'kov PL, Gan Z, Brey W, Rice D, Gronenborn AM, Polenova T. Magic angle spinning NMR reveals sequence-dependent structural plasticity, dynamics, and the spacer peptide 1 conformation in HIV-1 capsid protein assemblies. Journal of the American Chemical Society. 135: 17793-803. PMID 24164646 DOI: 10.1021/Ja406907H |
0.362 |
|
| 2013 |
Ji X, Wu Y, Yan J, Mehrens J, Yang H, DeLucia M, Hao C, Gronenborn AM, Skowronski J, Ahn J, Xiong Y. Mechanism of allosteric activation of SAMHD1 by dGTP. Nature Structural & Molecular Biology. 20: 1304-9. PMID 24141705 DOI: 10.1038/Nsmb.2692 |
0.398 |
|
| 2013 |
Zhao G, Perilla JR, Yufenyuy EL, Meng X, Chen B, Ning J, Ahn J, Gronenborn AM, Schulten K, Aiken C, Zhang P. Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics. Nature. 497: 643-6. PMID 23719463 DOI: 10.1038/Nature12162 |
0.696 |
|
| 2013 |
Byeon IJL, Ahn J, Mitra M, Byeon CH, Hercík K, Hritz J, Charlton LM, Levin JG, Gronenborn AM. NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity Nature Communications. 4. PMID 23695684 DOI: 10.1038/Ncomms2883 |
0.713 |
|
| 2013 |
Ji F, Koharudin LMI, Jung J, Gronenborn AM. Crystal structure of the cataract-causing P23T γD-crystallin mutant Proteins: Structure, Function and Bioinformatics. 81: 1493-1498. PMID 23670788 DOI: 10.1002/Prot.24321 |
0.338 |
|
| 2013 |
Koharudin LMI, Liu L, Gronenborn AM. Different 3D domain-swapped oligomeric cyanovirin-N structures suggest trapped folding intermediates Proceedings of the National Academy of Sciences of the United States of America. 110: 7702-7707. PMID 23610431 DOI: 10.1073/Pnas.1300327110 |
0.473 |
|
| 2013 |
Whitley MJ, Furey W, Kollipara S, Gronenborn AM. Burkholderia oklahomensis agglutinin is a canonical two-domain OAA-family lectin: Structures, carbohydrate binding and anti-HIV activity Febs Journal. 280: 2056-2067. PMID 23480609 DOI: 10.1111/Febs.12229 |
0.403 |
|
| 2013 |
Matei E, André S, Glinschert A, Infantino AS, Oscarson S, Gabius HJ, Gronenborn AM. Fluorinated carbohydrates as lectin ligands: Dissecting glycan-cyanovirin interactions by using 19F NMR spectroscopy Chemistry - a European Journal. 19: 5364-5374. PMID 23447543 DOI: 10.1002/Chem.201204070 |
0.372 |
|
| 2013 |
Yan J, Kaur S, DeLucia M, Hao C, Mehrens J, Wang C, Golczak M, Palczewski K, Gronenborn AM, Ahn J, Skowronski J. Tetramerization of SAMHD1 is required for biological activity and inhibition of HIV infection. The Journal of Biological Chemistry. 288: 10406-17. PMID 23426366 DOI: 10.1074/Jbc.M112.443796 |
0.329 |
|
| 2013 |
Koharudin LM, Boelens R, Kaptein R, Gronenborn AM. A NMR guided approach for CsrA-RNA crystallization. Journal of Biomolecular Nmr. 56: 31-9. PMID 23359257 DOI: 10.1007/S10858-013-9712-3 |
0.356 |
|
| 2013 |
Ji F, Jungs J, Koharudin LMI, Gronenborn AM. The human W42R γD-crystallin mutant structure provides a link between congenital and age-related cataracts Journal of Biological Chemistry. 288: 99-109. PMID 23124202 DOI: 10.1074/Jbc.M112.416354 |
0.365 |
|
| 2013 |
Koharudin LM, Gronenborn AM. Sweet entanglements-protein: Glycan interactions in two HIV-inactivating lectin families. Biopolymers. 99: 196-202. PMID 23023834 DOI: 10.1002/Bip.22106 |
0.386 |
|
| 2012 |
Yang H, Ji X, Zhao G, Ning J, Zhao Q, Aiken C, Gronenborn AM, Zhang P, Xiong Y. Structural insight into HIV-1 capsid recognition by rhesus TRIM5α Proceedings of the National Academy of Sciences of the United States of America. 109: 18372-18377. PMID 23091002 DOI: 10.1073/Pnas.1210903109 |
0.424 |
|
| 2012 |
Hou G, Byeon IJ, Ahn J, Gronenborn AM, Polenova T. Recoupling of chemical shift anisotropy by R-symmetry sequences in magic angle spinning NMR spectroscopy. The Journal of Chemical Physics. 137: 134201. PMID 23039592 DOI: 10.1063/1.4754149 |
0.361 |
|
| 2012 |
Meng X, Zhao G, Yufenyuy E, Ke D, Ning J, DeLucia M, Ahn J, Gronenborn AM, Aiken C, Zhang P. Protease Cleavage Leads to Formation of Mature Trimer Interface in HIV-1 Capsid Plos Pathogens. 8. PMID 22927821 DOI: 10.1371/Journal.Ppat.1002886 |
0.351 |
|
| 2012 |
Koharudin LMI, Kolliparas S, Aikens C, Gronenborn AM. Structural insights into the anti-HIV activity of the oscillatoria agardhii agglutinin homolog lectin family Journal of Biological Chemistry. 287: 33796-33811. PMID 22865886 DOI: 10.1074/Jbc.M112.388579 |
0.416 |
|
| 2012 |
Yang R, Shi J, Byeon IJ, Ahn J, Sheehan JH, Meiler J, Gronenborn AM, Aiken C. Second-site suppressors of HIV-1 capsid mutations: restoration of intracellular activities without correction of intrinsic capsid stability defects. Retrovirology. 9: 30. PMID 22515365 DOI: 10.1186/1742-4690-9-30 |
0.307 |
|
| 2012 |
Byeon IJ, Hou G, Han Y, Suiter CL, Ahn J, Jung J, Byeon CH, Gronenborn AM, Polenova T. Motions on the millisecond time scale and multiple conformations of HIV-1 capsid protein: implications for structural polymorphism of CA assemblies. Journal of the American Chemical Society. 134: 6455-66. PMID 22428579 DOI: 10.1021/Ja300937V |
0.44 |
|
| 2012 |
Ji F, Jung J, Gronenborn AM. Structural and biochemical characterization of the childhood cataract-associated R76S mutant of human γd-crystallin Biochemistry. 51: 2588-2596. PMID 22394327 DOI: 10.1021/Bi300199D |
0.347 |
|
| 2012 |
Ahn J, Hao C, Yan J, DeLucia M, Mehrens J, Wang C, Gronenborn AM, Skowronski J. HIV/Simian Immunodeficiency Virus (SIV) accessory virulence factor Vpx loads the host cell restriction factor SAMHD1 onto the E3 ubiquitin ligase complex CRL4 DCAF1 Journal of Biological Chemistry. 287: 12550-12558. PMID 22362772 DOI: 10.1074/Jbc.M112.340711 |
0.382 |
|
| 2012 |
Krzysiak TC, Jung J, Thompson J, Baker D, Gronenborn AM. APOBEC2 is a monomer in solution: Implications for APOBEC3G Models Biochemistry. 51: 2008-2017. PMID 22339232 DOI: 10.1021/Bi300021S |
0.419 |
|
| 2012 |
Liu L, Byeon IJL, Bahar I, Gronenborn AM. Domain swapping proceeds via complete unfolding: A 19F- and 1H-NMR study of the cyanovirin-N protein Journal of the American Chemical Society. 134: 4229-4235. PMID 22296296 DOI: 10.1021/Ja210118W |
0.469 |
|
| 2012 |
Sun S, Han Y, Paramasivam S, Yan S, Siglin AE, Williams JC, Byeon IJ, Ahn J, Gronenborn AM, Polenova T. Solid-state NMR spectroscopy of protein complexes. Methods in Molecular Biology (Clifton, N.J.). 831: 303-31. PMID 22167681 DOI: 10.1007/978-1-61779-480-3_17 |
0.413 |
|
| 2012 |
Liu L, Gronenborn AM, Bahar I. Longer simulations sample larger subspaces of conformations while maintaining robust mechanisms of motion Proteins: Structure, Function and Bioinformatics. 80: 616-625. PMID 22105881 DOI: 10.1002/Prot.23225 |
0.386 |
|
| 2012 |
Kilpatrick AM, Koharudin LMI, Calero GA, Gronenborn AM. Structural and binding studies of the C-terminal domains of yeast TFIIF subunits Tfg1 and Tfg2 Proteins: Structure, Function and Bioinformatics. 80: 519-529. PMID 22095626 DOI: 10.1002/Prot.23217 |
0.42 |
|
| 2011 |
Hou G, Byeon IJ, Ahn J, Gronenborn AM, Polenova T. 1H-13C/1H-15N heteronuclear dipolar recoupling by R-symmetry sequences under fast magic angle spinning for dynamics analysis of biological and organic solids. Journal of the American Chemical Society. 133: 18646-55. PMID 21995349 DOI: 10.1021/Ja203771A |
0.388 |
|
| 2011 |
Koharudin LMI, Gronenborn AM. Structural basis of the anti-HIV activity of the cyanobacterial Oscillatoria Agardhii agglutinin Structure. 19: 1170-1181. PMID 21827952 DOI: 10.1016/J.Str.2011.05.010 |
0.461 |
|
| 2011 |
Koharudin LM, Viscomi AR, Montanini B, Kershaw MJ, Talbot NJ, Ottonello S, Gronenborn AM. Structure-function analysis of a CVNH-LysM lectin expressed during plant infection by the rice blast fungus Magnaporthe oryzae. Structure (London, England : 1993). 19: 662-74. PMID 21565701 DOI: 10.1016/J.Str.2011.03.004 |
0.367 |
|
| 2011 |
Zhao G, Ke D, Vu T, Ahn J, Shah VB, Yang R, Aiken C, Charlton LM, Gronenborn AM, Zhang P. Rhesus TRIM5α disrupts the HIV-1 capsid at the inter-hexamer interfaces Plos Pathogens. 7. PMID 21455494 DOI: 10.1371/Journal.Ppat.1002009 |
0.4 |
|
| 2011 |
Dao KK, Pey AL, Gjerde AU, Teigen K, Byeon IJ, Døskeland SO, Gronenborn AM, Martinez A. The regulatory subunit of PKA-I remains partially structured and undergoes β-aggregation upon thermal denaturation. Plos One. 6: e17602. PMID 21394209 DOI: 10.1371/Journal.Pone.0017602 |
0.387 |
|
| 2011 |
Jung J, Byeon IJL, Ahn J, Gronenborn AM. Structure, dynamics, and Hck interaction of full-length HIV-1 Nef Proteins: Structure, Function and Bioinformatics. 79: 1609-1622. PMID 21365684 DOI: 10.1002/Prot.22986 |
0.445 |
|
| 2011 |
Matei E, Louis JM, Jee J, Gronenborn AM. NMR solution structure of a cyanovirin homolog from wheat head blight fungus Proteins: Structure, Function and Bioinformatics. 79: 1538-1549. PMID 21365681 DOI: 10.1002/Prot.22981 |
0.433 |
|
| 2011 |
Hou G, Yan S, Sun S, Han Y, Byeon IJ, Ahn J, Concel J, Samoson A, Gronenborn AM, Polenova T. Spin diffusion driven by R-symmetry sequences: applications to homonuclear correlation spectroscopy in MAS NMR of biological and organic solids. Journal of the American Chemical Society. 133: 3943-53. PMID 21361320 DOI: 10.1021/Ja108650X |
0.334 |
|
| 2011 |
Ahn J, Novince Z, Concel J, Byeon CH, Makhov AM, Byeon IJL, Zhang P, Gronenborn AM. The cullin-RING E3 ubiquitin ligase CRL4-DCAF1 complex dimerizes via a short helical region in DCAF1 Biochemistry. 50: 1359-1367. PMID 21226479 DOI: 10.1021/Bi101749S |
0.415 |
|
| 2011 |
Koharudin LMI, Furey W, Gronenborn AM. Novel fold and carbohydrate specificity of the potent anti-HIV cyanobacterial lectin from Oscillatoria agardhii Journal of Biological Chemistry. 286: 1588-1597. PMID 20961847 DOI: 10.1074/Jbc.M110.173278 |
0.457 |
|
| 2011 |
Zhao G, Meng X, Ke D, Vu T, Ahn J, Shah V, Yang R, Aiken C, Charlton L, Gronenborn A, Zhang P. Structure of HIV Capsid and Interactions with Rhesus TRIM5α Microscopy and Microanalysis. 17: 104-105. DOI: 10.1017/S1431927611001395 |
0.341 |
|
| 2011 |
Suiter CL, Hou G, Han Y, Ahn J, Gronenborn A, Ablan S, Freed E, Polenova T. Studies of HIV-1 Gag Protein Assemblies by Solid-State MAS NMR Spectroscopy Biophysical Journal. 100: 605a. DOI: 10.1016/J.Bpj.2010.12.3483 |
0.428 |
|
| 2011 |
Hou G, Han Y, Suiter C, Byeon IL, Ahn J, Concel J, Gronenborn AM, Polenova T. Dynamics Studies of HIV-1 CA Protein Assemblies by Solid-State MAS NMR Spectroscopy Biophysical Journal. 100: 604a. DOI: 10.1016/J.Bpj.2010.12.3480 |
0.409 |
|
| 2011 |
Liu L, Gronenborn AM, Bahar I. The Short-Time Dynamics of Proteins Near Native State Conditions Signal to Robust Mechanisms Accessible at Long Times Biophysical Journal. 100: 535a. DOI: 10.1016/J.Bpj.2010.12.3120 |
0.393 |
|
| 2011 |
Liu L, Byeon I, Bahar I, Gronenborn AM. Investigating Domain-Swapped Proteins by 19F NMR Biophysical Journal. 100: 397a-398a. DOI: 10.1016/J.Bpj.2010.12.2361 |
0.499 |
|
| 2010 |
Walsh JD, Meier K, Ishima R, Gronenborn AM. NMR studies on domain diffusion and alignment in modular GB1 repeats Biophysical Journal. 99: 2636-2646. PMID 20959105 DOI: 10.1016/J.Bpj.2010.08.036 |
0.342 |
|
| 2010 |
Hou G, Paramasivam S, Byeon IJ, Gronenborn AM, Polenova T. Determination of relative tensor orientations by γ-encoded chemical shift anisotropy/heteronuclear dipolar coupling 3D NMR spectroscopy in biological solids. Physical Chemistry Chemical Physics : Pccp. 12: 14873-83. PMID 20936218 DOI: 10.1039/C0Cp00795A |
0.357 |
|
| 2010 |
Ahn J, Vu T, Novince Z, Guerrero-Santoro J, Rapic-Otrin V, Gronenborn AM. 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 Journal of Biological Chemistry. 285: 37333-37341. PMID 20870715 DOI: 10.1074/Jbc.M110.133181 |
0.367 |
|
| 2010 |
Ahn J, Byeon IJL, Dharmasena S, Huber K, Concel J, Gronenborn AM, Sluis-Cremer N. The RNA binding protein HuR does not interact directly with HIV-1 reverse transcriptase and does not affect reverse transcription in vitro Retrovirology. 7. PMID 20459669 DOI: 10.1186/1742-4690-7-40 |
0.409 |
|
| 2010 |
