Activation of Protein Kinase PKR Requires Dimerization-inducedcis-Phosphorylation within the Activation Loop

The Structural Basis for Control of Eukaryotic Protein Kinases

(2012) Jane A. Endicott et al.   Annual Review of Biochemistry

Novel role of PKR in inflammasome activation and HMGB1 release

(2012) Ben Lu et al.   NATURE

The structure of the PERK kinase domain suggests the mechanism for its activation

(2011) Wenjun Cui et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Molecular Mechanism of Scanning and Start Codon Selection in Eukaryotes

(2011) A. G. Hinnebusch   MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS

The pseudokinase domain of JAK2 is a dual-specificity protein kinase that negatively regulates cytokine signaling

(2011) Daniela Ungureanu et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Requirement for kinase-induced conformational change in eukaryotic initiation factor 2  (eIF2 ) restricts phosphorylation of Ser51

(2011) M. Dey et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Mutation that blocks ATP binding creates a pseudokinase stabilizing the scaffolding function of kinase suppressor of Ras, CRAF and BRAF

(2011) J. Hu et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Pseudokinases-remnants of evolution or key allosteric regulators?

(2010) Elton Zeqiraj et al.   CURRENT OPINION IN STRUCTURAL BIOLOGY

Phosphorylation of the NFAR proteins by the dsRNA-dependent protein kinase PKR constitutes a novel mechanism of translational regulation and cellular defense

(2010) A. Harashima et al.   GENES & DEVELOPMENT

Pseudokinases: Functional Insights Gleaned from Structure

(2009) Alexandr P. Kornev et al.   STRUCTURE

Mechanism of PKR Activation by dsRNA

(2008) Peter A. Lemaire et al.   JOURNAL OF MOLECULAR BIOLOGY