Mechanistic Link between PKR Dimerization, Autophosphorylation, and eIF2α Substrate Recognition
Top Cited Papers
- 1 September 2005
- Vol. 122 (6), 901-913
- https://doi.org/10.1016/j.cell.2005.06.041
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Higher-Order Substrate Recognition of eIF2α by the RNA-Dependent Protein Kinase PKRCell, 2005
- PKR and GCN2 Kinases and Guanine Nucleotide Exchange Factor Eukaryotic Translation Initiation Factor 2B (eIF2B) Recognize Overlapping Surfaces on eIF2αMolecular and Cellular Biology, 2005
- Mechanism of PKR Activation: Dimerization and Kinase Activation in the Absence of Double-stranded RNAJournal of Molecular Biology, 2005
- The Crystal Structure of the N-terminal Region of the Alpha Subunit of Translation Initiation Factor 2 (eIF2α) from Saccharomyces cerevisiae Provides a View of the Loop Containing Serine 51, the Target of the eIF2α-specific KinasesJournal of Molecular Biology, 2003
- Crystal Structure of the N-terminal Segment of Human Eukaryotic Translation Initiation Factor 2αJournal of Biological Chemistry, 2002
- Tight Binding of the Phosphorylated α Subunit of Initiation Factor 2 (eIF2α) to the Regulatory Subunits of Guanine Nucleotide Exchange Factor eIF2B Is Required for Inhibition of Translation InitiationMolecular and Cellular Biology, 2001
- Binding of Double-stranded RNA to Protein Kinase PKR Is Required for Dimerization and Promotes Critical Autophosphorylation Events in the Activation LoopJournal of Biological Chemistry, 2001
- A Model for the Double-stranded RNA (dsRNA)-dependent Dimerization and Activation of the dsRNA-activated Protein Kinase PKRJournal of Biological Chemistry, 1997
- Mechanism of Interferon ActionVirology, 1996
- A synthetic peptide substrate for initiation factor-2 kinasesBiochemical and Biophysical Research Communications, 1991