Evidence map›Paper›PMID 17544277›Full record

ReviewBioorganic & medicinal chemistry2007

Targeting cytochrome P450 enzymes: a new approach in anti-cancer drug development.

Robert D Bruno, Vincent C O Njar

Open access · greenAbstract readReview
In one paragraph

Review in Bioorganic & medicinal chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
18.0field-weighted citation impact, top 1% 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

70 citing papers in PubMed, 248 citations in OpenAlex.

  1. Discovery of 2-phenylethyl chromones as potent and selective CYP1B1 inhibitors.Journal of enzyme inhibition and medicinal chemistry · 2026
    Article
  2. Article
  3. Review
  4. Review
  5. RSC advances · 2024
    Article
  6. Cytochrome P450 genes expression in human prostate cancer.Molecular genetics and metabolism reports · 2024
    Article
  7. Review
  8. Article
  9. Article
  10. Designing cytochrome P450 enzymes for use in cancer gene therapy.Frontiers in bioengineering and biotechnology · 2024
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

10 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.

Robert D BrunoDepartment of Pharmacology and Experimental Therapeutics, University of Maryland School of Medicine, Baltimore, MD 21201-1559, USA.
Vincent C O Njar
University of Maryland, Baltimore · USUniversity of Maryland Marlene and Stewart Greenebaum Comprehensive Cancer Center

Funding

Training in Molecular and Mechanistic ToxicologyT32ES007263 · NIEHS · UNIVERSITY OF MARYLAND BALTIMORE · PI ALBUQUERQUE, EDSON X · 1990 to 2012
$2.4M
Retinoids, RAMBAs, and Histone Deacetylase InhibitorsR21CA117991 · NCI · UNIVERSITY OF MARYLAND BALTIMORE · PI NJAR, VINCENT COLLINS OFUKA · 2005 to 2006
$347k
NCI NIH HHS R21 CA117991NCI NIH HHS R21 CA117991-01/02NIEHS NIH HHS 2 T32 ES007263-16A1NIEHS NIH HHS T32 ES007263
6 · The paper itself

Abstract

Cytochrome P450s (CYPs) represent a large class of heme-containing enzymes that catalyze the metabolism of multitudes of substrates both endogenous and exogenous. Until recently, however, CYPs have been largely overlooked in cancer drug development, acknowledged only for their role in phase I metabolism of chemotherapeutics. The first successful strategy targeting CYP enzymes in cancer therapy was the development of potent inhibitors of CYP19 (aromatase) for the treatment of breast cancer. Aromatase inhibitors ushered in a new era in hormone ablation therapy for estrogen dependent cancers, and have paved the way for similar strategies (i.e., inhibition of CYP17) that combat androgen dependent prostate cancer. Identification of CYPs involved in the inactivation of anti-cancer metabolites of vitamin D(3) and vitamin A has triggered development of agents that target these enzymes as well. The discovery of the over-expression of exogenous metabolizing CYPs, such as CYP1B1, in cancer cells has roused interest in the development of inhibitors for chemoprevention and of prodrugs designed to be activated by CYPs only in cancer cells. Finally, the expression of CYPs within tumors has been utilized in the development of bioreductive molecules that are activated by CYPs only under hypoxic conditions. This review offers the first comprehensive analysis of strategies in drug development that either inhibit or exploit CYP enzymes for the treatment of cancer.

Indexed as

Cytochrome P-450 Enzyme InhibitorsAntineoplastic AgentsCytochrome P-450 Enzyme SystemNeoplasmsAntineoplastic AgentsCytochrome P-450 Enzyme InhibitorsCytochrome P-450 Enzyme System

Identifiers

PMID17544277
PMCPMC1958998
OpenAlexW1981398318

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.