Byeon IJL, Dao KK, Jung J, Keen J, Leiros I, Døskeland SO, Martinez A, Gronenborn AM. Allosteric communication between cAMP binding sites in the RI subunit of protein kinase A revealed by NMR Journal of Biological Chemistry. 285: 14062-14070. PMID 20197278 DOI: 10.1074/Jbc.M110.106666 |
0.375 |
|
| 2010 |
Matei E, Zheng A, Furey W, Rose J, Aiken C, Gronenborn AM. Anti-HIV activity of defective cyanovirin-N mutants is restored by dimerization Journal of Biological Chemistry. 285: 13057-13065. PMID 20147291 DOI: 10.1074/Jbc.M109.094938 |
0.403 |
|
| 2010 |
Han Y, Ahn J, Concel J, Byeon IJ, Gronenborn AM, Yang J, Polenova T. Solid-state NMR studies of HIV-1 capsid protein assemblies. Journal of the American Chemical Society. 132: 1976-87. PMID 20092249 DOI: 10.1021/Ja908687K |
0.407 |
|
| 2010 |
Jung J, Byeon IJL, Ahn J, Concel J, Gronenborn AM. 1H, 15N and 13C assignments of the dimeric C-terminal domain of HIV-1 capsid protein Biomolecular Nmr Assignments. 4: 21-23. PMID 19921549 DOI: 10.1007/S12104-009-9198-9 |
0.391 |
|
| 2010 |
Walsh JD, Meier K, Ishima R, Gronenborn AM. Diffusion and Alignment of Domain Repeats in Modular Proteins - A NMR Study Biophysical Journal. 98: 2-8. DOI: 10.1016/J.Bpj.2009.12.1292 |
0.383 |
|
| 2009 |
Byeon IJL, Meng X, Jung J, Zhao G, Yang R, Ahn J, Shi J, Concel J, Aiken C, Zhang P, Gronenborn AM. Structural Convergence between Cryo-EM and NMR Reveals Intersubunit Interactions Critical for HIV-1 Capsid Function Cell. 139: 780-790. PMID 19914170 DOI: 10.1016/J.Cell.2009.10.010 |
0.403 |
|
| 2009 |
Iwatani Y, Chan DS, Liu L, Yoshii H, Shibata J, Yamamoto N, Levin JG, Gronenborn AM, Sugiura W. HIV-1 Vif-mediated ubiquitination/degradation of APOBEC3G involves four critical lysine residues in its C-terminal domain. Proceedings of the National Academy of Sciences of the United States of America. 106: 19539-44. PMID 19887642 DOI: 10.1073/Pnas.0906652106 |
0.44 |
|
| 2009 |
Wang J, Zuo X, Yu P, Byeon IJL, Jung J, Wang X, Dyba M, Seifert S, Schwieters CD, Qin J, Gronenborn AM, Wang YX. Determination of multicomponent protein structures in solution using global orientation and shape restraints Journal of the American Chemical Society. 131: 10507-10515. PMID 19722627 DOI: 10.1021/Ja902528F |
0.427 |
|
| 2009 |
Liu L, Koharudin LMI, Gronenborn AM, Bahar I. A comparative analysis of the equilibrium dynamics of a designed protein inferred from NMR, X-ray, and computations Proteins: Structure, Function and Bioinformatics. 77: 927-939. PMID 19688820 DOI: 10.1002/Prot.22518 |
0.44 |
|
| 2009 |
Koharudin LMI, Furey W, Gronenborn AM. A designed chimeric cyanovirin-N homolog lectin: Structure and molecular basis of sucrose binding Proteins: Structure, Function and Bioinformatics. 77: 904-915. PMID 19639634 DOI: 10.1002/Prot.22514 |
0.449 |
|
| 2009 |
Koharudin LMI, Furey W, Liu H, Liu YJ, Gronenborn AM. 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) Journal of Biological Chemistry. 284: 23697-23707. PMID 19553671 DOI: 10.1074/Jbc.M109.008995 |
0.408 |
|
| 2009 |
Ahn J, Byeon IJL, Byeon CH, Gronenborn AM. Insight into the structural basis of pro- and antiapoptotic p53 modulation by ASPP proteins Journal of Biological Chemistry. 284: 13812-13822. PMID 19246451 DOI: 10.1074/Jbc.M808821200 |
0.341 |
|
| 2009 |
Jung J, Byeon IJL, Wang Y, King J, Gronenborn AM. The structure of the cataract-causing P23T mutant of human γD-crystallin exhibits distinctive local conformational and dynamic changes Biochemistry. 48: 2597-2609. PMID 19216553 DOI: 10.1021/Bi802292Q |
0.401 |
|
| 2009 |
Gronenborn AM. Protein acrobatics in pairs - dimerization via domain swapping Current Opinion in Structural Biology. 19: 39-49. PMID 19162470 DOI: 10.1016/J.Sbi.2008.12.002 |
0.431 |
|
| 2009 |
Koharudin L, Gronenborn A. NMR structures of a designed Cyanovirin-N homolog lectin; LKAMG Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr16339 |
0.35 |
|
| 2009 |
Liu L, Koharudin LM, Gronenborn AM, Bahar I. A Detailed Comparison Between The NMR Ensemble, Two X-ray Models And Computational Predictions Of Motions For A Designed Sugar Binding Protein Biophysical Journal. 96: 323a. DOI: 10.1016/J.Bpj.2008.12.1623 |
0.485 |
|
| 2009 |
Xu J, Tcherkasskaya O, Gronenborn AM, Callis P, Toptygin D, Gleason FK, Brand L, Knutson JR. Ultrafast Decay of Trp in Biological Macromolecules Biophysical Journal. 96: 46a. DOI: 10.1016/J.Bpj.2008.12.133 |
0.326 |
|
| 2008 |
Matei E, Furey W, Gronenborn AM. Solution and Crystal Structures of a Sugar Binding Site Mutant of Cyanovirin-N: No Evidence of Domain Swapping Structure. 16: 1183-1194. PMID 18682220 DOI: 10.1016/J.Str.2008.05.011 |
0.425 |
|
| 2008 |
Koharudin LMI, Viscomi AR, Jee JG, Ottonello S, Gronenborn AM. The Evolutionarily Conserved Family of Cyanovirin-N Homologs: Structures and Carbohydrate Specificity Structure. 16: 570-584. PMID 18400178 DOI: 10.1016/J.Str.2008.01.015 |
0.401 |
|
| 2008 |
Sandström C, Hakkarainen B, Matei E, Glinchert A, Lahmann M, Oscarson S, Kenne L, Gronenborn AM. Atomic mapping of the sugar interactions in one-site and two-site mutants of cyanovirin-N by NMR spectroscopy Biochemistry. 47: 3625-3635. PMID 18311923 DOI: 10.1021/Bi702200M |
0.414 |
|
| 2008 |
Jee J, Byeon IJL, Louis JM, Gronenborn AM. The point mutation A34F causes dimerization of GB1 Proteins: Structure, Function and Genetics. 71: 1420-1431. PMID 18076051 DOI: 10.1002/Prot.21831 |
0.414 |
|
| 2008 |
Jee J, Ishima R, Gronenborn AM. Characterization of specific protein association by15N CPMG relaxation dispersion NMR: The GB1A34F monomer-dimer equilibrium Journal of Physical Chemistry B. 112: 6008-6012. PMID 18004837 DOI: 10.1021/Jp076094H |
0.385 |
|
| 2007 |
Iwatani Y, Chan DS, Wang F, Maynard KS, Sugiura W, Gronenborn AM, Rouzina I, Williams MC, Musier-Forsyth K, Levin JG. Deaminase-independent inhibition of HIV-1 reverse transcription by APOBEC3G. Nucleic Acids Research. 35: 7096-108. PMID 17942420 DOI: 10.1093/Nar/Gkm750 |
0.318 |
|
| 2007 |
Yang LW, Eyal E, Chennubhotla C, Jee J, Gronenborn AM, Bahar I. Insights into Equilibrium Dynamics of Proteins from Comparison of NMR and X-Ray Data with Computational Predictions Structure. 15: 741-749. PMID 17562320 DOI: 10.1016/J.Str.2007.04.014 |
0.319 |
|
| 2007 |
Shahkhatuni AA, Shahkhatuni AG, Panosyan HA, Sahakyan AB, Byeon IJ, Gronenborn AM. Assessment of solvent effects: do weak alignment media affect the structure of the solute? Magnetic Resonance in Chemistry : Mrc. 45: 557-63. PMID 17534883 DOI: 10.1002/Mrc.2004 |
0.332 |
|
| 2007 |
Vega-Rocha S, Gronenborn B, Gronenborn AM, Campos-Olivas R. 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 circoviras structures Biochemistry. 46: 6201-6212. PMID 17472345 DOI: 10.1021/Bi700159Q |
0.41 |
|
| 2007 |
Vega-Rocha S, Byeon IJL, Gronenborn B, Gronenborn AM, Campos-Olivas R. Solution Structure, Divalent Metal and DNA Binding of the Endonuclease Domain from the Replication Initiation Protein from Porcine Circovirus 2 Journal of Molecular Biology. 367: 473-487. PMID 17275023 DOI: 10.1016/J.Jmb.2007.01.002 |
0.433 |
|
| 2007 |
Vega-Rocha S, Gronenborn AM, Gronenborn B, Campos-Olivas R. 1H, 13C, and 15N NMR assignment of the master Rep protein nuclease domain from the Nanovirus FBNYV [3] Journal of Biomolecular Nmr. 38: 169. PMID 17043745 DOI: 10.1007/S10858-006-9085-Y |
0.379 |
|
| 2007 |
Ermolenko DN, Dangi B, Gvritishvili A, Gronenborn AM, Makhatadze GI. Elimination of the C-cap in ubiquitin-structure, dynamics and thermodynamic consequences Biophysical Chemistry. 126: 25-35. PMID 16713063 DOI: 10.1016/J.Bpc.2006.03.017 |
0.41 |
|
| 2007 |
Gronenborn AM. Some basic biomolecular NMR for protein structure determination Supramolecular Structure and Function 9. 33-44. DOI: 10.1007/978-1-4020-6466-1_3 |
0.308 |
|
| 2006 |
Toptygin D, Gronenborn AM, Brand L. Nanosecond relaxation dynamics of protein GB1 identified by the time-dependent red shift in the fluorescence of tryptophan and 5-fluorotryptophan. The Journal of Physical Chemistry. B. 110: 26292-302. PMID 17181288 DOI: 10.1021/Jp064528N |
0.318 |
|
| 2006 |
Barrientos LG, Matei E, Lasala F, Delgado R, Gronenborn AM. Dissecting carbohydrate-Cyanovirin-N binding by structure-guided mutagenesis: functional implications for viral entry inhibition. Protein Engineering, Design & Selection : Peds. 19: 525-35. PMID 17012344 DOI: 10.1093/Protein/Gzl040 |
0.338 |
|
| 2005 |
Zubkov S, Gronenborn AM, Byeon IJL, Mohanty S. Structural consequences of the pH-induced conformational switch in A. polyphemus pheromone-binding protein: Mechanisms of ligand release Journal of Molecular Biology. 354: 1081-1090. PMID 16289114 DOI: 10.1016/J.Jmb.2005.10.015 |
0.353 |
|
| 2005 |
Byeon IJL, Li H, Song H, Gronenborn AM, Tsai MD. Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67 Nature Structural and Molecular Biology. 12: 987-993. PMID 16244663 DOI: 10.1038/Nsmb1008 |
0.377 |
|
| 2005 |
Mangold SL, Morgan JR, Strohmeyer GC, Gronenborn AM, Cloninger MJ. Cyanovirin-N binding to Manα1-2Man functionalized dendrimers Organic and Biomolecular Chemistry. 3: 2354-2358. PMID 16010372 DOI: 10.1039/B417789D |
0.358 |
|
| 2005 |
Louis JM, Byeon IJL, Baxa U, Gronenborn AM. The GB1 amyloid fibril: Recruitment of the peripheral β-strands of the domain swapped dimer into the polymeric interface Journal of Molecular Biology. 348: 687-698. PMID 15826664 DOI: 10.1016/J.Jmb.2005.02.071 |
0.379 |
|
| 2005 |
Barrientos LG, Gronenborn AM. The highly specific carbohydrate-binding protein cyanovirin-N: structure, anti-HIV/Ebola activity and possibilities for therapy. Mini Reviews in Medicinal Chemistry. 5: 21-31. PMID 15638789 DOI: 10.2174/1389557053402783 |
0.336 |
|
| 2005 |
CLORE GM, GRONENBORN AM, MITCHINSON C, GREEN NM. 1H-NMR Studies on Nucleotide Binding to the Sarcoplasmic Reticulum Ca2+ ATPase European Journal of Biochemistry. 128: 113-117. DOI: 10.1111/J.1432-1033.1982.Tb06940.X |
0.337 |
|
| 2005 |
Gronenborn AM, Byeon I-L, Louis JM. The amazing versatility of proteins - structural polymorphism and evolution Acta Crystallographica Section A. 61: 10-10. DOI: 10.1107/S0108767305099587 |
0.345 |
|
| 2004 |
Sandström C, Berteau O, Gemma E, Oscarson S, Kenne L, Gronenborn AM. Atomic mapping of the interactions between the antiviral agent cyanovirin-N and oligomannosides by saturation-transfer difference NMR. Biochemistry. 43: 13926-31. PMID 15518540 DOI: 10.1021/Bi048676K |
0.436 |
|
| 2004 |
Barrientos LG, Lasala F, Delgado R, Sanchez A, Gronenborn AM. Flipping the switch from monomeric to dimeric CV-N has little effect on antiviral activity. Structure (London, England : 1993). 12: 1799-807. PMID 15458629 DOI: 10.1016/J.Str.2004.07.019 |
0.324 |
|
| 2004 |
Byeon IJ, Louis JM, Gronenborn AM. A captured folding intermediate involved in dimerization and domain-swapping of GB1. Journal of Molecular Biology. 340: 615-25. PMID 15210358 DOI: 10.1016/J.Jmb.2004.04.069 |
0.421 |
|
| 2004 |
Ding K, Gronenborn AM. Protein Backbone 1H(N)-13Calpha and 15N-13Calpha residual dipolar and J couplings: new constraints for NMR structure determination. Journal of the American Chemical Society. 126: 6232-3. PMID 15149211 DOI: 10.1021/Ja049049L |
0.396 |
|
| 2004 |
Ding K, Gronenborn AM. Sensitivity-enhanced IPAP experiments for measuring one-bond 13C'-13Calpha and 13Calpha-1Halpha residual dipolar couplings in proteins. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 167: 253-8. PMID 15040980 DOI: 10.1016/J.Jmr.2003.12.016 |
0.319 |
|
| 2004 |
Mohanty S, Zubkov S, Gronenborn AM. The solution NMR structure of Antheraea polyphemus PBP provides new insight into pheromone recognition by pheromone-binding proteins Journal of Molecular Biology. 337: 443-451. PMID 15003458 DOI: 10.1016/J.Jmb.2004.01.009 |
0.377 |
|
| 2004 |
Ding K, Louis JM, Gronenborn AM. Insights into Conformation and Dynamics of Protein GB1 during Folding and Unfolding by NMR Journal of Molecular Biology. 335: 1299-1307. PMID 14729345 DOI: 10.1016/J.Jmb.2003.11.042 |
