| Year |
Citation |
Score |
| 2024 |
Montepietra D, Tesei G, Martins JM, Kunze MBA, Best RB, Lindorff-Larsen K. FRETpredict: a Python package for FRET efficiency predictions using rotamer libraries. Communications Biology. 7: 298. PMID 38461354 DOI: 10.1038/s42003-024-05910-6 |
0.341 |
|
| 2023 |
Sottini A, Borgia A, Borgia MB, Bugge K, Nettels D, Chowdhury A, Heidarsson PO, Zosel F, Best RB, Kragelund BB, Schuler B. Author Correction: Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes. Nature Communications. 14: 5864. PMID 37735166 DOI: 10.1038/s41467-023-41573-3 |
0.551 |
|
| 2023 |
Galvanetto N, Ivanović MT, Chowdhury A, Sottini A, Nüesch MF, Nettels D, Best RB, Schuler B. Extreme dynamics in a biomolecular condensate. Nature. PMID 37468629 DOI: 10.1038/s41586-023-06329-5 |
0.602 |
|
| 2023 |
Montepietra D, Tesei G, Martins JOM, Kunze MBA, Best RB, Lindorff-Larsen K. FRETpredict: A Python package for FRET efficiency predictions using rotamer libraries. Biorxiv : the Preprint Server For Biology. PMID 36789411 DOI: 10.1101/2023.01.27.525885 |
0.337 |
|
| 2022 |
Heidarsson PO, Mercadante D, Sottini A, Nettels D, Borgia MB, Borgia A, Kilic S, Fierz B, Best RB, Schuler B. Release of linker histone from the nucleosome driven by polyelectrolyte competition with a disordered protein. Nature Chemistry. PMID 34992286 DOI: 10.1038/s41557-021-00839-3 |
0.562 |
|
| 2022 |
Best RB. Analysis of Molecular Dynamics Simulations of Protein Folding. Methods in Molecular Biology (Clifton, N.J.). 2376: 317-329. PMID 34845617 DOI: 10.1007/978-1-0716-1716-8_17 |
0.413 |
|
| 2021 |
Nüesch MF, Ivanović MT, Claude JB, Nettels D, Best RB, Wenger J, Schuler B. Single-molecule Detection of Ultrafast Biomolecular Dynamics with Nanophotonics. Journal of the American Chemical Society. PMID 34970909 DOI: 10.1021/jacs.1c09387 |
0.59 |
|
| 2021 |
Okuno Y, Yoo J, Schwieters CD, Best RB, Chung HS, Clore GM. Atomic view of cosolute-induced protein denaturation probed by NMR solvent paramagnetic relaxation enhancement. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 34404723 DOI: 10.1073/pnas.2112021118 |
0.369 |
|
| 2021 |
Henry ER, Metaferia B, Li Q, Harper J, Best RB, Glass KE, Cellmer T, Dunkelberger EB, Conrey A, Thein SL, Bunn HF, Eaton WA. Treatment of sickle cell disease by increasing oxygen affinity of hemoglobin. Blood. PMID 34197597 DOI: 10.1182/blood.2021012070 |
0.437 |
|
| 2021 |
Wruck F, Tian P, Kudva R, Best RB, von Heijne G, Tans SJ, Katranidis A. The ribosome modulates folding inside the ribosomal exit tunnel. Communications Biology. 4: 523. PMID 33953328 DOI: 10.1038/s42003-021-02055-8 |
0.4 |
|
| 2021 |
Dannenhoffer-Lafage T, Best RB. A Data-Driven Hydrophobicity Scale for Predicting Liquid-Liquid Phase Separation of Proteins. The Journal of Physical Chemistry. B. 125: 4046-4056. PMID 33876938 DOI: 10.1021/acs.jpcb.0c11479 |
0.339 |
|
| 2021 |
Souza PCT, Alessandri R, Barnoud J, Thallmair S, Faustino I, Grünewald F, Patmanidis I, Abdizadeh H, Bruininks BMH, Wassenaar TA, Kroon PC, Melcr J, Nieto V, Corradi V, Khan HM, ... ... Best RB, et al. Martini 3: a general purpose force field for coarse-grained molecular dynamics. Nature Methods. PMID 33782607 DOI: 10.1038/s41592-021-01098-3 |
0.305 |
|
| 2021 |
Shea JE, Best RB, Mittal J. Physics-based computational and theoretical approaches to intrinsically disordered proteins. Current Opinion in Structural Biology. 67: 219-225. PMID 33545530 DOI: 10.1016/j.sbi.2020.12.012 |
0.306 |
|
| 2021 |
Best RB. Computational Protocol for Determining Conformational Ensembles of Intrinsically Disordered Proteins. Methods in Molecular Biology (Clifton, N.J.). 2141: 413-427. PMID 32696369 DOI: 10.1007/978-1-0716-0524-0_20 |
0.354 |
|
| 2020 |
