Aggregation of β-crystallin through covalent binding to 1,2-naphthoquinone is rescued by α-crystallin chaperone-Reference-Cited by-同舟云学术

Aggregation of β-crystallin through covalent binding to 1,2-naphthoquinone is rescued by α-crystallin chaperone

Published:2020 Issue:1 Volume:45 Page:37-43
ISSN:0388-1350
Container-title:The Journal of Toxicological Sciences
language:en
Short-container-title:J. Toxicol. Sci.

Author:

Shinkai Yasuhiro¹²,Ding Yunjie²,Miura Takashi²,Kumagai Yoshito¹²

Affiliation:

1. Environmental Biology Laboratory, Faculty of Medicine, University of Tsukuba

2. Doctoral Program in Biomedical Sciences, Graduate School of Comprehensive Human Sciences, University of Tsukuba

Publisher

Japanese Society of Toxicology

Subject

Toxicology

Link

https://www.jstage.jst.go.jp/article/jts/45/1/45_37/_pdf

Reference29 articles.

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3. Horwitz, J. (1992): Alpha-crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. USA, 89, 10449-10453.

4. Iwamoto, N., Sumi, D., Ishii, T., Uchida, K., Cho, A.K., Froines, J.R. and Kumagai, Y. (2007): Chemical knockdown of protein-tyrosine phosphatase 1B by 1,2-naphthoquinone through covalent modification causes persistent transactivation of epidermal growth factor receptor. J. Biol. Chem., 282, 33396-33404.

5. Kelly, S.P., Thornton, J., Edwards, R., Sahu, A. and Harrison, R. (2005): Smoking and cataract: review of causal association. J. Cataract Refract. Surg., 31, 2395-2404.

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