0.4 |
|
| 2004 |
McKinney J, Knappskog PM, Pereira J, Ekern T, Toska K, Kuitert BB, Levine D, Gronenborn AM, Martinez A, Haavik J. Expression and purification of human tryptophan hydroxylase from Escherichia coli and Pichia pastoris Protein Expression and Purification. 33: 185-194. PMID 14711505 DOI: 10.1016/J.Pep.2003.09.014 |
0.3 |
|
| 2004 |
Mohanty S, Zubkov S, Gronenborn AM. Erratum to “The Solution NMR Structure of Antheraea polyphemus PBP Provides New Insight into Pheromone Recognition by Pheromone-binding Proteins” [J. Mol. Biol. (2004) 337, 443–451] Journal of Molecular Biology. 338: 1037. DOI: 10.1016/J.Jmb.2004.03.052 |
0.37 |
|
| 2003 |
Gronenborn AM. Rapid screening of E. coli extracts by heteronuclear NMR. Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. Unit 7.11. PMID 18429247 DOI: 10.1002/0471140864.Ps0711S31 |
0.413 |
|
| 2003 |
Byeon IJL, Louis JM, Gronenborn AM. A protein contortionist: Core mutations of GB1 that induce dimerization and domain swapping Journal of Molecular Biology. 333: 141-152. PMID 14516749 DOI: 10.1016/S0022-2836(03)00928-8 |
0.437 |
|
| 2003 |
Ding K, Gronenborn AM. Simultaneous and accurate determination of one-bond 15N- 13C′ and two-bond 1HN- 13C′ dipolar couplings Journal of the American Chemical Society. 125: 11504-11505. PMID 13129346 DOI: 10.1021/Ja035954E |
0.318 |
|
| 2003 |
Dobrodumov A, Gronenborn AM. Filtering and selection of structural models: Combining docking and NMR Proteins: Structure, Function and Genetics. 53: 18-32. PMID 12945046 DOI: 10.1002/Prot.10439 |
0.436 |
|
| 2003 |
Ishima R, Torchia DA, Lynch SM, Gronenborn AM, Louis JM. Solution structure of the mature HIV-1 protease monomer: insight into the tertiary fold and stability of a precursor. The Journal of Biological Chemistry. 278: 43311-9. PMID 12933791 DOI: 10.1074/Jbc.M307549200 |
0.422 |
|
| 2003 |
Ding K, Gronenborn AM. Sensitivity-enhanced 2D IPAP, TROSY-anti-TROSY, and E.COSY experiments: Alternatives for measuring dipolar 15N-1HN couplings Journal of Magnetic Resonance. 163: 208-214. PMID 12914836 DOI: 10.1016/S1090-7807(03)00081-8 |
0.349 |
|
| 2003 |
Katoh E, Louis JM, Yamazaki T, Gronenborn AM, Torchia DA, Ishima R. A solution NMR study of the binding kinetics and the internal dynamics of an HIV-1 protease-substrate complex. Protein Science : a Publication of the Protein Society. 12: 1376-85. PMID 12824484 DOI: 10.1110/Ps.0300703 |
0.382 |
|
| 2003 |
Barrientos LG, O'Keefe BR, Bray M, Sanchez A, Gronenborn AM, Boyd MR. Cyanovirin-N binds to the viral surface glycoprotein, GP1,2 and inhibits infectivity of Ebola virus Antiviral Research. 58: 47-56. PMID 12719006 DOI: 10.1016/S0166-3542(02)00183-3 |
0.314 |
|
| 2003 |
Mesleh MF, Valentine KG, Opella SJ, Louis JM, Gronenborn AM. Myristoylation as a general method for immobilization and alignment of soluble proteins for solid-state NMR structural studies Journal of Biomolecular Nmr. 25: 55-61. PMID 12566999 DOI: 10.1023/A:1021964314987 |
0.446 |
|
| 2003 |
Barrientos LG, Louis JM, Ratner DM, Seeberger PH, Gronenborn AM. Solution structure of a circular-permuted variant of the potent HIV-inactivating protein cyanovirin-N: structural basis for protein stability and oligosaccharide interaction. Journal of Molecular Biology. 325: 211-23. PMID 12473463 DOI: 10.1016/S0022-2836(02)01205-6 |
0.448 |
|
| 2003 |
Louis JM, Ishima R, Nesheiwat I, Pannell LK, Lynch SM, Torchia DA, Gronenborn AM. Revisiting monomeric HIV-1 protease. Characterization and redesign for improved properties. The Journal of Biological Chemistry. 278: 6085-92. PMID 12468541 DOI: 10.1074/Jbc.M209726200 |
0.422 |
|
| 2003 |
Byeon I, Louis J, Gronenborn A. 1H, 13C, and 15N Chemical Shift Assignments of the dimeric mutant of GB1 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr5875 |
0.314 |
|
| 2003 |
Frank M, Dyda F, Dobrodumov A, Gronenborn A. A Protein Contorsionist-Core Mutations Switch Monomeric Protein GB1 into an Intertwined Tetramer Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr5654 |
0.301 |
|
| 2003 |
Byeon IL, Louis JM, Gronenborn AM. Erratum to “A Protein Contortionist: Core Mutations of GBI that Induce Dimerization and Domain Swapping” [J. Mol. Biol. 333 (2003) 141–152] Journal of Molecular Biology. 334: 605. DOI: 10.1016/J.Jmb.2003.10.001 |
0.323 |
|
| 2002 |
Gronenborn AM. The importance of being ordered: Improving NMR structures using residual dipolar couplings Comptes Rendus - Biologies. 325: 957-966. PMID 12481689 DOI: 10.1016/S1631-0691(02)01512-3 |
0.392 |
|
| 2002 |
Campos-Olivas R, Louis JM, Clérot D, Gronenborn B, Gronenborn AM. 1H, 13C, and 15N assignment of the N-terminal, catalytic domain of the replication initiation protein from the geminivirus TYLCV [3] Journal of Biomolecular Nmr. 24: 73-74. PMID 12449422 DOI: 10.1023/A:1020664809314 |
0.352 |
|
| 2002 |
Ding K, Gronenborn AM. Sensitivity-enhanced E.COSY-type HSQC experiments for accurate measurements of one-bond 15N-1HN and 15N-13C′ and two-bond 13C′-1HN residual dipolar couplings in proteins Journal of Magnetic Resonance. 158: 173-177. PMID 12419684 DOI: 10.1016/S1090-7807(02)00024-1 |
0.378 |
|
| 2002 |
Barrientos LG, Gronenborn AM. The domain-swapped dimer of cyanovirin-N contains two sets of oligosaccharide binding sites in solution Biochemical and Biophysical Research Communications. 298: 598-602. PMID 12408994 DOI: 10.1016/S0006-291X(02)02489-0 |
0.403 |
|
| 2002 |
Shenoy SR, Barrientos LG, Ratner DM, O'Keefe BR, Seeberger PH, Gronenborn AM, Boyd MR. Multisite and multivalent binding between cyanovirin-N and branched oligomannosides: calorimetric and NMR characterization. Chemistry & Biology. 9: 1109-18. PMID 12401495 DOI: 10.1016/S1074-5521(02)00237-5 |
0.401 |
|
| 2002 |
Frank MK, Dyda F, Dobrodumov A, Gronenborn AM. Core mutations switch monomeric protein GB1 into an intertwined tetramer Nature Structural Biology. 9: 877-885. PMID 12379842 DOI: 10.1038/Nsb854 |
0.433 |
|
| 2002 |
Mori T, Barrientos LG, Han Z, Gronenborn AM, Turpin JA, Boyd MR. Functional homologs of cyanovirin-N amenable to mass production in prokaryotic and eukaryotic hosts Protein Expression and Purification. 26: 42-49. PMID 12356469 DOI: 10.1016/S1046-5928(02)00513-2 |
0.339 |
|
| 2002 |
Ermolenko DN, Thomas ST, Aurora R, Gronenborn AM, Makhatadze GI. Hydrophobic interactions at the Ccap position of the C-capping motif of alpha-helices. Journal of Molecular Biology. 322: 123-35. PMID 12215419 DOI: 10.1016/S0022-2836(02)00734-9 |
0.374 |
|
| 2002 |
Ding K, Gronenborn AM. Novel 2D triple-resonance NMR experiments for sequential resonance assignments of proteins Journal of Magnetic Resonance. 156: 262-268. PMID 12165262 DOI: 10.1006/Jmre.2002.2537 |
0.371 |
|
| 2002 |
Dangi B, Dobrodumov AV, Louis JM, Gronenborn AM. Solution structure and dynamics of the human - Escherichia coli thioredoxin chimera: Insights into thermodynamic stability Biochemistry. 41: 9376-9388. PMID 12135359 DOI: 10.1021/Bi0258501 |
0.414 |
|
| 2002 |
Campos-Olivas R, Louis JM, Clérot D, Gronenborn B, Gronenborn AM. The structure of a replication initiator unites diverse aspects of nucleic acid metabolism Proceedings of the National Academy of Sciences of the United States of America. 99: 10310-10315. PMID 12130667 DOI: 10.1073/Pnas.152342699 |
0.398 |
|
| 2002 |
Campos-Olivas R, Aziz R, Helms GL, Evans JN, Gronenborn AM. Placement of 19F into the center of GB1: effects on structure and stability. Febs Letters. 517: 55-60. PMID 12062409 DOI: 10.1016/S0014-5793(02)02577-2 |
0.382 |
|
| 2002 |
Barrientos LG, Louis JM, Botos I, Mori T, Han Z, O'Keefe BR, Boyd MR, Wlodawer A, Gronenborn AM. The domain-swapped dimer of cyanovirin-N is in a metastable folded state: Reconciliation of X-ray and NMR structures Structure. 10: 673-686. PMID 12015150 DOI: 10.1016/S0969-2126(02)00758-X |
0.447 |
|
| 2002 |
Rosner JL, Dangi B, Gronenborn AM, Martin RG. Posttranscriptional activation of the transcriptional activator Rob by dipyridyl in Escherichia coli Journal of Bacteriology. 184: 1407-1416. PMID 11844771 DOI: 10.1128/Jb.184.5.1407-1416.2002 |
0.312 |
|
| 2002 |
Barrientos LG, Louis JM, Hung J, Smith TH, O'Keefe BR, Gardella RS, Mori T, Boyd MR, Gronenborn AM. Design and initial characterization of a circular permuted variant of the potent HIV-inactivating protein cyanovirin-N Proteins: Structure, Function and Genetics. 46: 153-160. PMID 11807943 DOI: 10.1002/Prot.10024 |
0.427 |
|
| 2001 |
Dangi B, Pelupessey P, Martin RG, Rosner JL, Louis JM, Gronenborn AM. Structure and dynamics of MarA-DNA complexes: An NMR investigation Journal of Molecular Biology. 314: 113-127. PMID 11724537 DOI: 10.1006/Jmbi.2001.5106 |
0.433 |
|
| 2001 |
Ishima R, Ghirlando R, Tözsér J, Gronenborn AM, Torchia DA, Louis JM. Folded monomer of HIV-1 protease. The Journal of Biological Chemistry. 276: 49110-6. PMID 11598128 DOI: 10.1074/Jbc.M108136200 |
0.428 |
|
| 2001 |
Louis JM, Georgescu RE, Tasayco ML, Tcherkasskaya O, Gronenborn AM. Probing the structure and stability of a hybrid protein: The human - E. coli thioredoxin chimera Biochemistry. 40: 11184-11192. PMID 11551217 DOI: 10.1021/Bi010745X |
0.404 |
|
| 2001 |
Qin J, Vinogradova O, Gronenborn AM. Protein-protein interactions probed by nuclear magnetic resonance spectroscopy Methods in Enzymology. 339: 377-389. PMID 11462822 DOI: 10.1016/S0076-6879(01)39323-0 |
0.336 |
|
| 2001 |
Campos-Olivas R, Hörr I, Bormann C, Jung G, Gronenborn AM. Solution structure, backbone dynamics and chitin binding of the anti-fungal protein from Streptomyces tendae TÜ901 Journal of Molecular Biology. 308: 765-782. PMID 11350173 DOI: 10.1006/Jmbi.2001.4622 |
0.442 |
|
| 2001 |
Barrientos LG, Campos-Olivas R, Louis JM, Fiser A, Šali A, Gronenborn AM. 1H, 13N resonance assignments and fold verification of a circular permuted variant of the potent HIV-inactivating protein cyanovirin-N [6] Journal of Biomolecular Nmr. 19: 289-290. PMID 11330821 DOI: 10.1023/A:1011292919947 |
0.329 |
|
| 2001 |
Barrientos LG, Louis JM, Gronenborn AM. Characterization of the cholesteric phase of filamentous bacteriophage fd for molecular alignment Journal of Magnetic Resonance. 149: 154-158. PMID 11273766 DOI: 10.1006/Jmre.2000.2276 |
0.304 |
|
| 2001 |
Qin J, Yang Y, Velyvis A, Gronenborn A. Molecular views of redox regulation: three-dimensional structures of redox regulatory proteins and protein complexes. Antioxidants & Redox Signaling. 2: 827-40. PMID 11213487 DOI: 10.1089/Ars.2000.2.4-827 |
0.368 |
|
| 2000 |
Li H, Yamada H, Akasaka K, Gronenborn AM. Pressure alters electronic orbital overlap in hydrogen bonds Journal of Biomolecular Nmr. 18: 207-216. PMID 11142511 DOI: 10.1023/A:1026537609584 |
0.316 |
|
| 2000 |
Louis JM, Webert IT, Tözsér J, Marius Clore G, Gronenborn AM. HIV-I protease: Maturation, enzyme specificity, and drug resistance Advances in Pharmacology. 49: 111-146. PMID 11013762 DOI: 10.1016/S1054-3589(00)49025-3 |
0.305 |
|
| 2000 |
Tcherkasskaya O, Knutson JR, Bowley SA, Frank MK, Gronenborn AM. Nanosecond dynamics of the single tryptophan reveals multi-state equilibrium unfolding of protein GB1. Biochemistry. 39: 11216-26. PMID 10985767 DOI: 10.1021/Bi000345U |
0.34 |
|
| 2000 |
Tcherkasskaya O, Bychkova VE, Uversky VN, Gronenborn AM. Multisite fluorescence in proteins with multiple tryptophan residues: Apomyoglobin natural variants and site-directed mutants Journal of Biological Chemistry. 275: 36285-36294. PMID 10948189 DOI: 10.1074/Jbc.M003008200 |
0.394 |
|
| 2000 |
Castagné C, Murphy EC, Gronenborn AM, Delepierre M. NMR analysis of the DNA conformation induced by protein binding SRY/DNA complexes European Journal of Biochemistry. 267: 1223-1229. PMID 10672034 DOI: 10.1046/J.1432-1327.2000.01124.X |
0.327 |
|
| 2000 |
Gakh YG, Gakh AA, Gronenborn AM. Fluorine as an NMR probe for structural studies of chemical and biological systems Magnetic Resonance in Chemistry. 38: 551-558. DOI: 10.1002/1097-458X(200007)38:7<551::Aid-Mrc686>3.0.Co;2-Q |
