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163 related items for PubMed ID: 7835391
21. Calf lens alpha-crystallin, a molecular chaperone, builds stable complexes with beta s- and gamma-crystallins. Bours J. Ophthalmic Res; 1996; 28 Suppl 1():23-31. PubMed ID: 8727960 [Abstract] [Full Text] [Related]
22. Characterization of the alpha-gamma and alpha-beta complex: evidence for an in vivo functional role of alpha-crystallin as a molecular chaperone. Boyle D, Takemoto L. Exp Eye Res; 1994 Jan; 58(1):9-15. PubMed ID: 8157104 [Abstract] [Full Text] [Related]
23. Physicochemical studies on bovine eye lens proteins. II. Comparative physical study of the low-molecular-weight alpha-crystallins from calf lens cortical and nuclear fiber cells. Coopman S, de Block J, Aerts T, Peeters W, Moens L, Clauwaert J. Exp Eye Res; 1984 May; 38(5):463-76. PubMed ID: 6745323 [Abstract] [Full Text] [Related]
24. Lens alpha-crystallin: function and structure. Horwitz J, Bova MP, Ding LL, Haley DA, Stewart PL. Eye (Lond); 1999 Jun; 13 ( Pt 3b)():403-8. PubMed ID: 10627817 [Abstract] [Full Text] [Related]
25. [Comparative study of crystallins from the nucleus and cortex of the bovine ocular lens by the gel filtration and x-ray diffraction methods]. Krivandin AV, L'vov IuM, Ostrovskiĭ MA, Fedorovich IB, Feĭgin LA. Biofizika; 1985 Jun; 30(1):107-11. PubMed ID: 3978131 [Abstract] [Full Text] [Related]
26. 13C NMR studies of protein motional dynamics in bovine, human, rat, and chicken ocular lenses. Rydzewski JM, Wang SX, Stevens A, Serdahl C, Schleich T. Exp Eye Res; 1993 Mar; 56(3):305-16. PubMed ID: 8472786 [Abstract] [Full Text] [Related]
27. Purification and properties of the low-molecular-weight alpha-crystallin from normal goat lens: comparison with bovine lens. Roy B, Ghosh SK. Exp Eye Res; 1991 Dec; 53(6):693-701. PubMed ID: 1783007 [Abstract] [Full Text] [Related]
28. On the quaternary structure of high-molecular-weight proteins from the bovine eye lens. Kramps HA, Stols AL, Hoenders HJ. Eur J Biochem; 1975 Jan 15; 50(3):503-9. PubMed ID: 1112267 [Abstract] [Full Text] [Related]
29. Calf lens alpha-crystallin quaternary structure. A three-layer tetrahedral model. Tardieu A, Laporte D, Licinio P, Krop B, Delaye M. J Mol Biol; 1986 Dec 20; 192(4):711-24. PubMed ID: 3586011 [Abstract] [Full Text] [Related]
30. Alpha-crystallin can act as a chaperone under conditions of oxidative stress. Wang K, Spector A. Invest Ophthalmol Vis Sci; 1995 Feb 20; 36(2):311-21. PubMed ID: 7843902 [Abstract] [Full Text] [Related]
31. Spatial and temporal mapping of the age-related changes in human lens crystallins. McFall-Ngai MJ, Ding LL, Takemoto LJ, Horwitz J. Exp Eye Res; 1985 Dec 20; 41(6):745-58. PubMed ID: 3830737 [Abstract] [Full Text] [Related]
32. Intermolecular protein interactions in solutions of calf lens alpha-crystallin. Results from 1/T1 nuclear magnetic relaxation dispersion profiles. Koenig SH, Brown RD, Spiller M, Chakrabarti B, Pande A. Biophys J; 1992 Mar 20; 61(3):776-85. PubMed ID: 1504248 [Abstract] [Full Text] [Related]
33. 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. Lamba OP, Borchman D, Sinha SK, Shah J, Renugopalakrishnan V, Yappert MC. Biochim Biophys Acta; 1993 May 13; 1163(2):113-23. PubMed ID: 8490044 [Abstract] [Full Text] [Related]
34. Acetyl- L -carnitine decreases glycation of lens proteins: in vitro studies. Swamy-Mruthinti S, Carter AL. Exp Eye Res; 1999 Jul 13; 69(1):109-15. PubMed ID: 10375455 [Abstract] [Full Text] [Related]
35. A differential scanning calorimetric study of the bovine lens crystallins. Steadman BL, Trautman PA, Lawson EQ, Raymond MJ, Mood DA, Thomson JA, Middaugh CR. Biochemistry; 1989 Dec 12; 28(25):9653-8. PubMed ID: 2611254 [Abstract] [Full Text] [Related]
36. Variation in proportion and molecular weight of native crystallins from single human lenses upon aging and formation of nuclear cataract. Bessems GJ, Hoenders HJ, Wollensak J. Exp Eye Res; 1983 Dec 12; 37(6):627-37. PubMed ID: 6662209 [Abstract] [Full Text] [Related]