| Year |
Citation |
Score |
| 2023 |
Lin X, Haller PR, Bavi N, Faruk N, Perozo E, Sosnick TR. Folding of prestin's anion-binding site and the mechanism of outer hair cell electromotility. Elife. 12. PMID 38054956 DOI: 10.7554/eLife.89635 |
0.791 |
|
| 2023 |
Kik SK, Christopher D, Glauninger H, Hickernell CW, Bard JAM, Ford M, Sosnick TR, Drummond DA. An adaptive biomolecular condensation response is conserved across environmentally divergent species. Biorxiv : the Preprint Server For Biology. PMID 37546789 DOI: 10.1101/2023.07.28.551061 |
0.507 |
|
| 2023 |
Lin X, Haller P, Bavi N, Faruk N, Perozo E, Sosnick TR. Folding of Prestin's Anion-Binding Site and the Mechanism of Outer Hair Cell Electromotility. Biorxiv : the Preprint Server For Biology. PMID 36909622 DOI: 10.1101/2023.02.27.530320 |
0.787 |
|
| 2023 |
Faruk NF, Peng X, Sosnick TR. Factors That Control the Force Needed to Unfold a Membrane Protein in Silico Depend on the Mode of Denaturation. International Journal of Molecular Sciences. 24. PMID 36768981 DOI: 10.3390/ijms24032654 |
0.809 |
|
| 2023 |
Kroll KL, French AR, Sosnick TR, Rock RS. LILAC: enhanced actin imaging with an optogenetic Lifeact. Nature Methods. PMID 36717692 DOI: 10.1038/s41592-022-01761-3 |
0.74 |
|
| 2022 |
Lin X, Zmyslowski AM, Gagnon IA, Nakamoto RK, Sosnick TR. Development of in vivo HDX-MS with applications to a TonB-dependent transporter and other proteins. Protein Science : a Publication of the Protein Society. 31: e4402. PMID 36040258 DOI: 10.1002/pro.4402 |
0.747 |
|
| 2022 |
Zmyslowski AM, Baxa MC, Gagnon IA, Sosnick TR. HDX-MS performed on BtuB in outer membranes delineates the luminal domain's allostery and unfolding upon B12 and TonB binding. Proceedings of the National Academy of Sciences of the United States of America. 119: e2119436119. PMID 35549554 DOI: 10.1073/pnas.2119436119 |
0.783 |
|
| 2022 |
Faruk NF, Peng X, Freed KF, Roux B, Sosnick TR. Challenges and Advantages of Accounting for Backbone Flexibility in Prediction of Protein-Protein Complexes. Journal of Chemical Theory and Computation. 18: 2016-2032. PMID 35213808 DOI: 10.1021/acs.jctc.1c01255 |
0.822 |
|
| 2022 |
Gaffney KA, Guo R, Bridges MD, Muhammednazaar S, Chen D, Kim M, Yang Z, Schilmiller AL, Faruk NF, Peng X, Jones AD, Kim KH, Sun L, Hubbell WL, Sosnick TR, et al. Lipid bilayer induces contraction of the denatured state ensemble of a helical-bundle membrane protein. Proceedings of the National Academy of Sciences of the United States of America. 119. PMID 34969836 DOI: 10.1073/pnas.2109169119 |
0.826 |
|
| 2022 |
Baxa MC, Sosnick TR. Engineered Metal-Binding Sites to Probe Protein Folding Transition States: Psi Analysis. Methods in Molecular Biology (Clifton, N.J.). 2376: 31-63. PMID 34845602 DOI: 10.1007/978-1-0716-1716-8_2 |
0.817 |
|
| 2021 |
Peng X, Baxa M, Faruk N, Sachleben JR, Pintscher S, Gagnon IA, Houliston S, Arrowsmith CH, Freed KF, Rocklin GJ, Sosnick TR. Prediction and Validation of a Protein's Free Energy Surface Using Hydrogen Exchange and (Importantly) Its Denaturant Dependence. Journal of Chemical Theory and Computation. PMID 34936354 DOI: 10.1021/acs.jctc.1c00960 |
0.825 |
|
| 2021 |
Song KC, Molina AV, Chen R, Gagnon IA, Koh YH, Roux B, Sosnick TR. Folding and misfolding of potassium channel monomers during assembly and tetramerization. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 34413192 DOI: 10.1073/pnas.2103674118 |
0.827 |
|
| 2020 |
Bowman MA, Riback JA, Rodriguez A, Guo H, Li J, Sosnick TR, Clark PL. Properties of protein unfolded states suggest broad selection for expanded conformational ensembles. Proceedings of the National Academy of Sciences of the United States of America. PMID 32879005 DOI: 10.1073/Pnas.2003773117 |
0.796 |
|
| 2020 |
Clark PL, Plaxco KW, Sosnick TR. Water as a good solvent for unfolded proteins: Folding and collapse are fundamentally different. Journal of Molecular Biology. PMID 32044346 DOI: 10.1016/J.Jmb.2020.01.031 |
0.464 |
|
| 2020 |
Leon K, Cunningham RL, Riback JA, Feldman E, Li J, Sosnick TR, Zhao M, Monk KR, Araç D. Structural basis for adhesion G protein-coupled receptor Gpr126 function. Nature Communications. 11: 194. PMID 31924782 DOI: 10.1038/S41467-019-14040-1 |
0.74 |
|
| 2020 |
Guo R, Gaffney KA, Bridges MD, Kim M, Hubbell WL, Sosnick TR, Hong H. Membrane Induces Contraction but not Collapse of the Denatured State of a Helical Membrane Protein Biophysical Journal. 118: 27a. DOI: 10.1016/J.Bpj.2019.11.327 |
0.358 |
|
| 2020 |
Sosnick TR, Jumper JM, Wang Z, Peng X, Faruk NF, Freed KF. Upside: Protein Folding in CPU-Hours with Applications to Force-Unfolding of Membrane Proteins Biophysical Journal. 118: 353a. DOI: 10.1016/J.Bpj.2019.11.2034 |
0.817 |
|
| 2020 |
Natesh S, Hummels AR, Sachleben JR, Sosnick TR, Freed KF, Meredith SC, Haddadian EJ. Water Dynamics and Interactions Inside Amyloid-Beta Fibrils Biophysical Journal. 118: 216a. DOI: 10.1016/J.Bpj.2019.11.1284 |
0.418 |
|
| 2019 |
Wang Z, Jumper JM, Freed KF, Sosnick TR. On the Interpretation of Force-Induced Unfolding Studies of Membrane Proteins Using Fast Simulations. Biophysical Journal. PMID 31587831 DOI: 10.1016/J.Bpj.2019.09.011 |
0.801 |
|
| 2019 |
Zayner JP, Mathes T, Sosnick TR, Kennis JTM. Helical Contributions Mediate Light-Activated Conformational Change in the LOV2 Domain of Phototropin 1. Acs Omega. 4: 1238-1243. PMID 31459397 DOI: 10.1021/acsomega.8b02872 |
0.795 |
|
| 2019 |
Riback JA, Bowman MA, Zmyslowski AM, Plaxco KW, Clark PL, Sosnick TR. Commonly used FRET fluorophores promote collapse of an otherwise disordered protein. Proceedings of the National Academy of Sciences of the United States of America. PMID 30992378 DOI: 10.1073/Pnas.1813038116 |
0.813 |
|
| 2019 |
Sosnick TR, Riback JA, Bowman MA, Zmyslowski AM, Rodriguez A, Plaxco KW, Clark PL. The importance of measuring the solvent quality of unfolded proteins Acta Crystallographica Section a Foundations and Advances. 75: a419-a419. DOI: 10.1107/S0108767319095916 |
0.755 |
|
| 2019 |
