Steven T. Whitten, Ph.D. - Publications

Affiliations: 
2000 Johns Hopkins University, Baltimore, MD 
Area:
General Biophysics, Biochemistry

24 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
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  0.52
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. DOI: 10.1016/j.bpj.2015.06.008  0.52
2015 Dasari R, Masi M, Lisy R, Ferdérin M, English LR, Cimmino A, Mathieu V, Brenner AJ, Kuhn JG, Whitten ST, Evidente A, Kiss R, Kornienko A. Fungal metabolite ophiobolin A as a promising anti-glioma agent: In vivo evaluation, structure-activity relationship and unique pyrrolylation of primary amines Bioorganic and Medicinal Chemistry Letters. DOI: 10.1016/j.bmcl.2015.08.066  0.52
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  0.52
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  0.52
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  0.52
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  0.52
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  0.52
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  0.52
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  0.52
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  0.52
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  0.52
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  0.52
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  0.52
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  0.52
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+  0.52
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+  0.52
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  0.52
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  0.52
2005 Olmsted SS, Khanna KV, Ng EM, Whitten ST, Johnson ON, Markham RB, Cone RA, Moench TR. Low pH immobilizes and kills human leukocytes and prevents transmission of cell-associated HIV in a mouse model. Bmc Infectious Diseases. 5: 79. PMID 16194280 DOI: 10.1186/1471-2334-5-79  0.52
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  0.52
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  0.52
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  0.52
2000 Whitten ST, Garcia-Moreno EB. pH dependence of stability of staphylococcal nuclease: Evidence of substantial electrostatic interactions in the denatured state Biochemistry. 39: 14292-14304. PMID 11087378 DOI: 10.1021/bi001015c  0.52
Show low-probability matches.