Zheng W, Dignon GL, Jovic N, Xu X, Regy RM, Fawzi NL, Kim YC, Best RB, Mittal J. Molecular Details of Protein Condensates Probed by Microsecond Long Atomistic Simulations. The Journal of Physical Chemistry. B. PMID 33302617 DOI: 10.1021/acs.jpcb.0c10489 |
0.334 |
|
| 2020 |
Sottini A, Borgia A, Borgia MB, Bugge K, Nettels D, Chowdhury A, Heidarsson PO, Zosel F, Best RB, Kragelund BB, Schuler B. Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes. Nature Communications. 11: 5736. PMID 33184256 DOI: 10.1038/s41467-020-18859-x |
0.601 |
|
| 2020 |
Tian P, Best RB. Exploring the sequence fitness landscape of a bridge between protein folds. Plos Computational Biology. 16: e1008285. PMID 33048928 DOI: 10.1371/journal.pcbi.1008285 |
0.333 |
|
| 2020 |
Domański J, Sansom MSP, Stansfeld PJ, Best RB. Atomistic mechanism of transmembrane helix association. Plos Computational Biology. 16: e1007919. PMID 32497094 DOI: 10.1371/Journal.Pcbi.1007919 |
0.358 |
|
| 2019 |
Best RB. Emerging consensus on the collapse of unfolded and intrinsically disordered proteins in water. Current Opinion in Structural Biology. 60: 27-38. PMID 31805437 DOI: 10.1016/j.sbi.2019.10.009 |
0.335 |
|
| 2019 |
Holmstrom ED, Liu Z, Nettels D, Best RB, Schuler B. Disordered RNA chaperones can enhance nucleic acid folding via local charge screening. Nature Communications. 10: 2453. PMID 31165735 DOI: 10.1038/S41467-019-10356-0 |
0.616 |
|
| 2019 |
Zerze GH, Zheng W, Best RB, Mittal J. Evolution of All-atom Protein Force Fields to Improve Local and Global Properties. The Journal of Physical Chemistry Letters. PMID 30990694 DOI: 10.1021/Acs.Jpclett.9B00850 |
0.307 |
|
| 2018 |
Kudva R, Tian P, Pardo-Avila F, Carroni M, Best R, Bernstein HD, von Heijne G. The shape of the ribosome exit tunnel affects cotranslational protein folding. Elife. 7. PMID 30475203 DOI: 10.7554/eLife.36326 |
0.39 |
|
| 2018 |
Holmstrom ED, Holla A, Zheng W, Nettels D, Best RB, Schuler B. Accurate Transfer Efficiencies, Distance Distributions, and Ensembles of Unfolded and Intrinsically Disordered Proteins From Single-Molecule FRET. Methods in Enzymology. 611: 287-325. PMID 30471690 DOI: 10.1016/Bs.Mie.2018.09.030 |
0.594 |
|
| 2018 |
Tian P, Steward A, Kudva R, Su T, Shilling PJ, Nickson AA, Hollins JJ, Beckmann R, von Heijne G, Clarke J, Best RB. Folding pathway of an Ig domain is conserved on and off the ribosome. Proceedings of the National Academy of Sciences of the United States of America. PMID 30413621 DOI: 10.1073/Pnas.1810523115 |
0.586 |
|
| 2018 |
Guinn EJ, Tian P, Shin M, Best RB, Marqusee S. A small single-domain protein folds through the same pathway on and off the ribosome. Proceedings of the National Academy of Sciences of the United States of America. PMID 30409803 DOI: 10.1073/Pnas.1810517115 |
0.385 |
|
| 2018 |
Zheng W, Hofmann H, Schuler B, Best RB. Origin of Internal Friction in Disordered Proteins Depends on Solvent Quality. The Journal of Physical Chemistry. B. PMID 30277791 DOI: 10.1021/Acs.Jpcb.8B07425 |
0.674 |
|
| 2018 |
Best RB, Zheng W, Borgia A, Buholzer K, Borgia MB, Hofmann H, Soranno A, Nettels D, Gast K, Grishaev A, Schuler B. Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water". Science (New York, N.Y.). 361. PMID 30166459 DOI: 10.1126/Science.Aar7101 |
0.575 |
|
| 2018 |
De Sancho D, Schönfelder J, Best RB, Perez-Jimenez R, Muñoz V. Instrumental Effects in the Dynamics of an Ultrafast Folding Protein under Mechanical Force. The Journal of Physical Chemistry. B. PMID 30129367 DOI: 10.1021/Acs.Jpcb.8B05975 |
0.776 |
|
| 2018 |
De Sancho D, Kubas A, Wang PH, Blumberger J, Best RB. Correction to Identification of Mutational Hot Spots for Substrate Diffusion: Application to Myoglobin. Journal of Chemical Theory and Computation. PMID 29708751 DOI: 10.1021/Acs.Jctc.8B00325 |
0.612 |
|
| 2018 |