Roux B, Song K, Hoon Koh Y, Perozo E, Sosnick TR. Structural Dynamics of Potassium Channel Monomer in a Membrane Environment and Tetrameric Assembly Biophysical Journal. 116: 461a. DOI: 10.1016/J.Bpj.2018.11.2490 |
0.671 |
|
| 2019 |
Kahan DN, Chen R, Riback J, Katanski C, Drummond A, Sosnick TR. Molecular Factors Underlying Stress-Triggered Phase-Separation of Pab1 Biophysical Journal. 116: 350a. DOI: 10.1016/J.Bpj.2018.11.1903 |
0.696 |
|
| 2019 |
Song KC, Koh Y, Perozo E, Roux B, Sosnick TR. Controlling the Folding and Misfolding of Potassium Channels Biophysical Journal. 116: 301a. DOI: 10.1016/J.Bpj.2018.11.1630 |
0.658 |
|
| 2019 |
Wang Z, Jumper JM, Freed KF, Sosnick TR. Fast, Atomic-Level AFM and Magnetic Tweezers Simulations of the Unfolding of Membrane Proteins using a New Membrane Burial Potential with H-Bonding Biophysical Journal. 116: 300a-301a. DOI: 10.1016/J.Bpj.2018.11.1629 |
0.79 |
|
| 2018 |
Jumper JM, Faruk NF, Freed KF, Sosnick TR. Accurate calculation of side chain packing and free energy with applications to protein molecular dynamics. Plos Computational Biology. 14: e1006342. PMID 30589846 DOI: 10.1371/Journal.Pcbi.1006342 |
0.824 |
|
| 2018 |
Jumper JM, Faruk NF, Freed KF, Sosnick TR. Trajectory-based training enables protein simulations with accurate folding and Boltzmann ensembles in cpu-hours. Plos Computational Biology. 14: e1006578. PMID 30589834 DOI: 10.1371/Journal.Pcbi.1006578 |
0.816 |
|
| 2018 |
Wang Z, Jumper JM, Wang S, Freed KF, Sosnick TR. A Membrane Burial Potential with H-Bonds and Applications to Curved Membranes and Fast Simulations. Biophysical Journal. PMID 30413241 DOI: 10.1016/J.Bpj.2018.10.012 |
0.819 |
|
| 2018 |
Riback JA, Bowman MA, Zmyslowski A, Knoverek CR, Jumper J, Kaye EB, Freed KF, Clark PL, Sosnick TR. Response to Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water". Science (New York, N.Y.). 361. PMID 30166460 DOI: 10.1126/Science.Aar7949 |
0.795 |
|
| 2018 |
Riback JA, Bowman MA, Zmyslowski A, Knoverek CR, Jumper JM, Hinshaw J, Kaye EB, Freed KF, Clark PL, Sosnick TR. Measuring the solvent quality of water for disordered proteins from a single SAXS measurement Acta Crystallographica Section a Foundations and Advances. 74: a221-a221. DOI: 10.1107/S0108767318097787 |
0.784 |
|
| 2018 |
Riback JA, Bowman MA, Zmyslowski AM, Plaxco KW, Clark PL, Sosnick TR. Saxs Confirms that FRET Dyes Promote Collapse of an Otherwise Fully Disordered Protein Biophysical Journal. 114: 368a. DOI: 10.1016/J.Bpj.2017.11.2040 |
0.745 |
|
| 2017 |
Skinner JJ, Wang S, Lee J, Ong C, Sommese R, Sivaramakrishnan S, Koelmel W, Hirschbeck M, Schindelin H, Kisker C, Lorenz K, Sosnick TR, Rosner MR. Conserved salt-bridge competition triggered by phosphorylation regulates the protein interactome. Proceedings of the National Academy of Sciences of the United States of America. PMID 29208709 DOI: 10.1073/Pnas.1711543114 |
0.413 |
|
| 2017 |
Riback JA, Bowman MA, Zmyslowski AM, Knoverek CR, Jumper JM, Hinshaw JR, Kaye EB, Freed KF, Clark PL, Sosnick TR. Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water. Science (New York, N.Y.). 358: 238-241. PMID 29026044 DOI: 10.1126/Science.Aan5774 |
0.813 |
|
| 2017 |
Riback JA, Katanski CD, Kear-Scott JL, Pilipenko EV, Rojek AE, Sosnick TR, Drummond DA. Stress-Triggered Phase Separation Is an Adaptive, Evolutionarily Tuned Response. Cell. 168: 1028-1040.e19. PMID 28283059 DOI: 10.1016/J.Cell.2017.02.027 |
0.78 |
|
| 2017 |
Gates ZP, Baxa MC, Yu W, Riback JA, Li H, Roux B, Kent SB, Sosnick TR. Perplexing cooperative folding and stability of a low-sequence complexity, polyproline 2 protein lacking a hydrophobic core. Proceedings of the National Academy of Sciences of the United States of America. PMID 28193869 DOI: 10.1073/Pnas.1609579114 |
0.831 |
|
| 2017 |
French AR, Sosnick TR, Rock RS. Investigations of human myosin VI targeting using optogenetically controlled cargo loading. Proceedings of the National Academy of Sciences of the United States of America. PMID 28193860 DOI: 10.1073/Pnas.1614716114 |
0.777 |
|
| 2017 |
Sosnick TR, Skinner JJ, Wang S, Lee J, Sommese R, Sivaramakrishnan S, Kölmel W, Hirschbeck M, Schindelin H, Kisker C, Lorenz K, Rosner MR. A Phospho-Induced Theft of a Salt Bridge in RKIP Links Map Kinase and G Protein-Mediated Signaling Biophysical Journal. 112: 63a-64a. DOI: 10.1016/J.Bpj.2016.11.382 |
0.368 |
|
| 2017 |
Sherani A, Jumper JM, Ozkan E, Sosnick TR, Roux B. Molecular Determinants of Specificity in the Dpr-DIP Interaction Network Biophysical Journal. 112: 53a. DOI: 10.1016/J.Bpj.2016.11.325 |
0.765 |
|
| 2017 |
Faruk NF, Jumper J, Roux B, Sosnick TR. Extending Upside , a Near-Atomic Level Model for Fast Protein Folding, for Predicting Protein-Protein Interactions Biophysical Journal. 112: 359a. DOI: 10.1016/J.Bpj.2016.11.1946 |
0.786 |
|
| 2017 |
Riback JA, Bowman MA, Zmyslowski A, Knoverek CR, Jumper J, Hinshaw J, Kaye EB, Freed KF, Clark PL, Sosnick TR. Measuring the (Good) Solvent Quality of Water for Disordered Proteins from a Single SAXS Measurement Biophysical Journal. 112: 316a. DOI: 10.1016/J.Bpj.2016.11.1712 |
0.821 |
|
| 2017 |
Wang S, Wang Z, Jumper J, Freed KF, Sosnick TR, Xu J. Folding Membrane Proteins by Contacts Inferred from Non-Membrane Proteins and Near-Atomic Level Refinement Biophysical Journal. 112: 204a-205a. DOI: 10.1016/J.Bpj.2016.11.1130 |
0.814 |
|
| 2017 |
Riback JA, Katanski CA, Kear-Scott JL, Pilipenko EV, Sosnick TR, Drummond DA. How Evolution Tunes Stress-Triggered Protein Phase Separation to Promote Cell Fitness During Stress Biophysical Journal. 112: 5a. DOI: 10.1016/J.Bpj.2016.11.047 |
0.777 |
|
| 2016 |
Sachleben JR, Adhikari AN, Gawlak G, Hoey RJ, Liu G, Joachimiak A, Montelione GT, Sosnick TR, Koide S. Aromatic Claw: A new fold with high aromatic content that evades structural prediction. Protein Science : a Publication of the Protein Society. PMID 27750371 DOI: 10.1002/Pro.3069 |
0.789 |
|
| 2016 |
Poellmann MJ, Sosnick TR, Meredith SC, Lee RC. The Pentablock Amphiphilic Copolymer T1107 Prevents Aggregation of Denatured and Reduced Lysozyme. Macromolecular Bioscience. PMID 27615730 DOI: 10.1002/Mabi.201600217 |
