PKR and GCN2 kinases and guanine nucleotide exchange factor eukaryotic translation initiation factor 2B (eIF2B) recognize overlapping surfaces on eIF2alpha - Wikidata - awgldk - TriplyDB

PKR and GCN2 kinases and guanine nucleotide exchange factor eukaryotic translation initiation factor 2B (eIF2B) recognize overlapping surfaces on eIF2alpha

PKR and GCN2 kinases and guanine nucleotide exchange factor eukaryotic translation initiation factor 2B (eIF2B) recognize overlapping surfaces on eIF2alpha

http://www.wikidata.org/entity/Q33724522

about

Crystal structure of eukaryotic translation initiation factor 2B Double-stranded RNA-activated protein kinase PKR of fishes and amphibians: varying the number of double-stranded RNA binding domains and lineage-specific duplications.GCN2 phosphorylates HIV-1 integrase and decreases HIV-1 replication by limiting viral integration.Protein synthesis attenuation by phosphorylation of eIF2α is required for the differentiation of Trypanosoma cruzi into infective forms.Archaeal aIF2B interacts with eukaryotic translation initiation factors eIF2alpha and eIF2Balpha: Implications for aIF2B function and eIF2B regulation.The beta/Gcd7 subunit of eukaryotic translation initiation factor 2B (eIF2B), a guanine nucleotide exchange factor, is crucial for binding eIF2 in vivo Requirement for kinase-induced conformational change in eukaryotic initiation factor 2alpha (eIF2alpha) restricts phosphorylation of Ser51.An eIF2α-binding motif in protein phosphatase 1 subunit GADD34 and its viral orthologs is required to promote dephosphorylation of eIF2α.The amino terminus of the vaccinia virus E3 protein is necessary to inhibit the interferon response Activation-dependent substrate recruitment by the eukaryotic translation initiation factor 2 kinase PERK.Novel membrane-bound eIF2alpha kinase in the flagellar pocket of Trypanosoma brucei dsRNA-dependent protein kinase PKR and its role in stress, signaling and HCV infection.Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae.Variola virus E3L Zα domain, but not its Z-DNA binding activity, is required for PKR inhibition Activation of protein kinase PKR requires dimerization-induced cis-phosphorylation within the activation loop.Phosphorylation of eIF2α on Threonine 169 is not required for Trypanosoma brucei cell cycle arrest during differentiation.Evolution of the archaeal and mammalian information processing systems: towards an archaeal model for human disease.Essential amino acids regulate both initiation and elongation of mRNA translation independent of insulin in MAC-T cells and bovine mammary tissue slices.eIF2β is critical for eIF5-mediated GDP-dissociation inhibitor activity and translational control.Molecular dynamics reveal a novel kinase-substrate interface that regulates protein translation.Residues required for phosphorylation of translation initiation factor eIF2α under diverse stress conditions are divergent between yeast and human.Mae inhibits Pointed-P2 transcriptional activity by blocking its MAPK docking site.Activation of the integrated stress response during T helper cell differentiation.SMN deficiency reduces cellular ability to form stress granules, sensitizing cells to stress.

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PKR and GCN2 kinases and guanine nucleotide exchange factor eukaryotic translation initiation factor 2B (eIF2B) recognize overlapping surfaces on eIF2alpha

http://www.wikidata.org/entity/Q33724522

description

2005 nî lūn-bûn

@nan

2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2005年の論文

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2005年論文

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2005年論文

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2005年論文

@zh-hk

2005年論文

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2005年論文

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2005年论文

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name

PKR and GCN2 kinases and guani ...... rlapping surfaces on eIF2alpha

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PKR and GCN2 kinases and guani ...... rlapping surfaces on eIF2alpha

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PKR and GCN2 kinases and guani ...... rlapping surfaces on eIF2alpha

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PKR and GCN2 kinases and guani ...... rlapping surfaces on eIF2alpha

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MCB.25.8.3063-3075.2005

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Molecular and Cellular Biology

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PKR and GCN2 kinases and guani ...... rlapping surfaces on eIF2alpha

@en

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Arvin C Dar

http://www.w3.org/2001/XMLSchema#string

Bruce Trieselmann

http://www.w3.org/2001/XMLSchema#string

Chune Cao

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Emily G Locke

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Frank Sicheri

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Jingfang Lu

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Jinsheng Dong

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Madhusudan Dey

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Thanuja Krishnamoorthy

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P2860

Pancreatic eukaryotic initiation factor-2alpha kinase (PEK) homologues in humans, Drosophila melanogaster and Caenorhabditis elegans that mediate translational control in response to endoplasmic reticulum stress

Homologous regions of the alpha subunit of eukaryotic translational initiation factor 2 (eIF2alpha) and the vaccinia virus K3L gene product interact with the same domain within the dsRNA-activated protein kinase (PKR)

Mammalian eukaryotic initiation factor 2 alpha kinases functionally substitute for GCN2 protein kinase in the GCN4 translational control mechanism of yeast

Crystal structure of the N-terminal segment of human eukaryotic translation initiation factor 2alpha

X-ray crystal structure and functional analysis of vaccinia virus K3L reveals molecular determinants for PKR subversion and substrate recognition

The crystal structure of the N-terminal region of the alpha subunit of translation initiation factor 2 (eIF2alpha) from Saccharomyces cerevisiae provides a view of the loop containing serine 51, the target of the eIF2alpha-specific kinases

SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling

A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae

eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange.

Phosphorylation of initiation factor 2 alpha by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast.

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3063-3075

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scholarly article

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10.1128/MCB.25.8.3063-3075.2005

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8

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25

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1069625

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