Zheng W, Zerze GH, Borgia A, Mittal J, Schuler B, Best RB. Inferring properties of disordered chains from FRET transfer efficiencies. The Journal of Chemical Physics. 148: 123329. PMID 29604882 DOI: 10.1063/1.5006954 |
0.602 |
|
| 2018 |
Meng F, Bellaiche MMJ, Kim JY, Zerze GH, Best RB, Chung HS. Highly Disordered Amyloid-β Monomer Probed by Single-Molecule FRET and MD Simulation. Biophysical Journal. 114: 870-884. PMID 29490247 DOI: 10.1016/J.Bpj.2017.12.025 |
0.388 |
|
| 2018 |
Borgia A, Borgia MB, Bugge K, Kissling VM, Heidarsson PO, Fernandes CB, Sottini A, Soranno A, Buholzer KJ, Nettels D, Kragelund BB, Best RB, Schuler B. Extreme disorder in an ultrahigh-affinity protein complex. Nature. 555: 61-66. PMID 29466338 DOI: 10.1038/Nature25762 |
0.61 |
|
| 2018 |
Domański J, Sansom MSP, Stansfeld PJ, Best RB. Balancing Force Field Protein-Lipid Interactions To Capture Transmembrane Helix-Helix Association. Journal of Chemical Theory and Computation. PMID 29424543 DOI: 10.1021/Acs.Jctc.7B00983 |
0.394 |
|
| 2018 |
Dignon GL, Zheng W, Kim YC, Best RB, Mittal J. Sequence determinants of protein phase behavior from a coarse-grained model. Plos Computational Biology. 14: e1005941. PMID 29364893 DOI: 10.1371/Journal.Pcbi.1005941 |
0.326 |
|
| 2017 |
Best RB. Computational and theoretical advances in studies of intrinsically disordered proteins. Current Opinion in Structural Biology. 42: 147-154. PMID 28259050 DOI: 10.1016/j.sbi.2017.01.006 |
0.31 |
|
| 2017 |
Kubas A, Orain C, De Sancho D, Saujet L, Sensi M, Gauquelin C, Meynial-Salles I, Soucaille P, Bottin H, Baffert C, Fourmond V, Best RB, Blumberger J, Léger C. Mechanism of O2 diffusion and reduction in FeFe hydrogenases. Nature Chemistry. 9: 88-95. PMID 27995927 DOI: 10.1038/Nchem.2592 |
0.622 |
|
| 2017 |
Domański J, Hedger G, Best RB, Stansfeld PJ, Sansom MSP. Convergence and Sampling in Determining Free Energy Landscapes for Membrane Protein Association. The Journal of Physical Chemistry. B. 121: 3364-3375. PMID 27807980 DOI: 10.1021/Acs.Jpcb.6B08445 |
0.337 |
|
| 2016 |
de Sancho D, Best RB. Reconciling Intermediates in Mechanical Unfolding Experiments with Two-State Protein Folding in Bulk. The Journal of Physical Chemistry Letters. 7: 3798-3803. PMID 27626458 DOI: 10.1021/acs.jpclett.6b01722 |
0.745 |
|
| 2016 |
Zheng W, Borgia A, Buholzer K, Grishaev A, Schuler B, Best RB. Probing the Action of Chemical Denaturant on an Intrinsically Disordered Protein by Simulation and Experiment. Journal of the American Chemical Society. PMID 27583687 DOI: 10.1021/Jacs.6B05443 |
0.666 |
|
| 2016 |
Borgia A, Zheng W, Buholzer K, Borgia MB, Schüler A, Hofmann H, Soranno A, Nettels D, Gast K, Grishaev A, Best RB, Schuler B. Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods. Journal of the American Chemical Society. PMID 27583570 DOI: 10.1021/Jacs.6B05917 |
0.651 |
|
| 2016 |
Tian P, Best RB. Structural Determinants of Misfolding in Multidomain Proteins. Plos Computational Biology. 12: e1004933. PMID 27163669 DOI: 10.1371/journal.pcbi.1004933 |
0.372 |
|
| 2016 |
Best RB, Hummer G. Microscopic interpretation of folding ϕ-values using the transition path ensemble. Proceedings of the National Academy of Sciences of the United States of America. 113: 3263-8. PMID 26957599 DOI: 10.1073/Pnas.1520864113 |
0.568 |
|
| 2016 |
Zheng W, de Sancho D, Best RB. Modulation of Folding Internal Friction by Local and Global Barrier Heights. The Journal of Physical Chemistry Letters. 7: 1028-34. PMID 26947615 DOI: 10.1021/acs.jpclett.6b00329 |
0.706 |
|
| 2016 |
Sirur A, De Sancho D, Best RB. Markov state models of protein misfolding. The Journal of Chemical Physics. 144: 075101. PMID 26897000 DOI: 10.1063/1.4941579 |
0.741 |
|
| 2015 |
Tunbridge I, Best RB, Gain J, Kuttel MM. Simulation of Coarse-Grained Protein-Protein Interactions with Graphics Processing Units. Journal of Chemical Theory and Computation. 6: 3588-600. PMID 26617104 DOI: 10.1021/ct1003884 |
