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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 |
2002-5-15
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pubmed:abstractText |
The ATR protein is a member of the phosphoinositide 3-kinase-related kinase family and plays an important role in UV-induced DNA damage checkpoint response. Its role as a signal transducer in cell cycle checkpoint is well established, but it is currently unclear whether ATR functions as a damage sensor as well. Here we have purified the ATR protein and investigated its interaction with DNA by using biochemical analysis and electron microscopy. We find that ATR is a DNA-binding protein with higher affinity to UV-damaged than undamaged DNA. In addition, damaged DNA stimulates the kinase activity of ATR to a significantly higher level than undamaged DNA. Our data suggest that ATR may function as an initial sensor in the DNA damage checkpoint response.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-10102265,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-10359610,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-10373492,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-10410794,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-10435622,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-10559981,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-10588638,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-10597277,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-10648611,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-10660302,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-10679395,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-10777662,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-10871397,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-11069891,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-11100718,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-11124254,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-11137007,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-11163154,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-11248557,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-11340080,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-11544175,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-11572977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-11679674,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-11691833,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-11721054,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-11799063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-1314396,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-1779835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-4530290,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-7533216,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-78683,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-7991603,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-8610130,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-8626644,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-8811174,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-9427750,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-9710632,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-9872989,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12011431-9925639
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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:month |
May
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
99
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6673-8
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:12011431-Cell Cycle Proteins,
pubmed-meshheading:12011431-Cell Line, Transformed,
pubmed-meshheading:12011431-DNA,
pubmed-meshheading:12011431-DNA Damage,
pubmed-meshheading:12011431-DNA-Binding Proteins,
pubmed-meshheading:12011431-Humans,
pubmed-meshheading:12011431-Microscopy, Electron,
pubmed-meshheading:12011431-Oligodeoxyribonucleotides,
pubmed-meshheading:12011431-Peptide Fragments,
pubmed-meshheading:12011431-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:12011431-Phosphorylation,
pubmed-meshheading:12011431-Protein-Serine-Threonine Kinases,
pubmed-meshheading:12011431-Tumor Suppressor Protein p53,
pubmed-meshheading:12011431-Ultraviolet Rays
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pubmed:year |
2002
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pubmed:articleTitle |
Preferential binding of ATR protein to UV-damaged DNA.
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pubmed:affiliation |
Department of Biochemistry and Biophysics and Lineberger Comprehensive Cancer Center, University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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