Evidence map›Paper›PMID 28083596›Full record

ReviewCellular and molecular life sciences : CMLS2017

Cytochrome P450 2U1, a very peculiar member of the human P450s family.

L Dhers, L Ducassou, J-L Boucher, D Mansuy

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.3field-weighted citation impact, top 10% of its field
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

16 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Genetic pleiotropy between pulmonary function and age-related traits: The Long Life Family Study.The journals of gerontology. Series A, Biological sciences and medical sciences · 2022
    Article
  8. Review
  9. Human Orphan Cytochromes P450: An Update.Current drug metabolism · 2022
    Article
  10. Article
  11. Review
  12. Article
  13. Structural insights into the role of the acid-alcohol pair of residues required for dioxygen activation in cytochrome P450 enzymes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Article
  14. Article
  15. Review
  16. 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 at 3 institutions in 1 country.

L DhersUMR 8601 CNRS, Université Paris Descartes, Paris Sorbonne Cité, 45 rue des Saints Pères, 75006, Paris, France.
L DucassouUMR 8601 CNRS, Université Paris Descartes, Paris Sorbonne Cité, 45 rue des Saints Pères, 75006, Paris, France.
J-L BoucherUMR 8601 CNRS, Université Paris Descartes, Paris Sorbonne Cité, 45 rue des Saints Pères, 75006, Paris, France. jean-luc.boucher@parisdescartes.fr.
D MansuyUMR 8601 CNRS, Université Paris Descartes, Paris Sorbonne Cité, 45 rue des Saints Pères, 75006, Paris, France.
Centre National de la Recherche Scientifique · FRDélégation Paris 5 · FRUniversité Paris Cité · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytochrome P450 2U1 (CYP2U1) exhibits several distinctive characteristics among the 57 human CYPs, such as its presence in almost all living organisms with a highly conserved sequence, its particular gene organization with only five exons, its major location in thymus and brain, and its protein sequence involving an unusually long N-terminal region containing 8 proline residues and an insert of about 20 amino acids containing 5 arginine residues after the transmembrane helix. Few substrates, including fatty acids, N-arachidonoylserotonin (AS), and some drugs, have been reported so far. However, its biological roles remain largely unknown, even though CYP2U1 mutations have been involved in some pathological situations, such as complicated forms of hereditary spastic paraplegia. These data together with its ability to hydroxylate some fatty acids and AS suggest its possible role in lipid metabolism.

Indexed as

Amino Acid SequenceAnimalsArachidonic AcidsBrainCytochrome P450 Family 2Fatty AcidsHumansHydroxylationMolecular Docking SimulationMutationSequence AlignmentSerotoninSpastic Paraplegia, HereditarySubstrate SpecificityThymus GlandArachidonic AcidsarachidonoylserotoninCYP2U1 protein, humanCytochrome P450 Family 2Fatty AcidsSerotoninBrainFatty acid hydroxylationHereditary spastic paraplegiaN-ArachidonoylserotoninOrphan cytochrome P450Thymus

Identifiers

PMID28083596
PMCPMC11107762
OpenAlexW2576967464

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.