| Year |
Citation |
Score |
| 2023 |
Yarawsky AE, Ori AL, English LR, Whitten ST, Herr AB. Convergent behavior of extended stalk regions from staphylococcal surface proteins with widely divergent sequence patterns. Protein Science : a Publication of the Protein Society. e4707. PMID 37334491 DOI: 10.1002/pro.4707 |
0.304 |
|
| 2023 |
Yarawsky AE, Ori AL, English LR, Whitten ST, Herr AB. Convergent behavior of extended stalk regions from staphylococcal surface proteins with widely divergent sequence patterns. Biorxiv : the Preprint Server For Biology. PMID 36711672 DOI: 10.1101/2023.01.06.523059 |
0.333 |
|
| 2021 |
Paiz EA, Lewis KA, Whitten ST. Structural and Energetic Characterization of the Denatured State from the Perspectives of Peptides, the Coil Library, and Intrinsically Disordered Proteins. Molecules (Basel, Switzerland). 26. PMID 33530506 DOI: 10.3390/molecules26030634 |
0.464 |
|
| 2020 |
Whitten ST, English LR, Paiz EA. Heat Effects on Coil Hydrodynamic Size Reveal the Energetics of Denatured State Conformational Bias Biophysical Journal. 118: 182a. DOI: 10.1016/J.Bpj.2019.11.1112 |
0.341 |
|
| 2019 |
English LR, Voss SM, Tilton EC, Paiz EA, So S, Parra GL, Whitten ST. Impact of Heat on Coil Hydrodynamic Size Yields the Energetics of Denatured State Conformational Bias. The Journal of Physical Chemistry. B. PMID 31679343 DOI: 10.1021/Acs.Jpcb.9B09088 |
0.506 |
|
| 2019 |
Whitten ST, English LR. Conformational Bias in Unfolded Proteins Studied by Sequence Reversal Biophysical Journal. 116: 16a. DOI: 10.1016/J.Bpj.2018.11.130 |
0.459 |
|
| 2018 |
English LR, Tischer A, Demeler AK, Demeler B, Whitten ST. Sequence Reversal Prevents Chain Collapse and Yields Heat-Sensitive Intrinsic Disorder. Biophysical Journal. 115: 328-340. PMID 30021108 DOI: 10.1016/J.Bpj.2018.06.006 |
0.476 |
|
| 2017 |
Ezzell NA, Zhang Y, Whitten ST, Fitzkee NC. Improving the Performance of Simulations of the Intrinsically Disordered N-Terminal Domain from P53 Biophysical Journal. 112: 207a-208a. DOI: 10.1016/J.Bpj.2016.11.1146 |
0.486 |
|
| 2016 |
English LR, Tilton EC, Ricard BJ, Whitten ST. Intrinsic α helix propensities compact hydrodynamic radii in intrinsically disordered proteins. Proteins. PMID 27936491 DOI: 10.1002/Prot.25222 |
0.455 |
|
| 2016 |
Yarawsky AE, English LR, Whitten ST, Herr AB. The Proline/Glycine-Rich Region Of The Biofilm Adhesion Protein Aap Forms An Extended Stalk That Resists Compaction. Journal of Molecular Biology. PMID 27890783 DOI: 10.1016/J.Jmb.2016.11.017 |
0.361 |
|
| 2016 |
Tomasso ME, Tarver MJ, Devarajan D, Whitten ST. Hydrodynamic Radii of Intrinsically Disordered Proteins Determined from Experimental Polyproline II Propensities. Plos Computational Biology. 12: e1004686. PMID 26727467 DOI: 10.1371/Journal.Pcbi.1004686 |
0.471 |
|
| 2016 |
Whitten ST. Experimental Polyproline II Propensities Describe Sequence-Dependent Variability in the Hydrodynamic Size of Intrinsically Disordered Proteins Biophysical Journal. 110: 556a. DOI: 10.1016/J.Bpj.2015.11.2973 |
0.481 |
|
| 2015 |
Zimmermann MT, Tischer A, Whitten ST, Auton M. Structural origins of misfolding propensity in the platelet adhesive von willebrand factor A1 domain. Biophysical Journal. 109: 398-406. PMID 26200876 DOI: 10.1016/J.Bpj.2015.06.008 |
0.371 |
|
| 2014 |
Perez RB, Tischer A, Auton M, Whitten ST. Alanine and proline content modulate global sensitivity to discrete perturbations in disordered proteins. Proteins. 82: 3373-84. PMID 25244701 DOI: 10.1002/Prot.24692 |
0.513 |
|
| 2014 |
Langridge TD, Tarver MJ, Whitten ST. Temperature effects on the hydrodynamic radius of the intrinsically disordered N-terminal region of the p53 protein. Proteins. 82: 668-78. PMID 24150971 DOI: 10.1002/Prot.24449 |
0.433 |
|
| 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 |
0.472 |
|
| 2012 |
Schaub LJ, Campbell JC, Whitten ST. Thermal unfolding of the N-terminal region of p53 monitored by circular dichroism spectroscopy. Protein Science : a Publication of the Protein Society. 21: 1682-8. PMID 22915551 DOI: 10.1002/Pro.2146 |
0.423 |
|
| 2012 |
Campbell JC, Whitten ST. Mutational analysis of m-values as a strategy to identify cold-resistant substructures of the protein ensemble. Proteins. 80: 184-93. PMID 22038766 DOI: 10.1002/Prot.23178 |
0.489 |
|
| 2011 |
Bell-Upp P, Robinson AC, Whitten ST, Wheeler EL, Lin J, Stites WE, E BG. Thermodynamic principles for the engineering of pH-driven conformational switches and acid insensitive proteins. Biophysical Chemistry. 159: 217-26. PMID 21802194 DOI: 10.1016/J.Bpc.2011.06.016 |
0.457 |
|
| 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 |
0.527 |
|
| 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 |
0.51 |
|
| 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 |
0.488 |
|
| 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 |
0.438 |
|
| 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 |
0.604 |
|
| 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 |
0.513 |
|
| 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+ |
0.48 |
|
| 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+ |
0.367 |
|
| 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 |
0.474 |
|
| 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 |
0.498 |
|
| 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 |
0.509 |
|
| 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 |
0.517 |
|
| 2001 |
Whitten ST, Wooll JO, Razeghifard R, García-Moreno EB, Hilser VJ. The origin of pH-dependent changes in m-values for the denaturant-induced unfolding of proteins Journal of Molecular Biology. 309: 1165-1175. PMID 11399086 DOI: 10.1006/Jmbi.2001.4726 |
0.357 |
|
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