Evidence map›Paper›PMID 21103389›Full record

ReviewFuture medicinal chemistry2010

Structural features of cytochromes P450 and ligands that affect drug metabolism as revealed by X-ray crystallography and NMR.

Sean C Gay, Arthur G Roberts, James R Halpert

Erratum issuedAbstract readReview
In one paragraph

Review in Future medicinal chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing 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

47 citing papers in PubMed.

  1. Unraveling enantioselective metabolism: Human cytochrome P450s in arachidonic acid biotransformation.Drug metabolism and disposition: the biological fate of chemicals · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. 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. Genome-wide analysis of theFrontiers in plant science · 2024
    Article
  10. Article
  11. Review
  12. Article
  13. The Role of Cytochrome P450 AbyV in the Final Stages of Abyssomicin C Biosynthesis.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Functional Characterization of 21 Rare AllelicJournal of personalized medicine · 2021
    Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

3 authors.

Sean C Gayscgay@ucsd.edu
Arthur G Roberts
James R Halpert

Funding

Synthetic Organic Chemistry CoreP30ES006676 · NIEHS · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI ELFERINK, CORNELIS JOHAN · 1995 to 2017
$21.7M
STRUCTURAL BASIS OF SELECTIVE P-450 INACTIVATIONR01ES003619 · NIEHS · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI HALPERT, JAMES R · 1985 to 2016
$6.2M
NIEHS NIH HHS ES003619NIEHS NIH HHS ES006676NIEHS NIH HHS P30 ES006676NIEHS NIH HHS R01 ES003619
6 · The paper itself

Abstract

Cytochromes P450 (P450s) play a major role in the clearance of drugs, toxins, and environmental pollutants. Additionally, metabolism by P450s can result in toxic or carcinogenic products. The metabolism of pharmaceuticals by P450s is a major concern during the design of new drug candidates. Determining the interactions between P450s and compounds of very diverse structures is complicated by the variability in P450-ligand interactions. Understanding the protein structural elements and the chemical attributes of ligands that dictate their orientation in the P450 active site will aid in the development of effective and safe therapeutic agents. The goal of this review is to describe P450-ligand interactions from two perspectives. The first is the various structural elements that microsomal P450s have at their disposal to assume the different conformations observed in X-ray crystal structures. The second is P450-ligand dynamics analyzed by NMR relaxation studies.

Indexed as

PharmacokineticsCrystallography, X-RayCytochrome P-450 Enzyme SystemLigandsMagnetic Resonance SpectroscopyModels, MolecularProtein ConformationSubstrate SpecificityCytochrome P-450 Enzyme SystemLigandsCytochrome P450drug metabolismmammalianmicrosomalNMRP450plasticityprotein structurexenobioticX-ray crystallography

Identifiers

PMID21103389
PMCPMC2987628

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.