Evidence map›Paper›PMID 26959009›Full record

ReviewInternational journal of molecular sciences2016

The Functions of Metallothionein and ZIP and ZnT Transporters: An Overview and Perspective.

Tomoki Kimura, Taiho Kambe

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 201 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
201citing papers in PubMed, 3 pooled it
28.6field-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

201 citing papers in PubMed, 3 syntheses or guidelines pooled it, 409 citations in OpenAlex.

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  15. Frontiers in pharmacology · 2026
    Article
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  17. Modification of human metallothioneins by garlic organosulfur compounds, allicin and ajoene: direct effect on zinc homeostasis with relevance to immune regulation.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2025
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141 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

2 authors at 2 institutions in 1 country.

Tomoki KimuraDepartment of Life Science, Faculty of Science and Engineering, Setsunan University, Neyagawa, Osaka 572-8508, Japan. tomoki@lif.setsunan.ac.jp.
Taiho KambeDivision of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kyoto 606-8502, Japan. kambe1@kais.kyoto-u.ac.jp.
Kyoto University · JPSetsunan University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Around 3000 proteins are thought to bind zinc in vivo, which corresponds to ~10% of the human proteome. Zinc plays a pivotal role as a structural, catalytic, and signaling component that functions in numerous physiological processes. It is more widely used as a structural element in proteins than any other transition metal ion, is a catalytic component of many enzymes, and acts as a cellular signaling mediator. Thus, it is expected that zinc metabolism and homeostasis have sophisticated regulation, and elucidating the underlying molecular basis of this is essential to understanding zinc functions in cellular physiology and pathogenesis. In recent decades, an increasing amount of evidence has uncovered critical roles of a number of proteins in zinc metabolism and homeostasis through influxing, chelating, sequestrating, coordinating, releasing, and effluxing zinc. Metallothioneins (MT) and Zrt- and Irt-like proteins (ZIP) and Zn transporters (ZnT) are the proteins primarily involved in these processes, and their malfunction has been implicated in a number of inherited diseases such as acrodermatitis enteropathica. The present review updates our current understanding of the biological functions of MTs and ZIP and ZnT transporters from several new perspectives.

Indexed as

AcrodermatitisAnimalsCation Transport ProteinsEpigenesis, GeneticGene Expression RegulationGenetic Predisposition to DiseaseHomeostasisHumansMetallothioneinPhylogenyPolymorphism, Single NucleotideRepressor ProteinsZincCation Transport ProteinsMetallothioneinRepressor ProteinsZGPAT protein, humanZincchaperonemetallothioneinzincZIP and ZnT transporter

Identifiers

PMID26959009
PMCPMC4813198
OpenAlexW2288699132

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.