STRUCTURE AND STABILITY OF γ‐CRYSTALLINS‐IV. AGGREGATION AND STRUCTURAL DESTABILIZATION IN PHOTOSENSITIZED REACTIONS

Photochemistry and Photobiology

Volumn 47, Issue 4, 1988, Pages 583-591

  Mandal, Krishnagopal ^a   Kono, Masahiro ^a   Bose, Swapan K ^a   Thomson, John ^b   Chakrabarti, Bireswar ^a,c  

^a SCHEPENS EYE RESEARCH INSTITUTE   (United States)

^b MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^c HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTALLIN; METHYLENE BLUE; RIBOFLAVIN;

ARTICLE; KINETICS; LIGHT; PROTEIN CONFORMATION; RADIATION EXPOSURE; TIME; ULTRAVIOLET RADIATION;

CRYSTALLINS; KINETICS; LIGHT; METHYLENE BLUE; PROTEIN CONFORMATION; RIBOFLAVIN; SUPPORT, U.S. GOV'T, P.H.S.; TIME FACTORS; ULTRAVIOLET RAYS;

EID: 0023988274     PISSN: 00318655     EISSN: 17511097     Source Type: Journal    
DOI: 10.1111/j.1751-1097.1988.tb08848.x     Document Type: Article

References (43)

1. Spectroscopic investigations or bovine lens crystallins. 2. Fluorescent probes for polar‐apolar nature and sulfhydryl group accessibility
2. Changes in tertiary structure of calf‐lens α‐crystallin by near‐UV irradiation: role of hydrogen peroxide
3. Studies on γ‐crystallin from calf lens. II. Purification and some properties of the main protein components
4. Studies on γ‐crystallin from calf lens. III. Comparison of the main protein components by peptide mapping
5. Lens proteins
6. The molecular structure and stability of the eye lens: X‐ray analysis of γ‐crystallin II
7. Interactions of γ‐crystallin in relation to eye‐lens transparency
8. Fluorescence spectra of tryptophan residues in human and bovine lens proteins
9. The rates of photodestruction of tryptophan residues in human and bovine ocular lens proteins
10. Sensitized photooxidation of bovine α‐crystallin: change in microenvironments of thiol groups
11. Sensitizer‐induced conformational changes in lens crystallin‐II. Photodynamic action of riboflavin on bovine α‐crystallin
12. γ‐Crystallin family of the mouse lens: structural and evolutionary relationships
13. Conformation of mammalian lens proteins: photoinduced changes in relation to cataract formation
14. Light‐induced conformational changes of lens proteins: Photochemistry and photophysics of the process
15. Polypeptide chain pathway in γ‐crystallin Illb from calf lens at 3Å resolution
16. Low molecular weight proteins of the lens
17. A comparison of aerobic and anaerobic photolysis of lens protein
18. Studies on the oxidation of cysteine to cystine in lens proteins during cataract formation
19. Photosensitized oxidation and singlet oxygen: consequences in biological systems
20. Crosslinking and blue‐fluorescence of photooxidized calf‐lens α‐crystallin
21. Coloration of human lenses by near ultraviolet photo‐oxidized tryptophan
22. Structural proteins of the mammalian lens: a review with emphasis on changes in development, aging and cataract
23. Some properties of the low molecular weight a‐crystallin from normal human lens: Comparison with bovine lens
24. Conformation of gamma‐crystallins of the calf lens: Effects of temperature and denaturing agents
25. Structure and stability of γ‐crystaIlins‐V. Covalent and non‐covalent protein‐protein interactions in photosensitized reactions
26. Age‐related changes in protein conformation in bovine lens crystallins
27. Spectroscopic investigations of bovine lens crystallins. 1. Circular di‐chroism and intrinsic fluorescence
28. Sensitizer‐induced conformational changes in lens crystallin‐I. Photodynamic action of methylene blue and N‐formylkynurenine on bovine α‐crystallin
29. Structure and stability of γ‐crystallins. I. Spectroscopic evaluation of secondary and tertiary structure in solution
30. Structure and stability of γ‐crystallins. II. Differences in microenvironments and spatial arrangements of cysteine residues
31. Structure and stability of γ‐crystallins: Denatur‐ation and proteolysis behavior
32. Structural and evolutionary relationships among five members of the human γ‐crystallin gene family
33. Lens crystallins and their gene families
34. Formation of N′‐formylkynurenine in proteins from lens and other sources by exposure to sunlight
35. Monitoring light‐induced changes in isolated, intact eye lenses
36. The crystallin gene families
37. Superior resolution of γ‐crystallins from microdissected eye lens by cation‐exchange high‐performance liquid chromatography
38. Aging of the lens and cataract formation
39. X‐ray studies of the lens specific proteins: The crystallins
40. N‐formylkynurenine, a tryptophan photooxidation product, as a photodynamic sensitizer
41. X‐ray analysis of the eye lens protein γ‐II crystallin at 1.9 Å resolution
42. Photosensitized oxidation in the ocular lens: Evidence for photosensi‐tizers endogeneous to the human lens