Study of the chaperoning mechanism of bovine lens α-crystallin, a member of the α-small heat shock superfamily

Biophysical Journal

Volumn 80, Issue 4, 2001, Pages 1986-1995

  Abgar, Saïd ^a   Vanhoudt, Jos ^a   Aerts, Tony ^a   Clauwaert, Julius ^a  

^a UNIVERSITY OF ANTWERP   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; HEAT SHOCK PROTEIN; LYSOZYME;

ARTICLE; CATTLE; COMPLEX FORMATION; ENZYME SUBSTRATE COMPLEX; LENS; LIGHT SCATTERING; MOLECULAR INTERACTION; NONHUMAN; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY;

BOS TAURUS; BOVINAE;

EID: 0035071016     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(01)76168-1     Document Type: Article

References (44)

1. A possible structure for α-crystallin
2. CTF corrected structure of α-crystallin B by electron cryo-microscopy
3. The mode of chaperoning of dithiothreitol-denatured α-lactalbumin by α-crystallin
4. α-Crystallin does not require temperature activation for its chaperone-like activity
5. Bovine and human α-crystallins as molecular chaperones: Prevention of the inactivation of glutathione reductase by fructation
6. Supervising the fold: Functional principles of molecular chaperones
7. On the interaction of α-crystallin with unfolded proteins
8. Genealogy of the α-crystallin-small heat-shock protein superfamily
9. Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
10. Refinement of 3D structure of bovine αA-crystallin
11. Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies
12. The small heat-shock protein, αB-crystallin, has a variable quaternary structure
13. Image restrained modeling of αB-crystallin
14. Hsp26: A temperature-regulated chaperone
15. Transcription regulation of alpha B-crystallin in astrocytes: Analysis of HSF and AP1 activation by different types of physiological stress
16. Alpha-crystallin can function as a molecular chaperone
17. Lens α-crystallin: Chaperone-like properties
18. Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin
19. Crystal structure of a small heat-shock protein
20. Small heat shock protein of Methanococcus jannaschii, a hyperthermophile
21. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
22. Physiological role of the association complexes of α-crystallin and its substrates on the chaperone activity
23. Structural alterations of α-crystallin during its chaperone action
24. Temperature dependent chaperone-like activity of alpha-crystallin
25. Structural perturbation of α-crystallin and its chaperone-like activity
26. Kinetics of secondary structure recovery during the refolding of reduced hen egg white lysozyme
27. Mutations and modifications support a 'pitted-flexiball' model for α-crystallin
28. Methods for obtaining sedimentation coefficient distributions
29. On the thermal stability of α-crystallin: A new insight from infrared spectroscopy
30. Calf lens alpha-crystallin quaternary structure. A three-layer tetrahedral model
31. Thermodynamic examination of the self-association of brain tubulin to microtubules and other structures
32. The mammalian small heat-shock protein Hsp20 forms dimers and is a poor chaperone
33. A small-angle x-ray solution scattering study of bovine α-crystallin
34. Native quaternary structure of bovine α-crystallin
35. Quaternary structure of bovine α-crystallin: Influence of temperature
36. Experimental comparison of fiber receivers and a pinhole receiver for dynamic and static light scattering
37. The small heat-shock protein αB-crystallin as candidate autoantigen in multiple sclerosis
38. Second virial coefficient of alphacrystallin
39. The chaperone activity of bovine α-crystallin
40. Possible tetramer-based quaternary structures for α-crystallins and small heat shock proteins