Evidence map›Paper›PMID 28292631›Full record

ArticleDNA repair2017

Probing the activity of NTHL1 orthologs by targeting conserved amino acid residues.

Susan M Robey-Bond, Meredith A Benson, Ramiro Barrantes-Reynolds, Jeffrey P Bond, Susan S Wallace

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in DNA repair, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 45% 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

1 citing paper in PubMed, 5 citations in OpenAlex.

  1. Article
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 1 institution in 1 country.

Susan M Robey-BondDepartment of Microbiology and Molecular Genetics, The Markey Center for Molecular Genetics, University of Vermont, Stafford Hall, 95 Carrigan Drive, Burlington, VT 05405-0068, United States.
Meredith A BensonDepartment of Microbiology and Molecular Genetics, The Markey Center for Molecular Genetics, University of Vermont, Stafford Hall, 95 Carrigan Drive, Burlington, VT 05405-0068, United States.
Ramiro Barrantes-ReynoldsDepartment of Microbiology and Molecular Genetics, The Markey Center for Molecular Genetics, University of Vermont, Stafford Hall, 95 Carrigan Drive, Burlington, VT 05405-0068, United States.
Jeffrey P BondDepartment of Microbiology and Molecular Genetics, The Markey Center for Molecular Genetics, University of Vermont, Stafford Hall, 95 Carrigan Drive, Burlington, VT 05405-0068, United States.
Susan S WallaceDepartment of Microbiology and Molecular Genetics, The Markey Center for Molecular Genetics, University of Vermont, Stafford Hall, 95 Carrigan Drive, Burlington, VT 05405-0068, United States. Electronic address: swallace@uvm.edu.
University of Vermont · US

Funding

SUBSTRATE SPECIFICITY OF THE BER OXIDATIVE DNA GLYCOSYLASESP01CA098993 · NCI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI LEE, ANDREA J · 2004 to 2021
$25.9M
TUMOR GROWTH AND METASTASISP30CA022435 · NCI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI FOGARTY, JOHN P · 1985 to 2007
$9.6M
Repair of DNA Damages Induced by Ionizing RadiationR01CA033657 · NCI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI WALLACE, SUSAN S. · 1985 to 2009
$2.2M
NCI NIH HHS P01 CA098993NCI NIH HHS P30 CA022435NCI NIH HHS R01 CA033657
6 · The paper itself

Abstract

The base excision repair DNA glycosylases, EcoNth and hNTHL1, are homologous, with reported overlapping yet different substrate specificities. The catalytic amino acid residues are known and are identical between the two enzymes although the exact structures of the substrate binding pockets remain to be determined. We sought to explore the sequence basis of substrate differences using a phylogeny-based design of site-directed mutations. Mutations were made for each enzyme in the vicinity of the active site and we examined these variants for glycosylase and lyase activity. Single turnover kinetics were done on a subgroup of these, comparing activity on two lesions, 5,6-dihydrouracil and 5,6-dihydrothymine, with different opposite bases. We report that wild type hNTHL1 and EcoNth are remarkably alike with respect to the specificity of the glycosylase reaction, and although hNTHL1 is a much slower enzyme than EcoNth, the tighter binding of hNTHL1 compensates, resulting in similar k

Indexed as

Catalytic DomainDNA DamageMutationAmino Acid SequenceDeoxyribonuclease (Pyrimidine Dimer)DNAEscherichia coliEscherichia coli ProteinsHumansKineticsSubstrate SpecificityDeoxyribonuclease (Pyrimidine Dimer)DNAEscherichia coli ProteinsNTHL1 protein, humanNTH protein, E coliBase excision repairEndonuclease IIIEnzyme kinetics

Identifiers

PMID28292631
PMCPMC5421317
OpenAlexW2592328599

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.