Evidence map›Paper›PMID 32109332›Full record

ArticleAngewandte Chemie (International ed. in English)2020

An Excimer Clamp for Measuring Damaged-Base Excision by the DNA Repair Enzyme NTH1.

Yong Woong Jun, David L Wilson, Anna M Kietrys, Elizabeth R Lotsof, Savannah G Conlon, Sheila S David, Eric T Kool

Open access · greenAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 36% 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

6 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Chemical Tools for the Study of DNA Repair.Accounts of chemical research · 2022
    Article
  6. 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

7 authors at 2 institutions in 1 country.

Yong Woong JunDepartment of Chemistry, Stanford University, Stanford, CA, 94305, USA.ORCID 0000-0001-9359-1265
David L WilsonDepartment of Chemistry, Stanford University, Stanford, CA, 94305, USA.
Anna M KietrysDepartment of Chemistry, Stanford University, Stanford, CA, 94305, USA.
Elizabeth R LotsofDepartment of Chemistry, University of California, Davis, Davis, CA, 95616, USA.
Savannah G ConlonDepartment of Chemistry, University of California, Davis, Davis, CA, 95616, USA.
Sheila S DavidDepartment of Chemistry, University of California, Davis, Davis, CA, 95616, USA.
Eric T KoolDepartment of Chemistry, Stanford University, Stanford, CA, 94305, USA.ORCID 0000-0002-7310-2935
Stanford University · USUniversity of California, Davis · US

Funding

Translational Oncology Research Program (Project-005)P30CA124435 · NCI · STANFORD UNIVERSITY · PI Vittorio Sebastiano · 2007 to 2026
$71.4M
Chemistry and Biology of Oxidized Purine Lesions in DNAR01CA090689 · NCI · UNIVERSITY OF UTAH · PI BURROWS, CYNTHIA J, DAVID, SHEILA SUE · 2002 to 2019
$5.5M
Measuring and Modulating Oxidative DNA Damage Surveillance PathwaysR01CA217809 · NCI · STANFORD UNIVERSITY · PI KOOL, ERIC T. · 2017 to 2024
$3.7M
NCI NIH HHS R01 CA090689NCI NIH HHS R01 CA217809
6 · The paper itself

Abstract

Direct measurement of DNA repair enzyme activities is important both for the basic study of cellular repair pathways as well as for potential new translational applications in their associated diseases. NTH1, a major glycosylase targeting oxidized pyrimidines, prevents mutations arising from this damage, and the regulation of NTH1 activity is important in resisting oxidative stress and in suppressing tumor formation. Herein, we describe a novel molecular strategy for the direct detection of damaged DNA base excision activity by a ratiometric fluorescence change. This strategy utilizes glycosylase-induced excimer formation of pyrenes, and modified DNA probes, incorporating two pyrene deoxynucleotides and a damaged base, enable the direct, real-time detection of NTH1 activity in vitro and in cellular lysates. The probe design was also applied in screening for potential NTH1 inhibitors, leading to the identification of a new small-molecule inhibitor with sub-micromolar potency.

Indexed as

DNA RepairAntimutagenic AgentsDeoxyribonuclease (Pyrimidine Dimer)DNA DamageDrug Evaluation, PreclinicalEnzyme InhibitorsHumansOxidation-ReductionOxidative StressPyrimidinesAntimutagenic AgentsDeoxyribonuclease (Pyrimidine Dimer)Enzyme InhibitorsNTHL1 protein, humanPyrimidinesbase excision repairDNA damagefluorescent probesglycosylasesinhibitors

Identifiers

PMID32109332
PMCPMC7180134
OpenAlexW3007786685

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.