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Journal Abstract Search

306 related items for PubMed ID: 22272318

  • 1. Hydroimidazolone modification of the conserved Arg12 in small heat shock proteins: studies on the structure and chaperone function using mutant mimics.
    Nagaraj RH, Panda AK, Shanthakumar S, Santhoshkumar P, Pasupuleti N, Wang B, Biswas A.
    PLoS One; 2012; 7(1):e30257. PubMed ID: 22272318
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  • 3. Effect of methylglyoxal modification on stress-induced aggregation of client proteins and their chaperoning by human alphaA-crystallin.
    Biswas A, Wang B, Miyagi M, Nagaraj RH.
    Biochem J; 2008 Feb 01; 409(3):771-7. PubMed ID: 17941823
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  • 5. The IXI/V motif in the C-terminal extension of alpha-crystallins: alternative interactions and oligomeric assemblies.
    Pasta SY, Raman B, Ramakrishna T, Rao ChM.
    Mol Vis; 2004 Sep 08; 10():655-62. PubMed ID: 15448619
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  • 9. Structural and functional properties of NH(2)-terminal domain, core domain, and COOH-terminal extension of αA- and αB-crystallins.
    Asomugha CO, Gupta R, Srivastava OP.
    Mol Vis; 2011 Sep 08; 17():2356-67. PubMed ID: 21921988
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  • 10. 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 Sep 08; 11(2):187-97. PubMed ID: 16817325
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  • 14. The interaction between alphaA- and alphaB-crystallin is sequence-specific.
    Sreelakshmi Y, Sharma KK.
    Mol Vis; 2006 May 24; 12():581-7. PubMed ID: 16760894
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  • 15. Chaperone peptides of α-crystallin inhibit epithelial cell apoptosis, protein insolubilization, and opacification in experimental cataracts.
    Nahomi RB, Wang B, Raghavan CT, Voss O, Doseff AI, Santhoshkumar P, Nagaraj RH.
    J Biol Chem; 2013 May 03; 288(18):13022-35. PubMed ID: 23508955
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  • 16. The cataract-causing mutation G98R in human alphaA-crystallin leads to folding defects and loss of chaperone activity.
    Singh D, Raman B, Ramakrishna T, Rao ChM.
    Mol Vis; 2006 Nov 15; 12():1372-9. PubMed ID: 17149363
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  • 17. Role of cysteine residues in the enhancement of chaperone function in methylglyoxal-modified human alpha A-crystallin.
    Kanade SR, Pasupuleti N, Nagaraj RH.
    Mol Cell Biochem; 2009 Feb 15; 322(1-2):185-91. PubMed ID: 19020808
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  • 18. Enhancement of chaperone function of alpha-crystallin by methylglyoxal modification.
    Nagaraj RH, Oya-Ito T, Padayatti PS, Kumar R, Mehta S, West K, Levison B, Sun J, Crabb JW, Padival AK.
    Biochemistry; 2003 Sep 16; 42(36):10746-55. PubMed ID: 12962499
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  • 19. Real-time heterogeneous protein-protein interaction between αA-crystallin N-terminal mutants and αB-crystallin using quartz crystal microbalance (QCM).
    Ramkumar S, Fujii N, Sakaue H, Fujii N, Thankappan B, kumari RP, Natarajaseenivasan K, Anbarasu K.
    Amino Acids; 2015 May 16; 47(5):1035-43. PubMed ID: 25694240
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  • 20. Deamidation affects structural and functional properties of human alphaA-crystallin and its oligomerization with alphaB-crystallin.
    Gupta R, Srivastava OP.
    J Biol Chem; 2004 Oct 22; 279(43):44258-69. PubMed ID: 15284238
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