Importance of the positively charged residue at position 54 to the chaperoning function, conformational stability and amyloidogenic nature of human αA-crystallin-Reference-Cited by-同舟云学术

Importance of the positively charged residue at position 54 to the chaperoning function, conformational stability and amyloidogenic nature of human αA-crystallin

Published:2017-11-27 Issue:3 Volume:163 Page:187-199
ISSN:0021-924X
Container-title:The Journal of Biochemistry
language:en
Short-container-title:

Author:

Khoshaman Kazem¹,Yousefi Reza¹,Niazi Ali²,Oryan Ahmad³,Moosavi-Movahedi Ali Akbar⁴⁵,Kurganov Boris I⁶

Affiliation:

1. Protein Chemistry Laboratory (PCL), Department of Biology, School of Veterinary Medicine, Shiraz University, Shiraz, Iran

2. Institute of Biotechnology, School of Veterinary Medicine, Shiraz University, Shiraz, Iran

3. Department of Pathology, School of Veterinary Medicine, Shiraz University, Shiraz, Iran

4. Institute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran, Iran

5. UNESCO Chair on Interdisciplinary Research in Diabetes, University of Tehran, Iran

6. Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Moscow, Russia

Funder

INSF

Russian Science Foundation

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,General Medicine

Link

http://academic.oup.com/jb/article-pdf/163/3/187/24041800/mvx071.pdf

Reference47 articles.

1. Evolution of crystallins for a role in the vertebrate eye lens;Slingsby;Protein Sci,2013

2. The ageing lens and cataract: a model of normal and pathological ageing;Michael;Philos. Trans. R. Soc. Lond. B Biol. Sci,2011

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

4. Alpha-Cry;Horwitz;Exp. Eye Res,2003

5. Human αA- and αB-Crys bind to Bax and Bcl-Xs to sequester their translocation during staurosporine-induced apoptosis;Mao;Cell Death Differ,2004

Cited by 5 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. A novel method for the chaperone aided and efficient production of human proinsulin in the prokaryotic system;Journal of Biotechnology;2022-02

2. Relationship between the Structure and Chaperone Activity of Human αA-Crystallin after Its Modification with Diabetes-Associated Oxidative Agents and Protective Role of Antioxidant Compounds;Biochemistry (Moscow);2022-02

3. Связь между структурой и шаперонной активностью αA-кристаллина человека после его модификации ассоциированными с сахарным диабетом окислительными агентами и защитная роль антиоксидантных молекул;Биохимия;2022-02-01

4. Amyloid management by chaperones: The mystery underlying protein oligomers’ dual functions;Current Research in Structural Biology;2022

5. The concept of protein folding/unfolding and its impacts on human health;Apoptosis in Health and Disease - Part B;2021