Evidence map›Paper›PMID 29475945›Full record

ArticleThe Journal of biological chemistry2018

Solution structure of the cytochrome P450 reductase-cytochrome

Samuel L Freeman, Anne Martel, Juliette M Devos, Jaswir Basran, Emma L Raven, Gordon C K Roberts

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Conformational Landscape of Cytochrome P450 Reductase Interactions.International journal of molecular sciences · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. 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

6 authors.

Samuel L FreemanFrom the Departments of Chemistry and.
Anne MartelInstitut Laue-Langevin, 71 avenue des Martyrs, 38042 Grenoble, France.
Juliette M DevosInstitut Laue-Langevin, 71 avenue des Martyrs, 38042 Grenoble, France.
Jaswir BasranFrom the Departments of Chemistry and.
Emma L RavenFrom the Departments of Chemistry and emma.raven@le.ac.uk.
Gordon C K RobertsLeicester Institute of Structural and Chemical Biology, University of Leicester, Leicester LE1 7RH, United Kingdom and gcr@le.ac.uk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Electron transfer in all living organisms critically relies on formation of complexes between the proteins involved. The function of these complexes requires specificity of the interaction to allow for selective electron transfer but also a fast turnover of the complex, and they are therefore often transient in nature, making them challenging to study. Here, using small-angle neutron scattering with contrast matching with deuterated protein, we report the solution structure of the electron transfer complex between cytochrome P450 reductase (CPR) and its electron transfer partner cytochrome

Indexed as

Cytochromes cElectron TransportFlavin-Adenine DinucleotideFlavin MononucleotideKineticsNADPNADPH-Ferrihemoprotein ReductaseNeutron DiffractionNeutronsOxidation-ReductionProtein Structure, TertiaryScattering, Small AngleStructure-Activity RelationshipThermodynamicsCytochromes cFlavin-Adenine DinucleotideFlavin MononucleotideNADPNADPH-Ferrihemoprotein Reductasecytochrome ccytochrome P450cytochrome P450 reductaseelectron transferneutron scatteringprotein-protein interactionprotein structural dynamicsprotein structureSANSsolution structuretransient complex

Identifiers

PMID29475945
PMCPMC5892573

What OpenQuestion holds

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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.