Three Decades of Research on O-GlcNAcylation â€“ A Major Nutrient Sensor That Regulates Signaling, Transcription and Cellular Metabolism-Reference-Cited by-同舟云学术

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Three Decades of Research on O-GlcNAcylation â€“ A Major Nutrient Sensor That Regulates Signaling, Transcription and Cellular Metabolism

Published:2014-10-27 Issue: Volume:5 Page:
ISSN:1664-2392
Container-title:Frontiers in Endocrinology
language:
Short-container-title:Front. Endocrinol.

Author:

Hart Gerald W.

Publisher

Frontiers Media SA

Reference80 articles.

1. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes;Torres;J Biol Chem,1984

2. The subcellular distribution of terminal N-acetylglucosamine moieties. Localization of a novel protein-saccharide linkage, O-linked GlcNAc;Holt;J Biol Chem,1986

3. O-linked N-acetylglucosamine is attached to proteins of the nuclear pore. Evidence for cytoplasmic and nucleoplasmic glycoproteins;Hanover;J Biol Chem,1987

4. Nuclear pore complex contains a family of glycoproteins that includes p62: glycosylation through a previously unidentified cellular pathway;Davis;Proc Natl Acad Sci U S A,1987

5. Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine;Holt;J Cell Biol,1987

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