Matches in SemOpenAlex for { <https://semopenalex.org/work/W3010696483> ?p ?o ?g. }
Showing items 1 to 82 of
82
with 100 items per page.
- W3010696483 endingPage "1184" @default.
- W3010696483 startingPage "1184" @default.
- W3010696483 abstract "5043 Recent evidence from a wide variety of biological systems has indicated an important regulatory role for post-translation histone modifications in cellular processes such as regulation of gene expression, DNA damage response and recombination. Phosphorylation of histone H2AX at serine 139 is a critical event in the cellular response to DNA damage, yet little is known about the functional implications of this modification. To investigate the role of histone H2AX phosphorylation we ectopically expressed epitope-tagged H2AX or mutants at the phosphorylation site. GFP-tagged wild type H2AX, H2AX Ser139Ala or H2AX Ser139Glu proteins are efficiently expressed localizing exclusively to the interphase nucleus and to condensed chromosomes during mitosis. Moreover, biochemical fractionation indicates that epitope-tagged H2AX proteins are incorporated into nucleosomes. Expression of H2AX Ser139Ala, which disrupts the phosphorylation site, partially abrogated G2/M arrest following ionizing radiation. Conversely, expression of H2AX Ser139Glu, designed as a phosphorylation mimic, induced G2/M arrest in the absence of DNA damage. G2/M arrest induced by H2AX Ser139Glu was independent of the formation of 53BP1-containing foci and ATM activation. In addition, stable cell lines expressing H2AX Ser139Glu or H2AX Ser139Ala had a lower mitotic index than wild-type H2AX. Further analyses revealed that expression of either mutant induced apoptosis and induced higher caspase-3/7 activity compared to expression of wild-type H2AX. Taken together these results demonstrate a role for H2AX Serine 139 phosphorylation in cell cycle regulation and apoptosis." @default.
- W3010696483 created "2020-03-23" @default.
- W3010696483 creator A5001929189 @default.
- W3010696483 creator A5019761569 @default.
- W3010696483 creator A5032499070 @default.
- W3010696483 creator A5047919208 @default.
- W3010696483 creator A5056030818 @default.
- W3010696483 creator A5067789983 @default.
- W3010696483 date "2006-04-15" @default.
- W3010696483 modified "2023-10-17" @default.
- W3010696483 title "A role for histone H2AX in cell cycle control and apoptosis." @default.
- W3010696483 hasPublicationYear "2006" @default.
- W3010696483 type Work @default.
- W3010696483 sameAs 3010696483 @default.
- W3010696483 citedByCount "0" @default.
- W3010696483 crossrefType "journal-article" @default.
- W3010696483 hasAuthorship W3010696483A5001929189 @default.
- W3010696483 hasAuthorship W3010696483A5019761569 @default.
- W3010696483 hasAuthorship W3010696483A5032499070 @default.
- W3010696483 hasAuthorship W3010696483A5047919208 @default.
- W3010696483 hasAuthorship W3010696483A5056030818 @default.
- W3010696483 hasAuthorship W3010696483A5067789983 @default.
- W3010696483 hasConcept C104317684 @default.
- W3010696483 hasConcept C11960822 @default.
- W3010696483 hasConcept C134935766 @default.
- W3010696483 hasConcept C143065580 @default.
- W3010696483 hasConcept C143425029 @default.
- W3010696483 hasConcept C153911025 @default.
- W3010696483 hasConcept C190283241 @default.
- W3010696483 hasConcept C29537977 @default.
- W3010696483 hasConcept C54355233 @default.
- W3010696483 hasConcept C552990157 @default.
- W3010696483 hasConcept C56428682 @default.
- W3010696483 hasConcept C64927066 @default.
- W3010696483 hasConcept C86803240 @default.
- W3010696483 hasConcept C93304396 @default.
- W3010696483 hasConcept C95444343 @default.
- W3010696483 hasConceptScore W3010696483C104317684 @default.
- W3010696483 hasConceptScore W3010696483C11960822 @default.
- W3010696483 hasConceptScore W3010696483C134935766 @default.
- W3010696483 hasConceptScore W3010696483C143065580 @default.
- W3010696483 hasConceptScore W3010696483C143425029 @default.
- W3010696483 hasConceptScore W3010696483C153911025 @default.
- W3010696483 hasConceptScore W3010696483C190283241 @default.
- W3010696483 hasConceptScore W3010696483C29537977 @default.
- W3010696483 hasConceptScore W3010696483C54355233 @default.
- W3010696483 hasConceptScore W3010696483C552990157 @default.
- W3010696483 hasConceptScore W3010696483C56428682 @default.
- W3010696483 hasConceptScore W3010696483C64927066 @default.
- W3010696483 hasConceptScore W3010696483C86803240 @default.
- W3010696483 hasConceptScore W3010696483C93304396 @default.
- W3010696483 hasConceptScore W3010696483C95444343 @default.
- W3010696483 hasLocation W30106964831 @default.
- W3010696483 hasOpenAccess W3010696483 @default.
- W3010696483 hasPrimaryLocation W30106964831 @default.
- W3010696483 hasRelatedWork W1601491058 @default.
- W3010696483 hasRelatedWork W1964629190 @default.
- W3010696483 hasRelatedWork W2022984472 @default.
- W3010696483 hasRelatedWork W2032888205 @default.
- W3010696483 hasRelatedWork W2059548561 @default.
- W3010696483 hasRelatedWork W2070276655 @default.
- W3010696483 hasRelatedWork W2072857344 @default.
- W3010696483 hasRelatedWork W2079341201 @default.
- W3010696483 hasRelatedWork W2081947662 @default.
- W3010696483 hasRelatedWork W2088032208 @default.
- W3010696483 hasRelatedWork W2101082817 @default.
- W3010696483 hasRelatedWork W2145001669 @default.
- W3010696483 hasRelatedWork W2290155583 @default.
- W3010696483 hasRelatedWork W2563078585 @default.
- W3010696483 hasRelatedWork W2613625227 @default.
- W3010696483 hasRelatedWork W2726324967 @default.
- W3010696483 hasRelatedWork W2736914828 @default.
- W3010696483 hasRelatedWork W2766754455 @default.
- W3010696483 hasRelatedWork W2886175210 @default.
- W3010696483 hasRelatedWork W2905034674 @default.
- W3010696483 hasVolume "66" @default.
- W3010696483 isParatext "false" @default.
- W3010696483 isRetracted "false" @default.
- W3010696483 magId "3010696483" @default.
- W3010696483 workType "article" @default.