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Journal Abstract Search

115 related items for PubMed ID: 22727745

  • 1. 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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  • 2. 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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  • 3. Characterization of oligomers of heterogeneous size as precursors of amyloid fibril nucleation of an SH3 domain: an experimental kinetics study.
    Ruzafa D, Morel B, Varela L, Azuaga AI, Conejero-Lara F.
    PLoS One; 2012 Oct 04; 7(11):e49690. PubMed ID: 23209591
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  • 4. 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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  • 9. The in vivo and in vitro aggregation properties of globular proteins correlate with their conformational stability: the SH3 case.
    Espargaró A, Castillo V, de Groot NS, Ventura S.
    J Mol Biol; 2008 May 16; 378(5):1116-31. PubMed ID: 18423663
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  • 10. A single mutation induces amyloid aggregation in the alpha-spectrin SH3 domain: analysis of the early stages of fibril formation.
    Morel B, Casares S, Conejero-Lara F.
    J Mol Biol; 2006 Feb 17; 356(2):453-68. PubMed ID: 16375922
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  • 12. Obligatory steps in protein folding and the conformational diversity of the transition state.
    Martinez JC, Pisabarro MT, Serrano L.
    Nat Struct Biol; 1998 Aug 17; 5(8):721-9. PubMed ID: 9699637
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  • 20. Early amyloidogenic oligomerization studied through fluorescence lifetime correlation spectroscopy.
    Paredes JM, Casares S, Ruedas-Rama MJ, Fernandez E, Castello F, Varela L, Orte A.
    Int J Mol Sci; 2012 Aug 17; 13(8):9400-9418. PubMed ID: 22949804
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