| Year |
Citation |
Score |
| 2022 |
Chin AF, Wrabl JO, Hilser VJ. A thermodynamic atlas of proteomes reveals energetic innovation across the tree of life. Molecular Biology and Evolution. PMID 35038744 DOI: 10.1093/molbev/msac010 |
0.813 |
|
| 2022 |
Chin AF, Zheng Y, Hilser VJ. Phylogenetic convergence of phase separation and mitotic function in the disordered protein BuGZ. Protein Science : a Publication of the Protein Society. PMID 34984754 DOI: 10.1002/pro.4270 |
0.774 |
|
| 2021 |
White JT, Rives J, Tharp ME, Wrabl JO, Thompson EB, Hilser VJ. Tumor Susceptibility Gene 101 Regulates the Glucocorticoid Receptor through Disorder-Mediated Allostery. Biochemistry. PMID 34009973 DOI: 10.1021/acs.biochem.1c00079 |
0.792 |
|
| 2021 |
Grasso EM, Majumdar A, Wrabl JO, Frueh DP, Hilser VJ. Conserved allosteric ensembles in a disordered protein using TROSY/Anti-TROSY R-filtered spectroscopy. Biophysical Journal. PMID 33901472 DOI: 10.1016/j.bpj.2021.04.017 |
0.751 |
|
| 2020 |
Cho MH, Wrabl JO, Taylor J, Hilser VJ. Hidden dynamic signatures drive substrate selectivity in the disordered phosphoproteome. Proceedings of the National Academy of Sciences of the United States of America. PMID 32900925 DOI: 10.1073/Pnas.1921473117 |
0.742 |
|
| 2019 |
Wodak SJ, Paci E, Dokholyan NV, Berezovsky IN, Horovitz A, Li J, Hilser VJ, Bahar I, Karanicolas J, Stock G, Hamm P, Stote RH, Eberhardt J, Chebaro Y, Dejaegere A, et al. Allostery in Its Many Disguises: From Theory to Applications. Structure (London, England : 1993). PMID 30744993 DOI: 10.1016/J.Str.2019.01.003 |
0.371 |
|
| 2019 |
Chin AF, Hilser VJ, Zheng Y. The Disordered Protein Bugz Conserves Mitotic Function and Liquid-Liquid Phase Separation across 1.6 Billion Years of Evolution Biophysical Journal. 116: 179a-180a. DOI: 10.1016/J.Bpj.2018.11.997 |
0.751 |
|
| 2019 |
Hyung Cho M, Wrabl J, Hilser V, Taylor J. Phosphorylation Sites with S/T-P Motif: Possible Basal Anti-Aggregation Mechanism Biophysical Journal. 116: 65a. DOI: 10.1016/J.Bpj.2018.11.397 |
0.676 |
|
| 2019 |
Wrabl JO, Russo M, Hoffmann J, Sheetz K, Munoz A, Hilser VJ. Experimental Characterization of “Metamorphic” Proteins Predicted from an Ensemble-Based Thermodynamic Description Biophysical Journal. 116: 59a-60a. DOI: 10.1016/J.Bpj.2018.11.366 |
0.716 |
|
| 2019 |
Rives J, Rehfus J, Hilser VJ. Single-Molecule Force Spectroscopy of M-Value Mutants of Staphylococcal Nuclease Indicates Complex Protein Folding Landscape Biophysical Journal. 116: 186a-187a. DOI: 10.1016/J.Bpj.2018.11.1034 |
0.303 |
|
| 2018 |
Hoffmann J, Wrabl JO, Hilser VJ. The role of negative selection in protein evolution revealed through the energetics of the native sate ensemble. Proteins. 86: 1313. PMID 30549116 DOI: 10.1002/prot.25484 |
0.701 |
|
| 2018 |
Li J, Hilser VJ. Assessing Allostery in Intrinsically Disordered Proteins With Ensemble Allosteric Model. Methods in Enzymology. 611: 531-557. PMID 30471699 DOI: 10.1016/Bs.Mie.2018.09.004 |
0.569 |
|
| 2018 |
