Evidence map›Paper›PMID 41898684›Full record

ArticleInternational journal of molecular sciences2026

Temperature-Dependent Active-Site Rearrangements of PETaseSM14: Insights from Molecular Dynamics Simulations.

Ki Hyun Nam

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

1 author.

Ki Hyun NamCollege of General Education, Kookmin University, Seoul 02707, Republic of Korea.ORCID 0000-0003-3268-354X

Funding

Pohang Accelerator Laboratory XFEL2025-01
6 · The paper itself

Abstract

Polyethylene terephthalate (PET) is a synthetic polymer that is widely used in the production of textiles, packaging materials, and beverage bottles. However, its high durability and resistance to abiotic degradation result in serious environmental and health problems. PETase is an enzyme that can depolymerize PET into value-added products, thereby providing an environmentally friendly strategy for PET recycling. PETaseSM14 from a marine sponge,

Indexed as

Bacterial ProteinsHydrolasesMolecular Dynamics SimulationPolyethylene TerephthalatesStreptomycesAnimalsCatalytic DomainProtein ConformationSubstrate SpecificityTemperatureBacterial ProteinsHydrolasesPolyethylene Terephthalatesmolecular dynamics simulationPETasepolyethylene terephthalatesubstrate binding clefttemperature

Identifiers

PMID41898684
PMCPMC13026930

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.