ArticleMolecular and cellular biology2004
Quaternary structure of ATR and effects of ATRIP and replication protein A on its DNA binding and kinase activities.
Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
41 citing papers in PubMed, 100 citations in OpenAlex.
- Review
- Targeting the DNA damage response in cancer.MedComm · 2024Review
- Article
- Nuclear pCHK1 as a potential biomarker of increased sensitivity to ATR inhibition.The Journal of pathology · 2023Article
- SATMF Suppresses the Premature Senescence Phenotype of the ATM Loss-of-Function Mutant and Improves Its Fertility inInternational journal of molecular sciences · 2020Article
- Ddc2ATRIP promotes Mec1ATR activation at RPA-ssDNA tracts.PLoS genetics · 2019Article
- Sirtuin 1-mediated deacetylation of XPA DNA repair protein enhances its interaction with ATR protein and promotes cAMP-induced DNA repair of UV damage.The Journal of biological chemistry · 2018Article
- Insights into Rad3 kinase recruitment from the crystal structure of the DNA damage checkpoint protein Rad26.The Journal of biological chemistry · 2017Article
- Bringing It All Together: Coupling Excision Repair to the DNA Damage Checkpoint.Photochemistry and photobiology · 2017Review
- DNA mismatch repair and the DNA damage response.DNA repair · 2016Review
- And-1 coordinates with Claspin for efficient Chk1 activation in response to replication stress.The EMBO journal · 2015Article
- RPA70 depletion induces hSSB1/2-INTS3 complex to initiate ATR signaling.Nucleic acids research · 2015Article
- DNA damage: a sensible mediator of the differentiation decision in hematopoietic stem cells and in leukemia.International journal of molecular sciences · 2015Review
- Coupling of human DNA excision repair and the DNA damage checkpoint in a defined in vitro system.The Journal of biological chemistry · 2014Article
- Distinct roles for DNA-PK, ATM and ATR in RPA phosphorylation and checkpoint activation in response to replication stress.Nucleic acids research · 2012Article
- In vitro analysis of the role of replication protein A (RPA) and RPA phosphorylation in ATR-mediated checkpoint signaling.The Journal of biological chemistry · 2012Article
- The recombinases DMC1 and RAD51 are functionally and spatially separated during meiosis in Arabidopsis.The Plant cell · 2012Article
- ATR signalling: more than meeting at the fork.The Biochemical journal · 2011Review
- The intra-S phase checkpoint protein Tof1 collaborates with the helicase Rrm3 and the F-box protein Dia2 to maintain genome stability in Saccharomyces cerevisiae.The Journal of biological chemistry · 2011Article
- Multiple ATR-Chk1 pathway proteins preferentially associate with checkpoint-inducing DNA substrates.PloS one · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.