0.384 |
|
| 2016 |
Virtanen JJ, Sosnick TR, Freed KF. Erratum: "Ionic strength independence of charge distributions in solvation of biomolecules" [J. Chem. Phys. 141, 22D503 (2014)]. The Journal of Chemical Physics. 145: 059903. PMID 27497583 DOI: 10.1063/1.4959170 |
0.398 |
|
| 2016 |
Yu W, Baxa MC, Gagnon I, Freed KF, Sosnick TR. Cooperative folding near the downhill limit determined with amino acid resolution by hydrogen exchange. Proceedings of the National Academy of Sciences of the United States of America. PMID 27078098 DOI: 10.1073/Pnas.1522500113 |
0.825 |
|
| 2016 |
Basanta B, Chan KK, Barth P, King T, Hinshaw JR, Sosnick TR, Liu G, Everett J, Xiao R, Montelione GT, Baker D. Introduction of a polar core into the de novo designed protein Top7. Protein Science : a Publication of the Protein Society. PMID 26873166 DOI: 10.1002/Pro.2899 |
0.362 |
|
| 2016 |
Wang Z, Jumper JM, Freed KF, Sosnick TR. Including H-Bonding in Depth-Dependent Membrane Burial Potentials for Improving Folding Simulations Biophysical Journal. 110: 58a. DOI: 10.1016/J.Bpj.2015.11.378 |
0.813 |
|
| 2016 |
Riback J, Katanski C, Sosnick TR, Drummond DA. Hydrophobicity of Poly(A)-Binding Protein's Intrinsically Disordered Region Determines its Conformation and Organism Thermotolerance Biophysical Journal. 110: 558a. DOI: 10.1016/J.Bpj.2015.11.2986 |
0.82 |
|
| 2016 |
Natesh SR, Meredith SC, Sosnick TR, Freed KF, Haddadian EJ. Aβ Fibrils Act as Aqueous Pores: A Molecular Dynamics Study Biophysical Journal. 110: 553a. DOI: 10.1016/J.Bpj.2015.11.2959 |
0.482 |
|
| 2016 |
Sosnick TR, Jumper JM, Freed KF. Upside: A New Dynamics Method Capable of Cooperative De Novo Protein Folding in CPU-Hours Biophysical Journal. 110: 523a-524a. DOI: 10.1016/J.Bpj.2015.11.2801 |
0.784 |
|
| 2016 |
Song K, Roux B, Sosnick T. Dissecting the Folding Pathway of Potassium Channel Pore Domains Biophysical Journal. 110: 394a. DOI: 10.1016/J.Bpj.2015.11.2128 |
0.711 |
|
| 2016 |
French AR, Rock RS, Sosnick TR. An Optogenetic Method for Controlling Full-Length Myosin VI through its Cargo Binding Domain Biophysical Journal. 110: 194a. DOI: 10.1016/J.Bpj.2015.11.1078 |
0.795 |
|
| 2015 |
Baxa MC, Yu W, Adhikari AN, Ge L, Xia Z, Zhou R, Freed KF, Sosnick TR. Even with nonnative interactions, the updated folding transition states of the homologs Proteins G & L are extensive and similar. Proceedings of the National Academy of Sciences of the United States of America. PMID 26100906 DOI: 10.1073/Pnas.1503613112 |
0.828 |
|
| 2015 |
Watkins HM, Simon AJ, Sosnick TR, Lipman EA, Hjelm RP, Plaxco KW. Random coil negative control reproduces the discrepancy between scattering and FRET measurements of denatured protein dimensions. Proceedings of the National Academy of Sciences of the United States of America. 112: 6631-6. PMID 25964362 DOI: 10.1073/Pnas.1418673112 |
0.448 |
|
| 2015 |
Riback J, Laskowski P, Scott JL, Wallace EW, Rojek AE, Schwartz MH, Sosnick TR, Drummond DA. Heat Shock Triggers Assembly of tRNA Synthetases into an Active Supercomplex Biophysical Journal. 108: 221a. DOI: 10.1016/J.Bpj.2014.11.1219 |
0.791 |
|
| 2014 |
Virtanen JJ, Sosnick TR, Freed KF. Ionic strength independence of charge distributions in solvation of biomolecules. The Journal of Chemical Physics. 141: 22D503. PMID 25494774 DOI: 10.1063/1.4895522 |
0.472 |
|
| 2014 |
Skinner JJ, Yu W, Gichana EK, Baxa MC, Hinshaw JR, Freed KF, Sosnick TR. Benchmarking all-atom simulations using hydrogen exchange. Proceedings of the National Academy of Sciences of the United States of America. 111: 15975-80. PMID 25349413 DOI: 10.1073/Pnas.1404213111 |
0.824 |
|
| 2014 |
Baxa MC, Haddadian EJ, Jumper JM, Freed KF, Sosnick TR. Loss of conformational entropy in protein folding calculated using realistic ensembles and its implications for NMR-based calculations. Proceedings of the National Academy of Sciences of the United States of America. 111: 15396-401. PMID 25313044 DOI: 10.1073/Pnas.1407768111 |
0.826 |
|
| 2014 |
Zayner JP, Sosnick TR. Factors that control the chemistry of the LOV domain photocycle. Plos One. 9: e87074. PMID 24475227 DOI: 10.1371/Journal.Pone.0087074 |
0.803 |
|
| 2014 |
Johnson KW, Sosnick TR, Freed KF, Haddadian EJ. Differences in Dynamics and Stability of the Wild Type Beta-Amyloid Aβ1-40, and ΔE22-Aβ1-39 (Japanese) Mutant Protofibril Structures, a Molecular Dynamics Study Biophysical Journal. 106: 482a. DOI: 10.1016/J.Bpj.2013.11.2722 |
0.494 |
|
| 2013 |
Walters BT, Mayne L, Hinshaw JR, Sosnick TR, Englander SW. Folding of a large protein at high structural resolution. Proceedings of the National Academy of Sciences of the United States of America. 110: 18898-903. PMID 24191053 DOI: 10.1073/Pnas.1319482110 |
0.678 |
|
| 2013 |
Sosnick TR, Baxa MC. Revealing what gets buried first in protein folding. Proceedings of the National Academy of Sciences of the United States of America. 110: 16704-5. PMID 24096579 DOI: 10.1073/Pnas.1316158110 |
0.815 |
|
| 2013 |
Liu Y, Haddadian E, Sosnick TR, Freed KF, Gong H. A novel implicit solvent model for simulating the molecular dynamics of RNA. Biophysical Journal. 105: 1248-57. PMID 24010668 DOI: 10.1016/J.Bpj.2013.07.033 |
0.697 |
|
| 2013 |
Zayner JP, Antoniou C, French AR, Hause RJ, Sosnick TR. Investigating models of protein function and allostery with a widespread mutational analysis of a light-activated protein. Biophysical Journal. 105: 1027-36. PMID 23972854 DOI: 10.1016/J.Bpj.2013.07.010 |
0.8 |
|
| 2013 |
Adhikari AN, Freed KF, Sosnick TR. Simplified protein models: predicting folding pathways and structure using amino acid sequences. Physical Review Letters. 111: 028103. PMID 23889448 DOI: 10.1103/Physrevlett.111.028103 |
0.831 |
|
| 2013 |
Parisien M, Wang X, Perdrizet G, Lamphear C, Fierke CA, Maheshwari KC, Wilde MJ, Sosnick TR, Pan T. Discovering RNA-protein interactome by using chemical context profiling of the RNA-protein interface. Cell Reports. 3: 1703-13. PMID 23665222 DOI: 10.1016/J.Celrep.2013.04.010 |
