169 related articles for article (PubMed ID: 17105203)
1. N- and C-Terminal motifs in human alphaB crystallin play an important role in the recognition, selection, and solubilization of substrates.
Ghosh JG; Shenoy AK; Clark JI
Biochemistry; 2006 Nov; 45(46):13847-54. PubMed ID: 17105203
[TBL] [Abstract][Full Text] [Related]
2. 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; 11(2):187-97. PubMed ID: 16817325
[TBL] [Abstract][Full Text] [Related]
3. 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; 289(2):397-411. PubMed ID: 10366513
[TBL] [Abstract][Full Text] [Related]
4. Interactive domains for chaperone activity in the small heat shock protein, human alphaB crystallin.
Ghosh JG; Estrada MR; Clark JI
Biochemistry; 2005 Nov; 44(45):14854-69. PubMed ID: 16274233
[TBL] [Abstract][Full Text] [Related]
5. Structure-based analysis of the beta8 interactive sequence of human alphaB crystallin.
Ghosh JG; Estrada MR; Clark JI
Biochemistry; 2006 Aug; 45(32):9878-86. PubMed ID: 16893188
[TBL] [Abstract][Full Text] [Related]
6. Interactive sequences in the stress protein and molecular chaperone human alphaB crystallin recognize and modulate the assembly of filaments.
Ghosh JG; Houck SA; Clark JI
Int J Biochem Cell Biol; 2007; 39(10):1804-15. PubMed ID: 17590381
[TBL] [Abstract][Full Text] [Related]
7. Thermally induced disintegration of the oligomeric structure of alphaB-crystallin mutant F28S is associated with diminished chaperone activity.
Kelley PB; Abraham EC
Mol Cell Biochem; 2003 Oct; 252(1-2):273-8. PubMed ID: 14577602
[TBL] [Abstract][Full Text] [Related]
8. 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; 277(48):45821-8. PubMed ID: 12235146
[TBL] [Abstract][Full Text] [Related]
9. 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; 10():655-62. PubMed ID: 15448619
[TBL] [Abstract][Full Text] [Related]
10. Analysis of the alphaB-crystallin domain responsible for inhibiting tubulin aggregation.
Ohto-Fujita E; Fujita Y; Atomi Y
Cell Stress Chaperones; 2007; 12(2):163-71. PubMed ID: 17688195
[TBL] [Abstract][Full Text] [Related]
11. The lack of chaperonelike activity of Caenorhabditis elegans Hsp12.2 cannot be restored by domain swapping with human alphaB-crystallin.
Kokke BP; Boelens WC; de Jong WW
Cell Stress Chaperones; 2001 Oct; 6(4):360-7. PubMed ID: 11795473
[TBL] [Abstract][Full Text] [Related]
12. COOH-terminal truncations and site-directed mutations enhance thermostability and chaperone-like activity of porcine alphaB-crystallin.
Liao JH; Lee JS; Wu SH; Chiou SH
Mol Vis; 2009 Jul; 15():1429-44. PubMed ID: 19641632
[TBL] [Abstract][Full Text] [Related]
13. Structural and functional consequences of chaperone site deletion in αA-crystallin.
Santhoshkumar P; Karmakar S; Sharma KK
Biochim Biophys Acta; 2016 Nov; 1864(11):1529-38. PubMed ID: 27524665
[TBL] [Abstract][Full Text] [Related]
14. 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; 272(3):711-24. PubMed ID: 15670152
[TBL] [Abstract][Full Text] [Related]
15. Human alphaB-crystallin. Small heat shock protein and molecular chaperone.
Muchowski PJ; Bassuk JA; Lubsen NH; Clark JI
J Biol Chem; 1997 Jan; 272(4):2578-82. PubMed ID: 8999975
[TBL] [Abstract][Full Text] [Related]
16. Alpha-crystallin as a molecular chaperone.
Derham BK; Harding JJ
Prog Retin Eye Res; 1999 Jul; 18(4):463-509. PubMed ID: 10217480
[TBL] [Abstract][Full Text] [Related]
17. 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; 46(5):1117-27. PubMed ID: 17260942
[TBL] [Abstract][Full Text] [Related]
18. Maintenance of chaperone-like activity despite mutations in a conserved region of murine lens alphaB crystallin.
Hepburne-Scott HW; Crabbe MJ
Mol Vis; 1999 Aug; 5():15. PubMed ID: 10445957
[TBL] [Abstract][Full Text] [Related]
19. Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function.
Bova MP; Yaron O; Huang Q; Ding L; Haley DA; Stewart PL; Horwitz J
Proc Natl Acad Sci U S A; 1999 May; 96(11):6137-42. PubMed ID: 10339554
[TBL] [Abstract][Full Text] [Related]
20. C-terminal lysine truncation increases thermostability and enhances chaperone-like function of porcine alphaB-crystallin.
Liao JH; Lee JS; Chiou SH
Biochem Biophys Res Commun; 2002 Sep; 297(2):309-16. PubMed ID: 12237119
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]