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395 related items for PubMed ID: 23005341
1. The small heat-shock protein αB-crystallin uses different mechanisms of chaperone action to prevent the amorphous versus fibrillar aggregation of α-lactalbumin. Kulig M, Ecroyd H. Biochem J; 2012 Dec 15; 448(3):343-52. PubMed ID: 23005341 [Abstract] [Full Text] [Related]
2. Enhanced molecular chaperone activity of the small heat-shock protein alphaB-cystallin following covalent immobilization onto a solid-phase support. Garvey M, Griesser SS, Griesser HJ, Thierry B, Nussio MR, Shapter JG, Ecroyd H, Giorgetti S, Bellotti V, Gerrard JA, Carver JA. Biopolymers; 2011 Jun 15; 95(6):376-89. PubMed ID: 21225714 [Abstract] [Full Text] [Related]
3. Interaction of the molecular chaperone alphaB-crystallin with alpha-synuclein: effects on amyloid fibril formation and chaperone activity. Rekas A, Adda CG, Andrew Aquilina J, Barnham KJ, Sunde M, Galatis D, Williamson NA, Masters CL, Anders RF, Robinson CV, Cappai R, Carver JA. J Mol Biol; 2004 Jul 23; 340(5):1167-83. PubMed ID: 15236975 [Abstract] [Full Text] [Related]
4. The effect of small molecules in modulating the chaperone activity of alphaB-crystallin against ordered and disordered protein aggregation. Ecroyd H, Carver JA. FEBS J; 2008 Mar 23; 275(5):935-47. PubMed ID: 18218039 [Abstract] [Full Text] [Related]
5. AlphaB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid beta-peptide and beta2-microglobulin. Raman B, Ban T, Sakai M, Pasta SY, Ramakrishna T, Naiki H, Goto Y, Rao ChM. Biochem J; 2005 Dec 15; 392(Pt 3):573-81. PubMed ID: 16053447 [Abstract] [Full Text] [Related]
6. 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 15; 91(5):691-9. PubMed ID: 20732317 [Abstract] [Full Text] [Related]
7. Monitoring the prevention of amyloid fibril formation by alpha-crystallin. Temperature dependence and the nature of the aggregating species. Rekas A, Jankova L, Thorn DC, Cappai R, Carver JA. FEBS J; 2007 Dec 15; 274(24):6290-304. PubMed ID: 18005258 [Abstract] [Full Text] [Related]
14. Functional Amyloid Protection in the Eye Lens: Retention of α-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils. Garvey M, Ecroyd H, Ray NJ, Gerrard JA, Carver JA. Biomolecules; 2017 Sep 12; 7(3):. PubMed ID: 28895938 [Abstract] [Full Text] [Related]
15. The chaperone-like alpha-crystallin forms a complex only with the aggregation-prone molten globule state of alpha-lactalbumin. Rajaraman K, Raman B, Ramakrishna T, Rao CM. Biochem Biophys Res Commun; 1998 Aug 28; 249(3):917-21. PubMed ID: 9731236 [Abstract] [Full Text] [Related]
16. R120G alphaB-crystallin promotes the unfolding of reduced alpha-lactalbumin and is inherently unstable. Treweek TM, Rekas A, Lindner RA, Walker MJ, Aquilina JA, Robinson CV, Horwitz J, Perng MD, Quinlan RA, Carver JA. FEBS J; 2005 Feb 28; 272(3):711-24. PubMed ID: 15670152 [Abstract] [Full Text] [Related]
17. Crystallin proteins and amyloid fibrils. Ecroyd H, Carver JA. Cell Mol Life Sci; 2009 Jan 28; 66(1):62-81. PubMed ID: 18810322 [Abstract] [Full Text] [Related]
18. 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 Jan 28; 11(2):187-97. PubMed ID: 16817325 [Abstract] [Full Text] [Related]
19. Effect of a single AGE modification on the structure and chaperone activity of human alphaB-crystallin. Bhattacharyya J, Shipova EV, Santhoshkumar P, Sharma KK, Ortwerth BJ. Biochemistry; 2007 Dec 18; 46(50):14682-92. PubMed ID: 18027913 [Abstract] [Full Text] [Related]
20. 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] Page: [Next] [New Search]