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rdf:type |
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lifeskim:mentions |
umls-concept:C0033684,
umls-concept:C0037083,
umls-concept:C0430054,
umls-concept:C1155291,
umls-concept:C1332120,
umls-concept:C1336660,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1705053,
umls-concept:C1710082
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pubmed:issue |
6035
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pubmed:dateCreated |
2011-6-10
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pubmed:abstractText |
The DNA damage response (DDR) is brought about by a protein kinase cascade that orchestrates DNA repair through transcriptional and posttranslational mechanisms. Cell cycle arrest is a hallmark of the DDR. We screened for cells that lacked damage-induced cell cycle arrest and uncovered a critical role for Fanconi anemia and homologous recombination proteins in ATR (ataxia telangiectasia and Rad3-related) signaling. Three DDR candidates, the RNA processing protein INTS7, the circadian transcription factor CLOCK, and a previously uncharacterized protein RHINO, were recruited to sites of DNA damage. RHINO independently bound the Rad9-Rad1-Hus1 complex (9-1-1) and the ATR activator TopBP1. RHINO was recruited to sites of DNA damage by the 9-1-1 complex to promote Chk1 activation. We suggest that RHINO functions together with the 9-1-1 complex and TopBP1 to fully activate ATR.
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pubmed:grant |
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/ATR protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chemokines,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Exonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/HUS1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Rad1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/TOPBP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/VCC-1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/rad9 protein
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
10
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pubmed:volume |
332
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1313-7
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pubmed:meshHeading |
pubmed-meshheading:21659603-Carrier Proteins,
pubmed-meshheading:21659603-Cell Cycle,
pubmed-meshheading:21659603-Cell Cycle Proteins,
pubmed-meshheading:21659603-Cell Line, Tumor,
pubmed-meshheading:21659603-Chemokines,
pubmed-meshheading:21659603-DNA Damage,
pubmed-meshheading:21659603-DNA Repair,
pubmed-meshheading:21659603-DNA-Binding Proteins,
pubmed-meshheading:21659603-Exonucleases,
pubmed-meshheading:21659603-Humans,
pubmed-meshheading:21659603-Multiprotein Complexes,
pubmed-meshheading:21659603-Nuclear Proteins,
pubmed-meshheading:21659603-Protein-Serine-Threonine Kinases,
pubmed-meshheading:21659603-Signal Transduction
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pubmed:year |
2011
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pubmed:articleTitle |
A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1 interacting protein required for ATR signaling.
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pubmed:affiliation |
Department of Genetics, Harvard University Medical School, Howard Hughes Medical Institute, Division of Genetics, Brigham and Women's Hospital, Boston, MA 02115, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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