Saavedra HG, Wrabl JO, Anderson JA, Li J, Hilser VJ. Dynamic allostery can drive cold adaptation in enzymes. Nature. PMID 29875414 DOI: 10.1038/S41586-018-0183-2 |
0.784 |
|
| 2018 |
White JT, Li J, Grasso E, Wrabl JO, Hilser VJ. Ensemble allosteric model: energetic frustration within the intrinsically disordered glucocorticoid receptor. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 373. PMID 29735729 DOI: 10.1098/Rstb.2017.0175 |
0.834 |
|
| 2018 |
Li J, White JT, Saavedra H, Wrabl JO, Motlagh HN, Liu K, Sowers J, Schroer TA, Thompson EB, Hilser VJ. Correction: Genetically tunable frustration controls allostery in an intrinsically disordered transcription factor. Elife. 7. PMID 29431606 DOI: 10.7554/eLife.35768 |
0.741 |
|
| 2017 |
Li J, White JT, Saavedra H, Wrabl JO, Motlagh HN, Liu K, Sowers J, Schroer T, Thompson EB, Hilser VJ. Genetically tunable frustration controls allostery in an intrinsically disordered transcription factor. Elife. 6. PMID 29022880 DOI: 10.7554/Elife.30688 |
0.795 |
|
| 2017 |
White JT, Toptygin D, Cohen R, Murphy N, Hilser VJ. Structural Stability of the coiled-coil domain of Tumor Susceptibility Gene (TSG)-101. Biochemistry. PMID 28776372 DOI: 10.1021/Acs.Biochem.7B00469 |
0.759 |
|
| 2017 |
Chin AF, Hilser VJ. What's in an Average? An Ensemble View of Phosphorylation Effects. Structure (London, England : 1993). 25: 573-575. PMID 28380337 DOI: 10.1016/J.Str.2017.03.012 |
0.798 |
|
| 2016 |
Motlagh HN, Toptygin D, Kaiser CM, Hilser VJ. Single-Molecule Chemo-Mechanical Spectroscopy Provides Structural Identity of Folding Intermediates. Biophysical Journal. 110: 1280-1290. PMID 27028638 DOI: 10.1016/J.Bpj.2015.12.042 |
0.764 |
|
| 2016 |
Hoffmann J, Wrabl JO, Hilser VJ. The role of negative selection in protein evolution revealed through the energetics of the native state ensemble. Proteins. 84: 435-47. PMID 26800099 DOI: 10.1002/Prot.24989 |
0.754 |
|
| 2016 |
Chin AF, Toptygin D, Elam WA, Schrank TP, Hilser VJ. Phosphorylation Increases Persistence Length and End-to-End Distance of a Segment of Tau Protein. Biophysical Journal. 110: 362-71. PMID 26789759 DOI: 10.1016/J.Bpj.2015.12.013 |
0.816 |
|
| 2016 |
Anderson JA, Majumdar A, Hilser VJ. Catching Excited States in the Act: Functional Unfolding in E. Coli Adenylate Kinase Biophysical Journal. 110: 207a-208a. DOI: 10.1016/J.Bpj.2015.11.1155 |
0.397 |
|
| 2016 |
Hilser VJ. Simultaneous Tuning of Activation and Repression in Intrinsic Disorder-Mediated Allostery Biophysical Journal. 110: 2a-3a. DOI: 10.1016/J.Bpj.2015.11.054 |
0.514 |
|
| 2016 |
Hoffmann J, Wrabl JO, Hilser VJ. The role of negative selection in protein evolution revealed through the energetics of the native state ensemble Proteins: Structure, Function and Bioinformatics. 84: 435-447. DOI: 10.1002/prot.24989 |
0.706 |
|
| 2015 |
Motlagh HN, Anderson JA, Li J, Hilser VJ. Disordered allostery: lessons from glucocorticoid receptor. Biophysical Reviews. 7: 257-265. PMID 28510173 DOI: 10.1007/S12551-015-0173-7 |
0.798 |
|
| 2015 |
