Evidence map›Paper›PMID 22820933›Full record

ReviewNatural product reports2012

Diversity of P450 enzymes in the biosynthesis of natural products.

Larissa M Podust, David H Sherman

Abstract readReview
In one paragraph

Review in Natural product reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 120 papers.

0numbers the graph read from it
0cells of the map it votes in
120citing papers in PubMed
7.7field-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

120 citing papers in PubMed, 308 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Late-Stage Oxidation of C(spAngewandte Chemie (International ed. in English) · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. The Impact ofPathogens (Basel, Switzerland) · 2024
    Article
  18. Article
  19. Total Synthesis FacilitatesJournal of the American Chemical Society · 2024
    Article
  20. Review

60 more citing papers are in PubMed but not listed here.

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 1 country.

Larissa M PodustDepartment of Pathology, Molecular Structure Group and Center for Discovery and Innovation in Parasitic Diseases (CDIPD), University of California San Francisco, San Francisco, California 94158, USA. larissa.podust@ucsf.edu
David H Sherman
University of California, San Francisco · USUniversity of Michigan–Ann Arbor · US

Funding

of Natural Product based Drugs and Bioenergetic Materials from Costa Rican BiotaU01TW007404 · FIC · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SHERMAN, DAVID H · 2005 to 2013
$7.6M
Structure and Engineering of Natural Product Cytochrome P450 EnzymesR01GM078553 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MONTGOMERY, JOHN, PODUST, LARISSA M. · 2007 to 2015
$2.9M
FIC NIH HHS U01 TW007404NIGMS NIH HHS R01 GM078553
6 · The paper itself

Abstract

Diverse oxygenation patterns of natural products generated by secondary metabolic pathways in microorganisms and plants are largely achieved through the tailoring reactions catalysed by cytochrome P450 enzymes (P450s). P450s are a large family of oxidative hemoproteins found in all life forms from prokaryotes to humans. Understanding the reactivity and selectivity of these fascinating C-H bond-activating catalysts will advance their use in generating valuable pharmaceuticals and products for medicine, agriculture and industry. A major strength of this P450 group is its set of established enzyme-substrate relationships, the source of the most detailed knowledge on how P450 enzymes work. Engineering microbial-derived P450 enzymes to accommodate alternative substrates and add new functions continues to be an important near- and long-term practical goal driving the structural characterization of these molecules. Understanding the natural evolution of P450 structure-function should accelerate metabolic engineering and directed evolutionary approaches to enhance diversification of natural product structures and other biosynthetic applications.

Indexed as

Biological ProductsCatalysisCytochrome P-450 Enzyme SystemFungiHumansMolecular Sequence DataMolecular StructurePlantsBiological ProductsCytochrome P-450 Enzyme System

Identifiers

PMID22820933
PMCPMC3454455
OpenAlexW1981407107

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.