Evidence map›Paper›PMID 32210142›Full record

ReviewInternational journal of molecular sciences2020

Structures of Human Transglutaminase 2: Finding Clues for Interference in Cross-linking Mediated Activity.

Gi Eob Kim, Hyun Ho Park

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.0field-weighted citation impact, top 21% 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

12 citing papers in PubMed, 20 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

Gi Eob KimCollege of Pharmacy, Chung-Ang University, Seoul 06974, Korea.
Hyun Ho ParkCollege of Pharmacy, Chung-Ang University, Seoul 06974, Korea.ORCID 0000-0001-9928-0847
Chung-Ang University · KR

Funding

Korea Healthcare Technology R&D Project HI17C0155National Research Foundation of Korea NRF-2017M3A9D8062960National Research Foundation of Korea NRF-2018R1A2B2003635
6 · The paper itself

Abstract

Human transglutaminase 2 (TGase2) has various functions, including roles in various cellular processes such as apoptosis, development, differentiation, wound healing, and angiogenesis, and is linked to many diseases such as cancer. Although TGase2 has been considered an optimized drug target for the treatment of cancer, fibrosis, and neurodegenerative disorders, it has been difficult to generate TGase2-targeted drugs for clinical use because of the relatively flat and broad active site on TGase2. To design more specific and powerful inhibitors, detailed structural information about TGase2 complexed with various effector and inhibitor molecules is required. In this review, we summarized the current structural studies on TGase2, which will aid in designing drugs that can overcome the aforementioned limitations.

Indexed as

Models, MolecularProtein ConformationAmino Acid SequenceBinding SitesDrug DesignGTP-Binding ProteinsHumansLigandsPeptidesProtein BindingProtein Glutamine gamma Glutamyltransferase 2Structure-Activity RelationshipTransglutaminasesGTP-Binding ProteinsLigandsPeptidesProtein Glutamine gamma Glutamyltransferase 2Transglutaminasespeptide mimeticprotein structurestructure-based drug designtransglutaminase 2

Identifiers

PMID32210142
PMCPMC7139744
OpenAlexW3012672206

What OpenQuestion 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 OpenQuestion graph.