Evidence map›Paper›PMID 11598021›Full record

ArticleThe EMBO journal2001

Werner syndrome protein interacts with human flap endonuclease 1 and stimulates its cleavage activity.

R M Brosh, C von Kobbe, J A Sommers, P Karmakar, P L Opresko, J Piotrowski, I Dianova, G L Dianov, V A Bohr

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.

0numbers the graph read from it
0cells of the map it votes in
123citing papers in PubMed
9.3field-weighted citation impact, top 1% 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

123 citing papers in PubMed, 256 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. RecQ Helicase Somatic Alterations in Cancer.Frontiers in molecular biosciences · 2022
    Review
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Telomeres, Aging and Exercise: Guilty by Association?International journal of molecular sciences · 2017
    Review
  18. Review
  19. Review
  20. Article

63 more citing papers are in PubMed but not listed here.

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

9 authors at 1 institution in 1 country.

R M BroshLaboratory of Molecular Gerontology, National Institute on Aging, National Institutes of Health, 5600 Nathan Shock Drive, Baltimore, MD 21224, USA. BroshR@grc.nia.nih.gov
C von Kobbe
J A Sommers
P Karmakar
P L Opresko
J Piotrowski
I Dianova
G L Dianov
V A Bohr
National Institutes of Health · US

Funding

Function of RecQ helicases in genome stabilityZIAAG000726 · NIA · NATIONAL INSTITUTE ON AGING · PI BROSH, ROBERT · 2009 to 2025
$13.1M
Roles Of DNA Helicases In Pathways Required For Maintenance Of Genomic StabilityZIAAG000741 · NIA · NATIONAL INSTITUTE ON AGING · PI BROSH, ROBERT · 2009 to 2025
$7.6M
Function of RecQ helicases in genome stabilityZ01AG000726 · NIA · NATIONAL INSTITUTE ON AGING · PI BOHR, VILHELM A · 1993 to 2008
$2.9M
Roles Of Dna Helicases:Pathways Required For MaintenanceZ01AG000741 · NIA · NATIONAL INSTITUTE ON AGING · PI BROSH, ROBERT M · 2001 to 2008
$1.1M
6 · The paper itself

Abstract

Werner syndrome (WS) is a human premature aging disorder characterized by chromosomal instability. The cellular defects of WS presumably reflect compromised or aberrant function of a DNA metabolic pathway that under normal circumstances confers stability to the genome. We report a novel interaction of the WRN gene product with the human 5' flap endonuclease/5'-3' exonuclease (FEN-1), a DNA structure-specific nuclease implicated in DNA replication, recombination and repair. WS protein (WRN) dramatically stimulates the rate of FEN-1 cleavage of a 5' flap DNA substrate. The WRN-FEN-1 functional interaction is independent of WRN catalytic function and mediated by a 144 amino acid domain of WRN that shares homology with RecQ DNA helicases. A physical interaction between WRN and FEN-1 is demonstrated by their co-immunoprecipitation from HeLa cell lysate and affinity pull-down experiments using a recombinant C-terminal fragment of WRN. The underlying defect of WS is discussed in light of the evidence for the interaction between WRN and FEN-1.

Indexed as

Adenosine TriphosphatasesCatalysisDNADNA-Binding ProteinsDNA HelicasesEndodeoxyribonucleasesEnzyme ActivationExodeoxyribonucleasesExonucleasesFlap EndonucleasesHeLa CellsHumansMacromolecular SubstancesPeptide FragmentsProliferating Cell Nuclear AntigenProtein Structure, TertiaryAdenosine TriphosphatasesDNADNA-Binding ProteinsDNA HelicasesEndodeoxyribonucleasesExodeoxyribonucleasesExonucleasesFEN1 protein, humanFlap EndonucleasesMacromolecular SubstancesPeptide FragmentsProliferating Cell Nuclear AntigenRecombinant Fusion ProteinsRecQ HelicasesReplication Protein ARPA1 protein, humanWerner Syndrome HelicaseWRN protein, human

Identifiers

PMID11598021
PMCPMC125684
OpenAlexW2066253067

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.