Evidence map›Paper›PMID 27693351›Full record

ArticleCell2016

Replication-Dependent Unhooking of DNA Interstrand Cross-Links by the NEIL3 Glycosylase.

Daniel R Semlow, Jieqiong Zhang, Magda Budzowska, Alexander C Drohat, Johannes C Walter

Abstract read
In one paragraph

Article in Cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.

0numbers the graph read from it
0cells of the map it votes in
134citing papers in PubMed
11.1field-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

134 citing papers in PubMed, 204 citations in OpenAlex.

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  19. Structure andmBio · 2024
    Article
  20. An interstrand DNA crosslink glycosylase aidsProceedings of the National Academy of Sciences of the United States of America · 2024
    Article

74 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

5 authors at 2 institutions in 1 country.

Daniel R SemlowDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Jieqiong ZhangDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Magda BudzowskaDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Alexander C DrohatDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Johannes C WalterDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA; Howard Hughes Medical Institute, Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA. Electronic address: johannes_walter@hms.harvard.edu.
Harvard University · USUniversity of Maryland, Baltimore · US

Funding

The Fanconi anemia pathway: role in DNA interstrand cross-link repairR01HL098316 · NHLBI · HARVARD MEDICAL SCHOOL · PI Johannes Walter · 2010 to 2026
$6.3M
Structure and Mechanism of CpG specific DNA glycosylasesR01GM072711 · NIGMS · WADSWORTH CENTER · PI DROHAT, ALEX C · 2005 to 2020
$5.0M
Properties of the eukaryotic replicative DNA helicaseR01GM062267 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WALTER, JOHANNES · 2001 to 2014
$4.1M
NHLBI NIH HHS R01 HL098316NIGMS NIH HHS R01 GM062267NIGMS NIH HHS R01 GM072711
6 · The paper itself

Abstract

During eukaryotic DNA interstrand cross-link (ICL) repair, cross-links are resolved ("unhooked") by nucleolytic incisions surrounding the lesion. In vertebrates, ICL repair is triggered when replication forks collide with the lesion, leading to FANCI-FANCD2-dependent unhooking and formation of a double-strand break (DSB) intermediate. Using Xenopus egg extracts, we describe here a replication-coupled ICL repair pathway that does not require incisions or FANCI-FANCD2. Instead, the ICL is unhooked when one of the two N-glycosyl bonds forming the cross-link is cleaved by the DNA glycosylase NEIL3. Cleavage by NEIL3 is the primary unhooking mechanism for psoralen and abasic site ICLs. When N-glycosyl bond cleavage is prevented, unhooking occurs via FANCI-FANCD2-dependent incisions. In summary, we identify an incision-independent unhooking mechanism that avoids DSB formation and represents the preferred pathway of ICL repair in a vertebrate cell-free system.

Indexed as

DNA Breaks, Double-StrandedDNA RepairDNA ReplicationAnimalsCell-Free SystemCross-Linking ReagentsDNAFanconi Anemia Complementation Group D2 ProteinFanconi Anemia Complementation Group ProteinsFicusinN-Glycosyl HydrolasesXenopus laevisCross-Linking ReagentsDNAFanconi Anemia Complementation Group D2 ProteinFanconi Anemia Complementation Group ProteinsFicusinN-Glycosyl Hydrolasesabasic siteDNA interstrand cross-linkFANCD2FANCIFanconi anemiaICLNEIL3psoralen

Identifiers

PMID27693351
PMCPMC5237264
OpenAlexW2525711566

What OpenQuestion holds

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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.