Evidence map›Paper›PMID 38780930›Full record

ArticleBiochemistry2024

Modifying the Basicity of the dNTP Leaving Group Modulates Precatalytic Conformational Changes of DNA Polymerase β.

Khadijeh S Alnajjar, Katarina Wang, Isabel Alvarado-Cruz, Cristian Chavira, Amirsoheil Negahbani, Maryam Nakhjiri, Corinne Minard, Beatriz Garcia-Barboza, Boris A Kashemirov, Charles E McKenna and 2 more

Abstract read
In one paragraph

Article in Biochemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
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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

12 authors.

Khadijeh S AlnajjarDepartment of Cellular and Molecular Medicine, University of Arizona Cancer Center, University of Arizona, Tucson, Arizona 85724, United States.
Katarina WangTherapeutic Radiology Department, Yale University, New Haven, Connecticut 06520, United States.
Isabel Alvarado-CruzDepartment of Cellular and Molecular Medicine, University of Arizona Cancer Center, University of Arizona, Tucson, Arizona 85724, United States.
Cristian ChaviraFred and Pamela Buffett Cancer Center and Eppley Institute for Cancer Research, Omaha, Nebraska 68198, United States.ORCID 0009-0005-5901-8621
Amirsoheil NegahbaniDepartment of Chemistry, University of Southern California, Los Angeles, California 90089, United States.
Maryam NakhjiriDepartment of Chemistry, University of Southern California, Los Angeles, California 90089, United States.
Corinne MinardDepartment of Chemistry, University of Southern California, Los Angeles, California 90089, United States.
Beatriz Garcia-BarbozaDepartment of Chemistry, University of Southern California, Los Angeles, California 90089, United States.
Boris A KashemirovDepartment of Chemistry, University of Southern California, Los Angeles, California 90089, United States.
Charles E McKennaDepartment of Chemistry, University of Southern California, Los Angeles, California 90089, United States.ORCID 0000-0002-3540-6663
Myron F GoodmanDepartment of Chemistry, University of Southern California, Los Angeles, California 90089, United States.ORCID 0000-0001-9601-3284
Joann B SweasyFred and Pamela Buffett Cancer Center and Eppley Institute for Cancer Research, Omaha, Nebraska 68198, United States.ORCID 0000-0002-4503-0284

Funding

DNA POLYMERASE BETA AND MUTAGENESISR01CA080830 · NCI · YALE UNIVERSITY · PI SWEASY, JOANN B. · 1999 to 2018
$6.1M
Molecular Mechanisms of Human DNA Polymerase Beta Catalysis, Fidelity and Selective InhibitionU19CA177547 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI GOODMAN, MYRON · 2013 to 2017
$5.5M
The role of cysteines in the response of 8-oxoguanine glycosylase (OGG1) to oxidative stressK99ES029555 · NIEHS · UNIVERSITY OF ARIZONA · PI ALNAJJAR, KHADIJEH · 2019 to 2020
$198k
NCI NIH HHS R01 CA080830NCI NIH HHS U19 CA177547NIEHS NIH HHS K99 ES029555
6 · The paper itself

Abstract

The catalytic function of DNA polymerase β (pol β) fulfills the gap-filling requirement of the base excision DNA repair pathway by incorporating a single nucleotide into a gapped DNA substrate resulting from the removal of damaged DNA bases. Most importantly, pol β can select the correct nucleotide from a pool of similarly structured nucleotides to incorporate into DNA in order to prevent the accumulation of mutations in the genome. Pol β is likely to employ various mechanisms for substrate selection. Here, we use dCTP analogues that have been modified at the β,γ-bridging group of the triphosphate moiety to monitor the effect of leaving group basicity of the incoming nucleotide on precatalytic conformational changes, which are important for catalysis and selectivity. It has been previously shown that there is a linear free energy relationship between leaving group p

Indexed as

DNA Polymerase betaProtein ConformationDeoxycytosine NucleotidesDNADNA RepairHumansKineticsModels, MolecularSubstrate Specificity2'-deoxycytidine 5'-triphosphateDeoxycytosine NucleotidesDNADNA Polymerase betaPOLB protein, human

Identifiers

PMID38780930
PMCPMC11155676

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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.