Negative charge at aspartate 151 is important for human lens αA-crystallin stability and chaperone function-Reference-Cited by-同舟云学术

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Negative charge at aspartate 151 is important for human lens αA-crystallin stability and chaperone function

Published:2019-05 Issue: Volume:182 Page:10-18
ISSN:0014-4835
Container-title:Experimental Eye Research
language:en
Short-container-title:Experimental Eye Research

Author:

Takata Takumi,Matsubara Toshiya,Nakamura-Hirota Tooru,Fujii Noriko

Funder

Ministry of Education, Culture, Sports, Science and Technology of Japan

JSPS KAKENHI

Publisher

Elsevier BV

Subject

Cellular and Molecular Neuroscience,Sensory Systems,Ophthalmology

Reference55 articles.

1. Size of human lens beta-crystallin aggregates are distinguished by N-terminal truncation of betaB1;Ajaz;J. Biol. Chem.,1997

2. Crystallins and hereditary cataracts: molecular mechanisms and potential for therapy;Andley;Expert Rev. Mol. Med.,2006

3. Photoreactions of human lens monomeric crystallins;Andley;Biochim. Biophys. Acta,1989

4. Subunit exchange of polydisperse proteins: mass spectrometry reveals consequences of alphaA-crystallin truncation;Aquilina;J. Biol. Chem.,2005

5. The reaction of singlet oxygen with proteins, with special reference to crystallins;Balasubramanian;Photochem. Photobiol.,1990

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1. Characterization of different-sized human αA-crystallin homomers and implications to Asp151 isomerization;PLOS ONE;2024-07-11

2. Use of Informational Brochures on Knowledge of Cataracts in Rural Ecuador;Cureus;2023-02-27

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

4. The mechanism for thermal-enhanced chaperone-like activity of α-crystallin against UV irradiation-induced aggregation of γD-crystallin;Biophysical Journal;2022-06

5. Eye Lens Crystallins: Remarkable Long‐Lived Proteins;Long‐lived Proteins in Human Aging and Disease;2021-02-05

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