0.364 |
|
| 1999 |
Caffrey M, Kaufman J, Stahl S, Wingfield P, Gronenborn AM, Clore GM. Monomer-trimer equilibrium of the ectodomain of SIV gp41: Insight into the mechanism of peptide inhibition of HIV infection Protein Science. 8: 1904-1907. PMID 10493592 DOI: 10.1110/Ps.8.9.1904 |
0.315 |
|
| 1999 |
Louis JM, Marius Clore G, Gronenborn AM. Autoprocessing of HIV-1 protease is tightly coupled to protein folding Nature Structural Biology. 6: 868-875. PMID 10467100 DOI: 10.1038/12327 |
0.418 |
|
| 1999 |
Yang F, Bewley CA, Louis JM, Gustafson KR, Boyd MR, Gronenborn AM, Clore GM, Wlodawer A. Crystal structure of cyanovirin-N, a potent HIV-inactivating protein, shows unexpected domain swapping Journal of Molecular Biology. 288: 403-412. PMID 10329150 DOI: 10.1006/Jmbi.1999.2693 |
0.416 |
|
| 1999 |
Garrett DS, Seok YJ, Peterkofsky A, Gronenborn AM, Marius Clore G. Solution structure of the 40,000 M(r) phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr Nature Structural Biology. 6: 166-173. PMID 10048929 DOI: 10.1038/5854 |
0.432 |
|
| 1999 |
Gronenborn AM, Clore GM, Louis JM, Wingfield PT. Is human thioredoxin monomeric or dimeric? Protein Science. 8: 426-429. PMID 10048336 DOI: 10.1110/Ps.8.2.426 |
0.31 |
|
| 1999 |
Yu B, Blaber M, Gronenborn AM, Clore GM, Caspar DL. Disordered water within a hydrophobic protein cavity visualized by x-ray crystallography. Proceedings of the National Academy of Sciences of the United States of America. 96: 103-8. PMID 9874779 DOI: 10.1073/Pnas.96.1.103 |
0.303 |
|
| 1998 |
Caffrey M, Kaufman J, Stahl SJ, Wingfield PT, Gronenborn AM, Clore GM. 3D NMR Experiments for Measuring 15N Relaxation Data of Large Proteins: Application to the 44 kDa Ectodomain of SIV gp41 Journal of Magnetic Resonance. 135: 368-372. PMID 9878465 DOI: 10.1006/Jmre.1998.1583 |
0.353 |
|
| 1998 |
Cai M, Huang Y, Caffrey M, Zheng R, Craigie R, Marius Clore G, Gronenborn AM. Solution structure of the His12 → Cys mutant of the N-terminal zinc binding domain of HIV-1 integrase complexed to cadmium Protein Science. 7: 2669-2674. PMID 9865962 DOI: 10.1002/Pro.5560071221 |
0.417 |
|
| 1998 |
Clore GM, Gronenborn AM. NMR structure determination of proteins and protein complexes larger than 20 kDa Current Opinion in Chemical Biology. 2: 564-570. PMID 9818180 DOI: 10.1016/S1367-5931(98)80084-7 |
0.433 |
|
| 1998 |
Cai M, Huang Y, Zheng R, Wei SQ, Ghirlando R, Lee MS, Craigie R, Gronenborn AM, Clore GM. Solution structure of the cellular factor baf responsible for protecting retroviral dna from autointegration Nature Structural Biology. 5: 903-909. PMID 9783751 DOI: 10.1038/2345 |
0.413 |
|
| 1998 |
Clore GM, Murphy EC, Gronenborn AM, Bax A. Determination of Three-Bond 1H3′-31P Couplings in Nucleic Acids and Protein-Nucleic Acid Complexes by Quantitative J Correlation Spectroscopy Journal of Magnetic Resonance. 134: 164-167. PMID 9740744 DOI: 10.1006/Jmre.1998.1513 |
0.323 |
|
| 1998 |
Caffrey M, Cai M, Kaufman J, Stahl SJ, Wingfield PT, Covell DG, Gronenborn AM, Clore GM. Three-dimensional solution structure of the 44 kDa ectodomain of SIV gp41 Embo Journal. 17: 4572-4584. PMID 9707417 DOI: 10.1093/Emboj/17.16.4572 |
0.409 |
|
| 1998 |
Bewley CA, Gustafson KR, Boyd MR, Covell DG, Bax A, Clore GM, Gronenborn AM. Solution structure of cyanovirin-N, a potent HIV-inactivating protein Nature Structural Biology. 5: 571-578. PMID 9665171 DOI: 10.1038/828 |
0.476 |
|
| 1998 |
Clore GM, Gronenborn AM, Bax A. A Robust Method for Determining the Magnitude of the Fully Asymmetric Alignment Tensor of Oriented Macromolecules in the Absence of Structural Information Journal of Magnetic Resonance. 133: 216-221. PMID 9654491 DOI: 10.1006/Jmre.1998.1419 |
0.392 |
|
| 1998 |
Clore GM, Gronenborn AM. New methods of structure refinement for macromolecular structure determination by NMR Proceedings of the National Academy of Sciences of the United States of America. 95: 5891-5898. PMID 9600889 DOI: 10.1073/Pnas.95.11.5891 |
0.41 |
|
| 1998 |
Clore GM, Gronenborn AM, Tjandra N. Direct Structure Refinement against Residual Dipolar Couplings in the Presence of Rhombicity of Unknown Magnitude Journal of Magnetic Resonance. 131: 159-162. PMID 9533920 DOI: 10.1006/Jmre.1997.1345 |
0.394 |
|
| 1998 |
Starich MR, Wikström M, Schumacher S, Arst HN, Gronenborn AM, Clore GM. 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 Journal of Molecular Biology. 277: 621-634. PMID 9533884 DOI: 10.1006/Jmbi.1997.1626 |
0.399 |
|
| 1998 |
Starich MR, Wikström M, Arst HN, Clore GM, Gronenborn AM. The solution structure of a fungal AREA protein-DNA complex: An alternative binding mode for the basic carboxyl tail of GATA factors Journal of Molecular Biology. 277: 605-620. PMID 9533883 DOI: 10.1006/Jmbi.1998.1625 |
0.386 |
|
| 1998 |
Clore GM, Gronenborn AM. Determining the structures of large proteins and protein complexes by NMR Trends in Biotechnology. 16: 22-34. PMID 9470228 DOI: 10.1016/S0167-7799(97)01135-9 |
0.444 |
|
| 1998 |
Kuszewski J, Gronenborn AM, Clore GM. Improvements and extensions in the conformational database potential for the refinement of NMR and X-ray structures of proteins and nucleic acids. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 125: 171-7. PMID 9245376 DOI: 10.1006/Jmre.1997.1116 |
0.316 |
|
| 1998 |
Clore GM, Starich MR, Gronenborn AM. Measurement of residual dipolar couplings of macromolecules aligned in the nematic phase of a colloidal suspension of rod-shaped viruses [15] Journal of the American Chemical Society. 120: 10571-10572. DOI: 10.1021/Ja982592F |
0.345 |
|
| 1998 |
Garrett DS, Seok YJ, Peterkofsky A, Clore GM, Gronenborn AM. Tautomeric state and pK(a4) of the phosphorylated active site histidine in the N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system Protein Science. 7: 789-793. DOI: 10.1002/Pro.5560070329 |
0.338 |
|
| 1997 |
Werner MH, Clore GM, Fisher CL, Fisher RJ, Trinh L, Shiloach J, Gronenborn AM. Correction of the NMR structure of the ETS1/DNA complex Journal of Biomolecular Nmr. 10: 317-328. PMID 9460239 DOI: 10.1023/A:1018399711996 |
0.405 |
|
| 1997 |
Schumacher S, Clubb RT, Cai M, Mizuuchi K, Clore GM, Gronenborn AM. Solution structure of the Mu end DNA-binding ibeta subdomain of phage Mu transposase: modular DNA recognition by two tethered domains. The Embo Journal. 16: 7532-41. PMID 9405381 DOI: 10.1093/Emboj/16.24.7532 |
0.412 |
|
| 1997 |
Huth JR, Bewley CA, Jackson BM, Hinnebusch AG, Clore GM, Gronenborn AM. Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR Protein Science. 6: 2359-2364. PMID 9385638 DOI: 10.1002/Pro.5560061109 |
0.422 |
|
| 1997 |
Clore GM, Gronenborn AM. NMR structures of proteins and protein complexes beyond 20,000 M(r) Nature Structural Biology. 4: 849-853. PMID 9377157 |
0.315 |
|
| 1997 |
Clubb RT, Schumacher S, Mizuuchi K, Gronenborn AM, Clore GM. Solution structure of the I gamma subdomain of the Mu end DNA-binding domain of phage Mu transposase. Journal of Molecular Biology. 273: 19-25. PMID 9367742 DOI: 10.1006/Jmbi.1997.1312 |
0.404 |
|
| 1997 |
Tjandra N, Omichinski JG, Gronenborn AM, Marius Clore G, Bax A. Use of dipolar 1H-15N and 1H-13C couplings in the structure determination of magnetically oriented macromolecules in solution Nature Structural Biology. 4: 732-738. PMID 9303001 DOI: 10.1038/Nsb0997-732 |
0.373 |
|
| 1997 |
Caffrey M, Cai M, Kaufman J, Stahl SJ, Wingfield PT, Gronenborn AM, Clore GM. 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 Journal of Molecular Biology. 271: 819-826. PMID 9299329 DOI: 10.1006/Jmbi.1997.1217 |
0.438 |
|
| 1997 |
Wingfield PT, Stahl SJ, Kaufman J, Zlotnick A, Hyde CC, Gronenborn AM, Clore GM. The extracellular domain of immunodeficiency virus gp41 protein: Expression in Escherichia coli, purification, and crystallization Protein Science. 6: 1653-1660. PMID 9260278 DOI: 10.1002/Pro.5560060806 |
0.373 |
|
| 1997 |
Huth JR, Bewley CA, Nissen MS, Evans JNS, Reeves R, Gronenborn AM, Clore GM. The solution structure of an HMG-I(Y)-DNA complex defines a new architectural minor groove binding motif Nature Structural Biology. 4: 657-665. PMID 9253416 DOI: 10.1038/Nsb0897-657 |
0.388 |
|
| 1997 |
Cai M, Zheng R, Caffrey M, Craigie R, Clore GM, Gronenborn AM. Solution structure of the N-terminal zinc binding domain of HIV-1 integrase. Nature Structural Biology. 4: 567-77. PMID 9228950 DOI: 10.1038/Nsb0797-567 |
0.471 |
|
| 1997 |
Tjandra N, Garrett DS, Gronenborn AM, Bax A, Clore GM. Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy Nature Structural Biology. 4: 443-449. PMID 9187651 DOI: 10.1038/Nsb0697-443 |
0.396 |
|
| 1997 |
Pedone PV, Omichinski JG, Nony P, Trainor C, Gronenborn AM, Clore GM, Felsenfeld G. The N-terminal fingers of chicken GATA-2 and GATA-3 are independent sequence-specific DNA binding domains. The Embo Journal. 16: 2874-82. PMID 9184231 DOI: 10.1093/Emboj/16.10.2874 |
0.366 |
|
| 1997 |
Garrett DS, Seok YJ, Liao DI, Peterkofsky A, Gronenborn AM, Clore GM. 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: 2517-30. PMID 9054557 DOI: 10.1021/Bi962924Y |
0.447 |
|
| 1997 |
Omichinski JG, Pedone PV, Felsenfeld G, Gronenborn AM, Clore GM. The solution structure of a specific GAGA factor-DNA complex reveals a modular binding mode. Nature Structural Biology. 4: 122-32. PMID 9033593 DOI: 10.1038/Nsb0297-122 |
0.385 |
|
| 1997 |
Clore GM, Gronenborn AM. Dissecting intrinsic chaperonin activity. Proceedings of the National Academy of Sciences of the United States of America. 94: 7-8. PMID 8990150 DOI: 10.1073/Pnas.94.1.7 |
0.379 |
|
| 1997 |
Gronenborn AM, Frank MK, Clore GM. Core mutants of the immunoglobulin binding domain of streptococcal protein G: stability and structural integrity. Febs Letters. 398: 312-6. PMID 8977129 DOI: 10.1016/S0014-5793(96)01262-8 |
0.386 |
|
| 1997 |
Cai M, Zheng R, Caffrey M, Craigie R, Clore GM, Gronenborn AM. Erratum: Solution structure of the N-terminal zinc binding domain of HIV-1 integrase (Nature Structural Biology (July 1997) 4 (567-577)) Nature Structural & Molecular Biology. 4. DOI: 10.1038/Nsb1097-839 |
0.419 |
|
| 1996 |
Miller M, Lubkowski J, Rao JKM, Danishefsky AT, Omichinski JG, Sakaguchi K, Sakamoto H, Appella E, Gronenborn AM, Clore GM. The oligomerization domain of p53: Crystal structure of the trigonal form Febs Letters. 399: 166-170. PMID 8980144 DOI: 10.1016/S0014-5793(96)01231-8 |
0.358 |
|
| 1996 |
Gronenborn AM, Clore GM. Rapid screening for structural integrity of expressed proteins by heteronuclear NMR spectroscopy. Protein Science : a Publication of the Protein Society. 5: 174-7. PMID 8771212 DOI: 10.1002/Pro.5560050123 |
0.41 |
|
| 1996 |
Kuszewski J, Gronenborn AM, Clore GM. Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases. Protein Science : a Publication of the Protein Society. 5: 1067-80. PMID 8762138 DOI: 10.1107/S0108767396077070 |
0.424 |
|
| 1996 |
Qin J, Clore GM, Kennedy WP, Kuszewski J, Gronenborn AM. The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal. Structure (London, England : 1993). 4: 613-20. PMID 8736558 DOI: 10.1016/S0969-2126(96)00065-2 |
0.324 |
|
| 1996 |
Kuszewski J, Gronenborn AM, Clore GM. A potential involving multiple proton chemical-shift restraints for nonstereospecifically assigned methyl and methylene protons. Journal of Magnetic Resonance. Series B. 112: 79-81. PMID 8661311 DOI: 10.1006/Jmrb.1996.0113 |
0.365 |
|
| 1996 |
Werner MH, Gronenborn AM, Clore GM. Intercalation, DNA kinking, and the control of transcription. Science (New York, N.Y.). 271: 778-84. PMID 8628992 DOI: 10.1126/Science.271.5250.778 |
0.335 |
|
| 1996 |
Trainor CD, Omichinski JG, Vandergon TL, Gronenborn AM, Clore GM, Felsenfeld G. A palindromic regulatory site within vertebrate GATA-1 promoters requires both zinc fingers of the GATA-1 DNA-binding domain for high-affinity interaction. Molecular and Cellular Biology. 16: 2238-47. PMID 8628290 DOI: 10.1128/Mcb.16.5.2238 |
