Evidence map›Paper›PMID 31034893›Full record

ReviewJournal of molecular biology2019

Interplay between DNA Polymerases and DNA Ligases: Influence on Substrate Channeling and the Fidelity of DNA Ligation.

Melike Çağlayan

Open access · greenAbstract readReview
In one paragraph

Review in Journal of molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

18 citing papers in PubMed, 44 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

1 author at 1 institution in 1 country.

Melike ÇağlayanDepartment of Biochemistry and Molecular Biology, University of Florida, Gainesville, FL 32610, USA. Electronic address: caglayanm@ufl.edu.
University of Florida · US

Funding

Oxidant and environmental toxicant-induced effects compromise ligation in DNA repairR00ES026191 · NIEHS · UNIVERSITY OF FLORIDA · PI CAGLAYAN, MELIKE · 2018 to 2020
$730k
NIEHS NIH HHS R00 ES026191
6 · The paper itself

Abstract

DNA ligases are a highly conserved group of nucleic acid enzymes that play an essential role in DNA repair, replication, and recombination. This review focuses on functional interaction between DNA polymerases and DNA ligases in the repair of single- and double-strand DNA breaks, and discusses the notion that the substrate channeling during DNA polymerase-mediated nucleotide insertion coupled to DNA ligation could be a mechanism to minimize the release of potentially mutagenic repair intermediates. Evidence suggesting that DNA ligases are essential for cell viability includes the fact that defects or insufficiency in DNA ligase are casually linked to genome instability. In the future, it may be possible to develop small molecule inhibitors of mammalian DNA ligases and/or their functional protein partners that potentiate the effects of chemotherapeutic compounds and improve cancer treatment outcomes.

Indexed as

DNA BreaksProtein Interaction MapsAnimalsDNADNA-Directed DNA PolymeraseDNA LigasesDNA RepairGenomic InstabilityHumansDNADNA-Directed DNA PolymeraseDNA LigasesDNA ligaseDNA polymeraseDNA repairgenome stabilityligation failure

Identifiers

PMID31034893
PMCPMC6557440
OpenAlexW2941404794

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.