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PUBMED FOR HANDHELDS

Journal Abstract Search


132 related items for PubMed ID: 20823517

  • 1. High-resolution structure of an alpha-spectrin SH3-domain mutant with a redesigned hydrophobic core.
    Cámara-Artigas A, Andújar-Sánchez M, Ortiz-Salmerón E, Cuadri C, Cobos ES, Martin-Garcia JM.
    Acta Crystallogr Sect F Struct Biol Cryst Commun; 2010 Sep 01; 66(Pt 9):1023-7. PubMed ID: 20823517
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  • 5. 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. PubMed ID: 12684010
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  • 6. 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 04; 322(5):1147-58. PubMed ID: 12367534
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  • 9. The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved.
    Martínez JC, Serrano L.
    Nat Struct Biol; 1999 Nov 04; 6(11):1010-6. PubMed ID: 10542091
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  • 10. Obligatory steps in protein folding and the conformational diversity of the transition state.
    Martinez JC, Pisabarro MT, Serrano L.
    Nat Struct Biol; 1998 Aug 04; 5(8):721-9. PubMed ID: 9699637
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  • 11. High-resolution crystal structure of spectrin SH3 domain fused with a proline-rich peptide.
    Gushchina LV, Gabdulkhakov AG, Nikonov SV, Filimonov VV.
    J Biomol Struct Dyn; 2011 Dec 04; 29(3):485-95. PubMed ID: 22066535
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  • 12. 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 02; 7():22. PubMed ID: 17407569
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  • 13. Identification of a conserved aggregation-prone intermediate state in the folding pathways of Spc-SH3 amyloidogenic variants.
    Krobath H, Estácio SG, Faísca PFN, Shakhnovich EI.
    J Mol Biol; 2012 Oct 05; 422(5):705-722. PubMed ID: 22727745
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  • 14. Electrostatic effects in the folding of the SH3 domain of the c-Src tyrosine kinase: pH-dependence in 3D-domain swapping and amyloid formation.
    Bacarizo J, Martinez-Rodriguez S, Martin-Garcia JM, Andujar-Sanchez M, Ortiz-Salmeron E, Neira JL, Camara-Artigas A.
    PLoS One; 2014 Oct 05; 9(12):e113224. PubMed ID: 25490095
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  • 15. 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. PubMed ID: 9888794
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  • 16. Non-native local interactions in protein folding and stability: introducing a helical tendency in the all beta-sheet alpha-spectrin SH3 domain.
    Prieto J, Wilmans M, Jiménez MA, Rico M, Serrano L.
    J Mol Biol; 1997 May 16; 268(4):760-78. PubMed ID: 9175859
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  • 17. 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. PubMed ID: 18234212
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  • 18. [Design and structural and thermodynamic studies of a chimeric protein derived from spectrin SH3-domain].
    Gushchina LV, Gabdulkhakov AG, Filimonov VV.
    Mol Biol (Mosk); 2009 Mar 14; 43(3):483-91. PubMed ID: 19548534
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  • 19. Identification of a candidate human spectrin Src homology 3 domain-binding protein suggests a general mechanism of association of tyrosine kinases with the spectrin-based membrane skeleton.
    Ziemnicka-Kotula D, Xu J, Gu H, Potempska A, Kim KS, Jenkins EC, Trenkner E, Kotula L.
    J Biol Chem; 1998 May 29; 273(22):13681-92. PubMed ID: 9593709
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  • 20. 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. PubMed ID: 10764585
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