Hilser VJ, Anderson JA, Motlagh HN. Allostery vs. "allokairy". Proceedings of the National Academy of Sciences of the United States of America. 112: 11430-1. PMID 26372953 DOI: 10.1073/Pnas.1515239112 |
0.748 |
|
| 2015 |
Toptygin D, Chin AF, Hilser VJ. Effect of Diffusion on Resonance Energy Transfer Rate Distributions: Implications for Distance Measurements. The Journal of Physical Chemistry. B. 119: 12603-22. PMID 26358033 DOI: 10.1021/Acs.Jpcb.5B06567 |
0.729 |
|
| 2015 |
Choi JH, Laurent AH, Hilser VJ, Ostermeier M. Design of protein switches based on an ensemble model of allostery. Nature Communications. 6: 6968. PMID 25902417 DOI: 10.1038/Ncomms7968 |
0.384 |
|
| 2015 |
Martens AT, Taylor J, Hilser VJ. Ribosome A and P sites revealed by length analysis of ribosome profiling data. Nucleic Acids Research. 43: 3680-7. PMID 25805170 DOI: 10.1093/Nar/Gkv200 |
0.781 |
|
| 2015 |
Anderson JA, Hilser VJ. Functional Unfolding in E. coli Adenylate Kinase Biophysical Journal. 108: 30a. DOI: 10.1016/J.Bpj.2014.11.190 |
0.405 |
|
| 2015 |
Motlagh HN, Hilser VJ. Single-Molecule Force Spectroscopy on Unfolded and Intrinsically Disordered Proteins Biophysical Journal. 108: 229a. DOI: 10.1016/J.Bpj.2014.11.1263 |
0.776 |
|
| 2015 |
Chin AF, Toptygin D, Hilser VJ. Phosphorylation Modulates Conformational Bias of a Disordered Peptide Biophysical Journal. 108: 229a. DOI: 10.1016/J.Bpj.2014.11.1262 |
0.785 |
|
| 2015 |
Li J, Wrabl JO, Hilser VJ. Intrinsically Disordered Protein: A Thermodynamic Perspective Biophysical Journal. 108: 228a. DOI: 10.1016/J.Bpj.2014.11.1261 |
0.773 |
|
| 2015 |
Motlagh HN, Anderson JA, Li J, Hilser VJ. Disordered allostery: lessons from glucocorticoid receptor Biophysical Reviews. 7: 257-265. DOI: 10.1007/s12551-015-0173-7 |
0.727 |
|
| 2015 |
White JT, Motlagh HN, Li J, Brad Thompson E, Hilser VJ. Allosteric regulation and intrinsic disorder in nuclear hormone receptors Nuclear Receptors: From Structure to the Clinic. 73-91. DOI: 10.1007/978-3-319-18729-7_5 |
0.72 |
|
| 2014 |
Maillard RA, Liu T, Beasley DW, Barrett AD, Hilser VJ, Lee JC. Thermodynamic mechanism for the evasion of antibody neutralization in flaviviruses. Journal of the American Chemical Society. 136: 10315-24. PMID 24950171 DOI: 10.1021/Ja503318X |
0.366 |
|
| 2014 |
Motlagh HN, Wrabl JO, Li J, Hilser VJ. The ensemble nature of allostery. Nature. 508: 331-9. PMID 24740064 DOI: 10.1038/Nature13001 |
0.825 |
|
| 2014 |
Hilser VJ, Whitten ST. Using the COREX/BEST server to model the native-state ensemble. Methods in Molecular Biology (Clifton, N.J.). 1084: 255-69. PMID 24061926 DOI: 10.1007/978-1-62703-658-0_14 |
0.416 |
|
| 2013 |
Hadzipasic O, Wrabl JO, Hilser VJ. A horizontal alignment tool for numerical trend discovery in sequence data: application to protein hydropathy. Plos Computational Biology. 9: e1003247. PMID 24130469 DOI: 10.1371/Journal.Pcbi.1003247 |
0.714 |
|
| 2013 |
Hilser VJ. Structural biology: Signalling from disordered proteins. Nature. 498: 308-10. PMID 23783624 DOI: 10.1038/498308A |
0.446 |
|
| 2013 |
