Asp isomerization increases aggregation of α-crystallin and decreases its chaperone activity in human lens of various ages-Reference-Cited by-同舟云学术

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Asp isomerization increases aggregation of α-crystallin and decreases its chaperone activity in human lens of various ages

Published:2020-09 Issue:9 Volume:1868 Page:140446
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Fujii Noriko,Takata Takumi,Kim Ingu,Morishima Ken,Inoue Rintaro,Magami Kousuke,Matsubara Toshiya,Sugiyama Masaaki,Koide Tamaki

Funder

Ministry of Education, Culture, Sports, Science and Technology

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference40 articles.

1. Ageing and vision: structure, stability and function of lens crystallins;Bloemendal;Prog. Biophys. Mol. Biol.,2004

2. The vertebrate eye lens;Bloemendal;Science,1977

3. Deamidation of human beta B1 alters the elongated structure of the dimer;Lampi;Exp. Eye Res.,2001

4. Deamidation in human lens betaB2-crystallin destabilizes the dimer;Lampi;Biochemistry (Mosc),2006

5. Deamidation alters the structure and decreases the stability of human lens betaA3-crystallin;Takata;Biochemistry (Mosc),2007

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3. Insights into the biochemical and biophysical mechanisms mediating the longevity of the transparent optics of the eye lens;Journal of Biological Chemistry;2022-11

4. Binding of Alpha-Crystallin to Cortical and Nuclear Lens Lipid Membranes Derived from a Single Lens;International Journal of Molecular Sciences;2022-09-25

5. Identification of D-amino Acid Residues in Proteins Using Mass Spectrometry;BUNSEKI KAGAKU;2022-06-05

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