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• W2162249357 startingPage "1292" @default.
• W2162249357 abstract "ATR is an essential protein that functions as a damage sensor and a proximal kinase in the DNA damage checkpoint response in mammalian cells. It is a member of the phosphoinositide 3-kinase-like kinase (PIKK) family, which includes ATM, ATR, and DNA-dependent protein kinase. Recently, it was found that ATM is an oligomeric protein that is converted to an active monomeric form by phosphorylation in trans upon DNA damage, and this raised the possibility that other members of the PIKK family may be regulated in a similar manner. Here we show that ATR is a monomeric protein associated with a smaller protein called ATRIP with moderate affinity. The ATR protein by itself or in the form of the ATR-ATRIP heterodimer binds to naked or replication protein A (RPA)-covered DNAs with comparable affinities. However, the phosphorylation of RPA by ATR is dependent on single-stranded DNA and is stimulated by ATRIP. These findings suggest that the regulation and mechanism of action of ATR are fundamentally different from those of the other PIKK proteins." @default.
• W2162249357 created "2016-06-24" @default.
• W2162249357 creator A5007456999 @default.
• W2162249357 creator A5016678671 @default.
• W2162249357 date "2004-02-01" @default.
• W2162249357 modified "2023-10-16" @default.
• W2162249357 title "Quaternary Structure of ATR and Effects of ATRIP and Replication Protein A on Its DNA Binding and Kinase Activities" @default.
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• W2162249357 doi "https://doi.org/10.1128/mcb.24.3.1292-1300.2003" @default.
• W2162249357 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/321456" @default.
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• W2162249357 hasPublicationYear "2004" @default.
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