Evidence map›Paper›PMID 42699739›Full record

ArticleCurrent research in food science2026

Investigating the structural changes of myosin under high pressure processing by molecular dynamics simulations.

Xiaoyun Wang, Jie Tang, Hosahalli S Ramaswamy, Hanying Duan, Chao Wang

Abstract read
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In one paragraph

Article in Current research in food science, 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

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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.

Xiaoyun WangDepartment of Food Science and Technology, Jinan University, Guangzhou, 510632, China.
Jie TangDepartment of Food Science and Technology, Jinan University, Guangzhou, 510632, China.
Hosahalli S RamaswamyDepartment of Food Science and Agricultural Chemistry, Macdonald Campus of McGill University, Montreal, QC, Canada.
Hanying DuanDepartment of Food Science and Technology, Jinan University, Guangzhou, 510632, China.
Chao WangDepartment of Food Science and Technology, Jinan University, Guangzhou, 510632, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

High-pressure processing (HPP) exerts paradoxical effects on myosin, simultaneously promoting molecular unfolding and supramolecular aggregation, yet the underlying mechanisms remain unresolved at atomic resolution. This study employed all-atom molecular dynamics simulations at gradient pressures (0.1-450 MPa) using complementary monomer and motor domain contact models. The monomer exhibited pressure-induced disruption of intramolecular hydrogen bonds, increased per-residue flexibility (RMSF) and radius of gyration (

Indexed as

Binding free energyHigh-pressure processingMolecular dynamics simulationMyosinProtein conformational dynamics

Identifiers

PMID42699739
PMCPMC13544339

What OpenQuestion holds

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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.