Schrank TP, Wrabl JO, Hilser VJ. Conformational heterogeneity within the LID domain mediates substrate binding to Escherichia coli adenylate kinase: function follows fluctuations. Topics in Current Chemistry. 337: 95-121. PMID 23543318 DOI: 10.1007/128_2012_410 |
0.751 |
|
| 2013 |
Hegde ML, Tsutakawa SE, Hegde PM, Holthauzen LM, Li J, Oezguen N, Hilser VJ, Tainer JA, Mitra S. The disordered C-terminal domain of human DNA glycosylase NEIL1 contributes to its stability via intramolecular interactions. Journal of Molecular Biology. 425: 2359-71. PMID 23542007 DOI: 10.1016/J.Jmb.2013.03.030 |
0.459 |
|
| 2013 |
Elam WA, Schrank TP, Campagnolo AJ, Hilser VJ. Temperature and urea have opposing impacts on polyproline II conformational bias. Biochemistry. 52: 949-58. PMID 23350874 DOI: 10.1021/Bi301435P |
0.806 |
|
| 2013 |
Elam WA, Schrank TP, Campagnolo AJ, Hilser VJ. Evolutionary conservation of the polyproline II conformation surrounding intrinsically disordered phosphorylation sites. Protein Science : a Publication of the Protein Society. 22: 405-17. PMID 23341186 DOI: 10.1002/Pro.2217 |
0.81 |
|
| 2013 |
Hoffmann J, Wrabl JO, Hilser VJ. Towards the Design of Metamorphic Proteins using Ensemble-Based Energetic Information Biophysical Journal. 104: 564a. DOI: 10.1016/J.Bpj.2012.11.3127 |
0.75 |
|
| 2013 |
Motlagh HN, Hilser VJ. How Can a Ligand be a Positive and Negative Allosteric Effector for the Same Protein? Biophysical Journal. 104: 402a. DOI: 10.1016/J.Bpj.2012.11.2244 |
0.789 |
|
| 2012 |
Motlagh HN, Li J, Thompson EB, Hilser VJ. Interplay between allostery and intrinsic disorder in an ensemble. Biochemical Society Transactions. 40: 975-80. PMID 22988850 DOI: 10.1042/Bst20120163 |
0.793 |
|
| 2012 |
Li J, Motlagh HN, Chakuroff C, Thompson EB, Hilser VJ. Thermodynamic dissection of the intrinsically disordered N-terminal domain of human glucocorticoid receptor. The Journal of Biological Chemistry. 287: 26777-87. PMID 22669939 DOI: 10.1074/Jbc.M112.355651 |
0.793 |
|
| 2012 |
Hilser VJ, Wrabl JO, Motlagh HN. Structural and energetic basis of allostery. Annual Review of Biophysics. 41: 585-609. PMID 22577828 DOI: 10.1146/Annurev-Biophys-050511-102319 |
0.808 |
|
| 2012 |
Fu Y, Kasinath V, Moorman VR, Nucci NV, Hilser VJ, Wand AJ. Coupled motion in proteins revealed by pressure perturbation. Journal of the American Chemical Society. 134: 8543-50. PMID 22452540 DOI: 10.1021/Ja3004655 |
0.316 |
|
| 2012 |
Motlagh HN, Hilser VJ. Agonism/antagonism switching in allosteric ensembles. Proceedings of the National Academy of Sciences of the United States of America. 109: 4134-9. PMID 22388747 DOI: 10.1073/Pnas.1120519109 |
0.8 |
|
| 2012 |
Liu T, Pantazatos D, Li S, Hamuro Y, Hilser VJ, Woods VL. Quantitative assessment of protein structural models by comparison of H/D exchange MS data with exchange behavior accurately predicted by DXCOREX. Journal of the American Society For Mass Spectrometry. 23: 43-56. PMID 22012689 DOI: 10.1007/S13361-011-0267-9 |
0.396 |
|
| 2012 |
Elam WA, Schrank TP, Hilser VJ. Experimental and Computational Studies of Polyproline II Propensity Protein and Peptide Folding, Misfolding, and Non-Folding. 159-185. DOI: 10.1002/9781118183373.ch6 |
