Evidence map›Paper›PMID 19607800›Full record

ArticleAnalytical biochemistry2009

Characterization of DNA glycosylase activity by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.

Agus Darwanto, Alvin Farrel, Daniel K Rogstad, Lawrence C Sowers

Abstract read
In one paragraph

Article in Analytical biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

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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

4 authors.

Agus DarwantoDepartment of Basic Science, Loma Linda University School of Medicine, Loma Linda, CA 92350, USA.
Alvin Farrel
Daniel K Rogstad
Lawrence C Sowers

Funding

INFIDELITY OF CYTOSINE METHYLATION AND HUMAN CANCERR01CA084487 · NCI · UNIVERSITY OF TEXAS MED BR GALVESTON · PI SOWERS, LAWRENCE C · 2000 to 2016
$3.6M
HYDROLYTIC AND FREE RADICAL-MEDIATED DNA DAMAGER01GM050351 · NIGMS · UNIVERSITY OF TEXAS MED BR GALVESTON · PI SOWERS, LAWRENCE C · 1994 to 2012
$2.7M
NCI NIH HHS R01 CA084487NIGMS NIH HHS R01 GM050351
6 · The paper itself

Abstract

The DNA of all organisms is persistently damaged by endogenous reactive molecules. Most of the single-base endogenous damage is repaired through the base excision repair (BER) pathway that is initiated by members of the DNA glycosylase family. Although the BER pathway is often considered to proceed through a common abasic site intermediate, emerging evidence indicates that there are likely distinct branches reflected by the multitude of chemically different 3' and 5' ends generated at the repair site. In this study, we have applied matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) to the analysis of model DNA substrates acted on by recombinant glycosylases. We examine the chemical identity of several possible abasic site and nicked intermediates generated by monofunctional and bifunctional glycosylases. Our results suggest that the intermediate from endoIII/Nth might not be a simple beta-elimination product as described previously. On the basis of (18)O incorporation experiments, we propose a new mechanism for the endoIII/Nth family of glycosylases that may resolve several of the previous controversies. We further demonstrate that the use of an array of lesion-containing oligonucleotides can be used to rapidly examine the substrate preferences of a given glycosylase. Some of the lesions examined here can be acted on by more than one glycosylase, resulting in a spectrum of damaged intermediates for each lesion, suggesting that the sequence and coordination of repair activities that act on these lesions may influence the biological outcome of damage repair.

Indexed as

Base SequenceDNA DamageDNA GlycosylasesDNA RepairElectrophoresis, Polyacrylamide GelHumansOligodeoxyribonucleotidesSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSubstrate SpecificityUracil-DNA GlycosidaseDNA GlycosylasesOligodeoxyribonucleotidesUracil-DNA Glycosidase

Identifiers

PMID19607800
PMCPMC3990469

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Registered trials

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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.