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168 related items for PubMed ID: 24615724

  • 1. Group II archaeal chaperonin recognition of partially folded human γD-crystallin mutants.
    Sergeeva OA, Yang J, King JA, Knee KM.
    Protein Sci; 2014 Jun; 23(6):693-702. PubMed ID: 24615724
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  • 4. Interdomain side-chain interactions in human gammaD crystallin influencing folding and stability.
    Flaugh SL, Kosinski-Collins MS, King J.
    Protein Sci; 2005 Aug; 14(8):2030-43. PubMed ID: 16046626
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  • 8. Hydrophobic core mutations associated with cataract development in mice destabilize human gammaD-crystallin.
    Moreau KL, King J.
    J Biol Chem; 2009 Nov 27; 284(48):33285-95. PubMed ID: 19758984
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  • 9. Mechanism of the highly efficient quenching of tryptophan fluorescence in human gammaD-crystallin.
    Chen J, Flaugh SL, Callis PR, King J.
    Biochemistry; 2006 Sep 26; 45(38):11552-63. PubMed ID: 16981715
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  • 10. Contributions of aromatic pairs to the folding and stability of long-lived human γD-crystallin.
    Kong F, King J.
    Protein Sci; 2011 Mar 26; 20(3):513-28. PubMed ID: 21432932
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  • 12. Glutamine deamidation destabilizes human gammaD-crystallin and lowers the kinetic barrier to unfolding.
    Flaugh SL, Mills IA, King J.
    J Biol Chem; 2006 Oct 13; 281(41):30782-93. PubMed ID: 16891314
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  • 16. Early Stage UV-B Induced Molecular Modifications of Human Eye Lens γD-Crystallin.
    Weininger S, Neudorf M, Gröger S, Plato E, Broneske R, Saalwächter K, Weininger U, Balbach J.
    Macromol Biosci; 2023 May 13; 23(5):e2200526. PubMed ID: 36808690
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  • 17. 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 May 13; 7(5):e37256. PubMed ID: 22655036
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