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Journal Abstract Search

270 related items for PubMed ID: 23209591

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  • 2. Modulation of the stability of amyloidogenic precursors by anion binding strongly influences the rate of amyloid nucleation.
    Ruzafa D, Conejero-Lara F, Morel B.
    Phys Chem Chem Phys; 2013 Oct 07; 15(37):15508-17. PubMed ID: 23942905
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  • 5. Environmental conditions affect the kinetics of nucleation of amyloid fibrils and determine their morphology.
    Morel B, Varela L, Azuaga AI, Conejero-Lara F.
    Biophys J; 2010 Dec 01; 99(11):3801-10. PubMed ID: 21112305
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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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  • 13. 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 04; 9(12):e113224. PubMed ID: 25490095
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  • 14. Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates.
    Khurana R, Gillespie JR, Talapatra A, Minert LJ, Ionescu-Zanetti C, Millett I, Fink AL.
    Biochemistry; 2001 Mar 27; 40(12):3525-35. PubMed ID: 11297418
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  • 15. Time-dependent insulin oligomer reaction pathway prior to fibril formation: cooling and seeding.
    Sorci M, Grassucci RA, Hahn I, Frank J, Belfort G.
    Proteins; 2009 Oct 27; 77(1):62-73. PubMed ID: 19408310
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  • 16. Oligomeric states along the folding pathways of β2-microglobulin: kinetics, thermodynamics, and structure.
    Rennella E, Cutuil T, Schanda P, Ayala I, Gabel F, Forge V, Corazza A, Esposito G, Brutscher B.
    J Mol Biol; 2013 Aug 09; 425(15):2722-36. PubMed ID: 23648836
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  • 18. Direct characterization of amyloidogenic oligomers by single-molecule fluorescence.
    Orte A, Birkett NR, Clarke RW, Devlin GL, Dobson CM, Klenerman D.
    Proc Natl Acad Sci U S A; 2008 Sep 23; 105(38):14424-9. PubMed ID: 18796612
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  • 19. 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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  • 20. Defining the pathway of worm-like amyloid fibril formation by the mouse prion protein by delineation of the productive and unproductive oligomerization reactions.
    Jain S, Udgaonkar JB.
    Biochemistry; 2011 Feb 22; 50(7):1153-61. PubMed ID: 21214263
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