T cell development and the physiological role of O ‐GlcNAc

Author:

Abramowitz Lara K.1,Hanover John A.1

Affiliation:

1. Laboratory of Cellular and Molecular Biology National Institute of Diabetes and Digestive and Kidney Diseases National Institute of Health Bethesda MD USA

Funder

National Institute of Diabetes and Digestive and Kidney Diseases

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Reference45 articles.

1. Topography and polypeptide distribution of terminal N‐acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O‐linked GlcNAc;Torres CR;J Biol Chem,1984

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

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

4. Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine.

5. Monoclonal antibodies identify a group of nuclear pore complex glycoproteins.

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