Conserved intermolecular salt bridge required for activation of protein kinases PKR, GCN2, and PERK. (Q34597501)

3 August 2017

title

Conserved intermolecular salt bridge required for activation of protein kinases PKR, GCN2, and PERK. (English)

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3 August 2017

4

Thomas E Dever

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3 August 2017

Madhusudan Dey

1

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3 August 2017

Chune Cao

series ordinal

2

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3 August 2017

Frank Sicheri

series ordinal

3

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3 August 2017

language of work or name

English

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publication date

3 January 2007

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Journal of Biological Chemistry

3 August 2017

number of pages

8

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based on heuristic

inferred from page(s)

published in

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3 August 2017

volume

282

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3 August 2017

issue

9

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3 August 2017

page(s)

6653-6660

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Gene-specific regulation by general translation factors

3 August 2017

cites work

1 reference

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Translational regulation of GCN4 and the general amino acid control of yeast

21 January 2018

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Mutations activating the yeast eIF-2 alpha kinase GCN2: isolation of alleles altering the domain related to histidyl-tRNA synthetases

21 January 2018

1 reference

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

21 January 2018

1 reference

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Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control

21 January 2018

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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

21 January 2018

1 reference

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Dimerization by translation initiation factor 2 kinase GCN2 is mediated by interactions in the C-terminal ribosome-binding region and the protein kinase domain

21 January 2018

1 reference

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Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response

21 January 2018

1 reference

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Heterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M607897200

Binding of double-stranded RNA to protein kinase PKR is required for dimerization and promotes critical autophosphorylation events in the activation loop.

21 January 2018

1 reference

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Dimerization and release of molecular chaperone inhibition facilitate activation of eukaryotic initiation factor-2 kinase in response to endoplasmic reticulum stress

21 January 2018

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On the mechanism of sensing unfolded protein in the endoplasmic reticulum

21 January 2018

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

21 January 2018

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Cytoprotection by pre-emptive conditional phosphorylation of translation initiation factor 2

21 January 2018

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Structural basis for autoinhibition and mutational activation of eukaryotic initiation factor 2alpha protein kinase GCN2.

21 January 2018

1 reference

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Regulation of the protein kinase PKR by the vaccinia virus pseudosubstrate inhibitor K3L is dependent on residues conserved between the K3L protein and the PKR substrate eIF2alpha.

21 January 2018

1 reference

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Uncharged tRNA activates GCN2 by displacing the protein kinase moiety from a bipartite tRNA-binding domain

21 January 2018

1 reference

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Autophosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2alpha kinases PKR and GCN2

21 January 2018

1 reference

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Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase

21 January 2018

1 reference

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EIF2AK3, encoding translation initiation factor 2-alpha kinase 3, is mutated in patients with Wolcott-Rallison syndrome

21 January 2018

1 reference

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Wolcott-Rallison Syndrome: clinical, genetic, and functional study of EIF2AK3 mutations and suggestion of genetic heterogeneity

21 January 2018

1 reference

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M607897200

Higher-Order Substrate Recognition of eIF2α by the RNA-Dependent Protein Kinase PKR

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M607897200

21 January 2018

Identifiers

DOI

10.1074/JBC.M607897200

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3 August 2017

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