DOI: 10.1016/s0167-4838(99)00178-8. Eye lens αA- and αB-crystallin: complex stability versus chaperone-like activity

Eye lens αA- and αB-crystallin: complex stability versus chaperone-like activity

10.1016/s0167-4838(99)00178-8

Crossref journal-article

Elsevier BV

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology (78)

Bibliography

van Boekel, M. A. M., de Lange, F., de Grip, W. J., & de Jong, W. W. (1999). Eye lens Î±A- and Î±B-crystallin: complex stability versus chaperone-like activity. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1434(1), 114â123.

Authors 4

Martinus A.M van Boekel (first)
Frank de Lange (additional)
Willem J de Grip (additional)
Wilfried W de Jong (additional)

References 43 Referenced 47

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{'key': '10.1016/S0167-4838(99)00178-8_BIB12', 'first-page': '311', 'article-title': 'α-Crystallin can act as a chaperone under conditions of oxidative stress', 'volume': '36', 'author': 'Wang', 'year': '1995', 'journal-title': 'Invest. Ophthalmol. Vis. Sci.'} / Invest. Ophthalmol. Vis. Sci. / α-Crystallin can act as a chaperone under conditions of oxidative stress by Wang (1995)
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10.1006/bbrc.1998.9242 / Biochem. Biophys. Res. Commun. / The chaperone-like α-crystallin forms a complex only with the aggregation-prone globule state of α-lactalbumin by Rajaraman (1998)
10.1074/jbc.272.38.23559 / J. Biol. Chem. / Chaperone-like activity and temperature-induced structural changes of α-crystallin by Raman (1997)
10.1006/bbrc.1997.6950 / Biochem. Biophys. Res. Commun. / Detection and characterization of α-crystallin intermediate with maximal chaperone-like activity by Das (1997)
10.1016/0167-4838(91)90146-Q / Biochim. Biophys. Acta / Immunoreactive αA-crystallin in rat non-lenticular tissues detected with a sensitive immunoassay method by Kato (1991)
10.1016/S0006-291X(89)80215-3 / Biochem. Biophys. Res. Commun. / αB subunit of lens-specific protein α-crystallin is present in other ocular and non-ocular tissues by Bhat (1989)
10.1016/0304-4165(95)00125-5 / Biochim. Biophys. Acta / Evidence that α-crystallin prevents non-specific protein aggregation in the intact eye lens by Rao (1995)
M. Ehrnsperger, J. Buchner, M. Gaestel, Structure and function of small heat shock proteins, in: A.L. Fink, Y. Goto (Eds.), Molecular Chaperones in the Life Cycle of Proteins – Structure, Function and Mode of Action, Marcel Dekker, New York, 1997, pp. 533–575.
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Dates

Type	When
Created	23 years, 1 month ago (July 26, 2002, 12:31 a.m.)
Deposited	4 years, 3 months ago (May 14, 2021, 11:32 p.m.)
Indexed	1 month, 3 weeks ago (July 4, 2025, 7:04 a.m.)
Issued	25 years, 11 months ago (Sept. 1, 1999)
Published	25 years, 11 months ago (Sept. 1, 1999)
Published Print	25 years, 11 months ago (Sept. 1, 1999)

Funders 0

None

BibTeX

@article{van_Boekel_1999, title={Eye lens αA- and αB-crystallin: complex stability versus chaperone-like activity}, volume={1434}, ISSN={0167-4838}, url={http://dx.doi.org/10.1016/s0167-4838(99)00178-8}, DOI={10.1016/s0167-4838(99)00178-8}, number={1}, journal={Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology}, publisher={Elsevier BV}, author={van Boekel, Martinus A.M and de Lange, Frank and de Grip, Willem J and de Jong, Wilfried W}, year={1999}, month=sep, pages={114–123} }

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