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12. Illustration of HIV-1 protease folding through a molten-globule-like intermediate using an experimental model that implicates alpha-crystallin and calcium ions. Dash C; Sastry M; Rao M Biochemistry; 2005 Mar; 44(10):3725-34. PubMed ID: 15751949 [TBL] [Abstract][Full Text] [Related]
13. Wrapping the alpha-crystallin domain fold in a chaperone assembly. Stamler R; Kappé G; Boelens W; Slingsby C J Mol Biol; 2005 Oct; 353(1):68-79. PubMed ID: 16165157 [TBL] [Abstract][Full Text] [Related]
14. Alpha-crystallin can act as a chaperone under conditions of oxidative stress. Wang K; Spector A Invest Ophthalmol Vis Sci; 1995 Feb; 36(2):311-21. PubMed ID: 7843902 [TBL] [Abstract][Full Text] [Related]
15. Effect of glycation on alpha-crystallin structure and chaperone-like function. Kumar PA; Kumar MS; Reddy GB Biochem J; 2007 Dec; 408(2):251-8. PubMed ID: 17696877 [TBL] [Abstract][Full Text] [Related]
16. X-ray- and neutron-scattering studies of alpha-crystallin and evidence that the target protein sits in the fenestrations of the alpha-crystallin shell. Regini JW; Grossmann JG; Timmins P; Harding JJ; Quantock AJ; Hodson SA; Elliott GF Invest Ophthalmol Vis Sci; 2007 Jun; 48(6):2695-700. PubMed ID: 17525201 [TBL] [Abstract][Full Text] [Related]
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