Evidence map›Paper›PMID 30104534›Full record

ReviewMolecules (Basel, Switzerland)2018

Computational Molecular Docking and X-ray Crystallographic Studies of Catechins in New Drug Design Strategies.

Shogo Nakano, Shin-Ichi Megro, Tadashi Hase, Takuji Suzuki, Mamoru Isemura, Yoriyuki Nakamura, Sohei Ito

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

16 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
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  13. Review
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  15. Catechin in Human Health and Disease.Molecules (Basel, Switzerland) · 2019
    Article
  16. 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

7 authors at 4 institutions in 1 country.

Shogo NakanoSchool of Food and Nutritional Sciences, Shizuoka University, Yada, Shizuoka 422-8526, Japan. snakano@u-shizuoka-ken.ac.jp.
Shin-Ichi MegroBiological Science Research, Kao Corporation, Ichikai-machi, Haga-gun, Tochigi 321-3497, Japan. meguro.shinichi@kao.com.
Tadashi HaseResearch and Development, Core Technology, Kao Corporation, Sumida, Tokyo 131-8501, Japan. hase.tadashi@kao.com.
Takuji SuzukiFaculty of Education, Art and Science, Yamagata University, Yamagata 990-8560, Japan. taksuzuk@e.yamagata-u.ac.jp.
Mamoru IsemuraSchool of Food and Nutritional Sciences, Shizuoka University, Yada, Shizuoka 422-8526, Japan. isemura@u-shizuoka-ken.ac.jp.
Yoriyuki NakamuraSchool of Food and Nutritional Sciences, Shizuoka University, Yada, Shizuoka 422-8526, Japan. yori.naka222@u-shizuoka-ken.ac.jp.
Sohei ItoSchool of Food and Nutritional Sciences, Shizuoka University, Yada, Shizuoka 422-8526, Japan. itosohei@u-shizuoka-ken.ac.jp.
Shizuoka University · JPKao Corporation (Japan) · JPUniversity of Shizuoka · JPYamagata University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Epidemiological and laboratory studies have shown that green tea and green tea catechins exert beneficial effects on a variety of diseases, including cancer, metabolic syndrome, infectious diseases, and neurodegenerative diseases. In most cases, (-)-epigallocatechin gallate (EGCG) has been shown to play a central role in these effects by green tea. Catechins from other plant sources have also shown health benefits. Many studies have revealed that the binding of EGCG and other catechins to proteins is involved in its action mechanism. Computational docking analysis (CMDA) and X-ray crystallographic analysis (XCA) have provided detailed information on catechin-protein interactions. Several of these studies have revealed that the galloyl moiety anchors it to the cleft of proteins through interactions with its hydroxyl groups, explaining the higher activity of galloylated catechins such as EGCG and epicatechin gallate than non-galloylated catechins. In this paper, we review the results of CMDA and XCA of EGCG and other plant catechins to understand catechin-protein interactions with the expectation of developing new drugs with health-promoting properties.

Indexed as

Drug DesignMolecular Docking SimulationMolecular Dynamics SimulationBinding SitesCatechinCrystallography, X-RayHumansLigandsMolecular ConformationMolecular StructurePlant ExtractsProtein BindingProtein Interaction Domains and MotifsStructure-Activity RelationshipTeaCatechinLigandsPlant ExtractsTeacomputational molecular docking analysisEGCGgreen tea catechinsX-ray crystallographic analysis

Identifiers

PMID30104534
PMCPMC6222539
OpenAlexW2887988752

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.