Potential Regulation of Nuclear UDP-N-Acetylglucosaminyl Transferase (OGT) by Substrate Availability: Ability of Chromatin Protein to Bind UDP-N-Acetylglucosamine and Reduce OGT-Mediated O-Linked Glycosylation-Reference-Cited by-同舟云学术

Potential Regulation of Nuclear UDP-N-Acetylglucosaminyl Transferase (OGT) by Substrate Availability: Ability of Chromatin Protein to Bind UDP-N-Acetylglucosamine and Reduce OGT-Mediated O-Linked Glycosylation

Published:2004 Issue:8 Volume:27 Page:1293-1296
ISSN:0918-6158
Container-title:Biological and Pharmaceutical Bulletin
language:en
Short-container-title:Biol. Pharm. Bull.

Author:

Okuyama Ryo¹,Marshall Stephen¹

Affiliation:

1. Hexos, Inc.

Publisher

Pharmaceutical Society of Japan

Subject

Pharmaceutical Science,Pharmacology,General Medicine

Link

http://www.jstage.jst.go.jp/article/bpb/27/8/27_8_1293/_pdf

Reference16 articles.

1. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc.

2. The subcellular distribution of terminal N-acetylglucosamine moieties. Localization of a novel protein-saccharide linkage, O-linked GlcNAc.

3. Glycan‐dependent signaling: O‐linked N‐acetylglucosamine

4. Glycosylation of Nucleocytoplasmic Proteins: Signal Transduction and O-GlcNAc

5. Diverse regulation of protein function by O-GlcNAc: a nuclear and cytoplasmic carbohydrate post-translational modification

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