Evidence map›Paper›PMID 12589063›Full record

ArticleMolecular biology of the cell2003

In vitro and in vivo interactions of DNA ligase IV with a subunit of the condensin complex.

Marcin R Przewloka, Paige E Pardington, Steven M Yannone, David J Chen, Robert B Cary

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

12 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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

5 authors at 2 institutions in 1 country.

Marcin R PrzewlokaLos Alamos National Laboratory, Biosciences Division, New Mexico 87545, USA.
Paige E Pardington
Steven M Yannone
David J Chen
Robert B Cary
Los Alamos National Laboratory · USLawrence Berkeley National Laboratory · US

Funding

Roles of DNA PK in DNA Double Strand Break RepairR37CA050519 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI CHEN, DAVID J · 2003 to 2011
$3.5M
ROLES OF DNA PK IN DNA DOUBLE STRAND BREAK REPAIRR01CA050519 · NCI · UNIVERSITY OF CALIF-LOS ALAMOS NAT LAB · PI CHEN, DAVID J · 1989 to 2001
$946k
ANALYSIS OF THE DNA DOUBLE STRAND-BREAK REPAIR COMPLEXR01CA082198 · NCI · UNIVERSITY OF CALIF-LOS ALAMOS NAT LAB · PI CARY, ROBERT BRUCE · 1999 to 2001
$383k
NCI NIH HHS CA50519NCI NIH HHS CA82198NCI NIH HHS R01 CA050519NCI NIH HHS R37 CA050519
6 · The paper itself

Abstract

Several findings have revealed a likely role for DNA ligase IV, and interacting protein XRCC4, in the final steps of mammalian DNA double-strand break repair. Recent evidence suggests that the human DNA ligase IV protein plays a critical role in the maintenance of genomic stability. To identify protein-protein interactions that may shed further light on the molecular mechanisms of DSB repair and the biological roles of human DNA ligase IV, we have used the yeast two-hybrid system in conjunction with traditional biochemical methods. These efforts have resulted in the identification of a physical association between the DNA ligase IV polypeptide and the human condensin subunit known as hCAP-E. The hCAP-E polypeptide, a member of the Structural Maintenance of Chromosomes (SMC) super-family of proteins, coimmunoprecipitates from cell extracts with DNA ligase IV. Immunofluorescence studies reveal colocalization of DNA ligase IV and hCAP-E in the interphase nucleus, whereas mitotic cells display colocalization of both polypeptides on mitotic chromosomes. Strikingly, the XRCC4 protein is excluded from the area of mitotic chromosomes, suggesting the formation of specialized DNA ligase IV complexes subject to cell cycle regulation. We discuss our findings in light of known and hypothesized roles for ligase IV and the condensin complex.

Indexed as

Adenosine TriphosphatasesCell CycleChromatinCloning, MolecularDNA-Binding ProteinsDNA DamageDNA Ligase ATPDNA LigasesDNA RepairFluorescent Antibody Technique, IndirectGene LibraryHeLa CellsHumansInterphaseMicroscopy, FluorescenceMitosisAdenosine TriphosphatasesChromatincondensin complexesDNA-Binding ProteinsDNA Ligase ATPDNA LigasesLIG4 protein, humanMultiprotein ComplexesXRCC4 protein, humanNon-programmatic

Identifiers

PMID12589063
PMCPMC150001
OpenAlexW2149121764

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.