Evidence map›Paper›PMID 30633872›Full record

ArticleJournal of molecular biology2019

Divalent Cations Alter the Rate-Limiting Step of PrimPol-Catalyzed DNA Elongation.

Wenyan Xu, Wenxin Zhao, Nana Morehouse, Maya O Tree, Linlin Zhao

Abstract read
In one paragraph

Article in Journal of molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

10 citing papers in PubMed, 14 citations in OpenAlex.

  1. Mouse PrimPol Outperforms Its Human Counterpart as a Robust DNA Primase.International journal of molecular sciences · 2025
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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

5 authors at 1 institution in 1 country.

Wenyan XuDepartment of Chemistry and Biochemistry, Central Michigan University, Mount Pleasant, MI 48859, USA.
Wenxin ZhaoDepartment of Chemistry and Biochemistry, Central Michigan University, Mount Pleasant, MI 48859, USA.
Nana MorehouseDepartment of Chemistry and Biochemistry, Central Michigan University, Mount Pleasant, MI 48859, USA.
Maya O TreeDepartment of Chemistry and Biochemistry, Central Michigan University, Mount Pleasant, MI 48859, USA.
Linlin ZhaoDepartment of Chemistry and Biochemistry, Central Michigan University, Mount Pleasant, MI 48859, USA; Biochemistry, Cellular and Molecular Biology Graduate Program, Central Michigan University, Mount Pleasant, MI 48859, USA. Electronic address: linlin.zhao@cmich.edu.
Central Michigan University · US

Funding

Novel functions of PrimPol in ribonucleotide-induced genome instabilityR15GM117522 · NIGMS · CENTRAL MICHIGAN UNIVERSITY · PI ZHAO, LINLIN · 2016 to 2016
$432k
NIGMS NIH HHS R15 GM117522
6 · The paper itself

Abstract

PrimPol is the most recently discovered human DNA polymerase/primase and plays an emerging role in nuclear and mitochondrial genomic maintenance. As a member of archaeo-eukaryotic primase superfamily enzymes, PrimPol possesses DNA polymerase and primase activities that are important for replication fork progression in vitro and in cellulo. The enzymatic activities of PrimPol are critically dependent on the nucleotidyl-transfer reaction to incorporate deoxyribonucleotides successively; however, our knowledge concerning the kinetic mechanism of the reaction remains incomplete. Using enzyme kinetic analyses and computer simulations, we dissected the mechanism by which PrimPol transfers a nucleotide to a primer-template DNA, which comprises DNA binding, conformational transition, nucleotide binding, phosphoester bond formation, and dissociation steps. We obtained the rate constants of the steps by steady-state and pre-steady-state kinetic analyses and simulations. Our data demonstrate that the rate-limiting step of PrimPol-catalyzed DNA elongation depends on the metal cofactor involved. In the presence of Mn

Indexed as

CatalysisCations, DivalentDeoxyribonucleotidesDNA, CatalyticDNA-Directed DNA PolymeraseDNA PrimaseDNA PrimersDNA ReplicationHumansKineticsMultifunctional EnzymesCations, DivalentDeoxyribonucleotidesDNA, CatalyticDNA-Directed DNA PolymeraseDNA PrimaseDNA PrimersMultifunctional EnzymesPrimPol protein, humanDNA polymeraseDNA replicationenzyme kineticsenzyme mechanismenzymology

Identifiers

PMID30633872
PMCPMC6435277
OpenAlexW2909495600

What Socratic 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 Socratic graph.