Immobilization of the C-terminal Extension of Bovine αA-Crystallin Reduces Chaperone-like Activity-Reference-Cited by-同舟云学术

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Immobilization of the C-terminal Extension of Bovine αA-Crystallin Reduces Chaperone-like Activity

Published:1996-11 Issue:46 Volume:271 Page:29060-29066
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Smulders Ronald H.P.H.,Carver John A.,Lindner Robyn A.,van Boekel Martinus A.M.,Bloemendal Hans,de Jong Wilfried W.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference61 articles.

1. Structure and Modifications of the Junior Chaperone alpha-Crystallin. From Lens Transparency to Molecular Pathology

2. Immunoreactive αA crystallin in rat non-lenticular tissues detected with a sensitive immunoassay method

3. alpha A-crystallin is expressed in non-ocular tissues

4. Alpha A- and alpha B-crystallin in the retina. Association with the post-Golgi compartment of frog retinal photoreceptors

5. αB subunit of lens-specific protein α-crystallin is present in other ocular and non-ocular tissues

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2. Structure–function relationship of α-crystallin in the context of vertebrate lens evolution and its role in eye disorders;Journal of Proteins and Proteomics;2022-12-07

3. Real-time label-free assessment of T7 DNA polymerase immobilization;Materials Today Nano;2022-08

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