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Items: 1 to 20 of 109

1.

Mechanistic insights into the stabilization of srcSH3 by PEGylation.

Meng W, Guo X, Qin M, Pan H, Cao Y, Wang W.

Langmuir. 2012 Nov 20;28(46):16133-40. doi: 10.1021/la303466w. Epub 2012 Nov 8.

PMID:
23106398
2.

Criteria for selecting PEGylation sites on proteins for higher thermodynamic and proteolytic stability.

Lawrence PB, Gavrilov Y, Matthews SS, Langlois MI, Shental-Bechor D, Greenblatt HM, Pandey BK, Smith MS, Paxman R, Torgerson CD, Merrell JP, Ritz CC, Prigozhin MB, Levy Y, Price JL.

J Am Chem Soc. 2014 Dec 17;136(50):17547-60. doi: 10.1021/ja5095183. Epub 2014 Dec 4.

PMID:
25409346
3.

Folding dynamics of the src SH3 domain.

Grantcharova VP, Baker D.

Biochemistry. 1997 Dec 16;36(50):15685-92.

PMID:
9398297
4.

The effect of surface tethering on the folding of the src-SH3 protein domain.

Zhuang Z, Jewett AI, Soto P, Shea JE.

Phys Biol. 2009 Feb 10;6(1):015004. doi: 10.1088/1478-3975/6/1/015004.

PMID:
19208934
5.

Effects of PEG size on structure, function and stability of PEGylated BSA.

Plesner B, Fee CJ, Westh P, Nielsen AD.

Eur J Pharm Biopharm. 2011 Oct;79(2):399-405. doi: 10.1016/j.ejpb.2011.05.003. Epub 2011 May 18.

PMID:
21620970
6.

Experiment and theory highlight role of native state topology in SH3 folding.

Riddle DS, Grantcharova VP, Santiago JV, Alm E, Ruczinski I, Baker D.

Nat Struct Biol. 1999 Nov;6(11):1016-24.

PMID:
10542092
7.

Dramatic stabilization of an SH3 domain by a single substitution: roles of the folded and unfolded states.

Mok YK, Elisseeva EL, Davidson AR, Forman-Kay JD.

J Mol Biol. 2001 Mar 30;307(3):913-28.

PMID:
11273710
8.

Detection and characterization of partially unfolded oligomers of the SH3 domain of alpha-spectrin.

Casares S, Sadqi M, López-Mayorga O, Conejero-Lara F, van Nuland NA.

Biophys J. 2004 Apr;86(4):2403-13.

9.

Analysis of the thermodynamics of binding of an SH3 domain to proline-rich peptides using a chimeric fusion protein.

Candel AM, van Nuland NA, Martin-Sierra FM, Martinez JC, Conejero-Lara F.

J Mol Biol. 2008 Mar 14;377(1):117-35. doi: 10.1016/j.jmb.2007.11.060. Epub 2007 Nov 28.

PMID:
18234212
10.

A thermodynamic and kinetic analysis of the folding pathway of an SH3 domain entropically stabilised by a redesigned hydrophobic core.

Cobos ES, Filimonov VV, Vega MC, Mateo PL, Serrano L, Martínez JC.

J Mol Biol. 2003 Apr 18;328(1):221-33.

PMID:
12684010
12.

Four-state folding of a SH3 domain: salt-induced modulation of the stabilities of the intermediates and native state.

Dasgupta A, Udgaonkar JB.

Biochemistry. 2012 Jun 12;51(23):4723-34. doi: 10.1021/bi300223b. Epub 2012 May 30.

PMID:
22646838
13.

Purification of pegylated proteins.

Fee CJ, Van Alstine JM.

Methods Biochem Anal. 2011;54:339-62. Review.

PMID:
21954785
14.

Better biomolecule thermodynamics from kinetics.

Girdhar K, Scott G, Chemla YR, Gruebele M.

J Chem Phys. 2011 Jul 7;135(1):015102. doi: 10.1063/1.3607605.

PMID:
21744920
15.

PEGylation enhancement of pH stability of uricase via inhibitive tetramer dissociation.

Tian H, Guo Y, Gao X, Yao W.

J Pharm Pharmacol. 2013 Jan;65(1):53-63. doi: 10.1111/j.2042-7158.2012.01575.x. Epub 2012 Jul 30.

PMID:
23215688
16.

Stability and folding of the SH3 domain of Bruton's tyrosine kinase.

Chen YJ, Lin SC, Tzeng SR, Patel HV, Lyu PC, Cheng JW.

Proteins. 1996 Dec;26(4):465-71.

PMID:
8990499
18.

Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition.

Viguera AR, Martínez JC, Filimonov VV, Mateo PL, Serrano L.

Biochemistry. 1994 Mar 1;33(8):2142-50.

PMID:
7509635
19.

The relationship between conservation, thermodynamic stability, and function in the SH3 domain hydrophobic core.

Di Nardo AA, Larson SM, Davidson AR.

J Mol Biol. 2003 Oct 24;333(3):641-55.

PMID:
14556750
20.

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