Evidence map›Paper›PMID 23661295›Full record

ArticleProtein science : a publication of the Protein Society2013

Functional studies of N-terminally modified CYP2J2 epoxygenase in model lipid bilayers.

Daniel R McDougle, Amrita Palaria, Eric Magnetta, Daryl D Meling, Aditi Das

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

24 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Anthracycline derivatives inhibit cardiac CYP2J2.Journal of inorganic biochemistry · 2022
    Article
  6. Article
  7. Nanodiscs and Mass Spectrometry: Making Membranes Fly.International journal of mass spectrometry · 2020
    Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. The relationships between cytochromes P450 and HJournal of inorganic biochemistry · 2018
    Review
  14. Article
  15. Article
  16. Anti-inflammatory ω-3 endocannabinoid epoxides.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  17. Review
  18. Article
  19. Review
  20. Review
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 at 2 institutions in 1 country.

Daniel R McDougleDepartment of Comparative Biosciences, University of Illinois Urbana-Champaign, Urbana, Illinois 61802, USA.
Amrita Palaria
Eric Magnetta
Daryl D Meling
Aditi Das
University of Illinois Urbana-Champaign · USUniversity of Massachusetts Amherst · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

CYP2J2 epoxygenase is a membrane bound cytochrome P450 that converts omega-3 and omega-6 fatty acids into physiologically active epoxides. In this work, we present a comprehensive comparison of the effects of N-terminal modifications on the properties of CYP2J2 with respect to the activity of the protein in model lipid bilayers using Nanodiscs. We demonstrate that the complete truncation of the N-terminus changes the association of this protein with the E.coli membrane but does not disrupt incorporation in the lipid bilayers of Nanodiscs. Notably, the introduction of silent mutations at the N-terminus was used to express full length CYP2J2 in E. coli while maintaining wild-type functionality. We further show that lipid bilayers are essential for the productive use of NADPH for ebastine hydroxylation by CYP2J2. Taken together, it was determined that the presence of the N-terminus is not as critical as the presence of a membrane environment for efficient electron transfer from cytochrome P450 reductase to CYP2J2 for ebastine hydroxylation in Nanodiscs. This suggests that adopting the native-like conformation of CYP2J2 and cytochrome P450 reductase in lipid bilayers is essential for effective use of reducing equivalents from NADPH for ebastine hydroxylation.

Indexed as

Amino Acid SequenceButyrophenonesCytochrome P-450 CYP2J2Cytochrome P-450 Enzyme SystemEscherichia coliHumansHydroxylationLipid BilayersModels, MolecularMolecular Sequence DataMutationNADPNanostructuresOxidation-ReductionPiperidinesProtein BindingButyrophenonesCYP2J2 protein, humanCytochrome P-450 CYP2J2Cytochrome P-450 Enzyme SystemebastineLipid BilayersNADPPiperidines

Identifiers

PMID23661295
PMCPMC3719090
OpenAlexW1942137053

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.