Decreased subunit exchange of heat-treated lens αA-crystallin

Biochemical and Biophysical Research Communications

Volumn 293, Issue 1, 2002, Pages 7-12

  Liang, Jack N ^a   Fu, Ling ^a  

^a BRIGHAM AND WOMEN S HOSPITAL   (United States)

Author keywords

Circular dichroism; Fluorescence resonance energy transfer; High molecular weight aggregation; Subunit exchange; A Crystallin

Indexed keywords

4,4' DIANILINO 1,1' BINAPHTHALENE 5,5' DISULFONIC ACID; ALPHA CRYSTALLIN; ALPHAA CRYSTALLIN; CYSTEINE; SULFONIC ACID DERIVATIVE; THIOFLAVINE; UNCLASSIFIED DRUG;

ARTICLE; CIRCULAR DICHROISM; ENERGY TRANSFER; FLUORESCENCE; HEATING; HYDROPHOBICITY; MOLECULAR WEIGHT; OXIDATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION; SPECTROSCOPY; ULTRAVIOLET RADIATION;

CIRCULAR DICHROISM; CRYSTALLINS; FLUORESCENT DYES; HEAT; LENS, CRYSTALLINE; MOLECULAR WEIGHT; PROTEIN CONFORMATION; PROTEIN SUBUNITS; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY;

EID: 0036290404     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(02)00176-6     Document Type: Article

References (32)

1. Structure and modifications of the junior chaperone α-crystallin. From lens transparency to molecular pathology
2. Heat-induced conformational change and increased chaperone activity of lens α-crystallin
3. Heat-induced conformational change of human lens recombinant αA- and αB-crystallins
4. Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity ofα-crystallin
5. Correlation between the chaperone-like activity and aggregate size of α-crystallin with increasing temperature
6. Human lens high-molecular-weight α-crystallin aggregates
7. A dynamic quaternary structure of bovine α-crystallin as indicated from intermolecular exchange of subunits
8. Intermolecular exchange and stabilization of human lens recombinant αA- and αB-crystallins
9. Subunit exchange of αA-crystallin
10. Subunit exchange of lens α-crystallin: A fluorescence energy transfer study with the fluorescent labeled α-crystallin mutant W9F as a probe
11. Conformational and functional differences between recombinant human lens αA- and αB-crystallin
12. Measurement of protein using bicinchoninic acid
13. Reaction of purified (Na, K)-ATPase with the fluorescent sulfhydryl probe 2-(4′-maleimidylanilino)naphthalene 6-sulfonic acid. Characterization and the effects of ligands
14. Spectroscopic studies of lens crystallins. II. Fluorescence probes for polar-apolar nature and sulfhydryl group accessibility
15. Spectroscopic studies of lens crystallins. I. Circular dichroism and intrinsic fluorescence
16. Estimation of the secondary structure and conformation of bovine lens crystallins by infrared spectroscopy: Quantitative analysis and resolution by Fourier self-deconvolution and curve fit
17. Intermolecular interaction of lens crystallins: From rotationally mobile to immobile states at high protein concentrations
18. Spectroscopic analysis of lens recombinant βB2- and γC-crystallins
19. Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1
20. Interaction between β-amyloid and lens αB-crystallin
21. Oxidation of human lens recombinant αA-crystallin and cysteine-deficient mutants
22. On the quaternary structure of high-molecular-weight proteins from the bovine eye lens
23. Crystal structure of a small heat-shock protein
24. Site-directed mutation within the core "α-crystallin" domain of the small heat-shock protein, human αB-crystallin, diminish molecular chaperone functions
25. The small heat-shock protein, αB-crystallin, has a variable quaternary structure
26. Lens α-crystallin: Function and structure
27. Empirical predictions of protein conformation
28. Native quaternary structure of bovine α-crystallin
29. Subunit exchange of small heat shock proteins. Analysis of oligomer formation of αA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations
30. α-Crystallin can function as a molecular chaperone
31. Molecular chaperone properties of the high molecular weight aggregate from aged lens