Evidence map›Paper›PMID 28262582›Full record

ReviewDNA repair2017

A role for the base excision repair enzyme NEIL3 in replication-dependent repair of interstrand DNA cross-links derived from psoralen and abasic sites.

Zhiyu Yang, Maryam Imani Nejad, Jacqueline Gamboa Varela, Nathan E Price, Yinsheng Wang, Kent S Gates

Open access · greenAbstract readReview
In one paragraph

Review in DNA repair, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

27 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Research progress on the role of the NEIL family in cancer.Frontiers in cell and developmental biology · 2025
    Review
  3. COProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Review
  5. CObioRxiv : the preprint server for biology · 2024
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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

6 authors at 2 institutions in 1 country.

Zhiyu YangUniversity of Missouri Department of Chemistry, 125 Chemistry Building Columbia, MO 65211, United States.
Maryam Imani NejadUniversity of Missouri Department of Chemistry, 125 Chemistry Building Columbia, MO 65211, United States.
Jacqueline Gamboa VarelaUniversity of Missouri Department of Chemistry, 125 Chemistry Building Columbia, MO 65211, United States.
Nathan E PriceUniversity of California-Riverside, Department of Chemistry, 501 Big Springs Road Riverside, CA 92521-0403, United States.
Yinsheng WangUniversity of California-Riverside, Department of Chemistry, 501 Big Springs Road Riverside, CA 92521-0403, United States.
Kent S GatesUniversity of Missouri Department of Chemistry, 125 Chemistry Building Columbia, MO 65211, United States; University of Missouri Department of Biochemistry, 125 Chemistry Building Columbia, MO 65211, United States. Electronic address: gatesk@missouri.edu.
University of Missouri · USUniversity of California, Riverside · US

Funding

Research Training in Environmental ToxicologyT32ES018827 · NIEHS · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI Yinsheng Wang · 2010 to 2026
$5.3M
Cross-links At Abasic Sites in Duplex DNAR01ES021007 · NIEHS · UNIVERSITY OF MISSOURI-COLUMBIA · PI GATES, KENT S, WANG, YINSHENG · 2012 to 2023
$3.7M
NIEHS NIH HHS R01 ES021007NIEHS NIH HHS T32 ES018827
6 · The paper itself

Abstract

Interstrand DNA-DNA cross-links are highly toxic lesions that are important in medicinal chemistry, toxicology, and endogenous biology. In current models of replication-dependent repair, stalling of a replication fork activates the Fanconi anemia pathway and cross-links are "unhooked" by the action of structure-specific endonucleases such as XPF-ERCC1 that make incisions flanking the cross-link. This process generates a double-strand break, which must be subsequently repaired by homologous recombination. Recent work provided evidence for a new, incision-independent unhooking mechanism involving intrusion of a base excision repair (BER) enzyme, NEIL3, into the world of cross-link repair. The evidence suggests that the glycosylase action of NEIL3 unhooks interstrand cross-links derived from an abasic site or the psoralen derivative trioxsalen. If the incision-independent NEIL3 pathway is blocked, repair reverts to the incision-dependent route. In light of the new model invoking participation of NEIL3 in cross-link repair, we consider the possibility that various BER glycosylases or other DNA-processing enzymes might participate in the unhooking of chemically diverse interstrand DNA cross-links.

Indexed as

DNA DamageDNA RepairAnimalsCross-Linking ReagentsDNA AdductsFurocoumarinsHumansN-Glycosyl HydrolasesCross-Linking ReagentsDNA AdductsFurocoumarinsNEIL3 protein, humanN-Glycosyl Hydrolasespsoralen-DNA adductAbasic siteBase excision repairCross-link repairDNA cross-linkFanconi anemiaHomologous recombinationNEILPsoralenXPF-ERCC1

Identifiers

PMID28262582
PMCPMC5424475
OpenAlexW2590140128

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.