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Items: 47

1.

Calmodulin-Calcineurin Interaction beyond the Calmodulin-Binding Region Contributes to Calcineurin Activation.

Sun B, Vaughan D, Tikunova S, Creamer TP, Davis JP, Kekenes-Huskey PM.

Biochemistry. 2019 Oct 1;58(39):4070-4085. doi: 10.1021/acs.biochem.9b00626. Epub 2019 Sep 19.

PMID:
31483613
2.

Novel calcineurin A (PPP3CA) variant associated with epilepsy, constitutive enzyme activation and downregulation of protein expression.

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, Brzozowska M, Domańska-Pakieła D, Jurkiewicz E, Stawiński P, Gromadka A, Zielenkiewicz P, Demkow U, Dziembowska M, Kuźnicki J, Creamer TP, Płoski R.

Eur J Hum Genet. 2019 Jan;27(1):61-69. doi: 10.1038/s41431-018-0254-8. Epub 2018 Sep 25.

3.

Electrostatic control of calcineurin's intrinsically-disordered regulatory domain binding to calmodulin.

Sun B, Cook EC, Creamer TP, Kekenes-Huskey PM.

Biochim Biophys Acta Gen Subj. 2018 Dec;1862(12):2651-2659. doi: 10.1016/j.bbagen.2018.07.027. Epub 2018 Jul 31.

4.

1H, 15N, and 13C chemical shift assignments of the regulatory domain of human calcineurin.

Yadav DK, Tata SR, Hunt J, Cook EC, Creamer TP, Fitzkee NC.

Biomol NMR Assign. 2017 Oct;11(2):215-219. doi: 10.1007/s12104-017-9751-x. Epub 2017 Aug 12.

5.

Calcineurin in a Crowded World.

Cook EC, Creamer TP.

Biochemistry. 2016 Jun 7;55(22):3092-101. doi: 10.1021/acs.biochem.6b00059. Epub 2016 May 19.

6.

Identification of a Binding Site for Unsaturated Fatty Acids in the Orphan Nuclear Receptor Nurr1.

de Vera IM, Giri PK, Munoz-Tello P, Brust R, Fuhrmann J, Matta-Camacho E, Shang J, Campbell S, Wilson HD, Granados J, Gardner WJ Jr, Creamer TP, Solt LA, Kojetin DJ.

ACS Chem Biol. 2016 Jul 15;11(7):1795-9. doi: 10.1021/acschembio.6b00037. Epub 2016 Apr 29.

7.

Stoichiometry of the calcineurin regulatory domain-calmodulin complex.

Dunlap TB, Guo HF, Cook EC, Holbrook E, Rumi-Masante J, Lester TE, Colbert CL, Vander Kooi CW, Creamer TP.

Biochemistry. 2014 Sep 16;53(36):5779-90. doi: 10.1021/bi5004734. Epub 2014 Aug 29.

PMID:
25144868
8.

The distal helix in the regulatory domain of calcineurin is important for domain stability and enzyme function.

Dunlap TB, Cook EC, Rumi-Masante J, Arvin HG, Lester TE, Creamer TP.

Biochemistry. 2013 Dec 3;52(48):8643-51. doi: 10.1021/bi400483a. Epub 2013 Nov 15.

PMID:
24191726
9.

Transient disorder: Calcineurin as an example.

Creamer TP.

Intrinsically Disord Proteins. 2013 Sep 19;1(1):e26412. doi: 10.4161/idp.26412. eCollection 2013 Jan-Dec. Review.

10.

Phosphorylation of Calcineurin at a novel serine-proline rich region orchestrates hyphal growth and virulence in Aspergillus fumigatus.

Juvvadi PR, Gehrke C, Fortwendel JR, Lamoth F, Soderblom EJ, Cook EC, Hast MA, Asfaw YG, Moseley MA, Creamer TP, Steinbach WJ.

PLoS Pathog. 2013;9(8):e1003564. doi: 10.1371/journal.ppat.1003564. Epub 2013 Aug 22.

11.

Pyrvinium pamoate changes alternative splicing of the serotonin receptor 2C by influencing its RNA structure.