0.314 |
|
| 2015 |
Zheng W, Best RB. Reduction of All-Atom Protein Folding Dynamics to One-Dimensional Diffusion. The Journal of Physical Chemistry. B. PMID 26601695 DOI: 10.1021/acs.jpcb.5b09741 |
0.306 |
|
| 2015 |
Best RB, Zheng W, Mittal J. Correction to Balanced Protein-Water Interactions Improve Properties of Disordered Proteins and Non-Specific Protein Association. Journal of Chemical Theory and Computation. 11: 1978. PMID 26574399 DOI: 10.1021/Acs.Jctc.5B00219 |
0.323 |
|
| 2015 |
De Sancho D, Kubas A, Wang PH, Blumberger J, Best RB. Identification of Mutational Hot Spots for Substrate Diffusion: Application to Myoglobin. Journal of Chemical Theory and Computation. 11: 1919-27. PMID 26574395 DOI: 10.1021/Ct5011455 |
0.677 |
|
| 2015 |
Zheng W, Borgia A, Borgia MB, Schuler B, Best RB. Empirical Optimization of Interactions between Proteins and Chemical Denaturants in Molecular Simulations. Journal of Chemical Theory and Computation. 11: 5543-53. PMID 26574341 DOI: 10.1021/Acs.Jctc.5B00778 |
0.658 |
|
| 2015 |
Borgia A, Kemplen KR, Borgia MB, Soranno A, Shammas S, Wunderlich B, Nettels D, Best RB, Clarke J, Schuler B. Transient misfolding dominates multidomain protein folding. Nature Communications. 6: 8861. PMID 26572969 DOI: 10.1038/Ncomms9861 |
0.698 |
|
| 2015 |
Zerze GH, Best RB, Mittal J. Sequence- and Temperature-Dependent Properties of Unfolded and Disordered Proteins from Atomistic Simulations. The Journal of Physical Chemistry. B. PMID 26498157 DOI: 10.1021/Acs.Jpcb.5B08619 |
0.356 |
|
| 2015 |
Best RB, Hofmann H, Nettels D, Schuler B. Quantitative interpretation of FRET experiments via molecular simulation: force field and validation. Biophysical Journal. 108: 2721-31. PMID 26039173 DOI: 10.1016/J.Bpj.2015.04.038 |
0.628 |
|
| 2015 |
Zheng W, De Sancho D, Hoppe T, Best RB. Dependence of internal friction on folding mechanism. Journal of the American Chemical Society. 137: 3283-90. PMID 25721133 DOI: 10.1021/ja511609u |
0.672 |
|
| 2014 |
Best RB, Zheng W, Mittal J. Balanced Protein-Water Interactions Improve Properties of Disordered Proteins and Non-Specific Protein Association. Journal of Chemical Theory and Computation. 10: 5113-5124. PMID 25400522 DOI: 10.1021/Ct500569B |
0.392 |
|
| 2014 |
Zerze GH, Best RB, Mittal J. Modest influence of FRET chromophores on the properties of unfolded proteins Biophysical Journal. 107: 1654-1660. PMID 25296318 DOI: 10.1016/J.Bpj.2014.07.071 |
0.401 |
|
| 2014 |
de Sancho D, Sirur A, Best RB. Molecular origins of internal friction effects on protein-folding rates. Nature Communications. 5: 4307. PMID 24986114 DOI: 10.1038/ncomms5307 |
0.733 |
|
| 2014 |
Wuttke R, Hofmann H, Nettels D, Borgia MB, Mittal J, Best RB, Schuler B. Temperature-dependent solvation modulates the dimensions of disordered proteins Proceedings of the National Academy of Sciences of the United States of America. 111: 5213-5218. PMID 24706910 DOI: 10.1073/Pnas.1313006111 |
0.601 |
|
| 2014 |
Kubas A, De Sancho D, Best RB, Blumberger J. Aerobic damage to [FeFe]-hydrogenases: activation barriers for the chemical attachment of O2. Angewandte Chemie (International Ed. in English). 53: 4081-4. PMID 24615978 DOI: 10.1002/Anie.201400534 |
0.641 |
|
| 2013 |
Baker CM, Best RB. Insights into the Binding of Intrinsically Disordered Proteins from Molecular Dynamics Simulation. Wiley Interdisciplinary Reviews. Computational Molecular Science. 4: 182-198. PMID 34354764 DOI: 10.1002/wcms.1167 |
0.401 |
|
| 2013 |
De Sancho D, Mittal J, Best RB. Folding Kinetics and Unfolded State Dynamics of the GB1 Hairpin from Molecular Simulation. Journal of Chemical Theory and Computation. 9: 1743-53. PMID 26587632 DOI: 10.1021/Ct301033R |
0.728 |
|
| 2013 |