0.345 |
|
| 1996 |
Pedone PV, Ghirlando R, Clore GM, Gronenborn AM, Felsenfeld G, Omichinski JG. The single Cys2-His2 zinc finger domain of the GAGA protein flanked by basic residues is sufficient for high-affinity specific DNA binding. Proceedings of the National Academy of Sciences of the United States of America. 93: 2822-6. PMID 8610125 DOI: 10.1073/Pnas.93.7.2822 |
0.386 |
|
| 1996 |
Grzesiek S, Bax A, Clore GM, Gronenborn AM, Hu JS, Kaufman J, Palmer I, Stahl SJ, Wingfield PT. 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. Nature Structural Biology. 3: 340-5. PMID 8599760 DOI: 10.1038/Nsb0496-340 |
0.453 |
|
| 1996 |
Strzelecka TE, Clore GM, Gronenborn AM. The solution structure of the Mu Ner protein reveals a helix-turn-helix DNA recognition motif. Structure (London, England : 1993). 3: 1087-95. PMID 8590003 DOI: 10.1016/S0969-2126(01)00244-1 |
0.392 |
|
| 1996 |
Frank MK, Clore GM, Gronenborn AM. Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal protein G by multidimensional heteronuclear NMR spectroscopy. Protein Science : a Publication of the Protein Society. 4: 2605-15. PMID 8580852 DOI: 10.1002/Pro.5560041218 |
0.425 |
|
| 1996 |
Clubb RT, Mizuuchi M, Huth JR, Omichinski JG, Savilahti H, Mizuuchi K, Clore GM, Gronenborn AM. The wing of the enhancer-binding domain of Mu phage transposase is flexible and is essential for efficient transposition. Proceedings of the National Academy of Sciences of the United States of America. 93: 1146-50. PMID 8577730 DOI: 10.1073/Pnas.93.3.1146 |
0.41 |
|
| 1996 |
Gronenborn AM, Clore GM. Structures of protein complexes by multidimensional heteronuclear magnetic resonance spectroscopy. Critical Reviews in Biochemistry and Molecular Biology. 30: 351-85. PMID 8575189 DOI: 10.3109/10409239509083489 |
0.405 |
|
| 1996 |
Qin J, Clore GM, Gronenborn AM. 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: 7-13. PMID 8555200 DOI: 10.1021/Bi952299H |
0.327 |
|
| 1996 |
Werner MH, Clore M, Fisher CL, Fisher RJ, Trinh L, Shiloach J, Gronenborn AM. The solution structure of the human ETS1-DNA complex reveals a novel mode of binding and true side chain intercalation. Cell. 83: 761-71. PMID 8521493 DOI: 10.1016/0092-8674(95)90189-2 |
0.38 |
|
| 1995 |
Gronenborn AM, Clore GM. Where is NMR taking us? Proteins. 19: 273-6. PMID 7984623 DOI: 10.1002/Prot.340190402 |
0.33 |
|
| 1995 |
Ernst JA, Clubb RT, Zhou HX, Gronenborn AM, Clore GM. Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR. Science (New York, N.Y.). 267: 1813-7. PMID 7892604 DOI: 10.1126/Science.7892604 |
0.316 |
|
| 1995 |
Clore GM, Omichinski JG, Sakaguchi K, Zambrano N, Sakamoto H, Appella E, Gronenborn AM. Interhelical angles in the solution structure of the oligomerization domain of p53: Correction Science. 267: 1515-1516. PMID 7878474 DOI: 10.1126/Science.7878474 |
0.327 |
|
| 1995 |
Kuszewski J, Qin J, Gronenborn AM, Clore GM. The impact of direct refinement against 13C alpha and 13C beta chemical shifts on protein structure determination by NMR. Journal of Magnetic Resonance. Series B. 106: 92-6. PMID 7850178 DOI: 10.1006/Jmrb.1995.1017 |
0.346 |
|
| 1995 |
Clore GM, Gronenborn AM. Three-dimensional structures of alpha and beta chemokines. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 9: 57-62. PMID 7821760 DOI: 10.1096/Fasebj.9.1.7821760 |
0.314 |
|
| 1995 |
Clore GM, Ernst J, Clubb R, Omichinski JG, Poindexter Kennedy WM, Sakaguchi K, Appella E, Gronenborn AM. Refined solution structure of the oligomerization domain of the tumour suppressor p53 Nature Structural Biology. 2: 321-333. PMID 7796267 DOI: 10.1038/Nsb0495-321 |
0.406 |
|
| 1995 |
Qin J, Clore GM, Kennedy WP, Huth JR, Gronenborn AM. Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NFκB Structure. 3: 289-297. PMID 7788295 DOI: 10.1016/S0969-2126(01)00159-9 |
0.359 |
|
| 1995 |
Kuszewski J, Gronenborn AM, Clore GM. The impact of direct refinement against proton chemical shifts on protein structure determination by NMR. Journal of Magnetic Resonance. Series B. 107: 293-7. PMID 7788102 DOI: 10.1006/Jmrb.1995.1093 |
0.399 |
|
| 1995 |
Werner MH, Huth JR, Gronenborn AM, Clore GM. Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex. Cell. 81: 705-14. PMID 7774012 DOI: 10.1016/0092-8674(95)90532-4 |
0.392 |
|
| 1995 |
Kuszewski J, Clore GM, Gronenborn AM. Fast folding of a prototypic polypeptide: the immunoglobulin binding domain of streptococcal protein G. Protein Science : a Publication of the Protein Society. 3: 1945-52. PMID 7703841 DOI: 10.1002/Pro.5560031106 |
0.384 |
|
| 1995 |
Clubb RT, Omichinski JG, Sakaguchi K, Appella E, Gronenborn AM, Clore GM. Backbone dynamics of the oligomerization domain of p53 determined from 15N NMR relaxation measurements. Protein Science : a Publication of the Protein Society. 4: 855-62. PMID 7663341 DOI: 10.1002/Pro.5560040505 |
0.371 |
|
| 1995 |
Lodi PJ, Ernst JA, Kuszewski J, Hickman AB, Engelman A, Craigie R, Clore GM, Gronenborn AM. Solution structure of the DNA binding domain of HIV-1 integrase. Biochemistry. 34: 9826-33. PMID 7632683 DOI: 10.1021/Bi00031A002 |
0.393 |
|
| 1995 |
Balagurumoorthy P, Sakamoto H, Lewis MS, Zambrano N, Clore GM, Gronenborn AM, Appella E, Harrington RE. Four p53 DNA-binding domain peptides bind natural p53-response elements and bend the DNA. Proceedings of the National Academy of Sciences of the United States of America. 92: 8591-5. PMID 7567980 DOI: 10.1073/Pnas.92.19.8591 |
0.333 |
|
| 1995 |
Makhatadze GI, Clore GM, Gronenborn AM. Solvent isotope effect and protein stability Nature Structural Biology. 2: 852-855. PMID 7552708 DOI: 10.1038/Nsb1095-852 |
0.317 |
|
| 1995 |
Kraulis P, Clore G, Nilges M, Jones A, Petterson G, Knowles J, Gronenborn A. Determination of the Three-Dimensional Solution Structure of the C-Terminal Domain of CellobiohydrolOCe I from Trichodermi reesi. A Study using NMR and Hybrid distance Geometry-Dynamical Simulated Annealing. Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr192 |
0.378 |
|
| 1994 |
Werner MH, Clore GM, Gronenborn AM, Kondoh A, Fisher RJ. Refolding proteins by gel filtration chromatography Febs Letters. 345: 125-130. PMID 8200443 DOI: 10.1016/0014-5793(94)00401-3 |
0.379 |
|
| 1994 |
Barchi JJ, Grasberger B, Gronenborn AM, Clore GM. 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 Science. 3: 15-21. PMID 8142892 DOI: 10.1002/Pro.5560030103 |
0.427 |
|
| 1994 |
Lodi PJ, Garrett DS, Kuszewski J, Tsang ML, Weatherbee JA, Leonard WJ, Gronenborn AM, Clore GM. High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR. Science (New York, N.Y.). 263: 1762-7. PMID 8134838 DOI: 10.1126/Science.8134838 |
0.329 |
|
| 1994 |
Garrett DS, Lodi PJ, Shamoo Y, Williams KR, Clore GM, Gronenborn AM. 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: 2852-8. PMID 8130198 DOI: 10.1021/Bi00176A015 |
0.379 |
|
| 1994 |
Clore GM, Bax A, Omichinski JG, Gronenborn AM. Localization of bound water in the solution structure of a complex of the erythroid transcription factor GATA-1 with DNA Structure. 2: 89-94. PMID 8081746 DOI: 10.1016/S0969-2126(00)00011-3 |
0.355 |
|
| 1994 |
Rozwarski DA, Gronenborn AM, Clore GM, Bazan JF, Bohm A, Wlodawer A, Hatada M, Karplus PA. Structural comparisons among the short-chain helical cytokines Structure. 2: 159-173. PMID 8069631 DOI: 10.1016/S0969-2126(00)00018-6 |
0.37 |
|
| 1994 |
Garrett DS, Kuszewski J, Hancock TJ, Lodi PJ, Vuister GW, Gronenborn AM, Clore GM. The impact of direct refinement against three-bond HN-C alpha H coupling constants on protein structure determination by NMR. Journal of Magnetic Resonance. Series B. 104: 99-103. PMID 8025816 DOI: 10.1006/Jmrb.1994.1061 |
0.357 |
|
| 1994 |
Clore GM, Omichinski JG, Sakaguchi K, Zambrano N, Sakamoto H, Appella E, Gronenborn AM. High-resolution structure of the oligomerization domain of p53 by multidimensional NMR Science. 265: 386-391. PMID 8023159 DOI: 10.1126/Science.8023159 |
0.408 |
|
| 1994 |
Clore GM, Gronenborn AM. Young Investigator Award Lecture. Structures of larger proteins, protein-ligand and protein-DNA complexes by multidimensional heteronuclear NMR. Protein Science : a Publication of the Protein Society. 3: 372-90. PMID 8019409 DOI: 10.1002/Pro.5560030302 |
0.416 |
|
| 1994 |
Gronenborn AM, Clore GM. Identification of N-terminal helix capping boxes by means of 13C chemical shifts. Journal of Biomolecular Nmr. 4: 455-8. PMID 8019146 DOI: 10.1007/Bf00179351 |
0.351 |
|
| 1994 |
Wang AC, Lodi PJ, Qin J, Vuister GW, Gronenborn AM, Clore GM. An efficient triple-resonance experiment for proton-directed sequential backbone assignment of medium-sized proteins. Journal of Magnetic Resonance. Series B. 105: 196-8. PMID 7952935 DOI: 10.1006/Jmrb.1994.1123 |
0.32 |
|
| 1994 |
Clore GM, Gronenborn AM. Structures of larger proteins, protein-ligand and protein-DNA complexes by multi-dimensional heteronuclear NMR. Progress in Biophysics & Molecular Biology. 62: 153-184. PMID 7938541 DOI: 10.1016/0079-6107(94)90010-8 |
0.385 |
|
| 1994 |
Werner MH, Clore GM, Gronenborn AM, Nash HA. Symmetry and asymmetry in the function of Escherichia coli integration host factor: implications for target identification by DNA-binding proteins. Current Biology : Cb. 4: 477-87. PMID 7922368 DOI: 10.1016/S0960-9822(00)00108-1 |
0.353 |
|
| 1994 |
Grasberger BL, Clore GM, Gronenborn AM. High-resolution structure of Ascaris trypsin inhibitor in solution: direct evidence for a pH-induced conformational transition in the reactive site. Structure (London, England : 1993). 2: 669-78. PMID 7922043 DOI: 10.1016/S0969-2126(00)00067-8 |
0.326 |
|
| 1994 |
Qin J, Clore GM, Gronenborn AM. The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin. Structure (London, England : 1993). 2: 503-22. PMID 7922028 DOI: 10.1016/S0969-2126(00)00051-4 |
0.314 |
|
| 1994 |
Clubb RT, Omichinski JG, Savilahti H, Mizuuchi K, Gronenborn AM, Clore GM. A novel class of winged helix-turn-helix protein: the DNA-binding domain of Mu transposase. Structure (London, England : 1993). 2: 1041-8. PMID 7881904 DOI: 10.1016/S0969-2126(94)00107-3 |
0.431 |
|
| 1993 |
Sakaguchi K, Zambrano N, Baldwin ET, Shapiro BA, Erickson JW, Omichinski JG, Clore GM, Gronenborn AM, Appella E. Identification of a binding site for the human immunodeficiency virus type 1 nucleocapsid protein Proceedings of the National Academy of Sciences of the United States of America. 90: 5219-5223. PMID 8506369 DOI: 10.1073/Pnas.90.11.5219 |
0.324 |
|
| 1993 |
Clore GM, Robien MA, Gronenborn AM. Exploring the limits of precision and accuracy of protein structures determined by nuclear magnetic resonance spectroscopy. Journal of Molecular Biology. 231: 82-102. PMID 8496968 DOI: 10.1006/Jmbi.1993.1259 |
0.413 |
|
| 1993 |
Varley P, Gronenborn AM, Christensen H, Wingfield PT, Pain RH, Clore GM. Kinetics of folding of the all-beta sheet protein interleukin-1 beta. Science (New York, N.Y.). 260: 1110-3. PMID 8493553 DOI: 10.1126/Science.8493553 |
0.341 |
|
| 1993 |
Omichinski JG, Trainor C, Evans T, Gronenborn AM, Clore GM, Felsenfeld G. A small single-"finger" peptide from the erythroid transcription factor GATA-1 binds specifically to DNA as a zinc or iron complex. Proceedings of the National Academy of Sciences of the United States of America. 90: 1676-80. PMID 8446581 DOI: 10.1073/Pnas.90.5.1676 |
0.359 |
|
| 1993 |
Omichinski JG, Clore GM, Schaad O, Felsenfeld G, Trainor C, Appella E, Stahl SJ, Gronenborn AM. NMR structure of a specific DNA complex of Zn-containing DNA binding domain of GATA-1. Science (New York, N.Y.). 261: 438-46. PMID 8332909 DOI: 10.1126/Science.8332909 |
0.406 |
|
| 1993 |
Brünger AT, Clore GM, Gronenborn AM, Saffrich R, Nilges M. Assessing the quality of solution nuclear magnetic resonance structures by complete cross-validation. Science (New York, N.Y.). 261: 328-31. PMID 8332897 DOI: 10.1126/Science.8332897 |
0.334 |
|
| 1993 |