0.707 |
|
| 2011 |
Hilser VJ, Thompson EB. Structural dynamics, intrinsic disorder, and allostery in nuclear receptors as transcription factors. The Journal of Biological Chemistry. 286: 39675-82. PMID 21937423 DOI: 10.1074/Jbc.R111.278929 |
0.435 |
|
| 2011 |
Wrabl JO, Gu J, Liu T, Schrank TP, Whitten ST, Hilser VJ. The role of protein conformational fluctuations in allostery, function, and evolution. Biophysical Chemistry. 159: 129-41. PMID 21684672 DOI: 10.1016/J.Bpc.2011.05.020 |
0.78 |
|
| 2011 |
Schrank TP, Elam WA, Li J, Hilser VJ. Strategies for the thermodynamic characterization of linked binding/local folding reactions within the native state application to the LID domain of adenylate kinase from Escherichia coli. Methods in Enzymology. 492: 253-82. PMID 21333795 DOI: 10.1016/B978-0-12-381268-1.00020-3 |
0.797 |
|
| 2011 |
Hilser VJ. Structural biology: Finding the wet spots. Nature. 469: 166-7. PMID 21228863 DOI: 10.1038/469166A |
0.358 |
|
| 2011 |
Hilser VJ. Allostery in an Ensemble Biophysical Journal. 100: 26a. DOI: 10.1016/J.Bpj.2010.12.348 |
0.503 |
|
| 2011 |
Elam WA, Schrank TP, Hilser VJ. Direct Calorimetric Determination of a Complete Polyproline II (pII) Propensity Scale Reveals PII Enhancement in Intrinsically Disordered Proteins Biophysical Journal. 100: 229a. DOI: 10.1016/J.Bpj.2010.12.1463 |
0.804 |
|
| 2010 |
Wrabl JO, Hilser VJ. Investigating homology between proteins using energetic profiles. Plos Computational Biology. 6: e1000722. PMID 20361049 DOI: 10.1371/Journal.Pcbi.1000722 |
0.762 |
|
| 2010 |
Hilser VJ. Biochemistry. An ensemble view of allostery. Science (New York, N.Y.). 327: 653-4. PMID 20133562 DOI: 10.1126/Science.1186121 |
0.416 |
|
| 2009 |
Schrank TP, Bolen DW, Hilser VJ. Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins. Proceedings of the National Academy of Sciences of the United States of America. 106: 16984-9. PMID 19805185 DOI: 10.1073/Pnas.0906510106 |
0.447 |
|
| 2009 |
Vertrees J, Wrabl JO, Hilser VJ. An energetic representation of protein architecture that is independent of primary and secondary structure. Biophysical Journal. 97: 1461-70. PMID 19720035 DOI: 10.1016/J.Bpj.2009.06.020 |
0.76 |
|
| 2009 |
Gu J, Hilser VJ. Sequence-based analysis of protein energy landscapes reveals nonuniform thermal adaptation within the proteome. Molecular Biology and Evolution. 26: 2217-27. PMID 19592668 DOI: 10.1093/Molbev/Msp140 |
0.417 |
|
| 2009 |
Manson A, Whitten ST, Ferreon JC, Fox RO, Hilser VJ. Characterizing the role of ensemble modulation in mutation-induced changes in binding affinity. Journal of the American Chemical Society. 131: 6785-93. PMID 19397330 DOI: 10.1021/Ja809133U |
0.756 |
|
| 2009 |
Vertrees J, Wrabl JO, Hilser VJ. Energetic profiling of protein folds. Methods in Enzymology. 455: 299-327. PMID 19289211 DOI: 10.1016/S0076-6879(08)04211-0 |
0.752 |
|
| 2008 |
Gu J, Hilser VJ. Predicting the energetics of conformational fluctuations in proteins from sequence: a strategy for profiling the proteome. Structure (London, England : 1993). 16: 1627-37. PMID 19000815 DOI: 10.1016/J.Str.2008.08.016 |
