Evidence map›Paper›PMID 28668127›Full record

ArticleMethods in enzymology2017

Kinetic Methods for Studying DNA Glycosylases Functioning in Base Excision Repair.

Christopher T Coey, Alexander C Drohat

Abstract read
In one paragraph

Article in Methods in enzymology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Excision of 5-Carboxylcytosine by Thymine DNA Glycosylase.Journal of the American Chemical Society · 2019
    Article
  13. Defining the Role of Nucleotide Flipping in Enzyme Specificity UsingJournal of the American Chemical Society · 2019
    Article
  14. 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

2 authors.

Christopher T CoeyUniversity of Maryland School of Medicine, Baltimore, MD, United States.
Alexander C DrohatUniversity of Maryland School of Medicine, Baltimore, MD, United States; Marlene and Stewart Greenebaum Cancer Center, University of Maryland School of Medicine, Baltimore, MD, United States. Electronic address: adrohat@som.umaryland.edu.

Funding

Structure and Mechanism of CpG specific DNA glycosylasesR01GM072711 · NIGMS · WADSWORTH CENTER · PI DROHAT, ALEX C · 2005 to 2020
$5.0M
NIGMS NIH HHS R01 GM072711
6 · The paper itself

Abstract

Base excision repair (BER) is a conserved and ubiquitous pathway that is initiated by DNA glycosylases, which recognize and remove damaged or mismatched nucleobases, setting the stage for restoration of the correct DNA sequence by follow-on BER enzymes. DNA glycosylases employ a nucleotide-flipping step prior to cleavage of the N-glycosyl bond, and most exhibit slow release of the abasic DNA product and/or strong product inhibition. As such, studying the catalytic mechanism of these enzymes requires care in the design, execution, and interpretation of single- and multiple-turnover kinetics experiments, which is the topic of this chapter.

Indexed as

DNA RepairAnimalsDNA DamageDNA GlycosylasesEnzyme AssaysHumansKineticsDNA GlycosylasesBase excision repairCatalytic turnoverDNA glycosylaseDNA repairEnzyme kineticsMultiple-turnover kineticsSingle-turnover kinetics

Identifiers

PMID28668127
PMCPMC5761649

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.