Matches in SemOpenAlex for { <https://semopenalex.org/work/W1567209145> ?p ?o ?g. }
Showing items 1 to 89 of
89
with 100 items per page.
- W1567209145 endingPage "12951" @default.
- W1567209145 startingPage "12946" @default.
- W1567209145 abstract "Protein synthesis is dramatically reduced upon exposure of cells to elevated temperature. Concordant with this inhibition, multiple phosphorylation and dephosphorylation reactions occur on specific eukaryotic initiation factors that are required for protein synthesis. Most notably, phosphorylation of the alpha-subunit of eukaryotic initiation factor-2 (eIF-2 alpha) on serine residue 51 occurs. To identify the importance of phosphorylation in control of protein synthesis, we have evaluated the effects of expression of a mutant eIF-2 alpha which is resistant to phosphorylation. Expression of a serine to alanine mutant at residue 51 of eIF-2 alpha partially protected cells from the inhibition of protein synthesis in response to heat treatment. The overexpressed serine to alanine 51 mutant subunit was incorporated into the eIF-2 heterotrimer and was resistant to phosphorylation. These results are consistent with the hypothesis that heat shock inhibition of translation is mediated in part through phosphorylation of eIF-2 alpha. Expression of the wild type or mutant eIF-2 alpha did not affect cell survival or induction of hsp70 mRNA upon heat shock, indicating that although eIF-2 alpha is a heat shock-induced protein, its increased synthesis during heat shock does not alter the heat-shock response." @default.
- W1567209145 created "2016-06-24" @default.
- W1567209145 creator A5015378855 @default.
- W1567209145 creator A5018323994 @default.
- W1567209145 creator A5021373891 @default.
- W1567209145 creator A5036001933 @default.
- W1567209145 creator A5047698058 @default.
- W1567209145 creator A5088836753 @default.
- W1567209145 date "1993-06-01" @default.
- W1567209145 modified "2023-09-27" @default.
- W1567209145 title "Expression of a phosphorylation-resistant eukaryotic initiation factor 2 alpha-subunit mitigates heat shock inhibition of protein synthesis" @default.
- W1567209145 doi "https://doi.org/10.1016/s0021-9258(18)31477-7" @default.
- W1567209145 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8509427" @default.
- W1567209145 hasPublicationYear "1993" @default.
- W1567209145 type Work @default.
- W1567209145 sameAs 1567209145 @default.
- W1567209145 citedByCount "67" @default.
- W1567209145 countsByYear W15672091452012 @default.
- W1567209145 countsByYear W15672091452015 @default.
- W1567209145 countsByYear W15672091452017 @default.
- W1567209145 countsByYear W15672091452018 @default.
- W1567209145 countsByYear W15672091452019 @default.
- W1567209145 countsByYear W15672091452021 @default.
- W1567209145 countsByYear W15672091452022 @default.
- W1567209145 crossrefType "journal-article" @default.
- W1567209145 hasAuthorship W1567209145A5015378855 @default.
- W1567209145 hasAuthorship W1567209145A5018323994 @default.
- W1567209145 hasAuthorship W1567209145A5021373891 @default.
- W1567209145 hasAuthorship W1567209145A5036001933 @default.
- W1567209145 hasAuthorship W1567209145A5047698058 @default.
- W1567209145 hasAuthorship W1567209145A5088836753 @default.
- W1567209145 hasBestOaLocation W15672091451 @default.
- W1567209145 hasConcept C104292427 @default.
- W1567209145 hasConcept C104317684 @default.
- W1567209145 hasConcept C105580179 @default.
- W1567209145 hasConcept C11960822 @default.
- W1567209145 hasConcept C149364088 @default.
- W1567209145 hasConcept C159110408 @default.
- W1567209145 hasConcept C185592680 @default.
- W1567209145 hasConcept C205260736 @default.
- W1567209145 hasConcept C2775944032 @default.
- W1567209145 hasConcept C3675279 @default.
- W1567209145 hasConcept C49453240 @default.
- W1567209145 hasConcept C55493867 @default.
- W1567209145 hasConcept C64943373 @default.
- W1567209145 hasConcept C71924100 @default.
- W1567209145 hasConcept C83730767 @default.
- W1567209145 hasConcept C86803240 @default.
- W1567209145 hasConcept C93734116 @default.
- W1567209145 hasConcept C95444343 @default.
- W1567209145 hasConceptScore W1567209145C104292427 @default.
- W1567209145 hasConceptScore W1567209145C104317684 @default.
- W1567209145 hasConceptScore W1567209145C105580179 @default.
- W1567209145 hasConceptScore W1567209145C11960822 @default.
- W1567209145 hasConceptScore W1567209145C149364088 @default.
- W1567209145 hasConceptScore W1567209145C159110408 @default.
- W1567209145 hasConceptScore W1567209145C185592680 @default.
- W1567209145 hasConceptScore W1567209145C205260736 @default.
- W1567209145 hasConceptScore W1567209145C2775944032 @default.
- W1567209145 hasConceptScore W1567209145C3675279 @default.
- W1567209145 hasConceptScore W1567209145C49453240 @default.
- W1567209145 hasConceptScore W1567209145C55493867 @default.
- W1567209145 hasConceptScore W1567209145C64943373 @default.
- W1567209145 hasConceptScore W1567209145C71924100 @default.
- W1567209145 hasConceptScore W1567209145C83730767 @default.
- W1567209145 hasConceptScore W1567209145C86803240 @default.
- W1567209145 hasConceptScore W1567209145C93734116 @default.
- W1567209145 hasConceptScore W1567209145C95444343 @default.
- W1567209145 hasIssue "17" @default.
- W1567209145 hasLocation W15672091451 @default.
- W1567209145 hasOpenAccess W1567209145 @default.
- W1567209145 hasPrimaryLocation W15672091451 @default.
- W1567209145 hasRelatedWork W1480211327 @default.
- W1567209145 hasRelatedWork W1483055899 @default.
- W1567209145 hasRelatedWork W1495434193 @default.
- W1567209145 hasRelatedWork W1567209145 @default.
- W1567209145 hasRelatedWork W1943315623 @default.
- W1567209145 hasRelatedWork W2024892298 @default.
- W1567209145 hasRelatedWork W2066589921 @default.
- W1567209145 hasRelatedWork W2108804471 @default.
- W1567209145 hasRelatedWork W2407351991 @default.
- W1567209145 hasRelatedWork W4283726950 @default.
- W1567209145 hasVolume "268" @default.
- W1567209145 isParatext "false" @default.
- W1567209145 isRetracted "false" @default.
- W1567209145 magId "1567209145" @default.
- W1567209145 workType "article" @default.