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Identification of positive-acting domains in GCN2 protein kinase required for translational activation of GCN4 expression
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scholarly article
1 reference
stated in
PubMed
PubMed ID
2188100
retrieved
1 December 2016
title
Identification of positive-acting domains in GCN2 protein kinase required for translational activation of GCN4 expression
(English)
1 reference
stated in
PubMed
PubMed ID
2188100
retrieved
1 December 2016
main subject
Serine/threonine-protein kinase GCN2 YDR283C
1 reference
stated in
GOA release 2020-03-11
author name string
R C Wek
series ordinal
1
0 references
M Ramirez
series ordinal
2
0 references
B M Jackson
series ordinal
3
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A G Hinnebusch
series ordinal
4
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language of work or name
English
0 references
publication date
June 1990
0 references
published in
Molecular and Cellular Biology
1 reference
stated in
PubMed
PubMed ID
2188100
retrieved
1 December 2016
volume
10
0 references
page(s)
2820-31
0 references
issue
6
0 references
cites work
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Temporal analysis of general control of amino acid biosynthesis in Saccharomyces cerevisiae: role of positive regulatory genes in initiation and maintenance of mRNA derepression
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Positive Regulatory Interactions of the HIS4 Gene of Saccharomyces cerevisiae
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The general control of amino acid biosynthetic genes in the yeast Saccharomyces cerevisiae
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Molecular analysis of GCN3, a translational activator of GCN4: evidence for posttranslational control of GCN3 regulatory function
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Protein serine/threonine kinases
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Mutations in the structural genes for eukaryotic initiation factors 2 alpha and 2 beta of Saccharomyces cerevisiae disrupt translational control of GCN4 mRNA
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Juxtaposition of domains homologous to protein kinases and histidyl-tRNA synthetases in GCN2 protein suggests a mechanism for coupling GCN4 expression to amino acid availability
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Repeated DNA sequences upstream from HIS1 also occur at several other co-regulated genes in Saccharomyces cerevisiae
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Control of the yeast cell cycle is associated with assembly/disassembly of the Cdc28 protein kinase complex
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Phosphotransferase sequence homology
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https://pubmed.ncbi.nlm.nih.gov/2188100
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12 December 2020
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The fission yeast cdc2/cdc13/suc1 protein kinase: regulation of catalytic activity and nuclear localization
1 reference
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https://pubmed.ncbi.nlm.nih.gov/2188100
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based on heuristic
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Integration of amino acid biosynthesis into the cell cycle of Saccharomyces cerevisiae
1 reference
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PubMed
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https://pubmed.ncbi.nlm.nih.gov/2188100
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12 December 2020
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Mechanism of interferon action. The interferon-induced phosphoprotein P1 possesses a double-stranded RNA-dependent ATP-binding site
1 reference
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PubMed
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https://pubmed.ncbi.nlm.nih.gov/2188100
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based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1128/MCB.10.6.2820
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1112387
OpenCitations bibliographic resource ID
1112387
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1112387
PMCID
360643
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1112387
PubMed ID
2188100
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1112387
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