Evidence map›Paper›PMID 36511855›Full record

ArticleNucleic acids research2022

Cooperative interaction between AAG and UV-DDB in the removal of modified bases.

Sunbok Jang, Namrata Kumar, Mathew A Schaich, Zhou Zhong, Barbara van Loon, Simon C Watkins, Bennett Van Houten

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

13 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
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  13. DNA Alkylation Damage by Nitrosamines and Relevant DNA Repair Pathways.International journal of molecular sciences · 2023
    Review
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 3 institutions in 3 countries.

Sunbok JangDepartment of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, PA 15261, USA.
Namrata KumarUPMC Hillman Cancer Center, PA 15213, USA.
Mathew A SchaichDepartment of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, PA 15261, USA.
Zhou ZhongDepartment of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, PA 15261, USA.
Barbara van LoonDepartment of Clinical and Molecular Medicine, Faculty of Medicine and Health Sciences, Norwegian University of Science and Technology (NTNU), 7491, Trondheim, Norway.ORCID 0000-0002-7597-207X
Simon C WatkinsCenter for Biologic Imaging, University of Pittsburgh, PA 15261, USA.
Bennett Van HoutenDepartment of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, PA 15261, USA.ORCID 0000-0002-4009-2478
University of Pittsburgh · USEwha Womans University · KRNorwegian University of Science and Technology · NO

Funding

Watching cooperative interactions between base and nucleotide excision repair proteinsR35ES031638 · NIEHS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI Bennett Van Houten · 2020 to 2026
$6.2M
DNA damage recognition by nucleotide excision repair proteinsR01ES019566 · NIEHS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI VAN HOUTEN, BENNETT · 2011 to 2020
$3.9M
Damage Sensor role of UV-DDB during base excision repairR01ES028686 · NIEHS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI VAN HOUTEN, BENNETT · 2018 to 2019
$729k
NIEHS NIH HHS R01 ES019566NIEHS NIH HHS R01 ES028686NIEHS NIH HHS R35 ES031638
6 · The paper itself

Abstract

UV-DDB is a DNA damage recognition protein recently discovered to participate in the removal of 8-oxo-7,8-dihydro-2'-deoxyguanosine (8-oxoG) by stimulating multiple steps of base excision repair (BER). In this study, we examined whether UV-DDB has a wider role in BER besides oxidized bases and found it has specificity for two known DNA substrates of alkyladenine glycosylase (AAG)/N-methylpurine DNA glycosylase (MPG): 1, N6-ethenoadenine (ϵA) and hypoxanthine. Gel mobility shift assays show that UV-DDB recognizes these two lesions 4-5 times better than non-damaged DNA. Biochemical studies indicated that UV-DDB stimulated AAG activity on both substrates by 4- to 5-fold. Native gels indicated UV-DDB forms a transient complex with AAG to help facilitate release of AAG from the abasic site product. Single molecule experiments confirmed the interaction and showed that UV-DDB can act to displace AAG from abasic sites. Cells when treated with methyl methanesulfonate resulted in foci containing AAG and UV-DDB that developed over the course of several hours after treatment. While colocalization did not reach 100%, foci containing AAG and UV-DDB reached a maximum at three hours post treatment. Together these data indicate that UV-DDB plays an important role in facilitating the repair of AAG substrates.

Indexed as

DNA GlycosylasesDNADNA DamageDNA RepairHydrocarbons, ChlorinatedDDBDNADNA GlycosylasesHydrocarbons, Chlorinated

Identifiers

PMID36511855
PMCPMC9825174
OpenAlexW4311288254

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.