Evidence map›Paper›PMID 33982687›Full record

ArticleChemical communications (Cambridge, England)2021

Nanodisc reconstitution of flavin mononucleotide binding domain of cytochrome-P450-reductase enables high-resolution NMR probing.

Bankala Krishnarjuna, Toshio Yamazaki, G M Anantharamaiah, Ayyalusamy Ramamoorthy

Open access · greenAbstract read
In one paragraph

Article in Chemical communications (Cambridge, England), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

8 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Detergent-free isolation of CYP450-reductase's FMN-binding domain inChemical communications (Cambridge, England) · 2022
    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 3 countries.

Bankala KrishnarjunaBiophysics Program, Department of Chemistry, Biomedical Engineering, Macromolecular Science and Engineering, University of Michigan, Arbor, MI 48109, USA. ramamoor@umich.edu.
Toshio Yamazaki
G M Anantharamaiah
Ayyalusamy Ramamoorthy
University of Michigan · USRIKEN Center for Biosystems Dynamics Research · JPUniversity of Alabama at Birmingham · US

Funding

Development of biophysical approaches to investigate high-resolution structure and dynamics of membrane proteinsR35GM139573 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Ayyalusamy Ramamoorthy · 2021 to 2026
$2.0M
NIGMS NIH HHS R35 GM139573
6 · The paper itself

Abstract

Cytochrome-P450-reductase transfers electrons to cytochrome-P450 through its flavin mononucleotide binding domain (FBD). Despite the importance of membrane-anchoring for FBD function, studies have focused on its soluble domain lacking the transmembrane-domain. Here we demonstrate that the reconstitution of FBD in nanodiscs enables high-resolution NMR measurements and renders a stable conformation.

Indexed as

Nuclear Magnetic Resonance, BiomolecularBinding SitesElectron TransportFlavin MononucleotideModels, MolecularNADPH-Ferrihemoprotein ReductaseFlavin MononucleotideNADPH-Ferrihemoprotein Reductase

Identifiers

PMID33982687
PMCPMC8136615
OpenAlexW3152738732

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.