Negative regulation of the protection of eIF2α phosphorylation activity by a unique acidic domain present at the N-terminus of p67
- 15 February 2003
- journal article
- Published by Elsevier in Experimental Cell Research
- Vol. 283 (2) , 237-246
- https://doi.org/10.1016/s0014-4827(02)00042-3
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Gene-Specific Regulation by General Translation FactorsCell, 2002
- Protection of translation initiation factor eIF2 phosphorylation correlates with eIF2-associated glycoprotein p67 levels and requires the lysine-rich domain I of p67Published by Elsevier ,2001
- MAPs and POEP of the roads from prokaryotic to eukaryotic kingdomsBiochimie, 2000
- The Interferon-induced Double-stranded RNA-activated Protein Kinase PKR Will Phosphorylate Serine, Threonine, or Tyrosine at Residue 51 in Eukaryotic Initiation Factor 2αPublished by Elsevier ,1999
- A methionine aminopeptidase and putative regulator of translation initiation is required for cell growth and patterning in DrosophilaMechanisms of Development, 1999
- Molecular mechanisms in the control of translation by hormones and growth factorsBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1994
- elF-2 kinases: regulators of general and gene-specific translation initiationTrends in Biochemical Sciences, 1994
- Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold.Proceedings of the National Academy of Sciences, 1994
- Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzymeBiochemistry, 1993
- TRANSLATIONAL CONTROL IN MAMMALIAN CELLSAnnual Review of Biochemistry, 1991