The N-terminal lysine residue-rich domain II and the 340–430 amino acid segment of eukaryotic initiation factor 2-associated glycoprotein p67 are the binding sites for the γ-subunit of eIF2-Reference-Cited by-同舟云学术

The N-terminal lysine residue-rich domain II and the 340–430 amino acid segment of eukaryotic initiation factor 2-associated glycoprotein p67 are the binding sites for the γ-subunit of eIF2

Published:2006-10 Issue:16 Volume:312 Page:3184-3203
ISSN:0014-4827
Container-title:Experimental Cell Research
language:en
Short-container-title:Experimental Cell Research

Author:

Ghosh Arnab,Datta Rekha,Majumdar Avijit,Bhattacharya Mahasweta,Datta Bansidhar

Publisher

Elsevier BV

Subject

Cell Biology

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4. 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-2α-subunit;Datta;J. Biol. Chem.,1989

5. The eukaryotic initiation factor 2-associated 67-kDa polypetide (p67) plays a critical role in regulation of protein synthesis initiation in animal cells;Ray;Proc. Natl. Acad. Sci. U. S. A.,1992

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