O-GlcNAc modification: a nutritional sensor that modulates proteasome function-Reference-Cited by-同舟云学术

O-GlcNAc modification: a nutritional sensor that modulates proteasome function

Published:2004-05 Issue:5 Volume:14 Page:218-221
ISSN:0962-8924
Container-title:Trends in Cell Biology
language:en
Short-container-title:Trends in Cell Biology

Author:

Zachara Natasha E,Hart Gerald W

Publisher

Elsevier BV

Subject

Cell Biology

Reference26 articles.

1. Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc;Wells;Science,2001

2. Zachara, N.E. et al. Dynamic O-GlcNAc modification of nucleocytoplasmic proteins is a global mechanism for protecting mammalian cells from stress. Proc. Natl. Acad. Sci. U. S. A. (in press).

3. RNA polymerase II is a glycoprotein. Modification of the COOH-terminal domain by O-GlcNAc;Kelly;J. Biol. Chem.,1993

4. Insulin-dependent activation of endothelial nitric oxide synthase is impaired by O-linked glycosylation modification of signaling proteins in human coronary endothelial cells;Federici;Circulation,2002

5. Hyperglycemia inhibits endothelial nitric oxide synthase activity by posttranslational modification at the Akt site;Du;J. Clin. Invest.,2001

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