Evidence map›Paper›PMID 29385304›Full record

ArticleAngewandte Chemie (International ed. in English)2018

Cytochrome-P450-Induced Ordering of Microsomal Membranes Modulates Affinity for Drugs.

Carlo Barnaba, Bikash Ranjan Sahoo, Thirupathi Ravula, Ilce G Medina-Meza, Sang-Choul Im, G M Anantharamaiah, Lucy Waskell, Ayyalusamy Ramamoorthy

Open access · greenAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

33 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. The Nanodisc System for Investigating Protein-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2026
    Review
  3. Article
  4. Article
  5. The journal of physical chemistry. B · 2024
    Review
  6. A Review: Cytochrome P450 in Alcoholic and Non-Alcoholic Fatty Liver Disease.Diabetes, metabolic syndrome and obesity : targets and therapy · 2024
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
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  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Functional Assembly ofBiomolecules · 2021
    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

8 authors at 3 institutions in 1 country.

Carlo BarnabaBiophysics and Department of Chemistry, University of Michigan, Ann Arbor, MI, 48109-1055, USA.
Bikash Ranjan SahooBiophysics and Department of Chemistry, University of Michigan, Ann Arbor, MI, 48109-1055, USA.
Thirupathi RavulaBiophysics and Department of Chemistry, University of Michigan, Ann Arbor, MI, 48109-1055, USA.
Ilce G Medina-MezaDepartment of Biosystems and Agricultural Engineering, Michigan State University, East Lansing, MI, 48824-1323, USA.
Sang-Choul ImDepartment of Anesthesiology, University of Michigan and VA Medical Center, Ann Arbor, MI, 48105-1055, USA.
G M AnantharamaiahDepartment of Medicine, UAB Medical Center, Birmingham, Alabama, 35294, USA.
Lucy WaskellDepartment of Anesthesiology, University of Michigan and VA Medical Center, Ann Arbor, MI, 48105-1055, USA.
Ayyalusamy RamamoorthyBiophysics and Department of Chemistry, University of Michigan, Ann Arbor, MI, 48109-1055, USA.ORCID 0000-0003-1964-1900
University of Michigan · USBirmingham VA Medical Center · USMichigan State University · US

Funding

Supplement: Investigation of Membrane-Bound Cytochromes-P450-b5 InteractionsR01GM084018 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2009 to 2018
$3.8M
NIGMS NIH HHS R01 GM084018
6 · The paper itself

Abstract

Although membrane environment is known to boost drug metabolism by mammalian cytochrome P450s, the factors that stabilize the structural folding and enhance protein function are unclear. In this study, we use peptide-based lipid nanodiscs to "trap" the lipid boundaries of microsomal cytochrome P450 2B4. We report the first evidence that CYP2B4 is able to induce the formation of raft domains in a biomimetic compound of the endoplasmic reticulum. NMR experiments were used to identify and quantitatively determine the lipids present in nanodiscs. A combination of biophysical experiments and molecular dynamics simulations revealed a sphingomyelin binding region in CYP2B4. The protein-induced lipid raft formation increased the thermal stability of P450 and dramatically altered ligand binding kinetics of the hydrophilic ligand BHT. These results unveil membrane/protein dynamics that contribute to the delicate mechanism of redox catalysis in lipid membrane.

Indexed as

AnimalsCytochrome P-450 Enzyme SystemEndoplasmic ReticulumHumansKineticsMembrane LipidsMembrane ProteinsMolecular Dynamics SimulationNanoparticlesProtein BindingSphingomyelinsCytochrome P-450 Enzyme SystemMembrane LipidsMembrane ProteinsSphingomyelinsbiophysicshemeproteinslipidsmembranesnanodiscs

Identifiers

PMID29385304
PMCPMC6289274
OpenAlexW2790255702

What OpenQuestion holds

Textmetadata
LicenceTDM
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.