Evidence map›Paper›PMID 27580719›Full record

ArticleNucleic acids research2016

Structural basis of damage recognition by thymine DNA glycosylase: Key roles for N-terminal residues.

Christopher T Coey, Shuja S Malik, Lakshmi S Pidugu, Kristen M Varney, Edwin Pozharski, Alexander C Drohat

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

48 citing papers in PubMed, 65 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

6 authors at 2 institutions in 1 country.

Christopher T CoeyDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Shuja S MalikDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Lakshmi S PiduguDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Kristen M VarneyDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Edwin PozharskiDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA EPozharskiy@som.umaryland.edu.
Alexander C DrohatDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA adrohat@som.umaryland.edu.
University of Maryland, Baltimore · USInstitute for Bioscience and Biotechnology Research

Funding

ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 1985 to 2011
$38.9M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Structure and Mechanism of CpG specific DNA glycosylasesR01GM072711 · NIGMS · WADSWORTH CENTER · PI DROHAT, ALEX C · 2005 to 2020
$5.0M
NCRR NIH HHS P41 RR001209NIGMS NIH HHS P41 GM103393NIGMS NIH HHS R01 GM072711
6 · The paper itself

Abstract

Thymine DNA Glycosylase (TDG) is a base excision repair enzyme functioning in DNA repair and epigenetic regulation. TDG removes thymine from mutagenic G·T mispairs arising from deamination of 5-methylcytosine (mC), and it processes other deamination-derived lesions including uracil (U). Essential for DNA demethylation, TDG excises 5-formylcytosine and 5-carboxylcytosine, derivatives of mC generated by Tet (ten-eleven translocation) enzymes. Here, we report structural and functional studies of TDG

Indexed as

DNA DamageAmino Acid SequenceBinding SitesDNAEnzyme ActivationHumansHydrophobic and Hydrophilic InteractionsMagnetic Resonance SpectroscopyModels, MolecularMolecular ConformationProtein BindingProtein Interaction Domains and MotifsRecombinant ProteinsStructure-Activity RelationshipSubstrate SpecificityThymine DNA GlycosylaseDNARecombinant ProteinsThymine DNA Glycosylase

Identifiers

PMID27580719
PMCPMC5137436
OpenAlexW2517711883

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.