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Journal Abstract Search

177 related items for PubMed ID: 21224997

  • 1. Cataract-causing αAG98R-crystallin mutant dissociates into monomers having chaperone activity.
    Raju M, Santhoshkumar P, Sharma KK.
    Mol Vis; 2011 Jan 05; 17():7-15. PubMed ID: 21224997
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  • 2. Cataract-causing alphaAG98R mutant shows substrate-dependent chaperone activity.
    Murugesan R, Santhoshkumar P, Sharma KK.
    Mol Vis; 2007 Dec 18; 13():2301-9. PubMed ID: 18199971
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  • 3. αA-Crystallin-derived mini-chaperone modulates stability and function of cataract causing αAG98R-crystallin.
    Raju M, Santhoshkumar P, Sharma KK.
    PLoS One; 2012 Dec 18; 7(9):e44077. PubMed ID: 22970163
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  • 4. Substrate Protein Interactions and Methylglyoxal Modifications Reduce the Aggregation Propensity of Human Alpha-A-Crystallin G98R Mutant.
    Santhoshkumar P, Sharma KK.
    Front Mol Biosci; 2022 Dec 18; 9():875205. PubMed ID: 35463950
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  • 10. Functional Rescue of Cataract-Causing αA-G98R-Crystallin by Targeted Compensatory Suppressor Mutations in Human αA-Crystallin.
    Phadte AS, Mahalingam S, Santhoshkumar P, Sharma KK.
    Biochemistry; 2019 Oct 08; 58(40):4148-4158. PubMed ID: 31523965
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  • 14. Identification of subunit-subunit interaction sites in αA-WT crystallin and mutant αA-G98R crystallin using isotope-labeled cross-linker and mass spectrometry.
    Kannan R, Santhoshkumar P, Mooney BP, Sharma KK.
    PLoS One; 2013 Oct 08; 8(6):e65610. PubMed ID: 23755258
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  • 15. Differential role of arginine mutations on the structure and functions of α-crystallin.
    Panda AK, Nandi SK, Chakraborty A, Nagaraj RH, Biswas A.
    Biochim Biophys Acta; 2016 Jan 08; 1860(1 Pt B):199-210. PubMed ID: 26080000
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  • 17. 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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