Evidence map›Paper›PMID 24726325›Full record

ArticleMolecular cell2014

XPF-ERCC1 acts in Unhooking DNA interstrand crosslinks in cooperation with FANCD2 and FANCP/SLX4.

Daisy Klein Douwel, Rick A C M Boonen, David T Long, Anna A Szypowska, Markus Räschle, Johannes C Walter, Puck Knipscheer

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 210 papers.

0numbers the graph read from it
0cells of the map it votes in
210citing papers in PubMed
14.9field-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

210 citing papers in PubMed, 299 citations in OpenAlex.

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150 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

7 authors at 3 institutions in 3 countries.

Daisy Klein DouwelHubrecht Institute-KNAW, University Medical Center Utrecht and Cancer Genomics Netherlands, Uppsalalaan 8, 3584 CT Utrecht, the Netherlands.
Rick A C M BoonenHubrecht Institute-KNAW, University Medical Center Utrecht and Cancer Genomics Netherlands, Uppsalalaan 8, 3584 CT Utrecht, the Netherlands.
David T LongDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
Anna A SzypowskaHubrecht Institute-KNAW, University Medical Center Utrecht and Cancer Genomics Netherlands, Uppsalalaan 8, 3584 CT Utrecht, the Netherlands.
Markus RäschleDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Johannes C WalterDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
Puck KnipscheerHubrecht Institute-KNAW, University Medical Center Utrecht and Cancer Genomics Netherlands, Uppsalalaan 8, 3584 CT Utrecht, the Netherlands. Electronic address: p.knipscheer@hubrecht.eu.
University Medical Center Utrecht · NLHarvard University · USMax Planck Society · DE

Funding

The Fanconi anemia pathway: role in DNA interstrand cross-link repairR01HL098316 · NHLBI · HARVARD MEDICAL SCHOOL · PI Johannes Walter · 2010 to 2026
$6.3M
Dynamics of BRCA1-Mediated Double-Strand Break RepairK99GM102325 · NIGMS · HARVARD MEDICAL SCHOOL · PI LONG, DAVID THOMAS · 2013 to 2014
$112k
NHLBI NIH HHS HL098316NHLBI NIH HHS R01 HL098316NIGMS NIH HHS K99 GM102325NIGMS NIH HHS K99GM102325
6 · The paper itself

Abstract

DNA interstrand crosslinks (ICLs), highly toxic lesions that covalently link the Watson and Crick strands of the double helix, are repaired by a complex, replication-coupled pathway in higher eukaryotes. The earliest DNA processing event in ICL repair is the incision of parental DNA on either side of the ICL ("unhooking"), which allows lesion bypass. Incisions depend critically on the Fanconi anemia pathway, whose activation involves ubiquitylation of the FANCD2 protein. Using Xenopus egg extracts, which support replication-coupled ICL repair, we show that the 3' flap endonuclease XPF-ERCC1 cooperates with SLX4/FANCP to carry out the unhooking incisions. Efficient recruitment of XPF-ERCC1 and SLX4 to the ICL depends on FANCD2 and its ubiquitylation. These data help define the molecular mechanism by which the Fanconi anemia pathway promotes a key event in replication-coupled ICL repair.

Indexed as

DNA RepairAnimalsCell LineCells, CulturedDNA-Binding ProteinsDNA CleavageDNA DamageEndodeoxyribonucleasesEndonucleasesExodeoxyribonucleasesFanconi Anemia Complementation Group D2 ProteinHumansKineticsMultifunctional EnzymesProtein BindingRecombinasesDNA-Binding ProteinsEndodeoxyribonucleasesEndonucleasesERCC1 protein, humanExodeoxyribonucleasesFAN1 protein, humanFANCD2 protein, humanFanconi Anemia Complementation Group D2 ProteinMultifunctional EnzymesMUS81 protein, humanRecombinasesSLX4 protein, humanXenopus Proteinsxeroderma pigmentosum group F protein

Identifiers

PMID24726325
PMCPMC5067070
OpenAlexW1968245004

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.