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Journal Abstract Search

256 related items for PubMed ID: 21797671

  • 1. Contribution of disulfide bonds to stability, folding, and amyloid fibril formation: the PI3-SH3 domain case.
    Graña-Montes R, de Groot NS, Castillo V, Sancho J, Velazquez-Campoy A, Ventura S.
    Antioxid Redox Signal; 2012 Jan 01; 16(1):1-15. PubMed ID: 21797671
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  • 3. 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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  • 4. Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation.
    Bader R, Bamford R, Zurdo J, Luisi BF, Dobson CM.
    J Mol Biol; 2006 Feb 10; 356(1):189-208. PubMed ID: 16364365
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  • 5. Folding dynamics of the src SH3 domain.
    Grantcharova VP, Baker D.
    Biochemistry; 1997 Dec 16; 36(50):15685-92. PubMed ID: 9398297
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  • 6. Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy.
    Guijarro JI, Morton CJ, Plaxco KW, Campbell ID, Dobson CM.
    J Mol Biol; 1998 Feb 27; 276(3):657-67. PubMed ID: 9551103
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  • 7. NMR characterization of hydrophobic collapses in amyloidogenic unfolded states and their implications for amyloid formation.
    Lim KH, Nagchowdhuri P, Rathinavelan T, Im W.
    Biochem Biophys Res Commun; 2010 Jun 11; 396(4):800-5. PubMed ID: 20438713
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  • 8. Amyloid fibril formation by an SH3 domain.
    Guijarro JI, Sunde M, Jones JA, Campbell ID, Dobson CM.
    Proc Natl Acad Sci U S A; 1998 Apr 14; 95(8):4224-8. PubMed ID: 9539718
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  • 9. Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis.
    Polverino de Laureto P, Taddei N, Frare E, Capanni C, Costantini S, Zurdo J, Chiti F, Dobson CM, Fontana A.
    J Mol Biol; 2003 Nov 14; 334(1):129-41. PubMed ID: 14596805
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  • 10. 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. PubMed ID: 11273710
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  • 11. The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved.
    Martínez JC, Serrano L.
    Nat Struct Biol; 1999 Nov 30; 6(11):1010-6. PubMed ID: 10542091
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  • 12. High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure .
    Bayro MJ, Maly T, Birkett NR, Macphee CE, Dobson CM, Griffin RG.
    Biochemistry; 2010 Sep 07; 49(35):7474-84. PubMed ID: 20707313
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  • 19. NMR assignments of PI3-SH3 domain aided by protonless NMR spectroscopy.
    Hsu ST.
    Biomol NMR Assign; 2014 Oct 07; 8(2):291-5. PubMed ID: 23832674
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