Evidence map›Paper›PMID 40952473›Full record

ArticleThe Journal of membrane biology2025

Bilayer-Dependent Recognition of Docosahexaenoic Acid by the Transmembrane Domain of FATP3.

Yi Ding, Yonghua Wang, Wen Chen

Abstract read
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In one paragraph

Article in The Journal of membrane 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

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

3 authors.

Yi DingSouth China University of Technology, Guangzhou, China.
Yonghua WangSouth China University of Technology, Guangzhou, China.
Wen ChenSouth China University of Technology, Guangzhou, China. wenchen@scut.edu.cn.ORCID http://orcid.org/0000-0001-7387-4532

Funding

National Key Research and Development Program of China 2022YFC2104905
6 · The paper itself

Abstract

Fatty acid Transport Protein 3 (FATP3) is a single-pass transmembrane protein implicated in the uptake and intracellular transport of long-chain fatty acids, yet the molecular contribution of its transmembrane domain (TMD) remains poorly defined. Here, we establish an efficient and reproducible strategy for heterologous expression, purification, and in vitro reconstitution of FATP3-TMD. FATP3-TMD was over-expressed in Escherichia coli as a TrpLE fusion, liberated by cyanogen-bromide cleavage and polished by one-step reverse-phase HPLC, yielding milligram quantities of highly pure peptide.

Indexed as

Docosahexaenoic AcidsFatty Acid Transport ProteinsLipid BilayersEscherichia coliHumansProtein DomainsDocosahexaenoic AcidsFatty Acid Transport ProteinsLipid BilayersBicellesDHAFATP3-TMDMicellesNMR

Identifiers

What OpenQuestion holds

Textmetadata
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.