Evidence map›Paper›PMID 29795289›Full record

ArticleNature communications2018

Distinct roles of XPF-ERCC1 and Rad1-Rad10-Saw1 in replication-coupled and uncoupled inter-strand crosslink repair.

Ja-Hwan Seol, Cory Holland, Xiaolei Li, Christopher Kim, Fuyang Li, Melisa Medina-Rivera, Robin Eichmiller, Ignacio F Gallardo, Ilya J Finkelstein, Paul Hasty and 3 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

7 citing papers in PubMed, 18 citations in OpenAlex.

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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

13 authors at 3 institutions in 1 country.

Ja-Hwan SeolDepartment of Molecular Medicine, Institute of Biotechnology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX, 78229-3900, USA.
Cory HollandDepartment of Molecular Medicine, Institute of Biotechnology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX, 78229-3900, USA.
Xiaolei LiDepartment of Radiation Oncology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX, 78229-3900, USA.
Christopher KimDepartment of Molecular Medicine, Institute of Biotechnology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX, 78229-3900, USA.
Fuyang LiDepartment of Molecular Medicine, Institute of Biotechnology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX, 78229-3900, USA.
Melisa Medina-RiveraDepartment of Biochemistry, Jacobs School of Medicine and Biomedical Sciences, University at Buffalo, State University of New York, 955 Main Street, Buffalo, NY, 14203, USA.
Robin EichmillerDepartment of Biochemistry, Jacobs School of Medicine and Biomedical Sciences, University at Buffalo, State University of New York, 955 Main Street, Buffalo, NY, 14203, USA.
Ignacio F GallardoDepartment of Molecular Biosciences, Institute for Cellular and Molecular Biology, The University of Texas at Austin, Austin, TX, 78712, USA.
Ilya J FinkelsteinDepartment of Molecular Biosciences, Institute for Cellular and Molecular Biology, The University of Texas at Austin, Austin, TX, 78712, USA.ORCID http://orcid.org/0000-0002-9371-2431
Paul HastyDepartment of Molecular Medicine, Institute of Biotechnology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX, 78229-3900, USA.
Eun Yong ShimDepartment of Radiation Oncology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX, 78229-3900, USA.
Jennifer A SurteesDepartment of Biochemistry, Jacobs School of Medicine and Biomedical Sciences, University at Buffalo, State University of New York, 955 Main Street, Buffalo, NY, 14203, USA.
Sang Eun LeeDepartment of Molecular Medicine, Institute of Biotechnology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX, 78229-3900, USA. lees4@uthscsa.edu.
The University of Texas Health Science Center at San Antonio · USUniversity at Buffalo, State University of New York · USThe University of Texas at Austin · US

Funding

Mechanisms of Error Prone Repair of DNA BreaksR01GM071011 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI LEE, SANG EUN · 2004 to 2021
$4.5M
Enabling Access to Cutting-Edge Biomedical and Behavioral ScienceR25GM095459 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI DUBOCOVICH, MARGARITA L · 2012 to 2021
$4.4M
Mechanistic Characterization of the First Steps of Human DNA Break RepairR01GM120554 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI FINKELSTEIN, ILYA J · 2016 to 2020
$1.5M
Mechanism, specificity, and design of CRISPR RNA-mediated gene regulationR01GM124141 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI FINKELSTEIN, ILYA J · 2017 to 2020
$1.2M
NIGMS NIH HHS R01 GM071011NIGMS NIH HHS R01 GM120554NIGMS NIH HHS R01 GM124141NIGMS NIH HHS R25 GM095459NIH HHS CA188032NIH HHS ES022054NIH HHS GM066094NIH HHS GM097177NIH HHS GM71011NIH HHS GM87459
6 · The paper itself

Abstract

Yeast Rad1-Rad10 (XPF-ERCC1 in mammals) incises UV, oxidation, and cross-linking agent-induced DNA lesions, and contributes to multiple DNA repair pathways. To determine how Rad1-Rad10 catalyzes inter-strand crosslink repair (ICLR), we examined sensitivity to ICLs from yeast deleted for SAW1 and SLX4, which encode proteins that interact physically with Rad1-Rad10 and bind stalled replication forks. Saw1, Slx1, and Slx4 are critical for replication-coupled ICLR in mus81 deficient cells. Two rad1 mutations that disrupt interactions between Rpa1 and Rad1-Rad10 selectively disable non-nucleotide excision repair (NER) function, but retain UV lesion repair. Mutations in the analogous region of XPF also compromised XPF interactions with Rpa1 and Slx4, and are proficient in NER but deficient in ICLR and direct repeat recombination. We propose that Rad1-Rad10 makes distinct contributions to ICLR depending on cell cycle phase: in G1, Rad1-Rad10 removes ICL via NER, whereas in S/G2, Rad1-Rad10 facilitates NER-independent replication-coupled ICLR.

Indexed as

AnimalsCell CycleCHO CellsCricetulusCross-Linking ReagentsDNA-Binding ProteinsDNA DamageDNA RepairDNA Repair EnzymesEndonucleasesIntravital MicroscopyMutagenesis, Site-DirectedMutationSaccharomyces cerevisiae ProteinsSingle-Strand Specific DNA and RNA EndonucleasesUltraviolet RaysCross-Linking ReagentsDNA-Binding ProteinsDNA Repair EnzymesEndonucleasesRAD10 protein, S cerevisiaeRAD1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSaw1 protein, S cerevisiaeSingle-Strand Specific DNA and RNA Endonucleasesxeroderma pigmentosum group F protein

Identifiers

PMID29795289
PMCPMC5966407
OpenAlexW2804723602

What OpenQuestion holds

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Registered trials

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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.