Evidence map›Paper›PMID 18948542›Full record

ArticleScience (New York, N.Y.)2008

Functional targeting of DNA damage to a nuclear pore-associated SUMO-dependent ubiquitin ligase.

Shigeki Nagai, Karine Dubrana, Monika Tsai-Pflugfelder, Marta B Davidson, Tania M Roberts, Grant W Brown, Elisa Varela, Florence Hediger, Susan M Gasser, Nevan J Krogan

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 270 papers.

0numbers the graph read from it
0cells of the map it votes in
270citing papers in PubMed
17.7field-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

270 citing papers in PubMed, 443 citations in OpenAlex.

  1. Review
  2. The Role of Arp2/3 in End-Resection During DNA Double-Strand Break Repair.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  3. Review
  4. Article
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  10. Review
  11. Article
  12. Review
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  15. Article
  16. Yeast centrosomes act as organizing centers to promote Polo kinase-mediated adaptation to persistent DNA damage.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Article
  18. Review
  19. Nucleoporins cooperate with Polycomb silencers to promote transcriptional repression and repair at DNA double-strand breaks.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  20. Article

210 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

10 authors at 1 institution in 1 country.

Shigeki NagaiFriedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, 4058 Basel, Switzerland.
Karine Dubrana
Monika Tsai-Pflugfelder
Marta B Davidson
Tania M Roberts
Grant W Brown
Elisa Varela
Florence Hediger
Susan M Gasser
Nevan J Krogan
Friedrich Miescher Institute · CH

Funding

Genetic Analysis of the Nucleosome and RNA Polymerase II: A Systems ApproachR01GM084448 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KROGAN, NEVAN J · 2008 to 2012
$2.3M
NIGMS NIH HHS R01 GM084448
6 · The paper itself

Abstract

Recent findings suggest important roles for nuclear organization in gene expression. In contrast, little is known about how nuclear organization contributes to genome stability. Epistasis analysis (E-MAP) using DNA repair factors in yeast indicated a functional relationship between a nuclear pore subcomplex and Slx5/Slx8, a small ubiquitin-like modifier (SUMO)-dependent ubiquitin ligase, which we show physically interact. Real-time imaging and chromatin immunoprecipitation confirmed stable recruitment of damaged DNA to nuclear pores. Relocation required the Nup84 complex and Mec1/Tel1 kinases. Spontaneous gene conversion can be enhanced in a Slx8- and Nup84-dependent manner by tethering donor sites at the nuclear periphery. This suggests that strand breaks are shunted to nuclear pores for a repair pathway controlled by a conserved SUMO-dependent E3 ligase.

Indexed as

DNA Breaks, Double-StrandedChromatin ImmunoprecipitationDeoxyribonucleases, Type II Site-SpecificDNA-Binding ProteinsDNA, FungalDNA RepairGene ConversionGenes, FungalImmunoprecipitationIntracellular Signaling Peptides and ProteinsKineticsNuclear PoreNuclear Pore Complex ProteinsProtein Serine-Threonine KinasesRecombination, GeneticSaccharomyces cerevisiaeDeoxyribonucleases, Type II Site-SpecificDNA-Binding ProteinsDNA, FungalIntracellular Signaling Peptides and ProteinsMEC1 protein, S cerevisiaeNuclear Pore Complex ProteinsNUP84 protein, S cerevisiaeProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsSCEI protein, S cerevisiaeSlx5 protein, S cerevisiaeSlx8 protein, S cerevisiaeSmall Ubiquitin-Related Modifier ProteinsTEL1 protein, S cerevisiaeUbiquitin-Protein Ligases

Identifiers

PMID18948542
PMCPMC3518492
OpenAlexW2013158844

What OpenQuestion holds

Textmetadata
LicenceTDM
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.