Evidence map›Paper›PMID 19350454›Full record

ArticleXenobiotica; the fate of foreign compounds in biological systems2009

Sulfation of dietary flavonoids by human sulfotransferases.

C Huang, Y Chen, T Zhou, G Chen

Open access · greenAbstract read
In one paragraph

Article in Xenobiotica; the fate of foreign compounds in biological systems, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
5.7field-weighted citation impact, top 5% 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

15 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. In Vitro Liver Metabolism of Six Flavonoid C-Glycosides.Molecules (Basel, Switzerland) · 2021
    Article
  3. Article
  4. In Vitro Metabolism of Six C-Glycosidic Flavonoids fromInternational journal of molecular sciences · 2021
    Article
  5. Article
  6. The Role of Sulfotransferases in Liver Diseases.Drug metabolism and disposition: the biological fate of chemicals · 2020
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. 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

4 authors at 2 institutions in 2 countries.

C HuangPhysiological Sciences, Oklahoma State University, Stillwater, OK 74078, USA.
Y Chen
T Zhou
G Chen
Oklahoma State University · USPeking University · CN

Funding

Mechanisms and Functions of Human SulfotransferasesR01GM078606 · NIGMS · OKLAHOMA STATE UNIVERSITY STILLWATER · PI CHEN, GUANGPING · 2006 to 2009
$1.1M
ACTIVE SITE STUDIES OF HUMAN SULFOTRANSFERASESR01GM059873 · NIGMS · UNIVERSITY OF ARKANSAS MED SCIS LTL ROCK · PI CHEN, GUANGPING · 2000 to 2003
$759k
NIGMS NIH HHS GM 078606NIGMS NIH HHS R01 GM059873NIGMS NIH HHS R01 GM078606
6 · The paper itself

Abstract

Dietary flavonoids catechin, epicatechin, eriodictyol, and hesperetin were investigated as substrates and inhibitors of human sulfotransferases (hSULTs). Purified recombinant proteins and human intestine cytosol were used as enzyme sources. hSULT1A1 and hSULT1A3 as well as human intestine cytosol can catalyse the sulfation of the investigated flavonoids. Sulfation of catechin, epicatechin, eriodictyol, and hesperetin by recombinant hSULTs showed substrate inhibition at high flavonoid concentrations. Hesperetin and eriodictyol are potent inhibitors of purified hSULT1A1, hSULT1A3, hSULT1E1, and hSULT2A1. Catechin and epicatechin inhibited hSULT1A1 and hSULT1A3, but not hSULT1E1 and hSULT2A1. The sulfation efficacy and potency of inhibition is related to the C-ring structure of flavonoids. These results suggest that dietary flavonoids may regulate human SULT activity and, therefore, affect the regulation of hormones and neurotransmitters, detoxification of drugs, and the bioactivation of pro- carcinogens and pro-mutagens.

Indexed as

ArylsulfotransferaseCatechinCytosolFlavanonesHesperidinHumansKineticsMolecular StructureSulfotransferasesArylsulfotransferaseCatechineriodictyolFlavanoneshesperetinHesperidinmonoamine-sulfating phenol sulfotransferaseSulfotransferasesSULT1A1 protein, human

Identifiers

PMID19350454
PMCPMC3106293
OpenAlexW2137673490

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.