Evidence map›Paper›PMID 41388968›Full record

ArticleBiochemistry2026

Mechanistic and Molecular Dynamics Studies Reveal that Increased Loop 3 Mobility Alters Substrate Capture in an NADH:Quinone Oxidoreductase.

Benjamin D Dratch, Daniel Ouedraogo, Jacob Ball, Donald Hamelberg, Giovanni Gadda

Abstract read
In one paragraph

Article in Biochemistry, 2026. 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

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.

Benjamin D DratchDepartment of Chemistry, Georgia State University, Atlanta, Georgia 30302-3965, United States.
Daniel OuedraogoDepartment of Chemistry, Georgia State University, Atlanta, Georgia 30302-3965, United States.
Jacob BallDepartment of Chemistry, Georgia State University, Atlanta, Georgia 30302-3965, United States.
Donald HamelbergDepartment of Chemistry, Georgia State University, Atlanta, Georgia 30302-3965, United States.ORCID 0000-0002-3785-3037
Giovanni GaddaDepartment of Chemistry, Georgia State University, Atlanta, Georgia 30302-3965, United States.ORCID 0000-0002-7508-4195

Funding

Developing computational tools to complement experiments in understanding biomolecular function from conformational ensemblesR35GM153718 · NIGMS · GEORGIA STATE UNIVERSITY · PI Donald Hamelberg · 2024 to 2026
$1.2M
NIGMS NIH HHS R35 GM153718
6 · The paper itself

Abstract

Dynamic protein loops can act as molecular gates that stabilize enzyme-substrate complexes, yet the underlying motions are poorly defined. Here, we dissect the role of loop 3 in an NADH:quinone oxidoreductase (NQO, UniProt Q9I4V0) from

Indexed as

Bacterial ProteinsPseudomonas aeruginosaQuinone ReductasesKineticsMolecular Dynamics SimulationNADProtein ConformationSubstrate SpecificityUbiquinoneBacterial ProteinsNADQuinone ReductasesUbiquinone

Identifiers

PMID41388968
PMCPMC12781114

What OpenQuestion holds

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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.