Evidence map›Paper›PMID 11024166›Full record

ArticleNucleic acids research2000

Mitochondrial DNA ligase III function is independent of Xrcc1.

U Lakshmipathy, C Campbell

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

50 citing papers in PubMed, 98 citations in OpenAlex.

  1. Article
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  16. Article
  17. Coordination of DNA single strand break repair.Free radical biology & medicine · 2017
    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

2 authors at 1 institution in 1 country.

U LakshmipathyUniversity of Minnesota Medical School, Department of Pharmacology, 6-120 Jackson Hall, 321 Church Street SE, Minneapolis, MN 55455, USA.
C Campbell
University of Minnesota Medical Center · US

Funding

MAMMALIAN MITOCHONDRIAL DNA DOUBLE-STRAND-BREAK-REPAIRR01AG016678 · NIA · UNIVERSITY OF MINNESOTA TWIN CITIES · PI CAMPBELL, COLIN R · 2000 to 2003
$728k
RAD52 FUNCTION IN MAMMALIAN SOMATIC CELLSR29CA061906 · NCI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI CAMPBELL, COLIN R · 1997 to 2001
$205k
NCI NIH HHS R29-CA61906NIA NIH HHS R01 AG016678NIA NIH HHS R01-AG16678
6 · The paper itself

Abstract

Hamster EM9 cells, which lack Xrcc1 protein, have reduced levels of DNA ligase III and are defective in nuclear base excision repair. The Xrcc1 protein stabilizes DNA ligase III and may even play a direct role in catalyzing base excision repair. Since DNA ligase III is also thought to function in mitochondrial base excision repair, it seemed likely that mitochondrial DNA ligase III function would also be dependent upon Xrcc1. However, several lines of evidence indicate that this is not the case. First, western blot analysis failed to detect Xrcc1 protein in mitochondrial extracts. Second, DNA ligase III levels present in mitochondrial protein extracts from EM9 cells were indistinguishable from those seen in similar extracts from wild-type (AA8) cells. Third, the mitochondrial DNA content of both cell lines was identical. Fourth, EM9 cells displayed no defect in their ability to repair spontaneous mitochondrial DNA damage. Fifth, while EM9 cells were far more sensitive to the cytotoxic effects of ionizing radiation due to a defect in nuclear DNA repair, there was no apparent difference in the ability of EM9 and AA8 cells to restore their mitochondrial DNA to pre-irradiation levels. Thus, mitochondrial DNA ligase III function is independent of the Xrcc1 protein.

Indexed as

DNA RepairAnimalsBlotting, SouthernBlotting, WesternCell ExtractsCell LineCell NucleusCricetinaeDNA-Binding ProteinsDNA DamageDNA Ligase ATPDNA LigasesDNA, MitochondrialDose-Response Relationship, RadiationGamma RaysKineticsCell ExtractsDNA-Binding ProteinsDNA Ligase ATPDNA ligase III alpha protein, XenopusDNA LigasesDNA, MitochondrialNuclear ProteinsPoly-ADP-Ribose Binding ProteinsXenopus ProteinsX-ray Repair Cross Complementing Protein 1

Identifiers

PMID11024166
PMCPMC110795
OpenAlexW2094868973

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.