Kührová P, Banáš P, Best RB, Šponer J, Otyepka M. Computer Folding of RNA Tetraloops? Are We There Yet? Journal of Chemical Theory and Computation. 9: 2115-25. PMID 26583558 DOI: 10.1021/Ct301086Z |
0.3 |
|
| 2013 |
Bottaro S, Lindorff-Larsen K, Best RB. Variational Optimization of an All-Atom Implicit Solvent Force Field to Match Explicit Solvent Simulation Data. Journal of Chemical Theory and Computation. 9: 5641-5652. PMID 24748852 DOI: 10.1021/Ct400730N |
0.376 |
|
| 2013 |
Shi Y, Xia Z, Zhang J, Best R, Wu C, Ponder JW, Ren P. The Polarizable Atomic Multipole-based AMOEBA Force Field for Proteins. Journal of Chemical Theory and Computation. 9: 4046-4063. PMID 24163642 DOI: 10.1021/Ct4003702 |
0.364 |
|
| 2013 |
Henry ER, Best RB, Eaton WA. Comparing a simple theoretical model for protein folding with all-atom molecular dynamics simulations Proceedings of the National Academy of Sciences of the United States of America. 110: 17880-17885. PMID 24128764 DOI: 10.1073/Pnas.1317105110 |
0.618 |
|
| 2013 |
Best RB, Hummer G, Eaton WA. Native contacts determine protein folding mechanisms in atomistic simulations Proceedings of the National Academy of Sciences of the United States of America. 110: 17874-17879. PMID 24128758 DOI: 10.1073/Pnas.1311599110 |
0.71 |
|
| 2013 |
Tsytlonok M, Craig PO, Sivertsson E, Serquera D, Perrett S, Best RB, Wolynes PG, Itzhaki LS. Complex energy landscape of a giant repeat protein. Structure (London, England : 1993). 21: 1954-65. PMID 24120762 DOI: 10.1016/J.Str.2013.08.028 |
0.35 |
|
| 2013 |
Carter JW, Baker CM, Best RB, De Sancho D. Engineering folding dynamics from two-state to downhill: application to λ-repressor. The Journal of Physical Chemistry. B. 117: 13435-43. PMID 24079652 DOI: 10.1021/jp405904g |
0.711 |
|
| 2013 |
Sirur A, Knott M, Best RB. Effect of interactions with the chaperonin cavity on protein folding and misfolding. Physical Chemistry Chemical Physics : Pccp. 16: 6358-66. PMID 24077053 DOI: 10.1039/c3cp52872c |
0.395 |
|
| 2013 |
Best RB. How well does a funneled energy landscape capture the folding mechanism of spectrin domains? The Journal of Physical Chemistry. B. 117: 13235-44. PMID 23947368 DOI: 10.1021/jp403305a |
0.34 |
|
| 2013 |
Best RB. A "slow" protein folds quickly in the end. Proceedings of the National Academy of Sciences of the United States of America. 110: 5744-5. PMID 23572570 DOI: 10.1073/pnas.1303539110 |
0.341 |
|
| 2013 |
Sirur A, Best RB. Effects of interactions with the GroEL cavity on protein folding rates. Biophysical Journal. 104: 1098-106. PMID 23473493 DOI: 10.1016/j.bpj.2013.01.034 |
0.389 |
|
| 2013 |
Shim J, Zhu X, Best RB, MacKerell AD. (Ala)(4)-X-(Ala)4 as a model system for the optimization of the χ1 and χ2 amino acid side-chain dihedral empirical force field parameters. Journal of Computational Chemistry. 34: 593-603. PMID 23197420 DOI: 10.1002/jcc.23178 |
0.334 |
|
| 2012 |
Best RB, Zhu X, Shim J, Lopes PE, Mittal J, Feig M, Mackerell AD. Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone φ, ψ and side-chain χ(1) and χ(2) dihedral angles. Journal of Chemical Theory and Computation. 8: 3257-3273. PMID 23341755 DOI: 10.1021/Ct300400X |
0.395 |
|
| 2012 |
Best RB, Mittal J, Feig M, MacKerell AD. Inclusion of many-body effects in the additive CHARMM protein CMAP potential results in enhanced cooperativity of α-helix and β-hairpin formation. Biophysical Journal. 103: 1045-51. PMID 23009854 DOI: 10.1016/J.Bpj.2012.07.042 |
0.381 |
|
| 2012 |
Bhattacharya A, Best RB, Mittal J. Smoothing of the GB1 hairpin folding landscape by interfacial confinement Biophysical Journal. 103: 596-600. PMID 22947876 DOI: 10.1016/J.Bpj.2012.07.005 |
0.313 |
|
| 2012 |
Knott M, Best RB. A preformed binding interface in the unbound ensemble of an intrinsically disordered protein: evidence from molecular simulations. Plos Computational Biology. 8: e1002605. PMID 22829760 DOI: 10.1371/journal.pcbi.1002605 |
