Evidence map›Paper›PMID 40858268›Full record

ReviewOpen biology2025

The curious family of cytochrome P450 4F fatty acid ω-hydroxylases: recent developments in their function and relevance for human health.

Brisa Caroline Alves Chagas, Huiting Jia, Bjoern Brixius, Simone Brixius-Anderko

Abstract readReview
In one paragraph

Review in Open biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. 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

4 authors.

Brisa Caroline Alves ChagasDepartment of Pharmaceutical Sciences, University of Pittsburgh School of Pharmacy, Pittsburgh, PA, USA.ORCID 0000-0001-8975-0438
Huiting JiaDepartment of Pharmaceutical Sciences, University of Pittsburgh School of Pharmacy, Pittsburgh, PA, USA.
Bjoern BrixiusDepartment of Pharmaceutical Sciences, University of Pittsburgh School of Pharmacy, Pittsburgh, PA, USA.
Simone Brixius-AnderkoDepartment of Pharmaceutical Sciences, University of Pittsburgh School of Pharmacy, Pittsburgh, PA, USA.ORCID 0000-0002-3036-9285

Funding

STUDIES ON FATTY ACID METABOLIZING CYTOCHROME P450 ENZYMESR35GM155319 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI Simone Brixius-Anderko · 2024 to 2026
$1.1M
NIGMS NIH HHS R35 GM155319
6 · The paper itself

Abstract

Cytochrome P450 enzymes (CYP, P450) are indispensable for human health and catalyse a plethora of reactions contributing to the clearance of xenobiotics, steroid and bile acid biosynthesis, and the functionalization of vitamins in the human body. The family of CYP4F fatty acid ω-hydroxylases consists of five isoforms, CYP4F2, CYP4F3A, CYP4F3B, CYP4F11 and CYP4F22, which share a high amino acid sequence similarity but assume different physiological functions in humans. While CYP4F2 and CYP4F3B are the major enzymes producing a lipid mediator from arachidonic acid, CYP4F3A inactivates leukotriene B4 as anti-inflammatory response, CYP4F11 is capable of effectively metabolizing drugs, and CYP4F22 contributes to a healthy skin barrier. In this review, we provide an overview of recent developments in CYP4F function and discuss potential future directions underlining their growing relevance in human health and disease.

Indexed as

Cytochrome P-450 Enzyme SystemCytochrome P450 Family 4AnimalsHumansCYP4F2 protein, humanCytochrome P-450 Enzyme SystemCytochrome P450 Family 4arachidonic acidcytochrome P450fatty acid ω-hydroxylasesmetabolic diseases

Identifiers

PMID40858268
PMCPMC12380495

What OpenQuestion holds

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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.