The congenital cataract‐causing mutations P20R and A171T are associated with important changes in the amyloidogenic feature, structure and chaperone‐like activity of human αB‐crystallin-Reference-Cited by-同舟云学术

The congenital cataract‐causing mutations P20R and A171T are associated with important changes in the amyloidogenic feature, structure and chaperone‐like activity of human αB‐crystallin

Published:2020-02-28 Issue:5 Volume:111 Page:
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Ghahramani Maryam¹,Yousefi Reza¹^ORCID,Niazi Ali²,Kurganov Boris³

Affiliation:

1. Protein Chemistry Laboratory (PCL), Department of BiologyCollege of Sciences, Shiraz University Shiraz Iran

2. Institute of BiotechnologyShiraz University Shiraz Iran

3. Bach Institute of BiochemistryResearch Center of Biotechnology of the Russian Academy of Sciences Moscow Russia

Funder

Iran National Science Foundation

National Institute for Medical Research Development

Russian Science Foundation

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/bip.23350

Reference79 articles.

1. Ageing and vision: structure, stability and function of lens crystallins

2. sHSP in the eye lens: Crystallin mutations, cataract and proteostasis

3. Alpha-crystallin can function as a molecular chaperone.

4. Alpha-crystallin

5. Lens α-crystallin: Function and structure

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