Evidence map›Paper›PMID 40161823›Full record

ArticlebioRxiv : the preprint server for biology2025

"The

Luke G O'Neal, Madeline N Drucker, Ngoc Khanh Lai, Ashley F Clemente, Alyssa P Campbell, Lindsey E Way, Sinwoo Hong, Emily E Holmes, Sarah J Rancic, Nicholas Sawyer and 2 more

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors.

Luke G O'NealDepartment of Chemistry and Biochemistry, Fordham University, Bronx, NY 10458.ORCID 0009-0002-0293-837X
Madeline N DruckerDepartment of Chemistry and Biochemistry, Fordham University, Bronx, NY 10458.
Ngoc Khanh LaiDepartment of Biology, Indiana University, Bloomington, IN 47405.
Ashley F ClementeDepartment of Chemistry and Biochemistry, Fordham University, Bronx, NY 10458.
Alyssa P CampbellDepartment of Chemistry and Biochemistry, Fordham University, Bronx, NY 10458.
Lindsey E WayDepartment of Biology, Indiana University, Bloomington, IN 47405.
Sinwoo HongDepartment of Chemistry and Biochemistry, Fordham University, Bronx, NY 10458.
Emily E HolmesDepartment of Chemistry and Biochemistry, Fordham University, Bronx, NY 10458.
Sarah J RancicDepartment of Chemistry and Biochemistry, Fordham University, Bronx, NY 10458.
Nicholas SawyerDepartment of Chemistry and Biochemistry, Fordham University, Bronx, NY 10458.ORCID 0000-0002-6393-5626
Xindan WangDepartment of Biology, Indiana University, Bloomington, IN 47405.ORCID 0000-0001-6458-180X
Elizabeth S ThrallDepartment of Chemistry and Biochemistry, Fordham University, Bronx, NY 10458.ORCID 0000-0002-7670-3939

Funding

Physicochemical properties driving membraneless organelle assembly in bacteriaR01GM143182 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BITEEN, JULIE, MEYER, ANNE SARA · 2021 to 2024
$2.4M
Determining the molecular basis of gene silencing by MucR and defining its role in Brucella virulenceR01AI172822 · NIAID · EAST CAROLINA UNIVERSITY · PI ROY M ROOP · 2023 to 2026
$2.3M
How bacterial SMC complexes organize chromosomes (Equipment Supplement)R01GM141242 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI WANG, XINDAN · 2021 to 2025
$1.8M
Molecular Mechanisms of Y-Family Translesion Polymerase Activity in Bacillus subtilisR15GM151677 · NIGMS · FORDHAM UNIVERSITY · PI THRALL, ELIZABETH SIMMONS · 2023 to 2023
$495k
NIAID NIH HHS R01 AI172822NIGMS NIH HHS R01 GM141242NIGMS NIH HHS R01 GM143182NIGMS NIH HHS R15 GM151677
6 · The paper itself

Abstract

Ring-shaped sliding clamp proteins are essential components of the replication machinery, the replisome, across all domains of life. In bacteria, DNA polymerases bind the sliding clamp, DnaN, through conserved short peptide sequences called clamp-binding motifs. Clamp binding increases the processivity and rate of DNA synthesis and is generally required for polymerase activity. The current understanding of clamp-polymerase interactions was elucidated in the model bacterium

Indexed as

DNA polymeraseDNA replicationsingle-molecule imagingsliding clampsuper-resolution microscopy

Identifiers

PMID40161823
PMCPMC11952451

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.