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Trevor P. Creamer - Publications

Affiliations: 
University of Kentucky, Lexington, KY 
Area:
Biochemistry, General Biophysics
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53 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
2020 Cook EC, Creamer TP. Influence of Electrostatic Forces on the Association Kinetics and Conformational Ensemble of an Intrinsically Disordered Protein. Proteins. PMID 32654182 DOI: 10.1002/Prot.25979  0.419
2019 Sun B, Vaughan DM, Tikunova SB, Creamer TP, Davis JP, Kekenes-Huskey PM. Calmodulin/Calcineurin Interaction Beyond the Calmodulin-binding Region Contributes to Calcineurin Activation. Biochemistry. PMID 31483613 DOI: 10.1021/Acs.Biochem.9B00626  0.36
2018 Rydzanicz M, Wachowska M, Cook EC, Lisowski P, Kuźniewska B, Szymańska K, Diecke S, Prigione A, Szczałuba K, Szybińska A, Koppolu A, Murcia Pienkowski V, Kosińska J, Wiweger M, Kostrzewa G, ... ... Creamer TP, et al. Novel calcineurin A (PPP3CA) variant associated with epilepsy, constitutive enzyme activation and downregulation of protein expression. European Journal of Human Genetics : Ejhg. PMID 30254215 DOI: 10.1038/S41431-018-0254-8  0.339
2018 Sun B, Cook EC, Creamer TP, Kekenes-Huskey PM. Electrostatic control of calcineurin's intrinsically-disordered regulatory domain binding to calmodulin. Biochimica Et Biophysica Acta. PMID 30071273 DOI: 10.1016/J.Bbagen.2018.07.027  0.436
2017 Yadav DK, Tata SR, Hunt J, Cook EC, Creamer TP, Fitzkee NC. (1)H, (15)N, and (13)C chemical shift assignments of the regulatory domain of human calcineurin. Biomolecular Nmr Assignments. PMID 28803387 DOI: 10.1007/S12104-017-9751-X  0.312
2017 Kekenes-Huskey PM, Sun B, Cook EC, Creamer TP. The Competition between Electrostatic-Steering and Conformational Dynamics in the Diffusion-Limited Association of Calcineurin and Calmodulin Biophysical Journal. 112: 51a. DOI: 10.1016/J.Bpj.2016.11.312  0.442
2017 Creamer T. Role of Disordered Protein Ensembles in Protein-Protein Interactions: Calcineurin as a Model System Biophysical Journal. 112: 366a. DOI: 10.1016/J.Bpj.2016.11.1984  0.369
2016 Cook EC, Creamer TP. Calcineurin in a Crowded World. Biochemistry. PMID 27187005 DOI: 10.1021/Acs.Biochem.6B00059  0.384
2016 Creamer TP, Cook EC. Electrostatic Contributions to Calmodulin Interactions with Calcineurin Biophysical Journal. 110: 359a. DOI: 10.1016/J.Bpj.2015.11.1934  0.348
2015 Creamer TP, Cook EC, Dunlap TB. Transitional Disorder: Calcineurin as an Example Biophysical Journal. 108: 229a. DOI: 10.1016/J.Bpj.2014.11.1265  0.352
2014 Dunlap TB, Guo HF, Cook EC, Holbrook E, Rumi-Masante J, Lester TE, Colbert CL, Vander Kooi CW, Creamer TP. Stoichiometry of the calcineurin regulatory domain-calmodulin complex. Biochemistry. 53: 5779-90. PMID 25144868 DOI: 10.1021/Bi5004734  0.369
2013 Creamer TP. Transient disorder: Calcineurin as an example. Intrinsically Disordered Proteins. 1: e26412. PMID 28516023 DOI: 10.1016/J.Bpj.2013.11.2404  0.35
2013 Dunlap TB, Cook EC, Rumi-Masante J, Arvin HG, Lester TE, Creamer TP. The distal helix in the regulatory domain of calcineurin is important for domain stability and enzyme function. Biochemistry. 52: 8643-51. PMID 24191726 DOI: 10.1021/Bi400483A  0.409
2013 Juvvadi PR, Gehrke C, Fortwendel JR, Lamoth F, Soderblom EJ, Cook EC, Hast MA, Asfaw YG, Moseley MA, Creamer TP, Steinbach WJ. Phosphorylation of Calcineurin at a novel serine-proline rich region orchestrates hyphal growth and virulence in Aspergillus fumigatus. Plos Pathogens. 9: e1003564. PMID 23990785 DOI: 10.1371/Journal.Ppat.1003564  0.328
2013 Shen M, Bellaousov S, Hiller M, de La Grange P, Creamer TP, Malina O, Sperling R, Mathews DH, Stoilov P, Stamm S. Pyrvinium pamoate changes alternative splicing of the serotonin receptor 2C by influencing its RNA structure. Nucleic Acids Research. 41: 3819-32. PMID 23393189 DOI: 10.1093/Nar/Gkt063  0.325
2013 Dunlap TB, Kirk JM, Pena EA, Yoder MS, Creamer TP. Thermodynamics of binding by calmodulin correlates with target peptide α-helical propensity. Proteins. 81: 607-12. PMID 23180611 DOI: 10.1002/Prot.24215  0.452
