Evidence map›Paper›PMID 29722926›Full record

ArticleAngewandte Chemie (International ed. in English)2018

A Minimal Functional Complex of Cytochrome P450 and FBD of Cytochrome P450 Reductase in Nanodiscs.

Elke Prade, Mukesh Mahajan, Sang-Choul Im, Meng Zhang, Katherine A Gentry, 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 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
6.8field-weighted citation impact, top 3% 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

23 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. The Nanodisc System for Investigating Protein-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2026
    Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Detergent-free isolation of CYP450-reductase's FMN-binding domain inChemical communications (Cambridge, England) · 2022
    Article
  8. Article
  9. Solid-State NMR Study to Probe the Effects of Divalent Metal Ions (CaLangmuir : the ACS journal of surfaces and colloids · 2021
    Article
  10. Article
  11. Conformational Landscape of Cytochrome P450 Reductase Interactions.International journal of molecular sciences · 2021
    Article
  12. Article
  13. Article
  14. Article
  15. Conformational turn triggers regio-selectivity in the bioactivation of thiophene-contained compounds mediated by cytochrome P450.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019
    Article
  16. Article
  17. Article
  18. The hydrodynamic motion of Nanodiscs.Chemistry and physics of lipids · 2019
    Article
  19. Article
  20. Polymer nanodiscs: Advantages and limitations.Chemistry and physics of lipids · 2019
    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

8 authors at 2 institutions in 1 country.

Elke PradeBiophysics and Department of Chemistry, University of Michigan, Ann Arbor, MI, 48109-1055, USA.
Mukesh MahajanBiophysics and Department of Chemistry, University of Michigan, Ann Arbor, MI, 48109-1055, USA.
Sang-Choul ImDepartment of Anesthesiology, University of Michigan and VA Medical Center, Ann Arbor, MI, 48105-1055, USA.
Meng ZhangBiophysics and Department of Chemistry, University of Michigan, Ann Arbor, MI, 48109-1055, USA.
Katherine A GentryBiophysics and Department of Chemistry, University of Michigan, Ann Arbor, MI, 48109-1055, USA.
G M AnantharamaiahDepartment of Medicine, UAB Medical Center, Birmingham, AL, 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 · 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

Structural interactions that enable electron transfer to cytochrome-P450 (CYP450) from its redox partner CYP450-reductase (CPR) are a vital prerequisite for its catalytic mechanism. The first structural model for the membrane-bound functional complex to reveal interactions between the full-length CYP450 and a minimal domain of CPR is now reported. The results suggest that anchorage of the proteins in a lipid bilayer is a minimal requirement for CYP450 catalytic function. Akin to cytochrome-b

Indexed as

Cytochrome P-450 Enzyme SystemFlavin MononucleotideModels, MolecularNanostructuresOxidation-ReductionPeptidesCytochrome P-450 Enzyme SystemFlavin MononucleotidePeptidescytochrome P450cytochrome P450 reductasemembrane proteinsnanodiscs

Identifiers

PMID29722926
PMCPMC6248338
OpenAlexW2800908572

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.