Shen M, Bellaousov S, Hiller M, de La Grange P, Creamer TP, Malina O, Sperling R, Mathews DH, Stoilov P, Stamm S.

Nucleic Acids Res. 2013 Apr 1;41(6):3819-32. doi: 10.1093/nar/gkt063. Epub 2013 Feb 7.

12.

Thermodynamics of binding by calmodulin correlates with target peptide α-helical propensity.

Dunlap TB, Kirk JM, Pena EA, Yoder MS, Creamer TP.

Proteins. 2013 Apr;81(4):607-12. doi: 10.1002/prot.24215. Epub 2012 Dec 24.

PMID:
23180611
13.

Role of sequence and structure of the Hendra fusion protein fusion peptide in membrane fusion.

Smith EC, Gregory SM, Tamm LK, Creamer TP, Dutch RE.

J Biol Chem. 2012 Aug 24;287(35):30035-48. doi: 10.1074/jbc.M112.367862. Epub 2012 Jul 3.

14.

Beyond anchoring: the expanding role of the hendra virus fusion protein transmembrane domain in protein folding, stability, and function.

Smith EC, Culler MR, Hellman LM, Fried MG, Creamer TP, Dutch RE.

J Virol. 2012 Mar;86(6):3003-13. doi: 10.1128/JVI.05762-11. Epub 2012 Jan 11.

15.

Structural basis for activation of calcineurin by calmodulin.

Rumi-Masante J, Rusinga FI, Lester TE, Dunlap TB, Williams TD, Dunker AK, Weis DD, Creamer TP.

J Mol Biol. 2012 Jan 13;415(2):307-17. doi: 10.1016/j.jmb.2011.11.008. Epub 2011 Nov 12.

16.

Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism.

Thakur AK, Jayaraman M, Mishra R, Thakur M, Chellgren VM, Byeon IJ, Anjum DH, Kodali R, Creamer TP, Conway JF, Gronenborn AM, Wetzel R.

Nat Struct Mol Biol. 2009 Apr;16(4):380-9. doi: 10.1038/nsmb.1570. Epub 2009 Mar 8.

17.

Conformational properties of a peptide model for unfolded alpha-helices.

Firestine AM, Chellgren VM, Rucker SJ, Lester TE, Creamer TP.

Biochemistry. 2008 Mar 11;47(10):3216-24. doi: 10.1021/bi702474k. Epub 2008 Feb 12.

PMID:
18266321
18.

Leptospira interrogans endostatin-like outer membrane proteins bind host fibronectin, laminin and regulators of complement.

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.

PLoS One. 2007 Nov 14;2(11):e1188.

19.

Evidence for polyproline II helical structure in short polyglutamine tracts.

Chellgren BW, Miller AF, Creamer TP.

J Mol Biol. 2006 Aug 11;361(2):362-71. Epub 2006 Jul 5.

PMID:
16854433
20.

Rose is a rose is a rose. Especially if you're a George.

Creamer TP, Fetrow JS.

Proteins. 2006 May 1;63(2):268-72. No abstract available.

PMID:
16493653
21.

Pressure perturbation calorimetry of helical peptides.

Barrett DG, Minder CM, Mian MU, Whittington SJ, Cooper WJ, Fuchs KM, Tripathy A, Waters ML, Creamer TP, Pielak GJ.

Proteins. 2006 May 1;63(2):322-6.

PMID:
16372358
22.

Oligoproline effects on polyglutamine conformation and aggregation.

Bhattacharyya A, Thakur AK, Chellgren VM, Thiagarajan G, Williams AD, Chellgren BW, Creamer TP, Wetzel R.

J Mol Biol. 2006 Jan 20;355(3):524-35. Epub 2005 Nov 9.

PMID:
16321399
23.

Side-chain entropy effects on protein secondary structure formation.

Chellgren BW, Creamer TP.

Proteins. 2006 Feb 1;62(2):411-20.

PMID:
16315271
24.

Urea promotes polyproline II helix formation: implications for protein denatured states.