2012 Smith EC, Gregory SM, Tamm LK, Creamer TP, Dutch RE. Role of sequence and structure of the Hendra fusion protein fusion peptide in membrane fusion. The Journal of Biological Chemistry. 287: 30035-48. PMID 22761418 DOI: 10.1074/Jbc.M112.367862  0.423
2012 Smith EC, Culler MR, Hellman LM, Fried MG, Creamer TP, Dutch RE. Beyond anchoring: the expanding role of the hendra virus fusion protein transmembrane domain in protein folding, stability, and function. Journal of Virology. 86: 3003-13. PMID 22238302 DOI: 10.1128/Jvi.05762-11  0.408
2012 Rumi-Masante J, Rusinga FI, Lester TE, Dunlap TB, Williams TD, Dunker AK, Weis DD, Creamer TP. Structural basis for activation of calcineurin by calmodulin. Journal of Molecular Biology. 415: 307-17. PMID 22100452 DOI: 10.1016/J.Jmb.2011.11.008  0.426
2011 Creamer TP, Rumi-Masante J, Lester TE, Dunlap TM, Rusinga F, Dunker AK, Weis DD. Activation of Calcineurin Involves a Folding Upon Binding Event Biophysical Journal. 100: 5a. DOI: 10.1016/J.Bpj.2010.12.236  0.332
2009 Thakur AK, Jayaraman M, Mishra R, Thakur M, Chellgren VM, Byeon IJ, Anjum DH, Kodali R, Creamer TP, Conway JF, Gronenborn AM, Wetzel R. Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism. Nature Structural & Molecular Biology. 16: 380-9. PMID 19270701 DOI: 10.1038/Nsmb.1570  0.42
2009 Creamer TP, Chellgren VM, Jensen AE, Lester T. Characterization of the Disordered Regulatory Domain from Calcineurin Biophysical Journal. 96: 219a-220a. DOI: 10.1016/J.Bpj.2008.12.1917  0.328
2008 Firestine AM, Chellgren VM, Rucker SJ, Lester TE, Creamer TP. Conformational properties of a peptide model for unfolded alpha-helices. Biochemistry. 47: 3216-24. PMID 18266321 DOI: 10.1021/Bi702474K  0.524
2007 Stevenson B, Choy HA, Pinne M, Rotondi ML, Miller MC, Demoll E, Kraiczy P, Cooley AE, Creamer TP, Suchard MA, Brissette CA, Verma A, Haake DA. Leptospira interrogans endostatin-like outer membrane proteins bind host fibronectin, laminin and regulators of complement. Plos One. 2: e1188. PMID 18000555 DOI: 10.1371/Journal.Pone.0001188  0.332
2006 Chellgren BW, Miller AF, Creamer TP. Evidence for polyproline II helical structure in short polyglutamine tracts. Journal of Molecular Biology. 361: 362-71. PMID 16854433 DOI: 10.1016/J.Jmb.2006.06.044  0.78
2006 Barrett DG, Minder CM, Mian MU, Whittington SJ, Cooper WJ, Fuchs KM, Tripathy A, Waters ML, Creamer TP, Pielak GJ. Pressure perturbation calorimetry of helical peptides. Proteins. 63: 322-6. PMID 16372358 DOI: 10.1002/Prot.20819  0.377
2006 Bhattacharyya A, Thakur AK, Chellgren VM, Thiagarajan G, Williams AD, Chellgren BW, Creamer TP, Wetzel R. Oligoproline effects on polyglutamine conformation and aggregation. Journal of Molecular Biology. 355: 524-35. PMID 16321399 DOI: 10.1016/J.Jmb.2005.10.053  0.746
2006 Chellgren BW, Creamer TP. Side-chain entropy effects on protein secondary structure formation. Proteins. 62: 411-20. PMID 16315271 DOI: 10.1002/Prot.20766  0.765
2005 Whittington SJ, Chellgren BW, Hermann VM, Creamer TP. Urea promotes polyproline II helix formation: implications for protein denatured states. Biochemistry. 44: 6269-75. PMID 15835915 DOI: 10.1021/Bi050124U  0.779
2004 Chellgren BW, Creamer TP. Effects of H2O and D2O on polyproline II helical structure. Journal of the American Chemical Society. 126: 14734-5. PMID 15535694 DOI: 10.1021/Ja045425Q  0.752
2004 Chellgren BW, Creamer TP. Short sequences of non-proline residues can adopt the polyproline II helical conformation. Biochemistry. 43: 5864-9. PMID 15134460 DOI: 10.1021/Bi049922V  0.78
2004 Sim KL, Creamer TP. Protein simple sequence conservation. Proteins. 54: 629-38. PMID 14997559 DOI: 10.1002/Prot.10623  0.415
2003 Whittington SJ, Creamer TP. Salt bridges do not stabilize polyproline II helices. Biochemistry. 42: 14690-5. PMID 14661982 DOI: 10.1021/Bi035565X  0.56
2003 Rucker AL, Pager CT, Campbell MN, Qualls JE, Creamer TP. Host-guest scale of left-handed polyproline II helix formation. Proteins. 53: 68-75. PMID 12945050 DOI: 10.1002/Prot.10477  0.575
