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432 related items for PubMed ID: 20621668

  • 1. Partially folded aggregation intermediates of human gammaD-, gammaC-, and gammaS-crystallin are recognized and bound by human alphaB-crystallin chaperone.
    Acosta-Sampson L, King J.
    J Mol Biol; 2010 Aug 06; 401(1):134-52. PubMed ID: 20621668
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  • 2. Cataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone.
    Moreau KL, King JA.
    PLoS One; 2012 Aug 06; 7(5):e37256. PubMed ID: 22655036
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  • 3. Human αB-crystallin discriminates between aggregation-prone and function-preserving variants of a client protein.
    Sprague-Piercy MA, Wong E, Roskamp KW, Fakhoury JN, Freites JA, Tobias DJ, Martin RW.
    Biochim Biophys Acta Gen Subj; 2020 Mar 06; 1864(3):129502. PubMed ID: 31812542
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  • 4. Folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin.
    Mills IA, Flaugh SL, Kosinski-Collins MS, King JA.
    Protein Sci; 2007 Nov 06; 16(11):2427-44. PubMed ID: 17905830
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  • 8. Group II archaeal chaperonin recognition of partially folded human γD-crystallin mutants.
    Sergeeva OA, Yang J, King JA, Knee KM.
    Protein Sci; 2014 Jun 06; 23(6):693-702. PubMed ID: 24615724
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  • 13. Association of partially folded lens betaB2-crystallins with the alpha-crystallin molecular chaperone.
    Evans P, Slingsby C, Wallace BA.
    Biochem J; 2008 Feb 01; 409(3):691-9. PubMed ID: 17937660
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  • 15. Solution properties of γ-crystallins: compact structure and low frictional ratio are conserved properties of diverse γ-crystallins.
    Chen Y, Zhao H, Schuck P, Wistow G.
    Protein Sci; 2014 Jan 01; 23(1):76-87. PubMed ID: 24214907
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  • 16. The function of the beta3 interactive domain in the small heat shock protein and molecular chaperone, human alphaB crystallin.
    Ghosh JG, Estrada MR, Houck SA, Clark JI.
    Cell Stress Chaperones; 2006 Jan 01; 11(2):187-97. PubMed ID: 16817325
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  • 19. Interactions and chaperone function of alphaA-crystallin with T5P gammaC-crystallin mutant.
    Liang JJ.
    Protein Sci; 2004 Sep 01; 13(9):2476-82. PubMed ID: 15322286
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  • 20. The small heat-shock protein αB-crystallin uses different mechanisms of chaperone action to prevent the amorphous versus fibrillar aggregation of α-lactalbumin.
    Kulig M, Ecroyd H.
    Biochem J; 2012 Dec 15; 448(3):343-52. PubMed ID: 23005341
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