Glycosylation of eukaryotic peptide chain initiation factor 2 (eIF-2)-associated 67-kDa polypeptide (p67) and its possible role in the inhibition of eIF-2 kinase-catalyzed phosphorylation of the eIF-2 α-subunit-Reference-Cited by-同舟云学术

Glycosylation of eukaryotic peptide chain initiation factor 2 (eIF-2)-associated 67-kDa polypeptide (p67) and its possible role in the inhibition of eIF-2 kinase-catalyzed phosphorylation of the eIF-2 α-subunit

Published:1989-12 Issue:34 Volume:264 Page:20620-20624
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Datta B,Ray M.K.,Chakrabarti D,Wylie D.E.,Gupta N.K.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference18 articles.

1. Nuclear and cytoplasmic glycosylation: novel saccharide linkages in unexpected places

2. Roles of a 67-kDa polypeptide in reversal of protein synthesis inhibition in heme-deficient reticulocyte lysate.

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

4. Identification and characterization of a nuclear pore complex protein

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