| 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 |
0.677 |
|
| 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 |
0.544 |
|
| 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 |
0.64 |
|
| 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 |
0.652 |
|
| 2019 |
Sowers ML, Anderson APP, Wrabl JO, Yin YW. Networked Communication between Polymerase and Exonuclease Active Sites in Human Mitochondrial DNA Polymerase. Journal of the American Chemical Society. PMID 31251605 DOI: 10.1021/Jacs.9B04655 |
0.343 |
|
| 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 |
0.553 |
|
| 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 |
0.641 |
|
| 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 |
0.627 |
|
| 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 |
0.624 |
|
| 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 |
0.694 |
|
| 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 |
0.517 |
|
| 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 |
0.672 |
|
| 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 |
0.703 |
|
| 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 |
0.625 |
|
| 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 |
0.688 |
|
| 2014 |
Motlagh HN, Wrabl JO, Li J, Hilser VJ. The ensemble nature of allostery. Nature. 508: 331-9. PMID 24740064 DOI: 10.1038/Nature13001 |
0.68 |
|
| 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 |
0.65 |
|
| 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 |
0.664 |
|
| 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 |
0.698 |
|
| 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 |
0.66 |
|
| 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 |
0.715 |
|
| 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 |
0.71 |
|
| 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 |
0.706 |
|
| 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 |
0.699 |
|
| 2008 |
Zhu L, Wrabl JO, Hayashi AP, Rose LS, Thomas PJ. The torsin-family AAA+ protein OOC-5 contains a critical disulfide adjacent to Sensor-II that couples redox state to nucleotide binding. Molecular Biology of the Cell. 19: 3599-612. PMID 18550799 DOI: 10.1091/Mbc.E08-01-0015 |
0.411 |
|
| 2008 |
Wrabl JO, Grishin NV. Statistics of random protein superpositions: p-values for pairwise structure alignment. Journal of Computational Biology : a Journal of Computational Molecular Cell Biology. 15: 317-55. PMID 18333756 DOI: 10.1089/Cmb.2007.0161 |
0.359 |
|
| 2004 |
Wrabl JO, Grishin NV. Gaps in structurally similar proteins: towards improvement of multiple sequence alignment. Proteins. 54: 71-87. PMID 14705025 DOI: 10.1002/Prot.10508 |
0.42 |
|
| 2003 |
Kinch LN, Wrabl JO, Krishna SS, Majumdar I, Sadreyev RI, Qi Y, Pei J, Cheng H, Grishin NV. CASP5 assessment of fold recognition target predictions. Proteins. 53: 395-409. PMID 14579328 DOI: 10.1002/Prot.10557 |
0.361 |
|
| 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 |
0.691 |
|
| 2002 |
Wrabl JO, Grishin NV. Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily. Journal of Molecular Biology. 314: 365-74. PMID 11846551 DOI: 10.1006/Jmbi.2001.5151 |
0.499 |
|
| 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 |
0.651 |
|
| 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 |
0.629 |
|
| 2000 |
Wrabl JO, Shortle D, Woolf TB. Correlation between changes in nuclear magnetic resonance order parameters and conformational entropy: molecular dynamics simulations of native and denatured staphylococcal nuclease. Proteins. 38: 123-33. PMID 10656260 DOI: 10.1002/(Sici)1097-0134(20000201)38:2<123::Aid-Prot2>3.0.Co;2-H |
0.368 |
|
| 1999 |
Wrabl J, Shortle D. A model of the changes in denatured state structure underlying m value effects in staphylococcal nuclease Nature Structural Biology. 6: 876-883. PMID 10467101 DOI: 10.1038/12338 |
0.306 |
|
| 1996 |
Wrabl JO, Shortle D. Perturbations of the denatured state ensemble: Modeling their effects on protein stability and folding kinetics Protein Science. 5: 2343-2352. PMID 8931153 DOI: 10.1002/Pro.5560051121 |
0.43 |
|
| 1996 |
Shortle D, Wang Y, Gillespie JR, Wrabl JO. Protein folding for realists: A timeless phenomenon Protein Science. 5: 991-1000. PMID 8762131 DOI: 10.1002/Pro.5560050602 |
0.533 |
|
| 1994 |
Wrabl J, Holtzer ME, Holtzer A. Thermal unfolding equilibria in homodimeric chicken gizzard tropomyosin coiled coils Biopolymers. 34: 1659-1667. PMID 7849227 DOI: 10.1002/Bip.360341210 |
0.329 |
|
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