| Year |
Citation |
Score |
| 2024 |
Sedinkin SL, Roche J, Venditti V. Elucidation of the mechanisms of inter-domain coupling in the monomeric state of Enzyme I by high-pressure NMR. Journal of Molecular Biology. 168553. PMID 38548260 DOI: 10.1016/j.jmb.2024.168553 |
0.347 |
|
| 2021 |
Nguyen TT, Siang S, Roche J. High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States. Journal of Visualized Experiments : Jove. PMID 34279503 DOI: 10.3791/62701 |
0.417 |
|
| 2019 |
Roche J, Potoyan DA. Disorder Mediated Oligomerization of DISC1 Proteins Revealed by Coarse-Grained Molecular Dynamics Simulations. The Journal of Physical Chemistry. B. PMID 31614085 DOI: 10.1021/Acs.Jpcb.9B07467 |
0.351 |
|
| 2019 |
Alderson TR, Roche J, Gastall HY, Dias DM, Pritišanac I, Ying J, Bax A, Benesch JLP, Baldwin AJ. Local unfolding of the HSP27 monomer regulates chaperone activity. Nature Communications. 10: 1068. PMID 30842409 DOI: 10.1038/S41467-019-08557-8 |
0.367 |
|
| 2019 |
Roche J, Royer CA, Roumestand C. Exploring Protein Conformational Landscapes Using High-Pressure NMR. Methods in Enzymology. 614: 293-320. PMID 30611428 DOI: 10.1016/Bs.Mie.2018.07.006 |
0.515 |
|
| 2018 |
Roche J, Royer CA. Lessons from pressure denaturation of proteins. Journal of the Royal Society, Interface. 15. PMID 30282759 DOI: 10.1098/Rsif.2018.0244 |
0.472 |
|
| 2018 |
Baweja LK, Roche J. Pushing the Limits of Structure-Based Models: Prediction of Non-Globular Protein Folding and Fibrils Formation with Go-Model Simulations. The Journal of Physical Chemistry. B. PMID 29425042 DOI: 10.1021/Acs.Jpcb.7B12129 |
0.36 |
|
| 2017 |
Roche J, Royer CA, Roumestand C. Monitoring protein folding through high pressure NMR spectroscopy. Progress in Nuclear Magnetic Resonance Spectroscopy. 102: 15-31. PMID 29157491 DOI: 10.1016/J.Pnmrs.2017.05.003 |
0.49 |
|
| 2017 |
Shen Y, Roche J, Grishaev A, Bax A. Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins. Protein Science : a Publication of the Protein Society. PMID 28884933 DOI: 10.1002/Pro.3292 |
0.38 |
|
| 2017 |
Nguyen LM, Roche J. High-pressure NMR techniques for the study of protein dynamics, folding and aggregation. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 277: 179-185. PMID 28363306 DOI: 10.1016/J.Jmr.2017.01.009 |
0.482 |
|
| 2016 |
Agniswamy J, Louis JM, Roche J, Harrison RW, Weber IT. Structural Studies of a Rationally Selected Multi-Drug Resistant HIV-1 Protease Reveal Synergistic Effect of Distal Mutations on Flap Dynamics. Plos One. 11: e0168616. PMID 27992544 DOI: 10.1371/Journal.Pone.0168616 |
0.345 |
|
| 2016 |
Louis JM, Baber JL, Ghirlando R, Aniana A, Bax A, Roche J. Insights into the Conformation of the Membrane Proximal Regions Critical to the Trimerization of the HIV-1 gp41 Ectodomain Bound to Dodecyl Phosphocholine Micelles. Plos One. 11: e0160597. PMID 27513582 DOI: 10.1371/Journal.Pone.0160597 |
0.366 |
|
| 2016 |
Roche J, Ying J, Shen Y, Torchia DA, Bax A. ARTSY-J: Convenient and precise measurement of (3)JHNHα couplings in medium-size proteins from TROSY-HSQC spectra. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 268: 73-81. PMID 27179455 DOI: 10.1016/J.Jmr.2016.05.001 |
0.323 |
|
| 2016 |
Louis JM, Roche J. Evolution under drug pressure remodels the folding free-energy landscape of mature HIV-1 protease. Journal of Molecular Biology. PMID 27170547 DOI: 10.1016/J.Jmb.2016.05.005 |
0.467 |
|
| 2016 |
Roche J, Shen Y, Lee JH, Ying J, Bax A. Monomeric Aβ(1-40) and Aβ(1-42) Peptides in Solution Adopt Very Similar Ramachandran Map Distributions That Closely Resemble Random Coil. Biochemistry. 55: 762-75. PMID 26780756 DOI: 10.1021/Acs.Biochem.5B01259 |
0.325 |
|
| 2016 |
Roche J, Ying J, Bax A. Accurate measurement of (3)J(HNHα) couplings in small or disordered proteins from WATERGATE-optimized TROSY spectra. Journal of Biomolecular Nmr. 64: 1-7. PMID 26660434 DOI: 10.1007/S10858-015-0004-Y |