0.694 |
|
| 2013 |
Adhikari AN, Freed KF, Sosnick TR. Simplified protein models: Predicting folding pathways and structure using amino acid sequences Physical Review Letters. 111. DOI: 10.1103/PhysRevLett.111.028103 |
0.455 |
|
| 2013 |
Sánchez-Rodríguez JE, Khalili-Araghi F, Adhikari A, Sosnick T, Roux B, Holmgren M, Bezanilla F. Probing Conformational Changes of the Na+/K+ ATPase upon Ouabain Binding by using a Spectroscopic Approach Biophysical Journal. 104: 300a. DOI: 10.1016/J.Bpj.2012.11.1669 |
0.775 |
|
| 2012 |
Adhikari AN, Freed KF, Sosnick TR. De novo prediction of protein folding pathways and structure using the principle of sequential stabilization. Proceedings of the National Academy of Sciences of the United States of America. 109: 17442-7. PMID 23045636 DOI: 10.1073/Pnas.1209000109 |
0.812 |
|
| 2012 |
Baxa MC, Haddadian EJ, Jha AK, Freed KF, Sosnick TR. Context and force field dependence of the loss of protein backbone entropy upon folding using realistic denatured and native state ensembles. Journal of the American Chemical Society. 134: 15929-36. PMID 22928488 DOI: 10.1021/Ja3064028 |
0.819 |
|
| 2012 |
Shandiz AT, Baxa MC, Sosnick TR. A "Link-Psi" strategy using crosslinking indicates that the folding transition state of ubiquitin is not very malleable. Protein Science : a Publication of the Protein Society. 21: 819-27. PMID 22528473 DOI: 10.1002/Pro.2065 |
0.8 |
|
| 2012 |
Yoo TY, Adhikari A, Xia Z, Huynh T, Freed KF, Zhou R, Sosnick TR. The folding transition state of protein L is extensive with nonnative interactions (and not small and polarized). Journal of Molecular Biology. 420: 220-34. PMID 22522126 DOI: 10.1016/J.Jmb.2012.04.013 |
0.824 |
|
| 2012 |
Zayner JP, Antoniou C, Sosnick TR. The amino-terminal helix modulates light-activated conformational changes in AsLOV2. Journal of Molecular Biology. 419: 61-74. PMID 22406525 DOI: 10.1016/J.Jmb.2012.02.037 |
0.788 |
|
| 2012 |
Parisien M, Freed KF, Sosnick TR. On docking, scoring and assessing protein-DNA complexes in a rigid-body framework. Plos One. 7: e32647. PMID 22393431 DOI: 10.1371/Journal.Pone.0032647 |
0.512 |
|
| 2012 |
Strickland D, Lin Y, Wagner E, Hope CM, Zayner J, Antoniou C, Sosnick TR, Weiss EL, Glotzer M. TULIPs: tunable, light-controlled interacting protein tags for cell biology. Nature Methods. 9: 379-84. PMID 22388287 DOI: 10.1038/Nmeth.1904 |
0.81 |
|
| 2012 |
Perdrizet GA, Artsimovitch I, Furman R, Sosnick TR, Pan T. Transcriptional pausing coordinates folding of the aptamer domain and the expression platform of a riboswitch. Proceedings of the National Academy of Sciences of the United States of America. 109: 3323-8. PMID 22331895 DOI: 10.1073/Pnas.1113086109 |
0.692 |
|
| 2012 |
Yoo TY, Meisburger SP, Hinshaw J, Pollack L, Haran G, Sosnick TR, Plaxco K. Small-angle X-ray scattering and single-molecule FRET spectroscopy produce highly divergent views of the low-denaturant unfolded state. Journal of Molecular Biology. 418: 226-36. PMID 22306460 DOI: 10.1016/J.Jmb.2012.01.016 |
0.796 |
|
| 2012 |
Adhikari AN, Peng J, Wilde M, Xu J, Freed KF, Sosnick TR. Modeling large regions in proteins: applications to loops, termini, and folding. Protein Science : a Publication of the Protein Society. 21: 107-21. PMID 22095743 DOI: 10.1002/Pro.767 |
0.806 |
|
| 2012 |
Debartolo J, Jha A, Freed KF, Sosnick TR. Local Backbone Preferences and Nearest-Neighbor Effects in the Unfolded and Native States Protein and Peptide Folding, Misfolding, and Non-Folding. 79-98. DOI: 10.1002/9781118183373.ch3 |
0.79 |
|
| 2011 |
Sosnick TR, Hinshaw JR. Biochemistry. How proteins fold. Science (New York, N.Y.). 334: 464-5. PMID 22034424 DOI: 10.1126/Science.1214018 |
0.44 |
|
| 2011 |
Virtanen JJ, Makowski L, Sosnick TR, Freed KF. Modeling the hydration layer around proteins: applications to small- and wide-angle x-ray scattering. Biophysical Journal. 101: 2061-9. PMID 22004761 DOI: 10.1016/J.Bpj.2011.09.021 |
0.535 |
|
| 2011 |
Haddadian EJ, Gong H, Jha AK, Yang X, Debartolo J, Hinshaw JR, Rice PA, Sosnick TR, Freed KF. Automated real-space refinement of protein structures using a realistic backbone move set. Biophysical Journal. 101: 899-909. PMID 21843481 DOI: 10.1016/J.Bpj.2011.06.063 |
0.808 |
|
| 2011 |
Ralat LA, Kalas V, Zheng Z, Goldman RD, Sosnick TR, Tang WJ. Ubiquitin is a novel substrate for human insulin-degrading enzyme. Journal of Molecular Biology. 406: 454-66. PMID 21185309 DOI: 10.1016/J.Jmb.2010.12.026 |
0.601 |
|
| 2011 |
Sosnick TR, Barrick D. The folding of single domain proteins--have we reached a consensus? Current Opinion in Structural Biology. 21: 12-24. PMID 21144739 DOI: 10.1016/J.Bpj.2010.12.2223 |
0.42 |
|
| 2010 |
Baird NJ, Ludtke SJ, Khant H, Chiu W, Pan T, Sosnick TR. Discrete structure of an RNA folding intermediate revealed by cryo-electron microscopy. Journal of the American Chemical Society. 132: 16352-3. PMID 21038867 DOI: 10.1021/Ja107492B |
0.768 |
|
| 2010 |
Virtanen JJ, Makowski L, Sosnick TR, Freed KF. Modeling the hydration layer around proteins: HyPred. Biophysical Journal. 99: 1611-9. PMID 20816074 DOI: 10.1016/J.Bpj.2010.06.027 |
0.561 |
|
| 2010 |
Zhao F, Peng J, Debartolo J, Freed KF, Sosnick TR, Xu J. A probabilistic and continuous model of protein conformational space for template-free modeling. Journal of Computational Biology : a Journal of Computational Molecular Cell Biology. 17: 783-98. PMID 20583926 DOI: 10.1089/Cmb.2009.0235 |
0.817 |
|
| 2010 |
Strickland D, Yao X, Gawlak G, Rosen MK, Gardner KH, Sosnick TR. Rationally improving LOV domain-based photoswitches. Nature Methods. 7: 623-6. PMID 20562867 DOI: 10.1038/Nmeth.1473 |
0.319 |
|
| 2010 |
Baird NJ, Gong H, Zaheer SS, Freed KF, Pan T, Sosnick TR. Extended structures in RNA folding intermediates are due to nonnative interactions rather than electrostatic repulsion. Journal of Molecular Biology. 397: 1298-306. PMID 20188108 DOI: 10.1016/J.Jmb.2010.02.025 |
0.815 |
|
| 2010 |
Zheng Z, Sosnick TR. Protein vivisection reveals elusive intermediates in folding. Journal of Molecular Biology. 397: 777-88. PMID 20144618 DOI: 10.1016/J.Jmb.2010.01.056 |
