Features in the N and C Termini of the MAPK-interacting Kinase Mnk1 Mediate Its Nucleocytoplasmic Shuttling
Open Access
- 1 November 2003
- journal article
- Published by Elsevier BV
- Vol. 278 (45), 44197-44204
- https://doi.org/10.1074/jbc.m302398200
Abstract
No abstract availableThis publication has 28 references indexed in Scilit:
- Phosphorylation of eIF4E attenuates its interaction with mRNA 5′ cap analogs by electrostatic repulsion: Intein-mediated protein ligation strategy to obtain phosphorylated proteinRNA, 2003
- Phosphorylation of Eukaryotic Initiation Factor 4E Markedly Reduces Its Affinity for Capped mRNAPublished by Elsevier BV ,2002
- Regulation of translation initiation by FRAP/mTORGenes & Development, 2001
- eIF4 Initiation Factors: Effectors of mRNA Recruitment to Ribosomes and Regulators of TranslationAnnual Review of Biochemistry, 1999
- Phosphorylation of the Cap-Binding Protein Eukaryotic Translation Initiation Factor 4E by Protein Kinase Mnk1 In VivoMolecular and Cellular Biology, 1999
- Human eukaryotic translation initiation factor 4G (eIF4G) recruits Mnk1 to phosphorylate eIF4EThe EMBO Journal, 1999
- eIF4E expression in tumors: its possible role in progression of malignanciesThe International Journal of Biochemistry & Cell Biology, 1999
- PHAS/4E-BPs as regulators of mRNA translation and cell proliferationTrends in Biochemical Sciences, 1997
- Overexpression of eukaryotic protein synthesis initiation factor 4E in HeLa cells results in aberrant growth and morphology.Proceedings of the National Academy of Sciences of the United States of America, 1990
- Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5' capNature, 1990