Cataract-causing mutation S228P promotes βB1-crystallin aggregation and degradation by separating two interacting loops in C-terminal domain-Reference-Cited by-同舟云学术

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Cataract-causing mutation S228P promotes βB1-crystallin aggregation and degradation by separating two interacting loops in C-terminal domain

Published:2016-06-18 Issue:7 Volume:7 Page:501-515
ISSN:1674-800X
Container-title:Protein & Cell
language:en
Short-container-title:Protein Cell

Author:

Qi Liang-Bo,Hu Li-Dan,Liu Huihui,Li Hai-Yun,Leng Xiao-Yao,Yan Yong-Bin

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Drug Discovery,Biochemistry,Biotechnology

Link

http://link.springer.com/content/pdf/10.1007/s13238-016-0284-3.pdf

Reference48 articles.

1. Andley UP (2007) Crystallins in the eye: function and pathology. Prog Retin Eye Res. 26:78–98

2. Baldwin RL (2007) Energetics of protein folding. J Mol Biol 371:283–301

3. Bassnett S (2009) On the mechanism of organelle degradation in the vertebrate lens. Exp Eye Res 88:133–139

4. Bateman OA, Lubsen NH, Slingsby C (2001) Association behaviour of human βB1-crystallin and its truncated forms. Exp Eye Res 73:321–331

5. Bateman OA, Sarra R, van Genesen ST, Kapp G, Lubsen NH, Slingsby C (2003) The stability of human acidic β-crystallin oligomers and hetero-oligomers. Exp Eye Res 77:409–422

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1. Truncation mutations of CRYGD gene in congenital cataracts cause protein aggregation by disrupting the structural stability of γD-crystallin;International Journal of Biological Macromolecules;2024-10

2. Effect of ageing and cataract formation on the Raman spectroscopic profile of human lens: An observational study;Indian Journal of Ophthalmology;2024-08-23

3. Cataract-related variant R114C increases βA3-crystallin susceptibility to environmental stresses by disrupting the protein senior structure;International Journal of Biological Macromolecules;2024-03

4. Using genetics to investigate the association between lanosterol and cataract;Frontiers in Genetics;2024-02-19

5. Cataract-causing mutations S78F and S78P of γD-crystallin decrease protein conformational stability and drive aggregation;International Journal of Biological Macromolecules;2023-12

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