0.66 |
|
| 2010 |
DeBartolo J, Hocky G, Wilde M, Xu J, Freed KF, Sosnick TR. Protein structure prediction enhanced with evolutionary diversity: SPEED. Protein Science : a Publication of the Protein Society. 19: 520-34. PMID 20066664 DOI: 10.1002/Pro.330 |
0.818 |
|
| 2009 |
Zhao F, Peng J, Debartolo J, Freed KF, Sosnick TR, Xu J. A Probabilistic Graphical Model for Ab Initio Folding. Research in Computational Molecular Biology : ... Annual International Conference, Recomb ... : Proceedings. Recomb (Conference : 2005-). 5541: 59-73. PMID 23459639 DOI: 10.1007/978-3-642-02008-7_5 |
0.823 |
|
| 2009 |
Baxa MC, Freed KF, Sosnick TR. Psi-constrained simulations of protein folding transition states: implications for calculating. Journal of Molecular Biology. 386: 920-8. PMID 19244613 DOI: 10.1016/J.Jmb.2009.01.010 |
0.809 |
|
| 2009 |
DeBartolo J, Colubri A, Jha AK, Fitzgerald JE, Freed KF, Sosnick TR. Mimicking the folding pathway to improve homology-free protein structure prediction. Proceedings of the National Academy of Sciences of the United States of America. 106: 3734-9. PMID 19237560 DOI: 10.1073/Pnas.0811363106 |
0.825 |
|
| 2009 |
Bosco GL, Baxa M, Sosnick TR. Metal binding kinetics of bi-histidine sites used in psi analysis: evidence of high-energy protein folding intermediates. Biochemistry. 48: 2950-9. PMID 19220047 DOI: 10.1021/Bi802072U |
0.806 |
|
| 2009 |
Horn JR, Sosnick TR, Kossiakoff AA. Principal determinants leading to transition state formation of a protein-protein complex, orientation trumps side-chain interactions. Proceedings of the National Academy of Sciences of the United States of America. 106: 2559-64. PMID 19196954 DOI: 10.1073/Pnas.0809800106 |
0.443 |
|
| 2009 |
Baxa MC, Freed KF, Sosnick TR. Investigating the Origins of Fractional ψ-values in Protein Folding Transition States Biophysical Journal. 96: 78a. DOI: 10.1016/J.Bpj.2008.12.305 |
0.826 |
|
| 2008 |
Chung HS, Shandiz A, Sosnick TR, Tokmakoff A. Probing the folding transition state of ubiquitin mutants by temperature-jump-induced downhill unfolding. Biochemistry. 47: 13870-7. PMID 19053229 DOI: 10.1021/Bi801603E |
0.811 |
|
| 2008 |
Strickland D, Moffat K, Sosnick TR. Light-activated DNA binding in a designed allosteric protein. Proceedings of the National Academy of Sciences of the United States of America. 105: 10709-14. PMID 18667691 DOI: 10.1073/Pnas.0709610105 |
0.37 |
|
| 2008 |
Baxa MC, Freed KF, Sosnick TR. Quantifying the structural requirements of the folding transition state of protein A and other systems. Journal of Molecular Biology. 381: 1362-81. PMID 18625237 DOI: 10.1016/J.Jmb.2008.06.067 |
0.852 |
|
| 2008 |
Sosnick TR. Kinetic barriers and the role of topology in protein and RNA folding. Protein Science : a Publication of the Protein Society. 17: 1308-18. PMID 18502978 DOI: 10.1110/Ps.036319.108 |
0.412 |
|
| 2008 |
Qu X, Smith GJ, Lee KT, Sosnick TR, Pan T, Scherer NF. Single-molecule nonequilibrium periodic Mg2+-concentration jump experiments reveal details of the early folding pathways of a large RNA. Proceedings of the National Academy of Sciences of the United States of America. 105: 6602-7. PMID 18448679 DOI: 10.1073/Pnas.0801436105 |
0.341 |
|
| 2008 |
Smith GJ, Lee KT, Qu X, Xie Z, Pesic J, Sosnick TR, Pan T, Scherer NF. A large collapsed-state RNA can exhibit simple exponential single-molecule dynamics. Journal of Molecular Biology. 378: 943-53. PMID 18402978 DOI: 10.1016/J.Jmb.2008.01.078 |
0.376 |
|
| 2007 |
Shandiz AT, Capraro BR, Sosnick TR. Intramolecular cross-linking evaluated as a structural probe of the protein folding transition state. Biochemistry. 46: 13711-9. PMID 17985931 DOI: 10.1021/Bi701042E |
0.808 |
|
| 2007 |
Baird NJ, Fang XW, Srividya N, Pan T, Sosnick TR. Folding of a universal ribozyme: the ribonuclease P RNA. Quarterly Reviews of Biophysics. 40: 113-61. PMID 17931443 DOI: 10.1017/S0033583507004623 |
0.735 |
|
| 2007 |
Fitzgerald JE, Jha AK, Colubri A, Sosnick TR, Freed KF. Reduced C(beta) statistical potentials can outperform all-atom potentials in decoy identification. Protein Science : a Publication of the Protein Society. 16: 2123-39. PMID 17893359 DOI: 10.1110/Ps.072939707 |
0.5 |
|
| 2007 |
Jacob J, Dothager RS, Thiyagarajan P, Sosnick TR. Fully reduced ribonuclease A does not expand at high denaturant concentration or temperature. Journal of Molecular Biology. 367: 609-15. PMID 17292402 DOI: 10.1016/J.Jmb.2007.01.012 |
0.334 |
|
| 2007 |
Watters AL, Deka P, Corrent C, Callender D, Varani G, Sosnick T, Baker D. The highly cooperative folding of small naturally occurring proteins is likely the result of natural selection. Cell. 128: 613-24. PMID 17289578 DOI: 10.1016/J.Cell.2006.12.042 |
0.47 |
|
| 2007 |
Fitzgerald JE, Jha AK, Sosnick TR, Freed KF. Polypeptide motions are dominated by peptide group oscillations resulting from dihedral angle correlations between nearest neighbors. Biochemistry. 46: 669-82. PMID 17223689 DOI: 10.1021/Bi061575X |
0.468 |
|
| 2007 |
Pandit AD, Krantz BA, Dothager RS, Sosnick TR. Characterizing protein folding transition States using Psi-analysis. Methods in Molecular Biology (Clifton, N.J.). 350: 83-104. PMID 16957319 DOI: 10.1385/1-59745-189-4:83 |
0.819 |
|
| 2006 |
Ruczinski I, Sosnick TR, Plaxco KW. Methods for the accurate estimation of confidence intervals on protein folding phi-values. Protein Science : a Publication of the Protein Society. 15: 2257-64. PMID 17008714 DOI: 10.1110/Ps.062230106 |
0.38 |
|
| 2006 |
Colubri A, Jha AK, Shen MY, Sali A, Berry RS, Sosnick TR, Freed KF. Minimalist representations and the importance of nearest neighbor effects in protein folding simulations. Journal of Molecular Biology. 363: 835-57. PMID 16982067 DOI: 10.1016/J.Jmb.2006.08.035 |
0.559 |
|
| 2006 |
Pandit AD, Jha A, Freed KF, Sosnick TR. Small proteins fold through transition states with native-like topologies. Journal of Molecular Biology. 361: 755-70. PMID 16876194 DOI: 10.1016/J.Jmb.2006.06.041 |
