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Regulation of protein synthesis by heme-regulated eIF-2 alpha kinase
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scholarly article
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title
Regulation of protein synthesis by heme-regulated eIF-2 alpha kinase
(English)
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author name string
J J Chen
series ordinal
1
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I M London
series ordinal
2
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language of work or name
English
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publication date
March 1995
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published in
Trends in Biochemical Sciences
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volume
20
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issue
3
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page(s)
105-8
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cites work
Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
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Platelet-derived growth factor (PDGF)-induced disulfide-linked dimerization of PDGF receptor in living cells
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7 January 2021
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Regulation by heme of mitochondrial protein transport through a conserved amino acid motif
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7 January 2021
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The 90-kilodalton peptide of the heme-regulated eIF-2 alpha kinase has sequence similarity with the 90-kilodalton heat shock protein
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The phosphorylation state of the reticulocyte 90-kDa heat shock protein affects its ability to increase phosphorylation of peptide initiation factor 2 alpha subunit by the heme-sensitive kinase.
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Denatured proteins inhibit translation in hemin-supplemented rabbit reticulocyte lysate by inducing the activation of the heme-regulated eIF-2 alpha kinase
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7 January 2021
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The Roles of Sugar Phosphates and Thiol-Reducing Systems in the Control of Reticulocyte Protein Synthesis
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The Preparation and Properties of Gel-Filtered Rabbit-Reticulocyte Lysate Protein-Synthesis Systems
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Purification and characterisation of an initiation-factor-2 kinase from uninduced mouse erythroleukaemia cells
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7 January 2021
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Tissue distribution and immunoreactivity of heme-regulated eIF-2 alpha kinase determined by monoclonal antibodies
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reference URL
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7 January 2021
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Erythroid expression of the heme-regulated eIF-2 alpha kinase
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7 January 2021
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Activation in vitro of NF-kappa B by phosphorylation of its inhibitor I kappa B
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7 January 2021
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Identifiers
DOI
10.1016/S0968-0004(00)88975-6
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3490153
OpenCitations bibliographic resource ID
3490153
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3490153
PubMed ID
7709427
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3490153
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