0.34 |
|
| 2016 |
Roche J. Evolution under Drug Pressure Remodels the Folding Free-Energy Landscape of HIV-1 Protease Biophysical Journal. 110: 368. DOI: 10.1016/J.Bpj.2015.11.1987 |
0.381 |
|
| 2015 |
Roche J, Louis JM, Bax A, Best RB. Pressure-induced structural transition of mature HIV-1 protease from a combined NMR/MD simulation approach. Proteins. 83: 2117-23. PMID 26385843 DOI: 10.1002/Prot.24931 |
0.473 |
|
| 2015 |
Tugarinov V, Libich DS, Meyer V, Roche J, Clore GM. The Energetics of a Three-State Protein Folding System Probed by High-Pressure Relaxation Dispersion NMR Spectroscopy. Angewandte Chemie (International Ed. in English). 54: 11157-61. PMID 26352026 DOI: 10.1002/Anie.201505416 |
0.457 |
|
| 2015 |
Roche J, Dellarole M, Royer CA, Roumestand C. Exploring the Protein Folding Pathway with High-Pressure NMR: Steady-State and Kinetics Studies. Sub-Cellular Biochemistry. 72: 261-78. PMID 26174386 DOI: 10.1007/978-94-017-9918-8_13 |
0.477 |
|
| 2015 |
Dellarole M, Caro JA, Roche J, Fossat M, Barthe P, García-Moreno E B, Royer CA, Roumestand C. Evolutionarily Conserved Pattern of Interactions in a Protein Revealed by Local Thermal Expansion Properties. Journal of the American Chemical Society. 137: 9354-62. PMID 26135981 DOI: 10.1021/Jacs.5B04320 |
0.467 |
|
| 2015 |
Roche J, Louis JM, Aniana A, Ghirlando R, Bax A. Complete dissociation of the HIV-1 gp41 ectodomain and membrane proximal regions upon phospholipid binding. Journal of Biomolecular Nmr. 61: 235-48. PMID 25631354 DOI: 10.1007/S10858-015-9900-4 |
0.322 |
|
| 2015 |
Roche J, Louis JM, Bax A. Conformation of inhibitor-free HIV-1 protease derived from NMR spectroscopy in a weakly oriented solution. Chembiochem : a European Journal of Chemical Biology. 16: 214-8. PMID 25470009 DOI: 10.1002/Cbic.201402585 |
0.424 |
|
| 2015 |
Roche J, Louis JM, Bax A. Solution Conformation of the Unbound HIV-1 Protease Derived from Residual Dipolar Couplings Measured at Ambient and High-Pressure Conditions Biophysical Journal. 108: 203a. DOI: 10.1016/J.Bpj.2014.11.1122 |
0.469 |
|
| 2015 |
Roche J, Louis JM, Bax A. Cover Picture: Conformation of Inhibitor-Free HIV-1 Protease Derived from NMR Spectroscopy in a Weakly Oriented Solution (ChemBioChem 2/2015) Chembiochem. 16: 181-181. DOI: 10.1002/Cbic.201590000 |
0.348 |
|
| 2014 |
Louis JM, Aniana A, Lohith K, Sayer JM, Roche J, Bewley CA, Clore GM. Binding of HIV-1 gp41-directed neutralizing and non-neutralizing fragment antibody binding domain (Fab) and single chain variable fragment (ScFv) antibodies to the ectodomain of gp41 in the pre-hairpin and six-helix bundle conformations. Plos One. 9: e104683. PMID 25105806 DOI: 10.1371/Journal.Pone.0104683 |
0.313 |
|
| 2014 |
Maltsev AS, Grishaev A, Roche J, Zasloff M, Bax A. Improved cross validation of a static ubiquitin structure derived from high precision residual dipolar couplings measured in a drug-based liquid crystalline phase. Journal of the American Chemical Society. 136: 3752-5. PMID 24568736 DOI: 10.1021/Ja4132642 |
0.374 |
|
| 2014 |
Roche J, Louis JM, Grishaev A, Ying J, Bax A. Dissociation of the trimeric gp41 ectodomain at the lipid-water interface suggests an active role in HIV-1 Env-mediated membrane fusion. Proceedings of the National Academy of Sciences of the United States of America. 111: 3425-30. PMID 24550514 DOI: 10.1073/Pnas.1401397111 |
0.365 |
|
| 2014 |
Ying J, Roche J, Bax A. Homonuclear decoupling for enhancing resolution and sensitivity in NOE and RDC measurements of peptides and proteins. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 241: 97-102. PMID 24360766 DOI: 10.1016/J.Jmr.2013.11.006 |
0.385 |
|
| 2014 |
Roche J, Louis J, Grishaev A, Ying J, Bax A. Solution NMR structure of gp41 ectodomain monomer on a DPC micelle Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr19750 |