0.838 |
|
| 2006 |
Pan T, Sosnick T. RNA folding during transcription Annual Review of Biophysics and Biomolecular Structure. 35: 161-175. PMID 16689632 DOI: 10.1146/Annurev.Biophys.35.040405.102053 |
0.304 |
|
| 2006 |
Sosnick TR, Krantz BA, Dothager RS, Baxa M. Characterizing the protein folding transition state using psi analysis. Chemical Reviews. 106: 1862-76. PMID 16683758 DOI: 10.1021/Cr040431Q |
0.827 |
|
| 2006 |
Baird NJ, Srividya N, Krasilnikov AS, Mondragón A, Sosnick TR, Pan T. Structural basis for altering the stability of homologous RNAs from a mesophilic and a thermophilic bacterium. Rna (New York, N.Y.). 12: 598-606. PMID 16581805 DOI: 10.1261/Rna.2186506 |
0.765 |
|
| 2006 |
de los Rios MA, Muralidhara BK, Wildes D, Sosnick TR, Marqusee S, Wittung-Stafshede P, Plaxco KW, Ruczinski I. On the precision of experimentally determined protein folding rates and phi-values. Protein Science : a Publication of the Protein Society. 15: 553-63. PMID 16501226 DOI: 10.1110/Ps.051870506 |
0.377 |
|
| 2006 |
Shi Z, Chen K, Liu Z, Sosnick TR, Kallenbach NR. PII structure in the model peptides for unfolded proteins: studies on ubiquitin fragments and several alanine-rich peptides containing QQQ, SSS, FFF, and VVV. Proteins. 63: 312-21. PMID 16362932 DOI: 10.1002/Prot.20788 |
0.429 |
|
| 2005 |
Jha AK, Colubri A, Freed KF, Sosnick TR. Statistical coil model of the unfolded state: resolving the reconciliation problem. Proceedings of the National Academy of Sciences of the United States of America. 102: 13099-104. PMID 16131545 DOI: 10.1073/Pnas.0506078102 |
0.578 |
|
| 2005 |
Baird NJ, Westhof E, Qin H, Pan T, Sosnick TR. Structure of a folding intermediate reveals the interplay between core and peripheral elements in RNA folding. Journal of Molecular Biology. 352: 712-22. PMID 16115647 DOI: 10.1016/J.Jmb.2005.07.010 |
0.768 |
|
| 2005 |
Jha AK, Colubri A, Zaman MH, Koide S, Sosnick TR, Freed KF. Helix, sheet, and polyproline II frequencies and strong nearest neighbor effects in a restricted coil library. Biochemistry. 44: 9691-702. PMID 16008354 DOI: 10.1021/Bi0474822 |
0.513 |
|
| 2005 |
Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallée-Bélisle A, Main ER, Bemporad F, Qiu L, Teilum K, ... ... Sosnick TR, et al. Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Science : a Publication of the Protein Society. 14: 602-16. PMID 15689503 DOI: 10.1110/Ps.041205405 |
0.434 |
|
| 2005 |
Kohn JE, Millett IS, Jacob J, Zagrovic B, Dillon TM, Cingel N, Dothager RS, Seifert S, Thiyagarajan P, Sosnick TR, Hasan MZ, Pande VS, Ruczinski I, Doniach S, Plaxco KW. Erratum: Random-coil behavior and the dimensions of chemically unfolded proteins (Proceedings of The National Academy of Sciences of The United States of America (August 24, 2004) 101, 34 (12491-12496)) Proceedings of the National Academy of Sciences of the United States of America. 102. DOI: 10.1073/Pnas.0507472102 |
0.36 |
|
| 2005 |
Krantz B, Dothager R, Sosnick T. Erratum to “Discerning the Structure and Energy of Multiple Transition States in Protein Folding using ψ-Analysis” [J. Mol. Biol. (2004) 337, 463–475] Journal of Molecular Biology. 347: 1103. DOI: 10.1016/J.Jmb.2005.01.001 |
0.692 |
|
| 2004 |
Sosnick TR, Dothager RS, Krantz BA. Differences in the folding transition state of ubiquitin indicated by phi and psi analyses. Proceedings of the National Academy of Sciences of the United States of America. 101: 17377-82. PMID 15576508 DOI: 10.1073/Pnas.0407683101 |
0.719 |
|
| 2004 |
Meisner WK, Sosnick TR. Barrier-limited, microsecond folding of a stable protein measured with hydrogen exchange: Implications for downhill folding. Proceedings of the National Academy of Sciences of the United States of America. 101: 15639-44. PMID 15505204 DOI: 10.1073/Pnas.0404895101 |
0.813 |
|
| 2004 |
Sosnick TR. Comment on "Force-clamp spectroscopy monitors the folding trajectory of a single protein". Science (New York, N.Y.). 306: 411; author reply 41. PMID 15486276 DOI: 10.1126/Science.1100962 |
0.387 |
|
| 2004 |
Sosnick TR, Pan T. Reduced contact order and RNA folding rates. Journal of Molecular Biology. 342: 1359-65. PMID 15364565 DOI: 10.1016/J.Jmb.2004.08.002 |
0.373 |
|
| 2004 |
Meisner WK, Sosnick TR. Fast folding of a helical protein initiated by the collision of unstructured chains. Proceedings of the National Academy of Sciences of the United States of America. 101: 13478-82. PMID 15347811 DOI: 10.1073/Pnas.0404057101 |
0.8 |
|
| 2004 |
Kohn JE, Millett IS, Jacob J, Zagrovic B, Dillon TM, Cingel N, Dothager RS, Seifert S, Thiyagarajan P, Sosnick TR, Hasan MZ, Pande VS, Ruczinski I, Doniach S, Plaxco KW. Random-coil behavior and the dimensions of chemically unfolded proteins. Proceedings of the National Academy of Sciences of the United States of America. 101: 12491-6. PMID 15314214 DOI: 10.1073/Pnas.0403643101 |
0.395 |
|
| 2004 |
Jacob J, Krantz B, Dothager RS, Thiyagarajan P, Sosnick TR. Early collapse is not an obligate step in protein folding. Journal of Molecular Biology. 338: 369-82. PMID 15066438 DOI: 10.1016/J.Jmb.2004.02.065 |
0.736 |
|
| 2004 |
Krantz BA, Dothager RS, Sosnick TR. Discerning the structure and energy of multiple transition states in protein folding using psi-analysis. Journal of Molecular Biology. 337: 463-75. PMID 15003460 DOI: 10.1016/J.Jmb.2004.01.018 |
0.752 |
|
| 2004 |
Xie Z, Srividya N, Sosnick TR, Pan T, Scherer NF. Single-molecule studies highlight conformational heterogeneity in the early folding steps of a large ribozyme. Proceedings of the National Academy of Sciences of the United States of America. 101: 534-9. PMID 14704266 DOI: 10.1073/Pnas.2636333100 |
0.385 |
|
| 2003 |
Zaman MH, Shen MY, Berry RS, Freed KF, Sosnick TR. Investigations into sequence and conformational dependence of backbone entropy, inter-basin dynamics and the Flory isolated-pair hypothesis for peptides. Journal of Molecular Biology. 331: 693-711. PMID 12899838 DOI: 10.1016/S0022-2836(03)00765-4 |
0.503 |
|
| 2003 |
