Evidence map›Paper›PMID 29477978›Full record

ArticleDNA repair2018

XRCC1 phosphorylation affects aprataxin recruitment and DNA deadenylation activity.

Julie K Horton, Donna F Stefanick, Melike Çağlayan, Ming-Lang Zhao, Agnes K Janoshazi, Rajendra Prasad, Natalie R Gassman, Samuel H Wilson

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in DNA repair, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

7 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
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

8 authors at 3 institutions in 1 country.

Julie K HortonGenome Integrity and Structural Biology Laboratory, NIEHS, National Institutes of Health, Research Triangle Park, NC 27709, USA.
Donna F StefanickGenome Integrity and Structural Biology Laboratory, NIEHS, National Institutes of Health, Research Triangle Park, NC 27709, USA.
Melike ÇağlayanGenome Integrity and Structural Biology Laboratory, NIEHS, National Institutes of Health, Research Triangle Park, NC 27709, USA.
Ming-Lang ZhaoGenome Integrity and Structural Biology Laboratory, NIEHS, National Institutes of Health, Research Triangle Park, NC 27709, USA.
Agnes K JanoshaziFluorescence Microscopy and Imaging Center, Signal Transduction Laboratory, NIEHS, National Institutes of Health, Research Triangle Park, NC 27709, USA.
Rajendra PrasadGenome Integrity and Structural Biology Laboratory, NIEHS, National Institutes of Health, Research Triangle Park, NC 27709, USA.
Natalie R GassmanDepartment of Oncologic Sciences, University of South Alabama Mitchell Cancer Institute, Mobile, AL 36604, USA.
Samuel H WilsonGenome Integrity and Structural Biology Laboratory, NIEHS, National Institutes of Health, Research Triangle Park, NC 27709, USA. Electronic address: wilson5@niehs.nih.gov.
National Institutes of Health · USNational Institute of Environmental Health Sciences · USUniversity of South Alabama · US

Funding

BIOLOGY OF MAMMALIAN BASE EXCISION REPAIRZ01ES050159 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI WILSON, SAMUEL H · 1997 to 2008
$4.5M
Nucleic Acid Enzymes--Pol Beta And Base Repair EnzymesZ01ES050158 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI WILSON, SAMUEL H · 1997 to 2008
$2.8M
Intramural NIH HHS Z01 ES050158Intramural NIH HHS Z01 ES050159NIEHS NIH HHS Z01 ES050158NIEHS NIH HHS Z01 ES050159
6 · The paper itself

Abstract

Aprataxin (APTX) is a DNA-adenylate hydrolase that removes 5'-AMP blocking groups from abortive ligation repair intermediates. XRCC1, a multi-domain protein without catalytic activity, interacts with a number of known repair proteins including APTX, modulating and coordinating the various steps of DNA repair. CK2-phosphorylation of XRCC1 is thought to be crucial for its interaction with the FHA domain of APTX. In light of conflicting reports, the importance of XRCC1 phosphorylation and APTX function is not clear. In this study, a phosphorylation mutant of XRCC1 designed to eliminate APTX binding was stably expressed in Xrcc1

Indexed as

DNA DamageDNA RepairProtein Processing, Post-TranslationalAnimalsCell LineDNADNA-Binding ProteinsHumansMiceNuclear ProteinsPhosphorylationX-ray Repair Cross Complementing Protein 1APTX protein, humanAptx protein, mouseDNADNA-Binding ProteinsNuclear ProteinsX-ray Repair Cross Complementing Protein 1XRCC1 protein, humanXrcc1 protein, mouseAPTXDNA deadenylationXRCC1

Identifiers

PMID29477978
PMCPMC9295255
OpenAlexW2789465958

What OpenQuestion holds

Textmetadata
LicenceTDM
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.