Powers R, Garrett DS, March CJ, Frieden EA, Gronenborn AM, Clore GM. The high-resolution, three-dimensional solution structure of human interleukin-4 determined by multidimensional heteronuclear magnetic resonance spectroscopy. Biochemistry. 32: 6744-62. PMID 8329398 DOI: 10.1021/bi00077a030 |
0.301 |
|
| 1993 |
Clore G, Bax A, Ikura M, Gronenborn AM. Structure of calmodulin-target peptide complexes Current Opinion in Structural Biology. 3: 838-845. DOI: 10.1016/0959-440X(93)90146-C |
0.372 |
|
| 1993 |
Powers R, Clore G, Garrett D, Gronenborn A. Relationships Between the Precision of High-Resolution Protein NMR Structures, Solution-Order Parameters, and Crystallographic B Factors Journal of Magnetic Resonance, Series B. 101: 325-327. DOI: 10.1006/Jmrb.1993.1051 |
0.346 |
|
| 1993 |
Clore G, Gronenborn AM. Structural Studies of InterIeukin-1β, Interleukin-4, and lnterleukin-8 Immunomethods. 3: 56-81. DOI: 10.1006/Immu.1993.1040 |
0.309 |
|
| 1993 |
Gronenborn AM, Clore G. Structural Studies of Immunoglobulin-Binding Domains of Streptococcal Protein G Immunomethods. 2: 3-8. DOI: 10.1006/Immu.1993.1002 |
0.427 |
|
| 1992 |
Clore GM, Bax A, Gronenborn AM. Stereospecific assignment of beta-methylene protons in larger proteins using 3D 15N-separated Hartmann-Hahn and 13C-separated rotating frame Overhauser spectroscopy. Journal of Biomolecular Nmr. 1: 13-22. PMID 1668718 DOI: 10.1007/Bf01874566 |
0.32 |
|
| 1992 |
Powers R, Garrett DS, March CJ, Frieden EA, Gronenborn AM, Clore GM. Three-dimensional solution structure of human interleukin-4 by multidimensional heteronuclear magnetic resonance spectroscopy. Science (New York, N.Y.). 256: 1673-7. PMID 1609277 DOI: 10.1126/Science.256.5064.1673 |
0.403 |
|
| 1992 |
Ikura M, Clore GM, Gronenborn AM, Zhu G, Klee CB, Bax A. Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science (New York, N.Y.). 256: 632-8. PMID 1585175 DOI: 10.1126/Science.1585175 |
0.389 |
|
| 1992 |
Garrett DS, Powers R, March CJ, Frieden EA, Clore GM, Gronenborn AM. Determination of the secondary structure and folding topology of human interleukin-4 using three-dimensional heteronuclear magnetic resonance spectroscopy. Biochemistry. 31: 4347-53. PMID 1567881 DOI: 10.1021/Bi00132A027 |
0.369 |
|
| 1992 |
Powers R, Garrett DS, March CJ, Frieden EA, Gronenborn AM, Clore GM. 1H, 15N, 13C, and 13CO assignments of human interleukin-4 using three-dimensional double- and triple-resonance heteronuclear magnetic resonance spectroscopy. Biochemistry. 31: 4334-46. PMID 1567880 DOI: 10.1021/Bi00132A026 |
0.342 |
|
| 1992 |
Omichinski JG, Clore GM, Robien M, Sakaguchi K, Appella E, Gronenborn AM. High-resolution solution structure of the double Cys2His2 zinc finger from the human enhancer binding protein MBP-1 Biochemistry. 31: 3907-3917. PMID 1567844 DOI: 10.1021/Bi00131A004 |
0.448 |
|
| 1992 |
Robien MA, Clore GM, Omichinski JG, Perham RN, Appella E, Sakaguchi K, Gronenborn AM. 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: 3463-71. PMID 1554728 DOI: 10.1021/Bi00128A021 |
0.408 |
|
| 1992 |
Forman-Kay JD, Clore GM, Gronenborn AM. Relationship between electrostatics and redox function in human thioredoxin: Characterization of pH titration shifts using two-dimensional homo- and heteronuclear NMR Biochemistry. 31: 3442-3452. PMID 1554726 DOI: 10.1021/Bi00128A019 |
0.365 |
|
| 1992 |
Clore GM, Gronenborn AM. 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. Journal of Molecular Biology. 223: 853-6. PMID 1538400 DOI: 10.1016/0022-2836(92)90247-H |
0.371 |
|
| 1992 |
Shaanan B, Gronenborn AM, Cohen GH, Gilliland GL, Veerapandian B, Davies DR, Clore GM. Combining experimental information from crystal and solution studies: Joint X-ray and NMR refinement Science. 257: 961-964. PMID 1502561 DOI: 10.1126/Science.1502561 |
0.357 |
|
| 1992 |
Forman-Kay JD, Clore GM, Stahl SJ, Gronenborn AM. 1H and 15N resonance assignments and secondary structure of the human thioredoxin C62A, C69A, C73A mutant. Journal of Biomolecular Nmr. 2: 431-45. PMID 1422155 DOI: 10.1007/Bf02192807 |
0.355 |
|
| 1992 |
Achari A, Hale SP, Howard AJ, Clore GM, Gronenborn AM, Hardman KD, Whitlow M. 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: 10449-57. PMID 1420164 DOI: 10.1021/Bi00158A006 |
0.414 |
|
| 1992 |
Powers R, Clore GM, Stahl SJ, Wingfield PT, Gronenborn A. Analysis of the backbone dynamics of the ribonuclease H domain of the human immunodeficiency virus reverse transcriptase using 15N relaxation measurements. Biochemistry. 31: 9150-7. PMID 1382587 DOI: 10.1021/Bi00153A006 |
0.373 |
|
| 1992 |
Grzesiek S, Ikura M, Marius Clore G, Gronenborn AM, Bax A. A 3D triple-resonance NMR technique for qualitative measurement of carbonyl-Hβ J couplings in isotopically enriched proteins Journal of Magnetic Resonance (1969). 96: 215-221. DOI: 10.1016/0022-2364(92)90307-S |
0.315 |
|
| 1992 |
Omichinski JG, Sakaguchi K, Clore GM, Gronenborn AM, Appella E. High-resolution structure of a double zinc finger from the human enhancer binding protein MPB-1 in solution Journal of Protein Chemistry. 11: 408-409. DOI: 10.1007/Bf01673767 |
0.384 |
|
| 1991 |
Clore GM, Bax A, Driscoll PC, Wingfield PT, Gronenborn AM. 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: 8172-84. PMID 2261471 DOI: 10.1021/Bi00487A027 |
0.34 |
|
| 1991 |
Clore GM, Gronenborn AM. Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy. Science (New York, N.Y.). 252: 1390-9. PMID 2047852 DOI: 10.1126/Science.2047852 |
0.433 |
|
| 1991 |
Clore GM, Gronenborn AM. Comparison of the solution nuclear magnetic resonance and crystal structures of interleukin-8. Possible implications for the mechanism of receptor binding. Journal of Molecular Biology. 217: 611-20. PMID 2005614 DOI: 10.1016/0022-2836(91)90518-B |
0.422 |
|
| 1991 |
Clore GM, Wingfield PT, Gronenborn AM. High-resolution three-dimensional structure of interleukin 1 beta in solution by three- and four-dimensional nuclear magnetic resonance spectroscopy. Biochemistry. 30: 2315-23. PMID 2001363 DOI: 10.1021/Bi00223A005 |
0.363 |
|
| 1991 |
Forman-Kay JD, Clore GM, Wingfield PT, Gronenborn AM. High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution Biochemistry®. 30: 2685-2698. PMID 2001356 DOI: 10.1021/Bi00224A017 |
0.437 |
|
| 1991 |
Baldwin ET, Weber IT, St Charles R, Xuan JC, Appella E, Yamada M, Matsushima K, Edwards BF, Clore GM, Gronenborn AM. Crystal structure of interleukin 8: symbiosis of NMR and crystallography. Proceedings of the National Academy of Sciences of the United States of America. 88: 502-6. PMID 1988949 DOI: 10.1073/Pnas.88.2.502 |
0.396 |
|
| 1991 |
Clore GM, Kay LE, Bax A, Gronenborn AM. Four-dimensional 13C/13C-edited nuclear Overhauser enhancement spectroscopy of a protein in solution: application to interleukin 1 beta. Biochemistry. 30: 12-8. PMID 1988012 DOI: 10.1021/Bi00215A002 |
0.363 |
|
| 1991 |
Omichinski JG, Clore GM, Sakaguchi K, Appella E, Gronenborn AM. 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 Letters. 292: 25-30. PMID 1959614 DOI: 10.1016/0014-5793(91)80825-N |
0.421 |
|
| 1991 |
Clore GM, Gronenborn AM. Comparison of the solution nuclear magnetic resonance and X-ray crystal structures of human recombinant interleukin-1 beta. Journal of Molecular Biology. 221: 47-53. PMID 1920417 DOI: 10.1016/0022-2836(91)80202-6 |
0.322 |
|
| 1991 |
Gronenborn AM, Filpula DR, Essig NZ, Achari A, Whitlow M, Wingfield PT, Clore GM. A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G. Science (New York, N.Y.). 253: 657-61. PMID 1871600 DOI: 10.1126/Science.1871600 |
0.383 |
|
| 1991 |
Gronenborn AM, Clore GM. 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 Engineering. 4: 263-9. PMID 1857712 DOI: 10.1093/Protein/4.3.263 |
0.399 |
|
| 1991 |
Forman-Kay JD, Gronenborn AM, Wingfield PT, Clore GM. Determination of the positions of bound water molecules in the solution structure of reduced human thioredoxin by heteronuclear three-dimensional nuclear magnetic resonance spectroscopy Journal of Molecular Biology. 220: 209-216. PMID 1856855 DOI: 10.1016/0022-2836(91)90004-P |
0.336 |
|
| 1991 |
Powers R, Clore GM, Bax A, Garrett DS, Stahl SJ, Wingfield PT, Gronenborn AM. 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. Journal of Molecular Biology. 221: 1081-90. PMID 1719214 DOI: 10.1016/0022-2836(91)90920-2 |
0.463 |
|
| 1991 |
Clore GM, Omichinski JG, Gronenborn AM. Slow conformational dynamics at the metal coordination site of a zinc finger Journal of the American Chemical Society. 113: 4350-4351. DOI: 10.1021/Ja00011A059 |
0.41 |
|
| 1991 |
Clore GM, Driscoll PC, Wingfield PT, Gronenborn AM. 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: 312-312. DOI: 10.1021/Bi00215A043 |
0.31 |
|
| 1991 |
Clore G, Gronenborn AM. Applications of three- and four-dimensional heteronuclear NMR spectroscopy to protein structure determination Progress in Nuclear Magnetic Resonance Spectroscopy. 23: 43-92. DOI: 10.1016/0079-6565(91)80002-J |
0.408 |
|
| 1991 |
Powers R, Gronenborn AM, Marius Clore G, Bax A. Three-dimensional triple-resonance NMR of 13C/15N-enriched proteins using constant-time evolution Journal of Magnetic Resonance (1969). 94: 209-213. DOI: 10.1016/0022-2364(91)90312-H |
0.316 |
|
| 1990 |
Clore GM, Driscoll PC, Wingfield PT, Gronenborn AM. Low resolution structure of interleukin-1 beta in solution derived from 1H-15N heteronuclear three-dimensional nuclear magnetic resonance spectroscopy. Journal of Molecular Biology. 214: 811-7. PMID 2388269 DOI: 10.1016/0022-2836(90)90336-K |
0.39 |
|
| 1990 |
Clore GM, Bax A, Wingfield PT, Gronenborn AM. 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: 5671-6. PMID 2383553 DOI: 10.1021/Bi00476A004 |
0.366 |
|
| 1990 |
Kay LE, Clore GM, Bax A, Gronenborn AM. Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 beta in solution. Science (New York, N.Y.). 249: 411-4. PMID 2377896 DOI: 10.1126/Science.2377896 |
0.404 |
|
| 1990 |
Gronenborn AM, Nilges M, Peanasky RJ, Clore GM. Sequential resonance assignment and secondary structure determination of the Ascaris trypsin inhibitor, a member of a novel class of proteinase inhibitors Biochemistry. 29: 183-189. PMID 2322539 DOI: 10.1021/Bi00453A025 |
0.394 |
|
| 1990 |
Omichinski JG, Clore GM, Appella K, Sakaguchi K, Gronenborn AM. High-resolution three-dimensional structure of a single zinc finger from a human enhancer binding protein in solution Biochemistry®. 29: 9324-9334. PMID 2248949 DOI: 10.1021/Bi00492A004 |
0.469 |
|
| 1990 |
Clore GM, Appella E, Yamada M, Matsushima K, Gronenborn AM. Three-dimensional structure of interleukin 8 in solution. Biochemistry. 29: 1689-96. PMID 2184886 DOI: 10.1021/Bi00459A004 |
0.394 |
|
| 1990 |
Nilges M, Clore GM, Gronenborn AM. 1H-NMR stereospecific assignments by conformational data-base searches Biopolymers. 29: 813-822. PMID 2166604 DOI: 10.1002/Bip.360290415 |
0.334 |
|
| 1990 |
Becerra SP, Clore GM, Gronenborn AM, Karlström AR, Stahl SJ, Wilson SH, Wingfield PT. Purification and characterization of the RNase H domain of HIV-1 reverse transcriptase expressed in recombinant Escherichia coli. Febs Letters. 270: 76-80. PMID 1699794 DOI: 10.1016/0014-5793(90)81238-J |
0.381 |
|
| 1990 |
Ikura M, Bax A, Clore GM, Gronenborn AM. Detection of nuclear Overhauser effects between degenerate amide proton resonances by heteronuclear three-dimensional NMR spectroscopy Journal of the American Chemical Society. 112: 9020-9022. DOI: 10.1021/Ja00180A080 |
0.314 |
|
| 1990 |
Bax A, Clore G, Driscoll PC, Gronenborn AM, Ikura M, Kay LE. Practical aspects of proton-carbon-carbon-proton three-dimensional correlation spectroscopy of 13C-labeled proteins Journal of Magnetic Resonance (1969). 87: 620-627. DOI: 10.1016/0022-2364(90)90320-9 |
0.349 |
|
| 1989 |
Clore GM, Gronenborn AM, James MN, Kjaer M, McPhalen CA, Poulsen FM. Comparison of the solution and X-ray structures of barley serine proteinase inhibitor 2. Protein Engineering. 1: 313-8. PMID 3508282 DOI: 10.1093/Protein/1.4.313 |