Sosnick TR, Pan T. RNA folding: models and perspectives. Current Opinion in Structural Biology. 13: 309-16. PMID 12831881 DOI: 10.1016/S0959-440X(03)00066-6 |
0.343 |
|
| 2003 |
Fang XW, Srividya N, Golden BL, Sosnick TR, Pan T. Stepwise conversion of a mesophilic to a thermophilic ribozyme. Journal of Molecular Biology. 330: 177-83. PMID 12823959 DOI: 10.1016/S0022-2836(03)00582-5 |
0.354 |
|
| 2003 |
Fernández A, Shen MY, Colubri A, Sosnick TR, Berry RS, Freed KF. Large-scale context in protein folding: villin headpiece. Biochemistry. 42: 664-71. PMID 12534278 DOI: 10.1021/Bi026510I |
0.557 |
|
| 2003 |
Zaman MH, Sosnick TR, Berry RS. Temperature dependence of reactions with multiple pathways Physical Chemistry Chemical Physics. 5: 2589-2594. DOI: 10.1039/B212671K |
0.365 |
|
| 2002 |
Krantz BA, Mayne L, Rumbley J, Englander SW, Sosnick TR. Fast and slow intermediate accumulation and the initial barrier mechanism in protein folding. Journal of Molecular Biology. 324: 359-71. PMID 12441113 DOI: 10.1016/S0022-2836(02)01029-X |
0.778 |
|
| 2002 |
Shi Z, Olson CA, Kallenbach NR, Sosnick TR. D/H amide isotope effect in model alpha-helical peptides. Journal of the American Chemical Society. 124: 13994-5. PMID 12440888 DOI: 10.1021/Ja027740N |
0.363 |
|
| 2002 |
Sosnick TR, Berry RS, Colubri A, Fernández A. Distinguishing foldable proteins from nonfolders: when and how do they differ? Proteins. 49: 15-23. PMID 12211012 DOI: 10.1002/Prot.10193 |
0.442 |
|
| 2002 |
Fernández A, Sosnick TR, Colubri A. Dynamics of hydrogen bond desolvation in protein folding. Journal of Molecular Biology. 321: 659-75. PMID 12206781 DOI: 10.1016/S0022-2836(02)00679-4 |
0.376 |
|
| 2002 |
Zaman MH, Berry RS, Sosnick TR. Entropic benefit of a cross-link in protein association. Proteins. 48: 341-51. PMID 12112701 DOI: 10.1002/Prot.10165 |
0.381 |
|
| 2002 |
Fang XW, Thiyagarajan P, Sosnick TR, Pan T. The rate-limiting step in the folding of a large ribozyme without kinetic traps. Proceedings of the National Academy of Sciences of the United States of America. 99: 8518-23. PMID 12084911 DOI: 10.1073/Pnas.142288399 |
0.373 |
|
| 2002 |
Krantz BA, Srivastava AK, Nauli S, Baker D, Sauer RT, Sosnick TR. Understanding protein hydrogen bond formation with kinetic H/D amide isotope effects. Nature Structural Biology. 9: 458-63. PMID 11979278 DOI: 10.1038/Nsb794 |
0.715 |
|
| 2002 |
Shi Z, Krantz BA, Kallenbach N, Sosnick TR. Contribution of hydrogen bonding to protein stability estimated from isotope effects. Biochemistry. 41: 2120-9. PMID 11841202 DOI: 10.1021/Bi011307T |
0.697 |
|
| 2001 |
Krantz BA, Sosnick TR. Engineered metal binding sites map the heterogeneous folding landscape of a coiled coil. Nature Structural Biology. 8: 1042-7. PMID 11694889 DOI: 10.1038/Nsb723 |
0.717 |
|
| 2001 |
Qin H, Sosnick TR, Pan T. Modular construction of a tertiary RNA structure: the specificity domain of the Bacillus subtilis RNase P RNA. Biochemistry. 40: 11202-10. PMID 11551219 DOI: 10.1021/Bi010076N |
0.321 |
|
| 2001 |
Lee BC, Croonquist PA, Sosnick TR, Hoff WD. PAS domain receptor photoactive yellow protein is converted to a molten globule state upon activation. The Journal of Biological Chemistry. 276: 20821-3. PMID 11319215 DOI: 10.1074/Jbc.C100106200 |
0.427 |
|
| 2001 |
Shelton VM, Sosnick TR, Pan T. Altering the intermediate in the equilibrium folding of unmodified yeast tRNAPhe with monovalent and divalent cations. Biochemistry. 40: 3629-38. PMID 11297430 DOI: 10.1021/Bi002646+ |
0.371 |
|
| 2001 |
Fang XW, Golden BL, Littrell K, Shelton V, Thiyagarajan P, Pan T, Sosnick TR. The thermodynamic origin of the stability of a thermophilic ribozyme. Proceedings of the National Academy of Sciences of the United States of America. 98: 4355-60. PMID 11296284 DOI: 10.1073/Pnas.071050698 |
0.412 |
|
| 2001 |
Fang XW, Yang XJ, Littrell K, Niranjanakumari S, Thiyagarajan P, Fierke CA, Sosnick TR, Pan T. The Bacillus subtilis RNase P holoenzyme contains two RNase P RNA and two RNase P protein subunits. Rna (New York, N.Y.). 7: 233-41. PMID 11233980 DOI: 10.1017/S1355838201001352 |
0.304 |
|
| 2000 |
Fang X, Littrell K, Yang XJ, Henderson SJ, Siefert S, Thiyagarajan P, Pan T, Sosnick TR. Mg2+-dependent compaction and folding of yeast tRNAPhe and the catalytic domain of the B. subtilis RNase P RNA determined by small-angle X-ray scattering. Biochemistry. 39: 11107-13. PMID 10998249 DOI: 10.1021/Bi000724N |
0.345 |
|
| 2000 |
Krantz BA, Sosnick TR. Distinguishing between two-state and three-state models for ubiquitin folding. Biochemistry. 39: 11696-701. PMID 10995237 DOI: 10.1021/Bi000792+ |
0.701 |
|
| 2000 |
Krantz BA, Moran LB, Kentsis A, Sosnick TR. D/H amide kinetic isotope effects reveal when hydrogen bonds form during protein folding. Nature Structural Biology. 7: 62-71. PMID 10625430 DOI: 10.1038/71265 |
0.789 |
|
| 1999 |
Fang X, Pan T, Sosnick TR. A thermodynamic framework and cooperativity in the tertiary folding of a Mg2+-dependent ribozyme. Biochemistry. 38: 16840-6. PMID 10606517 DOI: 10.1021/Bi991700N |
0.382 |
|
| 1999 |
Shelton VM, Sosnick TR, Pan T. Applicability of urea in the thermodynamic analysis of secondary and tertiary RNA folding. Biochemistry. 38: 16831-9. PMID 10606516 DOI: 10.1021/Bi991699S |
0.361 |
|
| 1999 |
Fang XW, Pan T, Sosnick TR. Mg2+-dependent folding of a large ribozyme without kinetic traps. Nature Structural Biology. 6: 1091-5. PMID 10581546 DOI: 10.1038/70016 |
0.365 |
|
| 1999 |
Moran LB, Schneider JP, Kentsis A, Reddy GA, Sosnick TR. Transition state heterogeneity in GCN4 coiled coil folding studied by using multisite mutations and crosslinking. Proceedings of the National Academy of Sciences of the United States of America. 96: 10699-704. PMID 10485889 DOI: 10.1073/Pnas.96.19.10699 |
0.674 |
|
| 1999 |
Bhattacharyya RP, Sosnick TR. Viscosity dependence of the folding kinetics of a dimeric and monomeric coiled coil. Biochemistry. 38: 2601-9. PMID 10029555 DOI: 10.1021/Bi982209J |
0.437 |
|
| 1999 |
Pan T, Fang X, Sosnick T. Pathway modulation, circular permutation and rapid RNA folding under kinetic control. Journal of Molecular Biology. 286: 721-31. PMID 10024446 DOI: 10.1006/Jmbi.1998.2516 |
