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Items: 1 to 20 of 380

1.

Cooperative propagation of local stability changes from low-stability and high-stability regions in a SH3 domain.

Casares S, López-Mayorga O, Vega MC, Cámara-Artigas A, Conejero-Lara F.

Proteins. 2007 May 15;67(3):531-47.

PMID:
17330285
2.

Structural cooperativity in the SH3 domain studied by site-directed mutagenesis and amide hydrogen exchange.

Casares S, Sadqi M, López-Mayorga O, Martínez JC, Conejero-Lara F.

FEBS Lett. 2003 Mar 27;539(1-3):125-30.

3.

The native state conformational ensemble of the SH3 domain from alpha-spectrin.

Sadqi M, Casares S, Abril MA, López-Mayorga O, Conejero-Lara F, Freire E.

Biochemistry. 1999 Jul 13;38(28):8899-906.

PMID:
10413463
4.

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
5.
6.

pH dependence of the hydrogen exchange in the SH3 domain of alpha-spectrin.

Sadqi M, Casares S, López-Mayorga O, Martínez JC, Conejero-Lara F.

FEBS Lett. 2002 Mar 13;514(2-3):295-9.

7.

Thermodynamic analysis of alpha-spectrin SH3 and two of its circular permutants with different loop lengths: discerning the reasons for rapid folding in proteins.

Martínez JC, Viguera AR, Berisio R, Wilmanns M, Mateo PL, Filimonov VV, Serrano L.

Biochemistry. 1999 Jan 12;38(2):549-59.

PMID:
9888794
8.

The temperature dependence of the hydrogen exchange in the SH3 domain of alpha-spectrin.

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

FEBS Lett. 2002 Sep 11;527(1-3):86-90.

9.

Insights into the origin of the tendency of the PI3-SH3 domain to form amyloid fibrils.

Ventura S, Lacroix E, Serrano L.

J Mol Biol. 2002 Oct 4;322(5):1147-58.

PMID:
12367534
10.

A binding event converted into a folding event.

Martín-Sierra FM, Candel AM, Casares S, Filimonov VV, Martínez JC, Conejero-Lara F.

FEBS Lett. 2003 Oct 23;553(3):328-32.

11.

Folding dynamics of the src SH3 domain.

Grantcharova VP, Baker D.

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

PMID:
9398297
12.

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
13.

The high-resolution NMR structure of the R21A Spc-SH3:P41 complex: understanding the determinants of binding affinity by comparison with Abl-SH3.

Casares S, Ab E, Eshuis H, Lopez-Mayorga O, van Nuland NA, Conejero-Lara F.

BMC Struct Biol. 2007 Apr 2;7:22.

14.

Similarities between the spectrin SH3 domain denatured state and its folding transition state.

Kortemme T, Kelly MJ, Kay LE, Forman-Kay J, Serrano L.

J Mol Biol. 2000 Apr 14;297(5):1217-29.

PMID:
10764585
15.
16.

The effect of a proline residue on the rate of growth and the space group of alpha-spectrin SH3-domain crystals.

Cámara-Artigas A, Andújar-Sánchez M, Ortiz-Salmerón E, Cuadri C, Casares S.

Acta Crystallogr D Biol Crystallogr. 2009 Dec;65(Pt 12):1247-52. doi: 10.1107/S0907444909038037. Epub 2009 Nov 17.

PMID:
19966410
17.

The role of backbone motions in ligand binding to the c-Src SH3 domain.

Wang C, Pawley NH, Nicholson LK.

J Mol Biol. 2001 Nov 2;313(4):873-87.

PMID:
11697910
18.

The high-resolution NMR structure of a single-chain chimeric protein mimicking a SH3-peptide complex.

Candel AM, Conejero-Lara F, Martinez JC, van Nuland NA, Bruix M.

FEBS Lett. 2007 Feb 20;581(4):687-92. Epub 2007 Jan 22.

19.

Plasticity and steric strain in a parallel beta-helix: rational mutations in the P22 tailspike protein.

Schuler B, Fürst F, Osterroth F, Steinbacher S, Huber R, Seckler R.

Proteins. 2000 Apr 1;39(1):89-101.

PMID:
10737931
20.

Bergerac-SH3: "frustation" induced by stabilizing the folding nucleus.

Viguera AR, Serrano L.

J Mol Biol. 2001 Aug 10;311(2):357-71.

PMID:
11478866

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