Evidence map›Paper›PMID 22948311›Full record

ArticleThe Journal of biological chemistry2012

In vitro analysis of the role of replication protein A (RPA) and RPA phosphorylation in ATR-mediated checkpoint signaling.

Laura A Lindsey-Boltz, Joyce T Reardon, Marc S Wold, Aziz Sancar

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
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

21 citing papers in PubMed.

  1. Article
  2. Article
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  4. Article
  5. Article
  6. Review
  7. DNA repair and genomic stability in lungs affected by acute injury.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2019
    Review
  8. Article
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  11. Review
  12. Article
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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.

Laura A Lindsey-BoltzDepartment of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599-7260, USA.
Joyce T Reardon
Marc S Wold
Aziz Sancar

Funding

UNC-CH CENTER FOR ENVIRONMENTAL HEALTH &SUSCEPTIBILITYP30ES010126 · NIEHS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI Melissa A. Troester · 2001 to 2026
$36.3M
STRUCTURE AND FUNCTION OF UVRABC EXCISION NUCLEASER01GM032833 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SANCAR, AZIZ · 1985 to 2015
$8.9M
FUNCTIONAL ROLES OF CELLULAR PROTEINS IN DNA REPLICATIONR01GM044721 · NIGMS · UNIVERSITY OF IOWA · PI WOLD, MARC S · 1990 to 2009
$2.2M
NIEHS NIH HHS P30 ES010126NIGMS NIH HHS GM32833NIGMS NIH HHS GM44721NIGMS NIH HHS R01 GM032833NIGMS NIH HHS R01 GM044721
6 · The paper itself

Abstract

Replication protein A (RPA) plays essential roles in DNA metabolism, including replication, checkpoint, and repair. Recently, we described an in vitro system in which the phosphorylation of human Chk1 kinase by ATR (ataxia telangiectasia mutated and Rad3-related) is dependent on RPA bound to single-stranded DNA. Here, we report that phosphorylation of other ATR targets, p53 and Rad17, has the same requirements and that RPA is also phosphorylated in this system. At high p53 or Rad17 concentrations, RPA phosphorylation is inhibited and, in this system, RPA with phosphomimetic mutations cannot support ATR kinase function, whereas a non-phosphorylatable RPA mutant exhibits full activity. Phosphorylation of these ATR substrates depends on the recruitment of ATR and the substrates by RPA to the RPA-ssDNA complex. Finally, mutant RPAs lacking checkpoint function exhibit essentially normal activity in nucleotide excision repair, revealing RPA separation of function for checkpoint and excision repair.

Indexed as

Cell Cycle CheckpointsSignal TransductionAtaxia Telangiectasia Mutated ProteinsCell Cycle ProteinsCell-Free SystemCell LineCheckpoint Kinase 1DNA RepairDNA, Single-StrandedHumansMutationPhosphorylationProtein KinasesProtein Serine-Threonine KinasesReplication Protein ATumor Suppressor Protein p53Ataxia Telangiectasia Mutated ProteinsATR protein, humanCell Cycle ProteinsCheckpoint Kinase 1CHEK1 protein, humanDNA, Single-StrandedProtein KinasesProtein Serine-Threonine KinasesRad17 protein, humanReplication Protein ATP53 protein, humanTumor Suppressor Protein p53

Identifiers

PMID22948311
PMCPMC3476280

What OpenQuestion holds

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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.