Evidence map›Paper›PMID 22697360›Full record

ArticleJournal of agricultural and food chemistry2012

Grape seed and tea extracts and catechin 3-gallates are potent inhibitors of α-amylase and α-glucosidase activity.

Meltem Yilmazer-Musa, Anneke M Griffith, Alexander J Michels, Erik Schneider, Balz Frei

Open access · greenAbstract read
In one paragraph

Article in Journal of agricultural and food chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed, 1 pooled it
8.8field-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

99 citing papers in PubMed, 1 synthesis or guideline pooled it, 399 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Trial
  4. Article
  5. Review
  6. Proanthocyanidin-Rich Cranberry Extract Lowers Glycemia in Established Obesity by Delaying Glucose Absorption.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  7. Article
  8. Structure-effect relationship of phenolic compounds onCurrent research in food science · 2026
    Article
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  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
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  18. Review
  19. Article
  20. Article

39 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

5 authors at 1 institution in 1 country.

Meltem Yilmazer-MusaLinus Pauling Institute, Oregon State University, Corvallis, Oregon 97331, USA.
Anneke M Griffith
Alexander J Michels
Erik Schneider
Balz Frei
Oregon State University · US

Funding

MODE OF ACTION OF ENVIRONMENTAL TOXICANTST32ES007060 · NIEHS · OREGON STATE UNIVERSITY · PI Jamie DeWitt, Siva Kumar Kolluri · 1985 to 2026
$11.6M
NIEHS NIH HHS T32 ES007060
6 · The paper itself

Abstract

This study evaluated the inhibitory effects of plant-based extracts (grape seed, green tea, and white tea) and their constituent flavan-3-ol monomers (catechins) on α-amylase and α-glucosidase activity, two key glucosidases required for starch digestion in humans. To evaluate the relative potency of extracts and catechins, their concentrations required for 50 and 90% inhibition of enzyme activity were determined and compared to the widely used pharmacological glucosidase inhibitor, acarbose. Maximum enzyme inhibition was used to assess relative inhibitory efficacy. Results showed that grape seed extract strongly inhibited both α-amylase and α-glucosidase activity, with equal and much higher potency, respectively, than acarbose. Whereas tea extracts and catechin 3-gallates were less effective inhibitors of α-amylase, they were potent inhibitors of α-glucosidase. Nongallated catechins were ineffective. The data show that plant extracts containing catechin 3-gallates, in particular epigallocatechin gallate, are potent inhibitors of α-glucosidase activity and suggest that procyanidins in grape seed extract strongly inhibit α-amylase activity.

Indexed as

Glycoside Hydrolase Inhibitorsalpha-Amylasesalpha-GlucosidasesCamellia sinensisCatechinEnzyme InhibitorsFungal ProteinsHumansKineticsPlant ExtractsSaccharomycetalesSalivaSeedsVitisalpha-Amylasesalpha-GlucosidasesCatechincatechin gallateEnzyme InhibitorsFungal ProteinsGlycoside Hydrolase InhibitorsPlant Extracts

Identifiers

PMID22697360
PMCPMC4356113
OpenAlexW1978759852

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.