Evidence map›Paper›PMID 19555717›Full record

ReviewPharmacology & therapeutics2009

Cooperative properties of cytochromes P450.

Ilia G Denisov, Daniel J Frank, Stephen G Sligar

Open access · greenAbstract readReview
In one paragraph

Review in Pharmacology & therapeutics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
8.0field-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

56 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Structure-Function Analysis of the EssentialInternational journal of molecular sciences · 2024
    Article
  6. Natural Products Inhibition of Cytochrome P450 2B6 Activity and Methadone Metabolism.Drug metabolism and disposition: the biological fate of chemicals · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Anthracycline derivatives inhibit cardiac CYP2J2.Journal of inorganic biochemistry · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Screening a Strain ofMolecules (Basel, Switzerland) · 2021
    Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Ilia G DenisovDepartment of Biochemistry, University of Illinois, Urbana, IL 61801, United States of America.
Daniel J Frank
Stephen G Sligar
University of Illinois Urbana-Champaign · US

Funding

METALLOENZYME MECHANISMSR01GM033775 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SLIGAR, STEPHEN G. · 1985 to 2014
$5.2M
HEME PROTEIN REDUCTASESR37GM031756 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SLIGAR, STEPHEN G. · 1999 to 2008
$3.1M
HEME PROTEIN REDUCTASESR01GM031756 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SLIGAR, STEPHEN G. · 1985 to 2012
$1.5M
NIGMS NIH HHS GM31756NIGMS NIH HHS R01 GM031756NIGMS NIH HHS R01 GM033775NIGMS NIH HHS R37 GM031756PHS HHS 33737
6 · The paper itself

Abstract

Cytochromes P450 form a large and important class of heme monooxygenases with a broad spectrum of substrates and corresponding functions, from steroid hormone biosynthesis to the metabolism of xenobiotics. Despite decades of study, the molecular mechanisms responsible for the complex non-Michaelis behavior observed with many members of this superfamily during metabolism, often termed 'cooperativity', remain to be fully elucidated. Although there is evidence that oligomerization may play an important role in defining the observed cooperativity, some monomeric cytochromes P450, particularly those involved in xenobiotic metabolism, also display this behavior due to their ability to simultaneously bind several substrate molecules. As a result, formation of distinct enzyme-substrate complexes with different stoichiometry and functional properties can give rise to homotropic and heterotropic cooperative behavior. This review aims to summarize the current understanding of cooperativity in cytochromes P450, with a focus on the nature of cooperative effects in monomeric enzymes.

Indexed as

AnimalsCytochrome P-450 Enzyme SystemHumansKineticsLigandsModels, ChemicalProtein BindingSubstrate SpecificityCytochrome P-450 Enzyme SystemLigands

Identifiers

PMID19555717
PMCPMC2753496
OpenAlexW1987542967

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.