Evidence map›Paper›PMID 12011431›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

Preferential binding of ATR protein to UV-damaged DNA.

Keziban Unsal-Kaçmaz, Alexander M Makhov, Jack D Griffith, Aziz Sancar

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
6.7field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

69 citing papers in PubMed, 174 citations in OpenAlex.

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  14. PostExcision Events in Human Nucleotide Excision Repair.Photochemistry and photobiology · 2017
    Review
  15. Review
  16. Review
  17. Review
  18. Article
  19. Interplay between Mdm2 and HIPK2 in the DNA damage response.Journal of the Royal Society, Interface · 2014
    Article
  20. Article

9 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Keziban Unsal-KaçmazDepartment of Biochemistry and Biophysics and Lineberger Comprehensive Cancer Center, University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.
Alexander M Makhov
Jack D Griffith
Aziz Sancar
University of North Carolina at Chapel Hill · USBipar · FR

Funding

Virology Research Program (Program 4)P30CA016086 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI Deborah F. Tate · 1985 to 2026
$201.5M
STRUCTURE AND FUNCTION OF UVRABC EXCISION NUCLEASER01GM032833 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SANCAR, AZIZ · 1985 to 2015
$8.9M
HOMOLOOUS RECOMBINATION: ITS MOLECULAR CYTOLOGYR01GM031819 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI GRIFFITH, JACK D · 1985 to 2017
$5.2M
NCI NIH HHS CA16086NCI NIH HHS P30 CA016086NIGMS NIH HHS GM31819NIGMS NIH HHS GM32833NIGMS NIH HHS R01 GM031819NIGMS NIH HHS R01 GM032833
6 · The paper itself

Abstract

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.

Indexed as

DNA DamageAtaxia Telangiectasia Mutated ProteinsCell Cycle ProteinsCell Line, TransformedDNADNA-Binding ProteinsHumansMicroscopy, ElectronOligodeoxyribonucleotidesPeptide FragmentsPhosphatidylinositol 3-KinasesPhosphorylationProtein Serine-Threonine KinasesTumor Suppressor Protein p53Ultraviolet RaysAtaxia Telangiectasia Mutated ProteinsATR protein, humanCell Cycle ProteinsDNADNA-Binding ProteinsOligodeoxyribonucleotidesPeptide FragmentsPhosphatidylinositol 3-KinasesProtein Serine-Threonine KinasesTumor Suppressor Protein p53

Identifiers

PMID12011431
PMCPMC124461
OpenAlexW1992876574

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.