0.367 |
|
| 1998 |
Qi PX, Sosnick TR, Englander SW. The burst phase in ribonuclease A folding and solvent dependence of the unfolded state. Nature Structural Biology. 5: 882-4. PMID 9783747 DOI: 10.1038/2321 |
0.625 |
|
| 1998 |
Kentsis A, Sosnick TR. Trifluoroethanol promotes helix formation by destabilizing backbone exposure: desolvation rather than native hydrogen bonding defines the kinetic pathway of dimeric coiled coil folding. Biochemistry. 37: 14613-22. PMID 9772190 DOI: 10.1021/Bi981641Y |
0.658 |
|
| 1998 |
Englander SW, Sosnick TR, Mayne LC, Shtilerman M, Qi PX, Bai Y. Fast and Slow Folding in Cytochrome c Accounts of Chemical Research. 31: 737-744. DOI: 10.1021/Ar970085H |
0.617 |
|
| 1997 |
Pan T, Sosnick TR. Intermediates and kinetic traps in the folding of a large ribozyme revealed by circular dichroism and UV absorbance spectroscopies and catalytic activity. Nature Structural Biology. 4: 931-8. PMID 9360610 DOI: 10.1038/Nsb1197-931 |
0.416 |
|
| 1997 |
Sosnick TR, Shtilerman MD, Mayne L, Englander SW. Ultrafast signals in protein folding and the polypeptide contracted state. Proceedings of the National Academy of Sciences of the United States of America. 94: 8545-50. PMID 9238013 DOI: 10.1073/Pnas.94.16.8545 |
0.617 |
|
| 1997 |
Englander SW, Mayne L, Bai Y, Sosnick TR. Hydrogen exchange: the modern legacy of Linderstrøm-Lang. Protein Science : a Publication of the Protein Society. 6: 1101-9. PMID 9144782 DOI: 10.1002/Pro.5560060517 |
0.658 |
|
| 1996 |
Sosnick TR, Jackson S, Wilk RR, Englander SW, DeGrado WF. The role of helix formation in the folding of a fully alpha-helical coiled coil. Proteins. 24: 427-32. PMID 9162943 DOI: 10.1002/(Sici)1097-0134(199604)24:4<427::Aid-Prot2>3.0.Co;2-B |
0.645 |
|
| 1996 |
Sosnick TR, Mayne L, Englander SW. Molecular collapse: the rate-limiting step in two-state cytochrome c folding. Proteins. 24: 413-26. PMID 9162942 DOI: 10.1002/(Sici)1097-0134(199604)24:4<413::Aid-Prot1>3.0.Co;2-F |
0.619 |
|
| 1996 |
Englander SW, Sosnick TR, Englander JJ, Mayne L. Mechanisms and uses of hydrogen exchange. Current Opinion in Structural Biology. 6: 18-23. PMID 8696968 DOI: 10.1016/S0959-440X(96)80090-X |
0.594 |
|
| 1996 |
DeGrado WF, Sosnick TR. Protein minimization: downsizing through mutation. Proceedings of the National Academy of Sciences of the United States of America. 93: 5680-1. PMID 8650151 DOI: 10.1073/Pnas.93.12.5680 |
0.506 |
|
| 1995 |
Olah GA, Gray DM, Gray CW, Kergil DL, Sosnick TR, Mark BL, Vaughan MR, Trewhella J. Structures of fd gene 5 protein.nucleic acid complexes: a combined solution scattering and electron microscopy study. Journal of Molecular Biology. 249: 576-94. PMID 7783213 DOI: 10.1006/Jmbi.1995.0320 |
0.572 |
|
| 1995 |
Bai Y, Sosnick TR, Mayne L, Englander SW. Protein folding intermediates: native-state hydrogen exchange. Science (New York, N.Y.). 269: 192-7. PMID 7618079 DOI: 10.1126/Science.7618079 |
0.639 |
|
| 1994 |
Sosnick TR, Mayne L, Hiller R, Englander SW. The barriers in protein folding. Nature Structural Biology. 1: 149-56. PMID 7656032 DOI: 10.1038/Nsb0394-149 |
0.646 |
|
| 1993 |
Olah GA, Mitchell RD, Sosnick TR, Walsh DA, Trewhella J. Solution structure of the cAMP-dependent protein kinase catalytic subunit and its contraction upon binding the protein kinase inhibitor peptide. Biochemistry. 32: 3649-57. PMID 8385485 DOI: 10.1021/Bi00065A018 |
0.585 |
|
| 1992 |
Sosnick TR, Benjamin DC, Novotny J, Seeger PA, Trewhella J. Distances between the antigen-binding sites of three murine antibody subclasses measured using neutron and X-ray scattering. Biochemistry. 31: 1779-86. PMID 1737031 DOI: 10.1021/Bi00121A028 |
0.519 |
|
| 1992 |
Sosnick TR, Trewhella J. Denatured states of ribonuclease A have compact dimensions and residual secondary structure. Biochemistry. 31: 8329-35. PMID 1525171 |
0.594 |
|
| 1991 |
Sosnick T, Charles S, Stubbs G, Yau P, Bradbury EM, Timmins P, Trewhella J. Orienting rigid and flexible biological assemblies in ferrofluids for small-angle neutron scattering studies. Biophysical Journal. 60: 1178-89. PMID 19431809 DOI: 10.1016/S0006-3495(91)82153-1 |
0.705 |
|
| 1991 |
Sokol PE, Silver RN, Sosnick TR, Snow WM. Comment on "Final-state effects on the deep-inelastic response of liquid 4He" Physical Review Letters. 67: 524. PMID 10044916 |
0.718 |
|
| 1991 |
Sosnick TR, Snow WM, Silver RN, Sokol PE. Deviations from the impulse approximation in liquid 4He: An experimental test at Q=23 Å -1. Physical Review. B, Condensed Matter. 43: 216-228. PMID 9996206 DOI: 10.1103/Physrevb.43.216 |
0.695 |
|
| 1991 |
Sokol PE, Silver RN, Sosnick TR, Snow WM. Comment on final-state effects on the deep-inelastic response of liquid 4 Physical Review Letters. 67: 524. DOI: 10.1103/PhysRevLett.67.524 |
0.502 |
|
| 1991 |
Sosnick TR, Snow WM, Silver RN, Sokol PE. Deviations from the impulse approximation in liquid He4: An experimental test at Q=23 -1 Physical Review B. 43: 216-228. DOI: 10.1103/PhysRevB.43.216 |
0.46 |
|
| 1990 |
Sosnick TR, Snow WM, Sokol PE. Deep-inelastic neutron scattering from liquid 4He. Physical Review. B, Condensed Matter. 41: 11185-11202. PMID 9993539 DOI: 10.1103/Physrevb.41.11185 |
0.696 |
|
| 1990 |
Herwig KW, Sokol PE, Sosnick TR, Snow WM, Blasdell RC. Density dependence of the momentum distribution in normal liquid 4He. Physical Review. B, Condensed Matter. 41: 103-110. PMID 9992743 DOI: 10.1103/Physrevb.41.103 |
0.698 |
|
| 1990 |
Sosnick TR, Snow WM, Sokol PE. Deep-inelastic neutron scattering from liquid He4 Physical Review B. 41: 11185-11202. DOI: 10.1103/PhysRevB.41.11185 |
0.462 |
|
| 1990 |
Herwig KW, Sokol PE, Sosnick TR, Snow WM, Blasdell RC. Density dependence of the momentum distribution in normal liquid He4 Physical Review B. 41: 103-110. DOI: 10.1103/PhysRevB.41.103 |
0.452 |
|
| 1989 |
Sosnick TR, Snow WM, Sokol PE, Silver RN. Momentum distributions in liquid 4He Epl. 9: 707-712. DOI: 10.1209/0295-5075/9/7/016 |
0.507 |
|
| Show low-probability matches. |