2002 Sim KL, Creamer TP. Abundance and distributions of eukaryote protein simple sequences. Molecular & Cellular Proteomics : McP. 1: 983-95. PMID 12543934 DOI: 10.1074/Mcp.M200032-Mcp200  0.427
2002 Creamer TP, Campbell MN. Determinants of the polyproline II helix from modeling studies. Advances in Protein Chemistry. 62: 263-82. PMID 12418106 DOI: 10.1016/S0065-3233(02)62010-8  0.46
2002 Rucker AL, Creamer TP. Polyproline II helical structure in protein unfolded states: lysine peptides revisited. Protein Science : a Publication of the Protein Society. 11: 980-5. PMID 11910041 DOI: 10.1110/Ps.4550102  0.589
2001 Kelly MA, Chellgren BW, Rucker AL, Troutman JM, Fried MG, Miller AF, Creamer TP. Host-guest study of left-handed polyproline II helix formation. Biochemistry. 40: 14376-83. PMID 11724549 DOI: 10.1021/Bi011043A  0.787
2001 Creamer TP. Conformational entropy in protein folding. A guide to estimating conformational entropy via modeling and computation. Methods in Molecular Biology (Clifton, N.J.). 168: 117-32. PMID 11357622 DOI: 10.1385/1-59259-193-0:117  0.441
2000 Creamer TP. Side-chain conformational entropy in protein unfolded states. Proteins. 40: 443-50. PMID 10861935 DOI: 10.1002/1097-0134(20000815)40:3<443::Aid-Prot100>3.0.Co;2-L  0.471
1999 Stapley BJ, Creamer TP. A survey of left-handed polyproline II helices. Protein Science : a Publication of the Protein Society. 8: 587-95. PMID 10091661 DOI: 10.1110/Ps.8.3.587  0.589
1998 Creamer TP. Left-handed polyproline II helix formation is (very) locally driven. Proteins. 33: 218-26. PMID 9779789 DOI: 10.1002/(Sici)1097-0134(19981101)33:2<218::Aid-Prot6>3.0.Co;2-E  0.595
1997 Creamer TP, Srinivasan R, Rose GD. Modeling unfolded states of proteins and peptides. II. Backbone solvent accessibility. Biochemistry. 36: 2832-5. PMID 9062111 DOI: 10.1021/Bi962819O  0.416
1997 Aurora R, Creamer TP, Srinivasan R, Rose GD. Local interactions in protein folding: lessons from the alpha-helix. The Journal of Biological Chemistry. 272: 1413-6. PMID 9019474 DOI: 10.1074/Jbc.272.3.1413  0.377
1996 Aurora R, Creamer T, Lattman EE. 1996 Johns Hopkins Protein Folding Meeting Proteins. 25. PMID 8865335 DOI: 10.1002/Prot.340250402  0.399
1996 Creamer TP, Srinivasan R, Rose GD. Modeling unfolded states of peptides and proteins. Biochemistry. 34: 16245-50. PMID 8845348 DOI: 10.1021/Bi00050A003  0.508
1996 Wimley WC, Creamer TP, White SH. Solvation energies of amino acid side chains and backbone in a family of host - Guest pentapeptides Biochemistry. 35: 5109-5124. PMID 8611495 DOI: 10.1021/Bi9600153  0.408
1996 Wimley WC, Gawrisch K, Creamer TP, White SH. Direct measurement of salt-bridge solvation energies using a peptide model system: Implications for protein stability Proceedings of the National Academy of Sciences of the United States of America. 93: 2985-2990. PMID 8610155 DOI: 10.1073/Pnas.93.7.2985  0.364
1996 Creamer TP, Rose GD. Simple force field for study of peptide and protein conformational properties. Methods in Enzymology. 259: 576-89. PMID 8538473 DOI: 10.1016/0076-6879(95)59062-5  0.434
1995 Creamer TP, Rose GD. Interactions between hydrophobic side chains within alpha-helices. Protein Science : a Publication of the Protein Society. 4: 1305-14. PMID 7670373 DOI: 10.1002/Pro.5560040706  0.438
1995 Creamer TP, Srinivasan R, Rose GD. Evaluation of interactions between residues in α-helices by exhaustive conformational search Techniques in Protein Chemistry. 6: 443-450. DOI: 10.1016/S1080-8914(06)80054-2  0.514
1994 Creamer TP, Rose GD. Alpha-helix-forming propensities in peptides and proteins. Proteins. 19: 85-97. PMID 8090712 DOI: 10.1002/Prot.340190202  0.476
1992 Creamer TP, Rose GD. Side-chain entropy opposes alpha-helix formation but rationalizes experimentally determined helix-forming propensities. Proceedings of the National Academy of Sciences of the United States of America. 89: 5937-41. PMID 1631077 DOI: 10.1073/Pnas.89.13.5937  0.438
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