0.479 |
|
| 2008 |
Wang S, Gu J, Larson SA, Whitten ST, Hilser VJ. Denatured-state energy landscapes of a protein structural database reveal the energetic determinants of a framework model for folding. Journal of Molecular Biology. 381: 1184-201. PMID 18616947 DOI: 10.1016/J.Jmb.2008.06.046 |
0.439 |
|
| 2008 |
Whitten ST, Yang HW, Fox RO, Hilser VJ. Exploring the impact of polyproline II (PII) conformational bias on the binding of peptides to the SEM-5 SH3 domain. Protein Science : a Publication of the Protein Society. 17: 1200-11. PMID 18577755 DOI: 10.1110/Ps.033647.107 |
0.399 |
|
| 2008 |
Sayar K, Uğur O, Liu T, Hilser VJ, Onaran O. Exploring allosteric coupling in the alpha-subunit of heterotrimeric G proteins using evolutionary and ensemble-based approaches. Bmc Structural Biology. 8: 23. PMID 18454845 DOI: 10.1186/1472-6807-8-23 |
0.42 |
|
| 2008 |
Whitten ST, García-Moreno BE, Hilser VJ. Ligand effects on the protein ensemble: unifying the descriptions of ligand binding, local conformational fluctuations, and protein stability. Methods in Cell Biology. 84: 871-91. PMID 17964952 DOI: 10.1016/S0091-679X(07)84027-1 |
0.435 |
|
| 2007 |
Hilser VJ, Thompson EB. Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins. Proceedings of the National Academy of Sciences of the United States of America. 104: 8311-5. PMID 17494761 DOI: 10.1073/Pnas.0700329104 |
0.473 |
|
| 2007 |
Liu T, Whitten ST, Hilser VJ. Functional residues serve a dominant role in mediating the cooperativity of the protein ensemble. Proceedings of the National Academy of Sciences of the United States of America. 104: 4347-52. PMID 17360527 DOI: 10.1073/Pnas.0607132104 |
0.479 |
|
| 2006 |
Whitten ST, Kurtz AJ, Pometun MS, Wand AJ, Hilser VJ. Revealing the nature of the native state ensemble through cold denaturation. Biochemistry. 45: 10163-74. PMID 16922491 DOI: 10.1021/Bi060855+ |
0.433 |
|
| 2006 |
Hilser VJ, García-Moreno E B, Oas TG, Kapp G, Whitten ST. A statistical thermodynamic model of the protein ensemble. Chemical Reviews. 106: 1545-58. PMID 16683744 DOI: 10.1021/Cr040423+ |
0.335 |
|
| 2006 |
Fitch CA, Whitten ST, Hilser VJ, García-Moreno E B. Molecular mechanisms of pH-driven conformational transitions of proteins: insights from continuum electrostatics calculations of acid unfolding. Proteins. 63: 113-26. PMID 16400648 DOI: 10.1002/Prot.20797 |
0.372 |
|
| 2006 |
Liu T, Whitten ST, Hilser VJ. Ensemble-based signatures of energy propagation in proteins: a new view of an old phenomenon. Proteins. 62: 728-38. PMID 16284972 DOI: 10.1002/Prot.20749 |
0.459 |
|
| 2005 |
Vertrees J, Barritt P, Whitten S, Hilser VJ. COREX/BEST server: a web browser-based program that calculates regional stability variations within protein structures. Bioinformatics (Oxford, England). 21: 3318-9. PMID 15923205 DOI: 10.1093/Bioinformatics/Bti520 |
0.438 |
|
| 2005 |
