Evidence map›Paper›PMID 21399697›Full record

ArticlePloS one2011

Uracil DNA N-glycosylase promotes assembly of human centromere protein A.

Samantha G Zeitlin, Brian R Chapados, Norman M Baker, Caroline Tai, Geir Slupphaug, Jean Y J Wang

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

14 citing papers in PubMed, 26 citations in OpenAlex.

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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

6 authors at 4 institutions in 2 countries.

Samantha G ZeitlinMoores UCSD Cancer Center and Ludwig Institute for Cancer Research, University of California San Diego, La Jolla, California, United States of America. szeitlin@sciencegeeks.org
Brian R Chapados
Norman M Baker
Caroline Tai
Geir Slupphaug
Jean Y J Wang
University of California, San Diego · USLudwig Cancer Research · USNorwegian University of Science and Technology · NOScripps Research Institute · US

Funding

VIRAL MALIGNANCYP30CA023100 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DIANE M SIMEONE · 1985 to 2026
$124.9M
U of Calif, San Diego Neuroscience Microscopy ImagingP30NS047101 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GLEESON, JOSEPH G, ZHENG, BINHAI · 2003 to 2022
$9.0M
STRUCTURE AND FUNCTION OF THE C-ABL PROTO-ONCOPROTEINR01CA043054 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI WANG, JEAN Y.J. · 1986 to 2018
$4.4M
CELLULAR FUNCTION OF THE RETINOBLASTOMA GENE PRODUCTR01CA058320 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI WANG, JEAN Y.J. · 1992 to 2012
$4.0M
Nuclear Function of the c-Abl ProtooncoprotienR37CA043054 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI WANG, JEAN Y.J. · 1998 to 2007
$2.9M
Biochemical Basis of CENP-A Epigenetic InheritanceF32GM069297 · NIGMS · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI ZEITLIN, SAMANTHA G · 2003 to 2005
$139k
NCI NIH HHS 5R01CA058320-15NCI NIH HHS P30 CA023100NCI NIH HHS P30 CA23100NCI NIH HHS R01 CA043054NCI NIH HHS R01 CA058320NCI NIH HHS R37 CA043054NIGMS NIH HHS 5F32GM069297NIGMS NIH HHS F32 GM069297NINDS NIH HHS P30 NS047101
6 · The paper itself

Abstract

Uracil is removed from DNA by the conserved enzyme uracil DNA N-glycosylase (UNG). Previously, we observed that inhibiting UNG in Xenopus egg extracts blocked assembly of CENP-A, a histone H3 variant. CENP-A is an essential protein in all species, since it is required for chromosome segregation during mitosis. Thus, the implication of UNG in CENP-A assembly implies that UNG would also be essential, but UNG mutants lacking catalytic activity are viable in all species. In this paper, we present evidence that UNG2 colocalizes with CENP-A and H2AX phosphorylation at centromeres in normally cycling cells. Reduction of UNG2 in human cells blocks CENP-A assembly, and results in reduced cell proliferation, associated with increased frequencies of mitotic abnormalities and rapid cell death. Overexpression of UNG2 induces high levels of CENP-A assembly in human cells. Using a multiphoton laser approach, we demonstrate that UNG2 is rapidly recruited to sites of DNA damage. Taken together, our data are consistent with a model in which the N-terminus of UNG2 interacts with the active site of the enzyme and with chromatin.

Indexed as

AnimalsApoptosisAutoantigensCentromereCentromere Protein AChromosomal Proteins, Non-HistoneDNA DamageDNA GlycosylasesG2 PhaseGreen Fluorescent ProteinsHEK293 CellsHeLa CellsHistonesHumansLasersPhosphorylationAutoantigensCCNO protein, humanCENPA protein, humanCentromere Protein AChromosomal Proteins, Non-HistoneDNA GlycosylasesGreen Fluorescent ProteinsH2AX protein, humanHistonesRecombinant Fusion ProteinsRNA, Small Interferingvpr Gene Products, Human Immunodeficiency Virus

Identifiers

PMID21399697
PMCPMC3047565
OpenAlexW2110694293

What OpenQuestion holds

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LicenceCC BY
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.