0.346 |
|
| 1989 |
Clore GM, Gronenborn AM, Kjaer M, Poulsen FM. The determination of the three-dimensional structure of barley serine proteinase inhibitor 2 by nuclear magnetic resonance, distance geometry and restrained molecular dynamics. Protein Engineering. 1: 305-11. PMID 3508281 DOI: 10.1093/Protein/1.4.305 |
0.421 |
|
| 1989 |
Clore GM, Gronenborn AM. Determination of three-dimensional structures of proteins in solution by nuclear magnetic resonance spectroscopy. Protein Engineering. 1: 275-88. PMID 3334087 DOI: 10.1093/Protein/1.4.275 |
0.342 |
|
| 1989 |
Gent ME, Gärtner S, Gronenborn AM, Sandulache R, Clore GM. Site-directed mutants of the cAMP receptor protein--DNA binding of five mutant proteins. Protein Engineering. 1: 201-3. PMID 3333845 DOI: 10.1093/Protein/1.3.201 |
0.336 |
|
| 1989 |
Garin J, Vignais PV, Gronenborn AM, Clore GM, Gao Z, Baeuerlein E. 1H-NMR studies on nucleotide binding to the catalytic sites of bovine mitochondrial F1-ATPase. Febs Letters. 242: 178-82. PMID 2904888 DOI: 10.1016/0014-5793(88)81011-1 |
0.32 |
|
| 1989 |
Forman-Kay JD, Clore GM, Driscoll PC, Wingfield P, Richards FM, Gronenborn AM. A proton nuclear magnetic resonance assignment and secondary structure determination of recombinant human thioredoxin. Biochemistry. 28: 7088-97. PMID 2684271 DOI: 10.1021/Bi00443A045 |
0.408 |
|
| 1989 |
Clore GM, Gronenborn AM. Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy. Critical Reviews in Biochemistry and Molecular Biology. 24: 479-564. PMID 2676353 DOI: 10.3109/10409238909086962 |
0.367 |
|
| 1989 |
Marion D, Driscoll PC, Kay LE, Wingfield PT, Bax A, Gronenborn AM, Clore GM. 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: 6150-6. PMID 2675964 DOI: 10.1021/Bi00441A004 |
0.363 |
|
| 1989 |
Folkers PJ, Clore GM, Driscoll PC, Dodt J, Köhler S, Gronenborn AM. 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: 2601-17. PMID 2567183 DOI: 10.1021/Bi00432A038 |
0.46 |
|
| 1989 |
Driscoll PC, Gronenborn AM, Beress L, Clore GM. 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: 2188-98. PMID 2566326 DOI: 10.1021/Bi00431A033 |
0.422 |
|
| 1989 |
Driscoll PC, Clore GM, Beress L, Gronenborn AM. 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: 2178-87. PMID 2566325 DOI: 10.1021/Bi00431A032 |
0.371 |
|
| 1989 |
Driscoll PC, Gronenborn AM, Clore GM. 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 Letters. 243: 223-33. PMID 2563693 DOI: 10.1016/0014-5793(89)80134-6 |
0.416 |
|
| 1989 |
Kraulis PJ, Clore GM, Nilges M, Jones TA, Pettersson G, Knowles J, Gronenborn AM. 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: 7241-7257. PMID 2554967 DOI: 10.1021/Bi00444A016 |
0.392 |
|
| 1989 |
Gronenborn AM, Bax A, Wingfield PT, Clore GM. A powerful method of sequential proton resonance assignment in proteins using relayed 15N-1H multiple quantum coherence spectroscopy. Febs Letters. 243: 93-8. PMID 2537752 DOI: 10.1016/0014-5793(89)81224-4 |
0.366 |
|
| 1989 |
Wingfield P, Graber P, Shaw AR, Gronenborn AM, Clore GM, MacDonald HR. Preparation, characterization and application of interleukin-1β mutant proteins with surface-accessible cysteine residues European Journal of Biochemistry. 179: 565-571. PMID 2493373 DOI: 10.1111/J.1432-1033.1989.Tb14584.X |
0.375 |
|
| 1989 |
Clore G, Appella E, Yamada M, Matsushima K, Gronenborn A. Determination of the secondary structure of interleukin-8 by nuclear magnetic resonance spectroscopy. Journal of Biological Chemistry. 264: 18907-18911. DOI: 10.13018/Bmr280 |
0.386 |
|
| 1989 |
Oschkinat H, Cieslar C, Holak TA, Marius Clore G, Gronenborn AM. Practical and theoretical aspects of three-dimensional homonuclear Hartmann-Hahn-nuclear overhauser enhancement spectroscopy of proteins Journal of Magnetic Resonance (1969). 83: 450-472. DOI: 10.1016/0022-2364(89)90342-9 |
0.326 |
|
| 1989 |
Oschkinat H, Cieslar C, Gronenborn AM, Clore G. Three-dimensional homonuclear Hartmann-Hahn-nuclear overhauser enhancement spectroscopy in H2O and its application to proteins Journal of Magnetic Resonance (1969). 81: 212-216. DOI: 10.1016/0022-2364(89)90283-7 |
0.33 |
|
| 1988 |
Holak TA, Nilges M, Prestegard JH, Gronenborn AM, Clore GM. 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 European Journal of Biochemistry. 175: 9-15. PMID 3402450 DOI: 10.1111/J.1432-1033.1988.Tb14159.X |
0.433 |
|
| 1988 |
Oschkinat H, Griesinger C, Kraulis PJ, Sørensen OW, Ernst RR, Gronenborn AM, Clore GM. Three-dimensional NMR spectroscopy of a protein in solution. Nature. 332: 374-6. PMID 3352736 DOI: 10.1038/332374A0 |
0.402 |
|
| 1988 |
Meyer EF, Clore GM, Gronenborn AM, Hansen HA. Analysis of an enzyme-substrate complex by X-ray crystallography and transferred nuclear Overhauser enhancement measurements: porcine pancreatic elastase and a hexapeptide. Biochemistry. 27: 725-30. PMID 3349061 DOI: 10.1021/Bi00402A035 |
0.317 |
|
| 1988 |
Nilges M, Clore GM, Gronenborn AM. Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations Febs Letters. 229: 317-324. PMID 3345845 DOI: 10.1016/0014-5793(88)81148-7 |
0.35 |
|
| 1988 |
Zarbock J, Gennaro R, Romeo D, Clore GM, Gronenborn AM. A proton nuclear magnetic resonance study of the conformation of bovine anaphylatoxin C5a in solution. Febs Letters. 238: 289-94. PMID 3262536 DOI: 10.1016/0014-5793(88)80499-X |
0.405 |
|
| 1988 |
Holak TA, Engström A, Kraulis PJ, Lindeberg G, Bennich H, Jones TA, Gronenborn AM, Clore GM. The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study. Biochemistry. 27: 7620-9. PMID 3207693 DOI: 10.1021/bi00420a008 |
0.317 |
|
| 1988 |
Nilges M, Clore GM, Gronenborn AM. 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 Letters. 239: 129-136. PMID 3181419 DOI: 10.1016/0014-5793(88)80559-3 |
0.351 |
|
| 1988 |
Clore GM, Bax A, Wingfield P, Gronenborn AM. 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 Letters. 238: 17-21. PMID 3049156 DOI: 10.1016/0014-5793(88)80216-3 |
0.385 |
|
| 1988 |
Allet B, Payton M, Mattaliano RJ, Gronenborn AM, Clore GM, Wingfield PT. Purification and characterization of the DNA-binding protein Ner of bacteriophage Mu. Gene. 65: 259-68. PMID 2970420 DOI: 10.1016/0378-1119(88)90462-3 |
0.366 |
|
| 1988 |
Gronenborn AM, Wingfield PT, McDonald HR, Schmeissner U, Clore GM. Site directed mutants of human interleukin-1 alpha: a 1H-NMR and receptor binding study. Febs Letters. 231: 135-8. PMID 2966074 DOI: 10.1016/0014-5793(88)80717-8 |
0.38 |
|
| 1988 |
Nilges M, Gronenborn AM, Brünger AT, Clore GM. 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 Engineering. 2: 27-38. PMID 2855369 DOI: 10.1093/Protein/2.1.27 |
0.38 |
|
| 1988 |
Gronenborn AM, Sandulache R, Gärtner S, Clore GM. Mutations in the cyclic AMP binding site of the cyclic AMP receptor protein of Escherichia coli. The Biochemical Journal. 253: 801-7. PMID 2845936 DOI: 10.1042/Bj2530801 |
0.333 |
|
| 1988 |
Clore GM, Nilges M, Brünger A, Gronenborn AM. Determination of the backbone conformation of secretin by restrained molecular dynamics on the basis of interproton distance data. European Journal of Biochemistry / Febs. 171: 479-84. PMID 2831051 DOI: 10.1111/J.1432-1033.1988.Tb13814.X |
0.401 |
|
| 1988 |
Happ CS, Happ E, Clore GM, Gronenborn AM. 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 Letters. 236: 62-70. PMID 2456957 DOI: 10.1016/0014-5793(88)80286-2 |
0.375 |
|
| 1988 |
Happ CS, Happ E, Gronenborn AM, Clore GM. Synthesis and1-NMR Studies of DNA-RNA Hybrids for Structural Analysis Nucleosides and Nucleotides. 7: 733-736. DOI: 10.1080/07328318808056320 |
0.304 |
|
| 1988 |
Cieslar C, Marius Clore G, Gronenborn AM. Computer-aided sequential assignment of protein 1H NMR spectra Journal of Magnetic Resonance (1969). 80: 119-127. DOI: 10.1016/0022-2364(88)90063-7 |
0.354 |
|
| 1987 |
Brünger AT, Campbell RL, Clore GM, Gronenborn AM, Karplus M, Petsko GA, Teeter MM. Solution of a protein crystal structure with a model obtained from NMR interproton distance restraints. Science (New York, N.Y.). 235: 1049-53. PMID 17782253 DOI: 10.1126/Science.235.4792.1049 |
0.407 |
|
| 1987 |
Jansen C, Gronenborn AM, Clore GM. The binding of the cyclic AMP receptor protein to synthetic DNA sites containing permutations in the consensus sequence TGTGA. The Biochemical Journal. 246: 227-32. PMID 3675557 DOI: 10.1042/Bj2460227 |
0.319 |
|
| 1987 |
Clore GM, Sukumaran DK, Gronenborn AM, Teeter MM, Whitlow M, Jones BL. Nuclear magnetic resonance study of the solution structure of alpha 1-purothionin. Sequential resonance assignment, secondary structure and low resolution tertiary structure. Journal of Molecular Biology. 193: 571-8. PMID 3586031 DOI: 10.1016/0022-2836(87)90267-1 |
0.394 |
|
| 1987 |
Gronenborn AM, Clore GM. Overproduction of the cyclic AMP receptor protein of Escherichia coli and expression of the engineered C-terminal DNA-binding domain. The Biochemical Journal. 236: 643-9. PMID 3539103 DOI: 10.1042/Bj2360643 |
0.36 |
|
| 1987 |
Wingfield PT, Mattaliano RJ, MacDonald HR, Craig S, Clore GM, Gronenborn AM, Schmeissner U. Recombinant-derived interleukin-1 alpha stabilized against specific deamidation. Protein Engineering. 1: 413-7. PMID 3509874 DOI: 10.1093/Protein/1.5.413 |
0.323 |
|
| 1987 |
Clore GM, Gronenborn AM, Nilges M, Ryan CA. Three-dimensional structure of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics Biochemistry. 26: 8012-8023. PMID 3427120 DOI: 10.1021/Bi00398A069 |
0.432 |
|
| 1987 |
Gent ME, Gronenborn AM, Davies RW, Clore GM. Probing the sequence-specific interaction of the cyclic AMP receptor protein with DNA by site-directed mutagenesis. The Biochemical Journal. 242: 645-53. PMID 3109398 DOI: 10.1042/Bj2420645 |
0.34 |
|
| 1987 |
Clore GM, Nilges M, Brünger AT, Karplus M, Gronenborn AM. 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 Letters. 213: 269-77. PMID 3030815 DOI: 10.1016/0014-5793(87)81504-1 |
0.394 |
|
| 1987 |
Clore GM, Martin SR, Gronenborn AM. Solution structure of human growth hormone releasing factor. Combined use of circular dichroism and nuclear magnetic resonance spectroscopy. Journal of Molecular Biology. 191: 553-61. PMID 3029387 DOI: 10.1016/0022-2836(86)90147-6 |
0.367 |
|
| 1987 |
Minter SJ, Clore GM, Gronenborn AM, Davies RW. Cooperative DNA binding by lambda integration protein--a key component of specificity. European Journal of Biochemistry. 161: 727-31. PMID 3024982 DOI: 10.1111/J.1432-1033.1986.Tb10500.X |
0.32 |
|
| 1987 |
Wingfield P, Graber P, Movva NR, Gronenborn AM, Clore GM, MacDonald HR. N-terminal-methionylated interleukin-1 beta has reduced receptor-binding affinity. Febs Letters. 215: 160-4. PMID 2952523 DOI: 10.1016/0014-5793(87)80133-3 |
0.385 |
|
| 1987 |
MacDonald HR, Wingfield P, Schmeissner U, Shaw A, Clore GM, Gronenborn AM. Point mutations of human interleukin-1 with decreased receptor binding affinity. Febs Letters. 209: 295-8. PMID 2947813 DOI: 10.1016/0014-5793(86)81130-9 |
0.313 |
|
| 1987 |
Gronenborn AM, Bovermann G, Clore GM. A 1H-NMR study of the solution conformation of secretin. Resonance assignment and secondary structure. Febs Letters. 215: 88-94. PMID 2883029 DOI: 10.1016/0014-5793(87)80119-9 |
0.41 |
|
| 1987 |
Brünger AT, Clore GM, Gronenborn AM, Karplus M. 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 Engineering. 1: 399-406. PMID 2854259 DOI: 10.1093/Protein/1.5.399 |
0.381 |
|
| 1987 |
Clore GM, Sukumaran DK, Nilges M, Gronenborn AM. Three-dimensional structure of phoratoxin in solution: combined use of nuclear magnetic resonance, distance geometry, and restrained molecular dynamics Biochemistry. 26: 1732-1745. DOI: 10.1021/Bi00380A037 |
0.394 |
|
| 1987 |
Sukumaran DK, Clore GM, Preuss A, Zarbock J, Gronenborn AM. Proton nuclear magnetic resonance study of hirudin: resonance assignment and secondary structure Biochemistry. 26: 333-338. DOI: 10.1021/Bi00376A001 |
0.345 |
|
| 1987 |