Whitten ST, García-Moreno E B, Hilser VJ. Local conformational fluctuations can modulate the coupling between proton binding and global structural transitions in proteins. Proceedings of the National Academy of Sciences of the United States of America. 102: 4282-7. PMID 15767576 DOI: 10.1073/Pnas.0407499102 |
0.435 |
|
| 2004 |
Ferreon JC, Hamburger JB, Hilser VJ. An experimental strategy to evaluate the thermodynamic stability of highly dynamic binding sites in proteins using hydrogen exchange. Journal of the American Chemical Society. 126: 12774-5. PMID 15469262 DOI: 10.1021/Ja046255K |
0.733 |
|
| 2004 |
Hamburger JB, Ferreon JC, Whitten ST, Hilser VJ. Thermodynamic mechanism and consequences of the polyproline II (PII) structural bias in the denatured states of proteins. Biochemistry. 43: 9790-9. PMID 15274633 DOI: 10.1021/Bi049352Z |
0.762 |
|
| 2004 |
Larson SA, Hilser VJ. Analysis of the "thermodynamic information content" of a Homo sapiens structural database reveals hierarchical thermodynamic organization. Protein Science : a Publication of the Protein Society. 13: 1787-801. PMID 15215522 DOI: 10.1110/Ps.04706204 |
0.452 |
|
| 2004 |
Ferreon JC, Hilser VJ. Thermodynamics of binding to SH3 domains: the energetic impact of polyproline II (PII) helix formation. Biochemistry. 43: 7787-97. PMID 15196021 DOI: 10.1021/Bi049752M |
0.729 |
|
| 2004 |
Babu CR, Hilser VJ, Wand AJ. Direct access to the cooperative substructure of proteins and the protein ensemble via cold denaturation. Nature Structural & Molecular Biology. 11: 352-7. PMID 14990997 DOI: 10.1038/Nsmb739 |
0.428 |
|
| 2004 |
Ferguson MR, Fan X, Mukherjee M, Luo J, Khan R, Ferreon JC, Hilser VJ, Shope RE, Fox RO. Directed discovery of bivalent peptide ligands to an SH3 domain. Protein Science : a Publication of the Protein Society. 13: 626-32. PMID 14978303 DOI: 10.1110/Ps.03470504 |
0.699 |
|
| 2003 |
Ferreon JC, Volk DE, Luxon BA, Gorenstein DG, Hilser VJ. Solution structure, dynamics, and thermodynamics of the native state ensemble of the Sem-5 C-terminal SH3 domain Biochemistry. 42: 5582-5591. PMID 12741814 DOI: 10.1021/Bi030005J |
0.751 |
|
| 2003 |
Ferreon JC, Hilser VJ. Ligand-induced changes in dynamics in the RT loop of the C-terminal SH3 domain of Sem-5 indicate cooperative conformational coupling. Protein Science : a Publication of the Protein Society. 12: 982-96. PMID 12717021 DOI: 10.1110/Ps.0238003 |
0.711 |
|
| 2003 |
Ferreon JC, Hilser VJ. The effect of the polyproline II (PPII) conformation on the denatured state entropy. Protein Science : a Publication of the Protein Society. 12: 447-57. PMID 12592015 DOI: 10.1110/Ps.0237803 |
0.724 |
|
| 2002 |
Wrabl JO, Larson SA, Hilser VJ. Thermodynamic environments in proteins: fundamental determinants of fold specificity. Protein Science : a Publication of the Protein Society. 11: 1945-57. PMID 12142449 DOI: 10.1110/Ps.0203202 |
0.74 |
|
| 2001 |
Wrabl JO, Larson SA, Hilser VJ. Thermodynamic propensities of amino acids in the native state ensemble: Implications for fold recognition Protein Science. 10: 1032-1045. PMID 11316884 DOI: 10.1110/ps.01601 |
0.714 |
