Evidence map›Paper›PMID 23297356›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2013

Unusual properties of the cytochrome P450 superfamily.

David C Lamb, Michael R Waterman

Open access · bronzeAbstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
9.2field-weighted citation impact, top 2% 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

39 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. The Role of Cytochrome P450 AbyV in the Final Stages of Abyssomicin C Biosynthesis.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023
    Article
  9. Review
  10. Review
  11. Article
  12. 25-hydroxyvitamin D-1α-hydroxylase (CYP27B1) induces ectopic calcification.Journal of clinical biochemistry and nutrition · 2022
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  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

2 authors at 2 institutions in 2 countries.

David C LambInstitute of Life Science, Medical School, Swansea University, Singleton Park, Swansea SA2 8PP, UK. d.c.lamb@swansea.ac.uk
Michael R Waterman
Swansea University · GBVanderbilt University · US

Funding

S. coelicolor P450s: Structure/Function/EngineeringR01GM069970 · NIGMS · VANDERBILT UNIVERSITY · PI GUENGERICH, F PETER, WATERMAN, MICHAEL R · 2004 to 2011
$3.4M
NIGMS NIH HHS R01 GM069970NIGMS NIH HHS R01 GM69970Wellcome Trust
6 · The paper itself

Abstract

During the early years of cytochrome P450 research, a picture of conserved properties arose from studies of mammalian forms of these monooxygenases. They included the protohaem prosthetic group, the cysteine residue that coordinates to the haem iron and the reduced CO difference spectrum. Alternatively, the most variable feature of P450s was the enzymatic activities, which led to the conclusion that there are a large number of these enzymes, most of which have yet to be discovered. More recently, studies of these enzymes in other eukaryotes and in prokaryotes have led to the discovery of unexpected P450 properties. Many are variations of the original properties, whereas others are difficult to explain because of their unique nature relative to the rest of the known members of the superfamily. These novel properties expand our appreciation of the broad view of P450 structure and function, and generate curiosity concerning the evolution of P450s. In some cases, structural properties, previously not found in P450s, can lead to enzymatic activities impacting the biological function of organisms containing these enzymes; whereas, in other cases, the biological reason for the variations are not easily understood. Herein, we present particularly interesting examples in detail rather than cataloguing them all.

Indexed as

Biological EvolutionProtein Processing, Post-TranslationalBacteriaBinding SitesCytochrome P-450 Enzyme SystemElectron TransportEnzyme ActivationEukaryotaHemeHydroxylationModels, MolecularOxidation-ReductionOxygenPhosphorylationProtein BindingProtein Structure, TertiaryCytochrome P-450 Enzyme SystemHemeOxygen

Identifiers

PMID23297356
PMCPMC3538423
OpenAlexW2087955696

What OpenQuestion holds

Textmetadata
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.