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300 related items for PubMed ID: 21976952

  • 21. Paradoxical effects of substitution and deletion mutation of Arg56 on the structure and chaperone function of human alphaB-crystallin.
    Biswas A, Goshe J, Miller A, Santhoshkumar P, Luckey C, Bhat MB, Nagaraj RH.
    Biochemistry; 2007 Feb 06; 46(5):1117-27. PubMed ID: 17260942
    [Abstract] [Full Text] [Related]

  • 22. A quantitative NMR spectroscopic examination of the flexibility of the C-terminal extensions of the molecular chaperones, αA- and αB-crystallin.
    Treweek TM, Rekas A, Walker MJ, Carver JA.
    Exp Eye Res; 2010 Nov 06; 91(5):691-9. PubMed ID: 20732317
    [Abstract] [Full Text] [Related]

  • 23. Site-directed mutations within the core "alpha-crystallin" domain of the small heat-shock protein, human alphaB-crystallin, decrease molecular chaperone functions.
    Muchowski PJ, Wu GJ, Liang JJ, Adman ET, Clark JI.
    J Mol Biol; 1999 Jun 04; 289(2):397-411. PubMed ID: 10366513
    [Abstract] [Full Text] [Related]

  • 24. 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
    [Abstract] [Full Text] [Related]

  • 25. Conformational and functional differences between recombinant human lens alphaA- and alphaB-crystallin.
    Sun TX, Das BK, Liang JJ.
    J Biol Chem; 1997 Mar 07; 272(10):6220-5. PubMed ID: 9045637
    [Abstract] [Full Text] [Related]

  • 26. The biochemical association between R157H mutation in human αB-crystallin and development of cardiomyopathy: Structural and functional analyses of the mutant protein.
    Nasiri P, Ghahramani M, Tavaf Z, Niazi A, Moosavi-Movahedi AA, Kurganov BI, Yousefi R.
    Biochimie; 2021 Nov 07; 190():36-49. PubMed ID: 34237397
    [Abstract] [Full Text] [Related]

  • 27. Succinylation Is a Gain-of-Function Modification in Human Lens αB-Crystallin.
    Nandi SK, Rakete S, Nahomi RB, Michel C, Dunbar A, Fritz KS, Nagaraj RH.
    Biochemistry; 2019 Mar 05; 58(9):1260-1274. PubMed ID: 30758948
    [Abstract] [Full Text] [Related]

  • 28. Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formation.
    Treweek TM, Ecroyd H, Williams DM, Meehan S, Carver JA, Walker MJ.
    PLoS One; 2007 Oct 17; 2(10):e1046. PubMed ID: 17940610
    [Abstract] [Full Text] [Related]

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  • 30. Deamidation alters the structure and decreases the stability of human lens betaA3-crystallin.
    Takata T, Oxford JT, Brandon TR, Lampi KJ.
    Biochemistry; 2007 Jul 31; 46(30):8861-71. PubMed ID: 17616172
    [Abstract] [Full Text] [Related]

  • 31. Role of the C-terminal extensions of alpha-crystallins. Swapping the C-terminal extension of alpha-crystallin to alphaB-crystallin results in enhanced chaperone activity.
    Pasta SY, Raman B, Ramakrishna T, Rao ChM.
    J Biol Chem; 2002 Nov 29; 277(48):45821-8. PubMed ID: 12235146
    [Abstract] [Full Text] [Related]

  • 32. The influence of the N-terminal region proximal to the core domain on the assembly and chaperone activity of αB-crystallin.
    Jovcevski B, Andrew Aquilina J, Benesch JLP, Ecroyd H.
    Cell Stress Chaperones; 2018 Sep 29; 23(5):827-836. PubMed ID: 29520626
    [Abstract] [Full Text] [Related]

  • 33. Conserved F84 and P86 residues in alphaB-crystallin are essential to effectively prevent the aggregation of substrate proteins.
    Santhoshkumar P, Sharma KK.
    Protein Sci; 2006 Nov 29; 15(11):2488-98. PubMed ID: 17075130
    [Abstract] [Full Text] [Related]

  • 34. 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 29; 1864(3):129502. PubMed ID: 31812542
    [Abstract] [Full Text] [Related]

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  • 36. Deletion of Specific Conserved Motifs from the N-Terminal Domain of αB-Crystallin Results in the Activation of Chaperone Functions.
    Mahalingam S, Shankar G, Mooney BP, Singh K, Santhoshkumar P, Sharma KK.
    Int J Mol Sci; 2022 Jan 20; 23(3):. PubMed ID: 35163023
    [Abstract] [Full Text] [Related]

  • 37. AlphaA-crystallin interacting regions in the small heat shock protein, alphaB-crystallin.
    Sreelakshmi Y, Santhoshkumar P, Bhattacharyya J, Sharma KK.
    Biochemistry; 2004 Dec 21; 43(50):15785-95. PubMed ID: 15595834
    [Abstract] [Full Text] [Related]

  • 38. Truncation of alphaB-crystallin by the myopathy-causing Q151X mutation significantly destabilizes the protein leading to aggregate formation in transfected cells.
    Hayes VH, Devlin G, Quinlan RA.
    J Biol Chem; 2008 Apr 18; 283(16):10500-12. PubMed ID: 18230612
    [Abstract] [Full Text] [Related]

  • 39. 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 Apr 18; 7(1):e30257. PubMed ID: 22272318
    [Abstract] [Full Text] [Related]

  • 40. Acetylation of αA-crystallin in the human lens: effects on structure and chaperone function.
    Nagaraj RH, Nahomi RB, Shanthakumar S, Linetsky M, Padmanabha S, Pasupuleti N, Wang B, Santhoshkumar P, Panda AK, Biswas A.
    Biochim Biophys Acta; 2012 Feb 18; 1822(2):120-9. PubMed ID: 22120592
    [Abstract] [Full Text] [Related]

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