The Intermediate Filament Protein, Vimentin, in the Lens Is a Target for Cross-linking by Transglutaminase-Reference-Cited by-同舟云学术

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The Intermediate Filament Protein, Vimentin, in the Lens Is a Target for Cross-linking by Transglutaminase

Published:1998-03 Issue:13 Volume:273 Page:7604-7609
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Clément Sophie,Velasco Pauline T.,Murthy S.N. Prasanna,Wilson James H.,Lukas Thomas J.,Goldman Robert D.,Lorand Laszlo

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference65 articles.

1. Lens transglutaminase and cataract formation.

2. beta-Crystallin: endogenous substrate of lens transglutaminase Characterization of the acyl-donor site in the beta Bp chain

3. Labeling of epsilon-lysine crosslinking sites in proteins with peptide substrates of factor XIIIa and transglutaminase.

4. Sorting-out of acceptor-donor relationships in the transglutaminase-catalyzed cross-linking of crystallins by the enzyme-directed labeling of potential sites.

5. The carboxy-terminal lysine of alphaB-crystallin is an amine-donor substrate for tissue transglutaminase

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1. Aquaporin-0-protein interactions elucidated by crosslinking mass spectrometry;Biochemical and Biophysical Research Communications;2024-10

2. The Motility and Mesenchymal Features of Breast Cancer Cells Correlate with the Levels and Intracellular Localization of Transglutaminase Type 2;Cells;2021-11-06

3. Vimentin Intermediate Filaments Undergo Irreversible Conformational Changes during Cyclic Loading;Nano Letters;2019-09-06

4. Transglutaminase Regulation of Cell Function;Physiological Reviews;2014-04

5. Detyrosinated Glu-tubulin is a substrate for cellular Factor XIIIA transglutaminase in differentiating osteoblasts;Amino Acids;2014-03-19

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