|
| 2000 |
Pan H, Lee JC, Hilser VJ. Binding sites in Escherichia coli dihydrofolate reductase communicate by modulating the conformational ensemble Proceedings of the National Academy of Sciences of the United States of America. 97: 12020-12025. PMID 11035796 DOI: 10.1073/Pnas.220240297 |
0.448 |
|
| 2000 |
Wooll JO, Wrabl JO, Hilser VJ. Ensemble modulation as an origin of denaturant-independent hydrogen exchange in proteins Journal of Molecular Biology. 301: 247-256. PMID 10926507 DOI: 10.1006/Jmbi.2000.3889 |
0.719 |
|
| 1998 |
Hilser VJ, Dowdy D, Oas TG, Freire E. The structural distribution of cooperative interactions in proteins: analysis of the native state ensemble. Proceedings of the National Academy of Sciences of the United States of America. 95: 9903-8. PMID 9707573 DOI: 10.1073/Pnas.95.17.9903 |
0.405 |
|
| 1997 |
Hilser VJ, Townsend BD, Freire E. Structure-based statistical thermodynamic analysis of T4 lysozyme mutants: Structural mapping of cooperative interactions Biophysical Chemistry. 64: 69-79. PMID 9127939 DOI: 10.1016/S0301-4622(96)02220-X |
0.412 |
|
| 1997 |
Hilser VJ, Freire E. Predicting the equilibrium protein folding pathway: Structure-based analysis of staphylococcal nuclease Proteins: Structure, Function and Genetics. 27: 171-183. PMID 9061781 DOI: 10.1002/(Sici)1097-0134(199702)27:2<171::Aid-Prot3>3.0.Co;2-J |
0.603 |
|
| 1997 |
Hilser VJ, Freire E. The equilibrium ensemble of conformational states in staphylococcal nuclease Techniques in Protein Chemistry. 8: 767-781. DOI: 10.1016/S1080-8914(97)80075-0 |
0.594 |
|
| 1996 |
Hilser VJ, Gómez J, Freire E. The enthalpy change in protein folding and binding: Refinement of parameters for structure-based calculations Proteins: Structure, Function and Genetics. 26: 123-133. PMID 8916220 DOI: 10.1002/(Sici)1097-0134(199610)26:2<123::Aid-Prot2>3.0.Co;2-H |
0.587 |
|
| 1996 |
Hilser VJ, Freire E. Structure-based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors Journal of Molecular Biology. 262: 756-772. PMID 8876652 DOI: 10.1006/Jmbi.1996.0550 |
0.448 |
|
| 1996 |
D'Aquino JA, Gómez J, Hilser VJ, Lee KH, Amzel LM, Freire E. The magnitude of the backbone conformational entropy change in protein folding. Proteins. 25: 143-56. PMID 8811731 DOI: 10.1002/(Sici)1097-0134(199606)25:2<143::Aid-Prot1>3.0.Co;2-J |
0.579 |
|
| 1995 |
Hilser VJ, Freire E. Quantitative Analysis of Conformational Equilibrium Using Capillary Electrophoresis: Applications to Protein Folding Analytical Biochemistry. 224: 465-485. PMID 7733448 DOI: 10.1006/Abio.1995.1075 |
0.405 |
|
| 1995 |
Gomez J, Hilser VJ, Xie D, Freire E. The heat capacity of proteins Proteins: Structure, Function and Genetics. 22: 404-412. PMID 7479713 DOI: 10.1002/Prot.340220410 |
0.564 |
|
| 1993 |
Hilser VJ, Worosila GD, Freire E. Analysis of Thermally Induced Protein Folding/Unfolding Transitions Using Free Solution Capillary Electrophoresis Analytical Biochemistry. 208: 125-131. PMID 8434782 DOI: 10.1006/Abio.1993.1017 |
0.374 |
|
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