0.387 |
|
| 2012 |
Best RB, De Sancho D, Mittal J. Residue-specific α-helix propensities from molecular simulation Biophysical Journal. 102: 1462-1467. PMID 22455930 DOI: 10.1016/J.Bpj.2012.02.024 |
0.706 |
|
| 2012 |
Schulz JC, Schmidt L, Best RB, Dzubiella J, Netz RR. Peptide chain dynamics in light and heavy water: zooming in on internal friction. Journal of the American Chemical Society. 134: 6273-9. PMID 22414068 DOI: 10.1021/Ja211494H |
0.388 |
|
| 2012 |
Best RB. Atomistic molecular simulations of protein folding. Current Opinion in Structural Biology. 22: 52-61. PMID 22257762 DOI: 10.1016/j.sbi.2011.12.001 |
0.39 |
|
| 2011 |
Dudko OK, Graham TG, Best RB. Locating the barrier for folding of single molecules under an external force. Physical Review Letters. 107: 208301. PMID 22181779 DOI: 10.1103/Physrevlett.107.208301 |
0.304 |
|
| 2011 |
De Sancho D, Best RB. Modulation of an IDP binding mechanism and rates by helix propensity and non-native interactions: association of HIF1α with CBP. Molecular Biosystems. 8: 256-67. PMID 21892446 DOI: 10.1039/c1mb05252g |
0.692 |
|
| 2011 |
Best RB, Hummer G. Diffusion models of protein folding. Physical Chemistry Chemical Physics : Pccp. 13: 16902-11. PMID 21842082 DOI: 10.1039/C1Cp21541H |
0.555 |
|
| 2011 |
Best RB, Mittal J. Microscopic events in β-hairpin folding from alternative unfolded ensembles Proceedings of the National Academy of Sciences of the United States of America. 108: 11087-11092. PMID 21690352 DOI: 10.1073/Pnas.1016685108 |
0.364 |
|
| 2011 |
Borgia MB, Borgia A, Best RB, Steward A, Nettels D, Wunderlich B, Schuler B, Clarke J. Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins. Nature. 474: 662-5. PMID 21623368 DOI: 10.1038/Nature10099 |
0.656 |
|
| 2011 |
De Sancho D, Best RB. What is the time scale for α-helix nucleation? Journal of the American Chemical Society. 133: 6809-16. PMID 21480610 DOI: 10.1021/ja200834s |
0.735 |
|
| 2011 |
Best RB, Mittal J. Free-energy landscape of the GB1 hairpin in all-atom explicit solvent simulations with different force fields: Similarities and differences Proteins: Structure, Function and Bioinformatics. 79: 1318-1328. PMID 21322056 DOI: 10.1002/Prot.22972 |
0.374 |
|
| 2011 |
Graham TG, Best RB. Force-induced change in protein unfolding mechanism: discrete or continuous switch? The Journal of Physical Chemistry. B. 115: 1546-61. PMID 21271708 DOI: 10.1021/Jp110738M |
0.327 |
|
| 2010 |
Kim YC, Best RB, Mittal J. Macromolecular crowding effects on protein-protein binding affinity and specificity Journal of Chemical Physics. 133. PMID 21133453 DOI: 10.1063/1.3516589 |
0.305 |
|
| 2010 |
Mittal J, Best RB. Tackling force-field bias in protein folding simulations: Folding of Villin HP35 and Pin WW domains in explicit water Biophysical Journal. 99: L26-L28. PMID 20682244 DOI: 10.1016/J.Bpj.2010.05.005 |
0.364 |
|
| 2010 |
Best RB, Mittal J. Balance between α and β structures in Ab initio protein folding Journal of Physical Chemistry B. 114: 8790-8798. PMID 20536262 DOI: 10.1021/Jp102575B |
0.363 |
|
| 2010 |
Best RB, Hummer G. Coordinate-dependent diffusion in protein folding. Proceedings of the National Academy of Sciences of the United States of America. 107: 1088-93. PMID 20080558 DOI: 10.1073/Pnas.0910390107 |
0.548 |
|
| 2009 |
Vaiana SM, Best RB, Yau WM, Eaton WA, Hofrichter J. Evidence for a partially structured state of the amylin monomer Biophysical Journal. 97: 2948-2957. PMID 19948124 DOI: 10.1016/J.Bpj.2009.08.041 |
0.547 |
|
| 2009 |
Nettels D, Müller-Späth S, Küster F, Hofmann H, Haenni D, Rüegger S, Reymond L, Hoffmann A, Kubelka J, Heinz B, Gast K, Best RB, Schuler B. Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins. Proceedings of the National Academy of Sciences of the United States of America. 106: 20740-5. PMID 19933333 DOI: 10.1073/Pnas.0900622106 |
