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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2007-10-24
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pubmed:abstractText |
The histone variant histone H2A.X comprises up to 25% of the H2A complement in mammalian cells. It is rapidly phosphorylated following exposure of cells to double-strand break (DSB) inducing agents such as ionising radiation. Within minutes of DSB generation, H2AX molecules are phosphorylated in large chromatin domains flanking DNA double-strand breaks (DSBs); these domains can be observed by immunofluorescence microscopy and are termed gammaH2AX foci. H2AX phosphorylation is believed to have a role mounting an efficient cellular response to DNA damage. Theoretical considerations suggest an essentially random chromosomal distribution of X-ray induced DSBs, and experimental evidence does not consistently indicate otherwise. However, we observed an apparently uneven distribution of gammaH2AX foci following X-irradiation with regions of the nucleus devoid of foci.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1932-6203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
e1057
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pubmed:meshHeading |
pubmed-meshheading:17957241-Cell Line, Tumor,
pubmed-meshheading:17957241-Cell Nucleolus,
pubmed-meshheading:17957241-Cell Nucleus,
pubmed-meshheading:17957241-Chromatin,
pubmed-meshheading:17957241-DNA Damage,
pubmed-meshheading:17957241-DNA Replication,
pubmed-meshheading:17957241-Euchromatin,
pubmed-meshheading:17957241-Heterochromatin,
pubmed-meshheading:17957241-Histones,
pubmed-meshheading:17957241-Humans,
pubmed-meshheading:17957241-Microscopy, Fluorescence,
pubmed-meshheading:17957241-Models, Biological,
pubmed-meshheading:17957241-Phosphorylation,
pubmed-meshheading:17957241-Protein Structure, Tertiary,
pubmed-meshheading:17957241-Radiation, Ionizing
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pubmed:year |
2007
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pubmed:articleTitle |
gammaH2AX foci form preferentially in euchromatin after ionising-radiation.
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pubmed:affiliation |
Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, United Kingdom. i.g.cowell@ncl.ac.uk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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