Protection of translation initiation factor eIF2 phosphorylation correlates with eIF2-associated glycoprotein p67 levels and requires the lysine-rich domain I of p67
- 26 November 2001
- journal article
- Published by Elsevier
- Vol. 83 (10) , 919-931
- https://doi.org/10.1016/s0300-9084(01)01344-x
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- MAPs and POEP of the roads from prokaryotic to eukaryotic kingdomsBiochimie, 2000
- Increased Phosphorylation of Eukaryotic Initiation Factor 2α at the G2/M Boundary in Human Osteosarcoma Cells Correlates with Deglycosylation of p67 and a Decreased Rate of Protein SynthesisExperimental Cell Research, 1999
- A methionine aminopeptidase and putative regulator of translation initiation is required for cell growth and patterning in DrosophilaMechanisms of Development, 1999
- A Dominant Negative Mutation inSaccharomyces cerevisiaeMethionine Aminopeptidase-1 Affects Catalysis and Interferes with the Function of Methionine Aminopeptidase-2Archives of Biochemistry and Biophysics, 1997
- Cloning and Characterization of the Promoter Region of a Gene Encoding a 67-kDa GlycoproteinPublished by Elsevier ,1997
- p67 Transcription Regulates Translation in Serum-starved and Mitogen-activated KRC-7 CellsPublished by Elsevier ,1997
- Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases.Proceedings of the National Academy of Sciences, 1995
- Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes.Proceedings of the National Academy of Sciences, 1995
- 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