0.632 |
|
| 2009 |
Best RB, Hummer G. Optimized molecular dynamics force fields applied to the helix-coil transition of polypeptides. The Journal of Physical Chemistry. B. 113: 9004-15. PMID 19514729 DOI: 10.1021/Jp901540T |
0.505 |
|
| 2009 |
Best RB, Hummer G. Unfolding the Secrets of Calmodulin Science. 323: 593-594. PMID 19179519 DOI: 10.1126/Science.1169555 |
0.418 |
|
| 2008 |
Mittal J, Best RB. Thermodynamics and kinetics of protein folding under confinement. Proceedings of the National Academy of Sciences of the United States of America. 105: 20233-8. PMID 19073911 DOI: 10.1073/Pnas.0807742105 |
0.319 |
|
| 2008 |
Tikhonova IG, Best RB, Engel S, Gershengorn MC, Hummer G, Costanzi S. Atomistic insights into rhodopsin activation from a dynamic model. Journal of the American Chemical Society. 130: 10141-9. PMID 18620390 DOI: 10.1021/Ja0765520 |
0.508 |
|
| 2008 |
Best RB, Buchete NV, Hummer G. Are current molecular dynamics force fields too helical? Biophysical Journal. 95: L07-9. PMID 18456823 DOI: 10.1529/Biophysj.108.132696 |
0.509 |
|
| 2008 |
Turjanski AG, Gutkind JS, Best RB, Hummer G. Binding-induced folding of a natively unstructured transcription factor. Plos Computational Biology. 4. PMID 18404207 DOI: 10.1371/Journal.Pcbi.1000060 |
0.497 |
|
| 2008 |
Best RB, Hummer G. Protein folding kinetics under force from molecular simulation. Journal of the American Chemical Society. 130: 3706-3707. PMID 18307341 DOI: 10.1021/Ja0762691 |
0.579 |
|
| 2008 |
Best RB, Paci E, Hummer G, Dudko OK. Pulling direction as a reaction coordinate for the mechanical unfolding of single molecules. Journal of Physical Chemistry B. 112: 5968-5976. PMID 18251532 DOI: 10.1021/Jp075955J |
0.567 |
|
| 2008 |
Billings KS, Best RB, Rutherford TJ, Clarke J. Crosstalk between the protein surface and hydrophobic core in a core-swapped fibronectin type III domain. Journal of Molecular Biology. 375: 560-71. PMID 18035373 DOI: 10.1016/J.Jmb.2007.10.056 |
0.534 |
|
| 2007 |
Best RB, Merchant KA, Gopich IV, Schuler B, Bax A, Eaton WA. Effect of flexibility and cis residues in single-molecule FRET studies of polyproline. Proceedings of the National Academy of Sciences of the United States of America. 104: 18964-9. PMID 18029448 DOI: 10.1073/Pnas.0709567104 |
0.694 |
|
| 2007 |
Ng SP, Billings KS, Ohashi T, Allen MD, Best RB, Randles LG, Erickson HP, Clarke J. Designing an extracellular matrix protein with enhanced mechanical stability. Proceedings of the National Academy of Sciences of the United States of America. 104: 9633-7. PMID 17535921 DOI: 10.1073/Pnas.0609901104 |
0.529 |
|
| 2007 |
Merchant KA, Best RB, Louis JM, Gopich IV, Eaton WA. Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy any molecular simulations Proceedings of the National Academy of Sciences of the United States of America. 104: 1528-1533. PMID 17251351 DOI: 10.1073/Pnas.0607097104 |
0.632 |
|
| 2006 |
Francis CJ, Lindorff-Larsen K, Best RB, Vendruscolo M. Characterization of the residual structure in the unfolded state of the Delta131Delta fragment of staphylococcal nuclease. Proteins. 65: 145-52. PMID 16862593 DOI: 10.1002/Prot.21077 |
0.534 |
|
| 2006 |
Best RB, Lindorff-Larsen K, DePristo MA, Vendruscolo M. Relation between native ensembles and experimental structures of proteins. Proceedings of the National Academy of Sciences of the United States of America. 103: 10901-6. PMID 16829580 DOI: 10.1073/Pnas.0511156103 |
0.534 |
|
| 2006 |
Best RB, Hummer G. Diffusive model of protein folding dynamics with Kramers turnover in rate. Physical Review Letters. 96: 228104-228104. PMID 16803349 DOI: 10.1103/Physrevlett.96.228104 |
0.542 |
|
| 2006 |
