Evidence map›Paper›PMID 35238634›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Interlocking activities of DNA polymerase β in the base excision repair pathway.

Adarsh Kumar, Andrew J Reed, Walter J Zahurancik, Sasha M Daskalova, Sidney M Hecht, Zucai Suo

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

18 citing papers in PubMed, 26 citations in OpenAlex.

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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

6 authors at 3 institutions in 1 country.

Adarsh KumarDepartment of Biomedical Sciences, Florida State University College of Medicine, Tallahassee, FL 32306.
Andrew J ReedThe Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210.
Walter J ZahurancikThe Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210.
Sasha M DaskalovaBiodesign Center for BioEnergetics and School of Molecular Sciences, Arizona State University, Tempe, AZ 85287.ORCID 0000-0002-9946-6737
Sidney M HechtBiodesign Center for BioEnergetics and School of Molecular Sciences, Arizona State University, Tempe, AZ 85287.ORCID 0000-0002-5429-2462
Zucai SuoDepartment of Biomedical Sciences, Florida State University College of Medicine, Tallahassee, FL 32306.ORCID 0000-0003-3871-3420
BioEnergetics (United States) · USFlorida State University · USThe Ohio State University · US

Funding

Investigation of human DNA polymerase epsilon variantsR01ES028271 · NIEHS · TULANE UNIVERSITY OF LOUISIANA · PI Zachary F Pursell · 2017 to 2026
$3.6M
Biological Regulation Studied In Vitro and In Cellulo with Modified ProteinsR35GM140819 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI Sidney M. Hecht · 2021 to 2026
$2.9M
Investigation of DNA base excision repairR01GM122093 · NIGMS · FLORIDA STATE UNIVERSITY · PI SUO, ZUCAI · 2018 to 2021
$1.2M
NIEHS NIH HHS R01 ES028271NIGMS NIH HHS R01 GM122093NIGMS NIH HHS R35 GM140819
6 · The paper itself

Abstract

SignificanceBase excision repair (BER) is one of the major DNA repair pathways used to fix a myriad of cellular DNA lesions. The enzymes involved in BER, including DNA polymerase β (Polβ), have been identified and characterized, but how they act together to efficiently perform BER has not been fully understood. Through gel electrophoresis, mass spectrometry, and kinetic analysis, we discovered that the two enzymatic activities of Polβ can be interlocked, rather than functioning independently from each other, when processing DNA intermediates formed in BER. The finding prompted us to hypothesize a modified BER pathway. Through conventional and time-resolved X-ray crystallography, we solved 11 high-resolution crystal structures of cross-linked Polβ complexes and proposed a detailed chemical mechanism for Polβ's 5'-deoxyribose-5-phosphate lyase activity.

Indexed as

DNA DamageDNA RepairCrystallography, X-RayDNADNA Polymerase betaElectrophoresis, Polyacrylamide GelKineticsMass SpectrometryProtein ConformationSchiff BasesSubstrate SpecificityDNADNA Polymerase betaSchiff BasesDNA base excision repair pathwayDNA polymerase βdRP lyase chemical mechanismSchiff base formationβ-elimination

Identifiers

PMID35238634
PMCPMC8915974
OpenAlexW4214898670

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.