0.318 |
|
| 2014 |
Roche J, Louis JM, Bax A. GP41 Ectodomain Dissociates and Forms a Stable Monomer on Phospholipid Vesicles and Detergent Micelles: Implication for the HIV-1 Env-Mediated Membrane Fusion Biophysical Journal. 106: 708a. DOI: 10.1016/J.Bpj.2013.11.3929 |
0.376 |
|
| 2013 |
Louis JM, Tözsér J, Roche J, Matúz K, Aniana A, Sayer JM. Enhanced stability of monomer fold correlates with extreme drug resistance of HIV-1 protease. Biochemistry. 52: 7678-88. PMID 24079831 DOI: 10.1021/Bi400962R |
0.329 |
|
| 2013 |
Roche J, Dellarole M, Caro JA, Norberto DR, Garcia AE, Garcia-Moreno B, Roumestand C, Royer CA. Effect of internal cavities on folding rates and routes revealed by real-time pressure-jump NMR spectroscopy. Journal of the American Chemical Society. 135: 14610-8. PMID 23987660 DOI: 10.1021/Ja406682E |
0.481 |
|
| 2013 |
Roche J, Ying J, Maltsev AS, Bax A. Impact of hydrostatic pressure on an intrinsically disordered protein: a high-pressure NMR study of α-synuclein. Chembiochem : a European Journal of Chemical Biology. 14: 1754-61. PMID 23813793 DOI: 10.1002/Cbic.201300244 |
0.439 |
|
| 2013 |
Roche J, Caro JA, Dellarole M, Guca E, Royer CA, GarcÃa-Moreno BE, Garcia AE, Roumestand C. Structural, energetic, and dynamic responses of the native state ensemble of staphylococcal nuclease to cavity-creating mutations. Proteins. 81: 1069-80. PMID 23239146 DOI: 10.1002/Prot.24231 |
0.462 |
|
| 2013 |
Dellarole M, Roche J, Caro JA, Rouget J, Garcia AE, Garcia-Moreno B, Roumestand C, Royer CA. Assessing the Contribution of Cavity Density to Protein Partial Molar Expansivity by High-Pressure NMR Biophysical Journal. 104: 397a. DOI: 10.1016/J.Bpj.2012.11.2213 |
0.467 |
|
| 2012 |
Roche J, Dellarole M, Caro JA, Guca E, Norberto DR, Yang Y, Garcia AE, Roumestand C, GarcÃa-Moreno B, Royer CA. Remodeling of the folding free energy landscape of staphylococcal nuclease by cavity-creating mutations. Biochemistry. 51: 9535-46. PMID 23116341 DOI: 10.1021/Bi301071Z |
0.438 |
|
| 2012 |
Roche J, Caro JA, Norberto DR, Barthe P, Roumestand C, Schlessman JL, Garcia AE, GarcÃa-Moreno BE, Royer CA. Cavities determine the pressure unfolding of proteins. Proceedings of the National Academy of Sciences of the United States of America. 109: 6945-50. PMID 22496593 DOI: 10.1073/Pnas.1200915109 |
0.501 |
|
| 2012 |
Roche J, Caro JA, Norberto D, Barthe P, Roumestand C, Schlessman JL, Garcia AE, Garcia-Moreno E. B, Royer CA. Cavities in the Hydrophobic Core Govern Pressure Unfolding of Proteins Biophysical Journal. 102: 218a. DOI: 10.1016/J.Bpj.2011.11.1194 |
0.499 |
|
| 2011 |
Rouget JB, Aksel T, Roche J, Saldana JL, Garcia AE, Barrick D, Royer CA. Size and sequence and the volume change of protein folding. Journal of the American Chemical Society. 133: 6020-7. PMID 21446709 DOI: 10.1021/Ja200228W |
0.483 |
|
| 2011 |
Kitahara R, Hata K, Maeno A, Akasaka K, Chimenti MS, Garcia-Moreno E B, Schroer MA, Jeworrek C, Tolan M, Winter R, Roche J, Roumestand C, Montet de Guillen K, Royer CA. Structural plasticity of staphylococcal nuclease probed by perturbation with pressure and pH. Proteins. 79: 1293-305. PMID 21254234 DOI: 10.1002/Prot.22966 |
0.491 |
|
| 2011 |
Caro JA, Roche J, Rouget J, Schlessman J, García AE, Royer CA, García-Moreno B. Role of Internal Cavities as Determinants of Pressure Unfolding of Proteins Biophysical Journal. 100: 398a. DOI: 10.1016/J.Bpj.2010.12.2363 |
0.479 |
|
| 2010 |
Hata K, Kitahara R, Maeno A, Chimenti M, E BG, Roche J, Roumestand C, Guillen KMd, Royer CA, Akasaka K. 2P067 Conformational fluctuation of highly stable form of SNase Δ+PHS and its V66K variant studied by high pressure NMR spectroscopy(The 48th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 50. DOI: 10.2142/Biophys.50.S93_5 |
0.388 |
|
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