Evidence map›Paper›PMID 21070772›Full record

ArticleFEBS letters2010

Coilin interacts with Ku proteins and inhibits in vitro non-homologous DNA end joining.

Venkatramreddy Velma, Zunamys I Carrero, Angela M Cosman, Michael D Hebert

Open access · bronzeAbstract read
In one paragraph

Article in FEBS letters, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

23 citing papers in PubMed, 28 citations in OpenAlex.

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  10. Review
  11. Coilin: The first 25 years.RNA biology · 2015
    Review
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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 at 2 institutions in 1 country.

Venkatramreddy VelmaDepartment of Biochemistry, The University of Mississippi Medical Center, Jackson, MS 39216-4505, USA.
Zunamys I Carrero
Angela M Cosman
Michael D Hebert
Jackson Memorial Hospital · USUniversity of Mississippi Medical Center · US

Funding

Nuclear bodies and ribonucleoprotein biogenesisR01GM081448 · NIGMS · UNIVERSITY OF MISSISSIPPI MED CTR · PI HEBERT, MICHAEL D · 2008 to 2012
$1.5M
NIGMS NIH HHS R01 GM081448NIGMS NIH HHS R01GM081448
6 · The paper itself

Abstract

Coilin is a nuclear protein that plays a role in Cajal body formation. The function of nucleoplasmic coilin is unknown. Here we report that coilin interacts with Ku70 and Ku80, which are major players in the DNA repair process. Ku proteins compete with SMN and SmB' proteins for coilin interaction sites. The binding domain on coilin for Ku proteins cannot be localized to one discrete region, and only full-length coilin is capable of inhibiting in vitro non-homologous DNA end joining (NHEJ). Since Ku proteins do not accumulate in CBs, these findings suggest that nucleoplasmic coilin participates in the regulation of DNA repair.

Indexed as

Binding, CompetitiveDNA HelicasesDNA RepairHeLa CellsHumansKu AutoantigenNuclear ProteinsRecombination, GeneticsnRNP Core ProteinsSurvival of Motor Neuron 1 ProteinDNA HelicasesKu AutoantigenNuclear Proteinsp80-coilinsnRNP Core ProteinsSNRPB protein, humanSurvival of Motor Neuron 1 ProteinXRCC5 protein, human

Identifiers

PMID21070772
PMCPMC3000556
OpenAlexW1977146024

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.