Nilges M, Clore GM, Gronenborn AM. A simple method for delineating well-defined and variable regions in protein structures determined from interproton distance data Febs Letters. 219: 11-16. DOI: 10.1016/0014-5793(87)81181-X |
0.323 |
|
| 1987 |
Clore GM, Gronenborn AM, Nilges M, Sukumaran DK, Zarbock J. The polypeptide fold of the globular domain of histone H5 in solution. A study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics. The Embo Journal. 6: 1833-1842. DOI: 10.1002/J.1460-2075.1987.Tb02438.X |
0.456 |
|
| 1986 |
Clore GM, Nilges M, Sukumaran DK, Brünger AT, Karplus M, Gronenborn AM. The three-dimensional structure of alpha1-purothionin in solution: combined use of nuclear magnetic resonance, distance geometry and restrained molecular dynamics. The Embo Journal. 5: 2729-35. PMID 16453716 DOI: 10.1002/J.1460-2075.1986.Tb04557.X |
0.365 |
|
| 1986 |
Clore GM, Gronenborn AM. An investigation into the solution structure of the single-stranded DNA undecamer 5'd AAGTGTGATAT by means of nuclear Overhauser enhancement measurements. European Biophysics Journal : Ebj. 11: 95-102. PMID 6544681 DOI: 10.1007/Bf00276624 |
0.397 |
|
| 1986 |
Clore GM, Gronenborn AM, Carlson G, Meyer EF. 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. Journal of Molecular Biology. 190: 259-67. PMID 3641922 DOI: 10.1016/0022-2836(86)90297-4 |
0.429 |
|
| 1986 |
Clore GM, Gronenborn AM, Greipel J, Maass G. 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. Journal of Molecular Biology. 187: 119-24. PMID 3514922 DOI: 10.1016/0022-2836(86)90411-0 |
0.334 |
|
| 1986 |
Zarbock J, Clore GM, Gronenborn AM. Nuclear magnetic resonance study of the globular domain of chicken histone H5: resonance assignment and secondary structure. Proceedings of the National Academy of Sciences of the United States of America. 83: 7628-32. PMID 3463990 DOI: 10.1073/Pnas.83.20.7628 |
0.383 |
|
| 1986 |
Brünger AT, Clore GM, Gronenborn AM, Karplus M. Three-dimensional structure of proteins determined by molecular dynamics with interproton distance restraints: application to crambin. Proceedings of the National Academy of Sciences of the United States of America. 83: 3801-5. PMID 3459158 DOI: 10.1073/Pnas.83.11.3801 |
0.398 |
|
| 1986 |
Clore GM, Brünger AT, Karplus M, Gronenborn AM. Application of molecular dynamics with interproton distance restraints to three-dimensional protein structure determination. A model study of crambin. Journal of Molecular Biology. 191: 523-51. PMID 3029386 DOI: 10.1016/0022-2836(86)90146-4 |
0.409 |
|
| 1986 |
Gronenborn AM, Clore GM, Schmeissner U, Wingfield P. A 1H‐NMR study of human interleukin‐1β Febs Journal. 161: 37-43. PMID 3023086 DOI: 10.1111/J.1432-1033.1986.Tb10121.X |
0.396 |
|
| 1986 |
Nilsson L, Clore GM, Gronenborn AM, Brünger AT, Karplus M. 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. Journal of Molecular Biology. 188: 455-75. PMID 3016285 DOI: 10.1016/0022-2836(86)90168-3 |
0.325 |
|
| 1985 |
Clore GM, Lauble H, Frenkiel TA, Gronenborn AM. 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. European Journal of Biochemistry. 145: 629-36. PMID 6096144 DOI: 10.1111/J.1432-1033.1984.Tb08603.X |
0.335 |
|
| 1985 |
Clore GM, Gronenborn AM, Brünger AT, Karplus M. 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. Journal of Molecular Biology. 186: 435-55. PMID 3910844 DOI: 10.1016/0022-2836(85)90116-0 |
0.309 |
|
| 1985 |
Clore GM, Gronenborn AM, Moss DS, Tickle IJ. 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. Journal of Molecular Biology. 185: 219-26. PMID 2995686 DOI: 10.1016/0022-2836(85)90195-0 |
0.365 |
|
| 1985 |
Clore GM, Gronenborn AM, McLaughlin LW. 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. European Journal of Biochemistry / Febs. 151: 153-65. PMID 2992954 DOI: 10.1111/J.1432-1033.1985.Tb09080.X |
0.351 |
|
| 1985 |
Clore GM, Gronenborn AM. Probing the three-dimensional structures of DNA and RNA oligonucleotides in solution by nuclear Overhauser enhancement measurements. Febs Letters. 179: 187-98. PMID 2981703 DOI: 10.1016/0014-5793(85)80516-0 |
0.377 |
|
| 1985 |
Gronenborn AM, Clore G. Investigation of the solution structures of short nucleic acid fragments by means of nuclear overhauser enhancement measurements Progress in Nuclear Magnetic Resonance Spectroscopy. 17: 1-32. DOI: 10.1016/0079-6565(85)80004-2 |
0.316 |
|
| 1985 |
Clore G, Gronenborn A. 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. The Embo Journal. 4: 829-835. DOI: 10.1002/J.1460-2075.1985.Tb03705.X |
0.377 |
|
| 1984 |
Clore GM, Gronenborn AM. 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 Letters. 175: 117-23. PMID 6479329 DOI: 10.1016/0014-5793(84)80582-7 |
0.351 |
|
| 1984 |
Birdsall B, Bevan AW, Pascual C, Roberts GC, Feeney J, Gronenborn A, Clore GM. Multinuclear NMR characterization of two coexisting conformational states of the Lactobacillus casei dihydrofolate reductase-trimethoprim-NADP+ complex. Biochemistry. 23: 4733-42. PMID 6437442 DOI: 10.1021/Bi00315A032 |
0.373 |
|
| 1984 |
Antonjuk DJ, Birdsall B, Cheung HT, Clore GM, Feeney J, Gronenborn A, Roberts GC, Tran TQ. A 1H n.m.r. study of the role of the glutamate moiety in the binding of methotrexate to Lactobacillus casei dihydrofolate reductase. British Journal of Pharmacology. 81: 309-15. PMID 6423020 DOI: 10.1111/J.1476-5381.1984.Tb10080.X |
0.302 |
|
| 1984 |
Gronenborn AM, Clore GM, McLaughlin LW, Graeser E, Lorber B, Giegé R. Yeast tRNAAsp: codon and wobble codon-anticodon interactions. A transferred nuclear Overhauser enhancement study. European Journal of Biochemistry / Febs. 145: 359-64. PMID 6389132 DOI: 10.1111/J.1432-1033.1984.Tb08562.X |
0.4 |
|
| 1984 |
Clore GM, Gronenborn AM, McLaughlin LW. Structure of the ribotrinucleoside diphosphate codon UpUpC bound to tRNAPhe from yeast. A time-dependent transferred nuclear Overhauser enhancement study. Journal of Molecular Biology. 174: 163-73. PMID 6371248 DOI: 10.1016/0022-2836(84)90370-X |
0.336 |
|
| 1984 |
Clore GM, Gronenborn AM. 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. European Journal of Biochemistry. 141: 119-29. PMID 6327302 DOI: 10.1111/J.1432-1033.1984.Tb08166.X |
0.375 |
|
| 1984 |
Gronenborn AM, Clore GM, Jeffery J. An unusual conformation of NAD+ bound to sorbitol dehydrogenase? A time-dependent transferred nuclear Overhauser effect study. Journal of Molecular Biology. 172: 559-72. PMID 6319720 DOI: 10.1016/S0022-2836(84)80023-6 |
0.337 |
|
| 1984 |
Gronenborn AM, Clore GM, Jones MB, Jiricny J. 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 Letters. 165: 216-22. PMID 6319182 DOI: 10.1016/0014-5793(84)80172-6 |
0.35 |
|
| 1984 |
Clore GM, Gronenborn AM, Davies RW. 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 Letters. 164: 57-62. PMID 6317444 DOI: 10.1016/0014-5793(83)80018-0 |
0.326 |
|
| 1984 |
Gronenborn AM, Nermut MV, Eason P, Clore GM. Visualization of cAMP receptor protein-induced DNA kinking by electron microscopy. Journal of Molecular Biology. 179: 751-7. PMID 6094835 DOI: 10.1016/0022-2836(84)90166-9 |
0.318 |
|
| 1984 |
Clore GM, Gronenborn AM, Piper EA, McLaughlin LW, Graeser E, van Boom JH. The solution structure of a RNA pentadecamer comprising the anticodon loop and stem of yeast tRNAPhe. A 500 MHz 1H-n.m.r. study. The Biochemical Journal. 221: 737-51. PMID 6089745 DOI: 10.1042/Bj2210737 |
0.396 |
|
| 1983 |
Birdsall B, Gronenborn A, Hyde EI, Clore GM, Roberts GC, Feeney J, Burgen AS. 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: 5831-8. PMID 6817782 DOI: 10.1021/Bi00266A017 |
0.304 |
|
| 1983 |
Gronenborn AM, Kimber BJ, Clore GM, McLaughlin LW. A nuclear magnetic resonance study of the ribotrinucleoside diphophate UpUpC. Nucleic Acids Research. 11: 5691-9. PMID 6412213 DOI: 10.1093/Nar/11.16.5691 |
0.366 |
|
| 1983 |
Martin SR, Gronenborn AM, Clore GM. Specific DNA binding of the cyclic AMP receptor protein to a synthetic oligodeoxyribonucleotide. A circular dichroism study. Febs Letters. 159: 102-6. PMID 6307748 DOI: 10.1016/0014-5793(83)80425-6 |
0.364 |
|
| 1983 |
Clore G, Gronenborn A. Theory of the time dependent transferred nuclear Overhauser effect: Applications to structural analysis of ligand-protein complexes in solution Journal of Magnetic Resonance (1969). 53: 423-442. DOI: 10.1016/0022-2364(83)90215-9 |
0.356 |
|
| 1983 |
Clore G, Gronenborn A. Sequence-dependent structural variations in two right-handed alternating pyrimidine-purine DNA oligomers in solution determined by nuclear Overhauser enhancement measurements. The Embo Journal. 2: 2109-2115. DOI: 10.1002/J.1460-2075.1983.Tb01710.X |
0.401 |
|
| 1983 |
Unger B, Clore G, Gronenborn A, Hillen W. Specific DNA binding of the cAMP receptor protein within the lac operon stabilizes double-stranded DNA in the presence of cAMP. The Embo Journal. 2: 289-293. DOI: 10.1002/J.1460-2075.1983.Tb01419.X |
0.304 |
|
| 1982 |
Gronenborn AM, Clore GM, Davies RW. Modulation of specific binding of Lactobacillus casei dihydrofolate reductase to DNA by folinic acid. Febs Letters. 133: 92-4. PMID 6796432 DOI: 10.1016/0014-5793(81)80478-4 |
0.321 |
|
| 1982 |
Clore GM, Gronenborn AM. 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 Letters. 145: 197-202. PMID 6290269 DOI: 10.1016/0014-5793(82)80167-1 |
0.385 |
|
| 1982 |
Gronenborn AM, Clore GM. Proton nuclear magnetic resonance studies on cyclic nucleotide binding to the Escherichia coli adenosine cyclic 3',5'-phosphate receptor protein. Biochemistry. 21: 4040-8. PMID 6289868 DOI: 10.1021/Bi00260A020 |
0.43 |
|
| 1982 |
Clore GM, Gronenborn AM, Davies RW. 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. Journal of Molecular Biology. 155: 447-66. PMID 6283096 DOI: 10.1016/0022-2836(82)90481-8 |
0.342 |
|
| 1982 |
Gronenborn AM, Clore GM, Blazy B, Baudras A. Conformational selection of syn-cAMP upon binding to the cAMP: receptor protein. Febs Letters. 136: 160-4. PMID 6274700 DOI: 10.1016/0014-5793(81)81237-9 |
0.324 |
|
| 1982 |
Gronenborn AM, Clore GM. Conformation of NAD+ bound to yeast and horse liver alcohol dehydrogenase in solution. The use of the proton-proton transferred nuclear Overhauser enhancement. Journal of Molecular Biology. 157: 155-60. PMID 6213784 DOI: 10.1016/0022-2836(82)90518-6 |
0.302 |
|
| 1982 |
Clore G, Gronenborn A. 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 (1969). 48: 402-417. DOI: 10.1016/0022-2364(82)90073-7 |
0.351 |
|
| 1982 |
Takahashi M, Gronenborn A, Clore G, Blazy B, Baudras A. 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: 37-40. DOI: 10.1016/0014-5793(82)80481-X |
0.385 |
|
| 1981 |
Gronenborn A, Birdsall B, Hyde EI, Roberts GC, Feeney J, Burgen AS. Effects of coenzyme binding on histidine residues of Lactobacillus casei dihydrofolate reductase. Biochemistry. 20: 1717-22. PMID 6784757 DOI: 10.1021/Bi00510A003 |
0.351 |
|
| 1981 |
Gronenborn A, Birdsall B, Hyde EI, Roberts GCK, Feeney J, Burgen ASV. Direct observation by NMR of two coexisting conformations of an enzyme–ligand complex in solution Nature. 290: 273-274. DOI: 10.1038/290273A0 |
0.364 |
|
| 1981 |
Clore G, Roberts G, Gronenborn A, Birdsall B, Feeney J. Transfer-of-saturation NMR studies of protein-ligand complexes. Three-site exchange Journal of Magnetic Resonance (1969). 45: 151-161. DOI: 10.1016/0022-2364(81)90109-8 |
0.316 |
|
| 1980 |
Wyeth P, Gronenborn A, Birdsall B, Roberts GC, Feeney J, Burgen AS. Histidine residues of Lactobacillus casei dihydrofolate reductase: paramagnetic relaxation and deuterium-exchange studies and partial assignments. Biochemistry. 19: 2608-15. PMID 6772202 DOI: 10.1021/Bi00553A012 |
0.34 |
|
| 1980 |
Feeney J, Roberts GC, Kaptein R, Birdsall B, Gronenborn A, Burgen AS. Photo-CIDNP studies of the influence of ligand binding on the surface accessibility of aromatic residues in dihydrofolate reductase. Biochemistry. 19: 2466-72. PMID 6770894 DOI: 10.1021/Bi00552A026 |
0.364 |
|
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