Whittington SJ, Chellgren BW, Hermann VM, Creamer TP.

Biochemistry. 2005 Apr 26;44(16):6269-75.

PMID:
15835915
25.

Effects of H2O and D2O on polyproline II helical structure.

Chellgren BW, Creamer TP.

J Am Chem Soc. 2004 Nov 17;126(45):14734-5.

PMID:
15535694
26.

Short sequences of non-proline residues can adopt the polyproline II helical conformation.

Chellgren BW, Creamer TP.

Biochemistry. 2004 May 18;43(19):5864-9.

PMID:
15134460
27.

Protein simple sequence conservation.

Sim KL, Creamer TP.

Proteins. 2004 Mar 1;54(4):629-38.

PMID:
14997559
28.

Salt bridges do not stabilize polyproline II helices.

Whittington SJ, Creamer TP.

Biochemistry. 2003 Dec 16;42(49):14690-5.

PMID:
14661982
29.

Host-guest scale of left-handed polyproline II helix formation.

Rucker AL, Pager CT, Campbell MN, Qualls JE, Creamer TP.

Proteins. 2003 Oct 1;53(1):68-75.

PMID:
12945050
30.

Abundance and distributions of eukaryote protein simple sequences.

Sim KL, Creamer TP.

Mol Cell Proteomics. 2002 Dec;1(12):983-95.

31.

Determinants of the polyproline II helix from modeling studies.

Creamer TP, Campbell MN.

Adv Protein Chem. 2002;62:263-82. Review.

PMID:
12418106
32.
33.

Host-guest study of left-handed polyproline II helix formation.

Kelly MA, Chellgren BW, Rucker AL, Troutman JM, Fried MG, Miller AF, Creamer TP.

Biochemistry. 2001 Dec 4;40(48):14376-83.

PMID:
11724549
34.
35.

Side-chain conformational entropy in protein unfolded states.

Creamer TP.

Proteins. 2000 Aug 15;40(3):443-50.

PMID:
10861935
36.

A survey of left-handed polyproline II helices.

Stapley BJ, Creamer TP.

Protein Sci. 1999 Mar;8(3):587-95.

37.

Left-handed polyproline II helix formation is (very) locally driven.

Creamer TP.

Proteins. 1998 Nov 1;33(2):218-26.

PMID:
9779789
38.

Modeling unfolded states of proteins and peptides. II. Backbone solvent accessibility.

Creamer TP, Srinivasan R, Rose GD.

Biochemistry. 1997 Mar 11;36(10):2832-5.

PMID:
9062111
39.

Local interactions in protein folding: lessons from the alpha-helix.

Aurora R, Creamer TP, Srinivasan R, Rose GD.

J Biol Chem. 1997 Jan 17;272(3):1413-6. Review. No abstract available.

40.

Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides.

Wimley WC, Creamer TP, White SH.

Biochemistry. 1996 Apr 23;35(16):5109-24.

PMID:
8611495
41.

Direct measurement of salt-bridge solvation energies using a peptide model system: implications for protein stability.

Wimley WC, Gawrisch K, Creamer TP, White SH.

Proc Natl Acad Sci U S A. 1996 Apr 2;93(7):2985-90.

42.

Modeling unfolded states of peptides and proteins.

Creamer TP, Srinivasan R, Rose GD.

Biochemistry. 1995 Dec 19;34(50):16245-50.

PMID:
8845348
43.

Interactions between hydrophobic side chains within alpha-helices.

Creamer TP, Rose GD.

Protein Sci. 1995 Jul;4(7):1305-14.

44.

Simple force field for study of peptide and protein conformational properties.

Creamer TP, Rose GD.

Methods Enzymol. 1995;259:576-89. No abstract available.

PMID:
8538473
45.

Alpha-helix-forming propensities in peptides and proteins.

Creamer TP, Rose GD.

Proteins. 1994 Jun;19(2):85-97.

PMID:
8090712
46.

Protein folding: predicting predicting.

Rose GD, Creamer TP.

Proteins. 1994 May;19(1):1-3. No abstract available.

PMID:
8066081
47.

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