Mechanistic Link between PKR Dimerization, Autophosphorylation, and eIF2α Substrate Recognition

By Madhusudan Dey, C. Cao, A. Dar, T. Tamura, K. Ozato, Frank Sicheri, T. Dever. 2005

361 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/bffb305092cdc13f59bedb2e627e9ac589b3a9d0

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In Molecular Biology

1. Bryan R. G. Williams

Citations in the corpus

• A Novel Function of eIF2α Kinases as Inducers of the Phosphoinositide-3 Kinase Signaling Pathway (2007, background): “It was recently shown that introduction of T487D mutation in PKR abolishes its eIF2 kinase activity without affecting its capacity to autophosphorylate ( Dey et al., 2005 ).”
• Interferon-inducible antiviral effectors (2008, background): “Dimerization induces, and requires, autophosphorylation at several key residue”
• The eIF2α kinases: their structures and functions (2013, neutral): “The X-ray crystal structures of the catalytic domain of PKR in complex with eIF2α have further confirmed the importance of PKR dimerization mediated by the kinase domains in PKR activation and have also revealed how the eIF2α substrate docks to the PKR kinase [39, 45].”