Evidence map›Paper›PMID 20634321›Full record

ArticleGenes & development2010

Mechanism of Holliday junction resolution by the human GEN1 protein.

Ulrich Rass, Sarah A Compton, Joao Matos, Martin R Singleton, Stephen C Y Ip, Miguel G Blanco, Jack D Griffith, Stephen C West

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
–field-weighted citation impact
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

96 citing papers in PubMed, 165 citations in OpenAlex.

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36 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

8 authors at 2 institutions in 2 countries.

Ulrich RassLondon Research Institute, Cancer Research UK, Clare Hall Laboratories, South Mimms, Herts, United Kingdom.
Sarah A Compton
Joao Matos
Martin R Singleton
Stephen C Y Ip
Miguel G Blanco
Jack D Griffith
Stephen C West
Cancer Research UK · GBUNC Lineberger Comprehensive Cancer Center

Funding

HOMOLOOUS RECOMBINATION: ITS MOLECULAR CYTOLOGYR01GM031819 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI GRIFFITH, JACK D · 1985 to 2017
$5.2M
Nucleoprotein structures formed at sites of DNA damageR01ES013773 · NIEHS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI GRIFFITH, JACK D · 2005 to 2015
$3.2M
Breast Cancer Now 2009MAYPR01Cancer Research UK 11582NIEHS NIH HHS ES31773NIEHS NIH HHS R01 ES013773NIGMS NIH HHS GM31819NIGMS NIH HHS R01 GM031819
6 · The paper itself

Abstract

Holliday junction (HJ) resolution is essential for chromosome segregation at meiosis and the repair of stalled/collapsed replication forks in mitotic cells. All organisms possess nucleases that promote HJ resolution by the introduction of symmetrically related nicks in two strands at, or close to, the junction point. GEN1, a member of the Rad2/XPG nuclease family, was isolated recently from human cells and shown to promote HJ resolution in vitro and in vivo. Here, we provide the first biochemical/structural characterization of GEN1, showing that, like the Escherichia coli HJ resolvase RuvC, it binds specifically to HJs and resolves them by a dual incision mechanism in which nicks are introduced in the pair of continuous (noncrossing) strands within the lifetime of the GEN1-HJ complex. In contrast to RuvC, but like other Rad2/XPG family members such as FEN1, GEN1 is a monomeric 5'-flap endonuclease. However, the unique feature of GEN1 that distinguishes it from other Rad2/XPG nucleases is its ability to dimerize on HJs. This functional adaptation provides the two symmetrically aligned active sites required for HJ resolution.

Indexed as

DNA, CruciformDNA RepairEndodeoxyribonucleasesEscherichia coli ProteinsFlap EndonucleasesHolliday Junction ResolvasesHumansSubstrate SpecificityDNA, CruciformEndodeoxyribonucleasesEscherichia coli ProteinsFEN1 protein, humanFlap EndonucleasesGEN1 protein, humanHolliday Junction ResolvasesruvC protein, E coli

Identifiers

PMID20634321
PMCPMC2904945
OpenAlexW2167121797

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.