Evidence map›Paper›PMID 21969602›Full record

ArticleMolecular and cellular biology2011

The NF90/NF45 complex participates in DNA break repair via nonhomologous end joining.

Raghavendra A Shamanna, Mainul Hoque, Anita Lewis-Antes, Edouard I Azzam, David Lagunoff, Tsafi Pe'ery, Michael B Mathews

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

44 citing papers in PubMed, 71 citations in OpenAlex.

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  16. RNA stability protein ILF3 mediates cytokine-induced angiogenesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
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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

7 authors at 2 institutions in 1 country.

Raghavendra A ShamannaDepartments of Biochemistry and Molecular Biology, UMDNJ-New Jersey Medical School, and Graduate School of Biomedical Sciences, UMDNJ, Newark, New Jersey 07101-1709, USA.
Mainul Hoque
Anita Lewis-Antes
Edouard I Azzam
David Lagunoff
Tsafi Pe'ery
Michael B Mathews
Rutgers, The State University of New Jersey · USRutgers New Jersey Medical School

Funding

Functions of Double-stranded RNA Binding ProteinsR01AI034552 · NIAID · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI MATHEWS, MICHAEL B · 1993 to 2008
$4.4M
NIAID NIH HHS R01 AI034552
6 · The paper itself

Abstract

Nuclear factor 90 (NF90), an RNA-binding protein implicated in the regulation of gene expression, exists as a heterodimeric complex with NF45. We previously reported that depletion of the NF90/NF45 complex results in a multinucleated phenotype. Time-lapse microscopy revealed that binucleated cells arise by incomplete abscission of progeny cells followed by fusion. Multinucleate cells arose through aberrant division of binucleated cells and displayed abnormal metaphase plates and anaphase chromatin bridges suggestive of DNA repair defects. NF90 and NF45 are known to interact with the DNA-dependent protein kinase (DNA-PK), which is involved in telomere maintenance and DNA repair by nonhomologous end joining (NHEJ). We hypothesized that NF90 modulates the activity of DNA-PK. In an in vitro NHEJ assay system, DNA end joining was reduced by NF90/NF45 immunodepletion or by RNA digestion to an extent similar to that for catalytic subunit DNA-PKcs immunodepletion. In vivo, NF90/NF45-depleted cells displayed increased γ-histone 2A.X foci, indicative of an accumulation of double-strand DNA breaks (DSBs), and increased sensitivity to ionizing radiation consistent with decreased DSB repair. Further, NF90/NF45 knockdown reduced end-joining activity in vivo. These results identify the NF90/NF45 complex as a regulator of DNA damage repair mediated by DNA-PK and suggest that structured RNA may modulate this process.

Indexed as

DNA Breaks, Double-StrandedDNA End-Joining RepairAntigens, NuclearCell FusionCell NucleusDNADNA-Activated Protein KinaseDNA-Binding ProteinsEnzyme AssaysGene Knockdown TechniquesHeLa CellsHumansImmunoprecipitationKu AutoantigenMicroscopy, ConfocalMicroscopy, FluorescenceAntigens, NuclearDNADNA-Activated Protein KinaseDNA-Binding ProteinsILF2 protein, humanKu AutoantigenMultiprotein ComplexesNuclear Factor 45 ProteinNuclear Factor 90 ProteinsNuclear ProteinsPRKDC protein, humanXrcc6 protein, human

Identifiers

PMID21969602
PMCPMC3232927
OpenAlexW2120328543

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.