Evidence map›Paper›PMID 30563268›Full record

ReviewNutrients2018

Molecular Targets of Epigallocatechin-Gallate (EGCG): A Special Focus on Signal Transduction and Cancer.

Aide Negri, Valeria Naponelli, Federica Rizzi, Saverio Bettuzzi

Open access · goldAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Nutrients, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 132 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
132citing papers in PubMed, 1 pooled it
17.5field-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

132 citing papers in PubMed, 1 synthesis or guideline pooled it, 264 citations in OpenAlex.

  1. Pooled it
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  3. Exploring the anticancer potential of epigallocatechin gallate-loaded sodium alginate nanoparticles: impact of size variation on head and neck cancer cells.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2026
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72 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

4 authors at 1 institution in 1 country.

Aide NegriDepartment of Medicine and Surgery, University of Parma, Via Gramsci 14, 43126 Parma, Italy. aide.negri@unipr.it.
Valeria NaponelliDepartment of Medicine and Surgery, University of Parma, Via Gramsci 14, 43126 Parma, Italy. valeria.naponelli@unipr.it.ORCID 0000-0001-5210-1522
Federica RizziDepartment of Medicine and Surgery, University of Parma, Via Gramsci 14, 43126 Parma, Italy. federica.rizzi@unipr.it.ORCID 0000-0002-6670-2588
Saverio BettuzziDepartment of Medicine and Surgery, University of Parma, Via Gramsci 14, 43126 Parma, Italy. saverio.bettuzzi@unipr.it.
University of Parma · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Green tea is a beverage that is widely consumed worldwide and is believed to exert effects on different diseases, including cancer. The major components of green tea are catechins, a family of polyphenols. Among them, epigallocatechin-gallate (EGCG) is the most abundant and biologically active. EGCG is widely studied for its anti-cancer properties. However, the cellular and molecular mechanisms explaining its action have not been completely understood, yet. EGCG is effective in vivo at micromolar concentrations, suggesting that its action is mediated by interaction with specific targets that are involved in the regulation of crucial steps of cell proliferation, survival, and metastatic spread. Recently, several proteins have been identified as EGCG direct interactors. Among them, the trans-membrane receptor 67LR has been identified as a high affinity EGCG receptor. 67LR is a master regulator of many pathways affecting cell proliferation or apoptosis, also regulating cancer stem cells (CSCs) activity. EGCG was also found to be interacting directly with Pin1, TGFR-II, and metalloproteinases (MMPs) (mainly MMP2 and MMP9), which respectively regulate EGCG-dependent inhibition of NF-kB, epithelial-mesenchimal transaction (EMT) and cellular invasion. EGCG interacts with DNA methyltransferases (DNMTs) and histone deacetylases (HDACs), which modulates epigenetic changes. The bulk of this novel knowledge provides information about the mechanisms of action of EGCG and may explain its onco-suppressive function. The identification of crucial signalling pathways that are related to cancer onset and progression whose master regulators interacts with EGCG may disclose intriguing pharmacological targets, and eventually lead to novel combined treatments in which EGCG acts synergistically with known drugs.

Indexed as

Camellia sinensisCatechinDNA MethylationHumansMetalloproteasesMethyltransferasesNeoplasmsNIMA-Interacting Peptidylprolyl IsomerasePhytotherapyPlant ExtractsPolyphenolsReceptors, Cell SurfaceSignal TransductionTeaCatechinepigallocatechin gallateMetalloproteasesMethyltransferasesNIMA-Interacting Peptidylprolyl IsomerasePIN1 protein, humanPlant ExtractsPolyphenolsReceptors, Cell SurfaceTea67LRcancer apoptosiscell deathchemopreventionepigallocatechin-gallate (EGCG)gene expressiongreen tea catechins

Identifiers

PMID30563268
PMCPMC6315581
OpenAlexW2902806889

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.