Evidence map›Paper›PMID 29310511›Full record

ArticleXenobiotica; the fate of foreign compounds in biological systems2019

Cytochrome P450 2A6 and other human P450 enzymes in the oxidation of flavone and flavanone.

Kensaku Kakimoto, Norie Murayama, Shigeo Takenaka, Haruna Nagayoshi, Young-Ran Lim, Vitchan Kim, Donghak Kim, Hiroshi Yamazaki, Masayuki Komori, F Peter Guengerich and 1 more

Open access · greenAbstract read
In one paragraph

Article in Xenobiotica; the fate of foreign compounds in biological systems, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.6field-weighted citation impact, top 13% 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

10 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Genetic and Enzymatic Characteristics of CYP2A13 in Relation to Lung Damage.International journal of molecular sciences · 2021
    Review
  5. Article
  6. Article
  7. Preference forXenobiotica; the fate of foreign compounds in biological systems · 2020
    Article
  8. Article
  9. Site-specific oxidation of flavanone and flavone by cytochrome P450 2A6 in human liver microsomes.Xenobiotica; the fate of foreign compounds in biological systems · 2019
    Article
  10. Review
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

11 authors at 5 institutions in 3 countries.

Kensaku Kakimotoa Osaka Institute of Public Health , Higashinari-ku , Osaka , Japan.
Norie Murayamab Laboratory of Drug Metabolism and Pharmacokinetics, Showa Pharmaceutical University , Machida , Tokyo , Japan.
Shigeo Takenakac Graduate School of Comprehensive Rehabilitation, Osaka Prefecture University , Habikino , Osaka , Japan.
Haruna Nagayoshia Osaka Institute of Public Health , Higashinari-ku , Osaka , Japan.
Young-Ran Limd Department of Biological Sciences , Konkuk University , Seoul , Korea.
Vitchan Kimd Department of Biological Sciences , Konkuk University , Seoul , Korea.
Donghak Kimd Department of Biological Sciences , Konkuk University , Seoul , Korea.
Hiroshi Yamazakib Laboratory of Drug Metabolism and Pharmacokinetics, Showa Pharmaceutical University , Machida , Tokyo , Japan.ORCID http://orcid.org/0000-0002-1068-4261
Masayuki Komorie Laboratory of Cellular and Molecular Biology, Veterinary Sciences, Osaka Prefecture University , Izumisano , Osaka , Japan , and.
F Peter Guengerichf Department of Biochemistry , Vanderbilt University School of Medicine , Nashville , TN , USA.
Tsutomu Shimadae Laboratory of Cellular and Molecular Biology, Veterinary Sciences, Osaka Prefecture University , Izumisano , Osaka , Japan , and.
Konkuk University · KROsaka Prefecture University · JPOsaka Prefectural Institute of Public Health · JPShowa Pharmaceutical University · JPVanderbilt University · US

Funding

Metabolism of Carcinogens and Drugs by Human P450sR01GM118122 · NIGMS · VANDERBILT UNIVERSITY · PI GUENGERICH, F PETER · 2016 to 2023
$3.3M
NIGMS NIH HHS R01 GM118122
6 · The paper itself

Abstract

1. We previously reported that flavone and flavanone interact spectrally with cytochrome P450 (P450 or CYP) 2A6 and 2A13 and other human P450s and inhibit catalytic activities of these P450 enzymes. In this study, we studied abilities of CYP1A1, 1A2, 1B1, 2A6, 2A13, 2C9 and 3A4 to oxidize flavone and flavanone. 2. Human P450s oxidized flavone to 6- and 5-hydroxylated flavones, seven uncharacterized mono-hydroxylated flavones, and five di-hydroxylated flavones. CYP2A6 was most active in forming 6-hydroxy- and 5-hydroxyflavones and several mono- and di-hydroxylated products. 3. CYP2A6 was also very active in catalyzing flavanone to form 2'- and 6-hydroxyflavanones, the major products, at turnover rates of 4.8 min

Indexed as

Chromatography, LiquidCytochrome P-450 CYP2A6Cytochrome P-450 Enzyme SystemFlavanonesFlavonesHumansKineticsMass SpectrometryMolecular Docking SimulationOxidation-ReductionCytochrome P-450 CYP2A6Cytochrome P-450 Enzyme SystemflavanoneFlavanonesflavoneFlavonesflavanoneflavoneHumanoxidationP450 2A13P450 2A6P450s

Identifiers

PMID29310511
PMCPMC6430112
OpenAlexW2782828541

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.