Geierhaas CD, Best RB, Paci E, Vendruscolo M, Clarke J. Structural comparison of the two alternative transition states for folding of TI I27. Biophysical Journal. 91: 263-75. PMID 16603501 DOI: 10.1529/Biophysj.105.077057 |
0.653 |
|
| 2006 |
Best RB, Vendruscolo M. Structural interpretation of hydrogen exchange protection factors in proteins: characterization of the native state fluctuations of CI2. Structure (London, England : 1993). 14: 97-106. PMID 16407069 DOI: 10.1016/J.Str.2005.09.012 |
0.513 |
|
| 2006 |
Lindorff-Larsen K, Best RB, Vendruscolo M. Interpreting dynamically-averaged scalar couplings in proteins. Journal of Biomolecular Nmr. 32: 273-80. PMID 16211481 DOI: 10.1007/S10858-005-8873-0 |
0.497 |
|
| 2005 |
Best RB, Chen YG, Hummer G. Slow protein conformational dynamics from multiple experimental structures: the helix/sheet transition of arc repressor. Structure (London, England : 1993). 13: 1755-63. PMID 16338404 DOI: 10.1016/J.Str.2005.08.009 |
0.534 |
|
| 2005 |
Best RB, Clarke J, Karplus M. What contributions to protein side-chain dynamics are probed by NMR experiments? A molecular dynamics simulation analysis. Journal of Molecular Biology. 349: 185-203. PMID 15876377 DOI: 10.1016/J.Jmb.2005.03.001 |
0.628 |
|
| 2005 |
Best RB, Hummer G. Comment on "Force-clamp spectroscopy monitors the folding trajectory of a single protein". Science. 308: 498-498. PMID 15845835 DOI: 10.1126/Science.1106969 |
0.516 |
|
| 2005 |
Best RB, Hummer G. Reaction coordinates and rates from transition paths Proceedings of the National Academy of Sciences of the United States of America. 102: 6732-6737. PMID 15814618 DOI: 10.1073/Pnas.0408098102 |
0.499 |
|
| 2005 |
Lindorff-Larsen K, Best RB, Depristo MA, Dobson CM, Vendruscolo M. Simultaneous determination of protein structure and dynamics. Nature. 433: 128-32. PMID 15650731 DOI: 10.1038/Nature03199 |
0.634 |
|
| 2004 |
Best RB, Vendruscolo M. Determination of protein structures consistent with NMR order parameters. Journal of the American Chemical Society. 126: 8090-1. PMID 15225030 DOI: 10.1021/Ja0396955 |
0.468 |
|
| 2004 |
Best RB, Clarke J, Karplus M. The origin of protein sidechain order parameter distributions. Journal of the American Chemical Society. 126: 7734-5. PMID 15212494 DOI: 10.1021/Ja049078W |
0.589 |
|
| 2004 |
Best RB, Rutherford TJ, Freund SM, Clarke J. Hydrophobic core fluidity of homologous protein domains: relation of side-chain dynamics to core composition and packing. Biochemistry. 43: 1145-55. PMID 14756550 DOI: 10.1021/Bi035658E |
0.512 |
|
| 2003 |
Best RB, Fowler SB, Herrera JL, Steward A, Paci E, Clarke J. Mechanical unfolding of a titin Ig domain: structure of transition state revealed by combining atomic force microscopy, protein engineering and molecular dynamics simulations. Journal of Molecular Biology. 330: 867-77. PMID 12850153 DOI: 10.1016/S0022-2836(03)00618-1 |
0.585 |
|
| 2003 |
Williams PM, Fowler SB, Best RB, Toca-Herrera JL, Scott KA, Steward A, Clarke J. Hidden complexity in the mechanical properties of titin. Nature. 422: 446-9. PMID 12660787 DOI: 10.1038/Nature01517 |
0.507 |
|
| 2002 |
Fowler SB, Best RB, Toca Herrera JL, Rutherford TJ, Steward A, Paci E, Karplus M, Clarke J. Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering. Journal of Molecular Biology. 322: 841-9. PMID 12270718 DOI: 10.1016/S0022-2836(02)00805-7 |
0.677 |
|
| 2002 |
Best RB, Fowler SB, Toca-Herrera JL, Clarke J. A simple method for probing the mechanical unfolding pathway of proteins in detail. Proceedings of the National Academy of Sciences of the United States of America. 99: 12143-8. PMID 12218181 DOI: 10.1073/Pnas.192351899 |
0.605 |
|
| 2002 |
Best RB, Clarke J. What can atomic force microscopy tell us about protein folding? Chemical Communications (Cambridge, England). 183-92. PMID 12120362 DOI: 10.1039/B108159B |
0.581 |
|
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