Evidence map›Paper›PMID 31164399›Full record

ArticleThe Biochemical journal2019

The histidine-rich loop in the extracellular domain of ZIP4 binds zinc and plays a role in zinc transport.

Tuo Zhang, Eziz Kuliyev, Dexin Sui, Jian Hu

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

17 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. The Molecular Basis for Zinc Bioavailability.International journal of molecular sciences · 2023
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Transcription factors and transporters in zinc homeostasis: lessons learned from fungi.Critical reviews in biochemistry and molecular biology · 2020
    Review
  15. Asymmetric functions of a binuclear metal center within the transport pathway of a human zinc transporter ZIP4.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  16. Review
  17. 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

4 authors at 1 institution in 1 country.

Tuo ZhangDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, U.S.A.
Eziz KuliyevDepartment of Chemistry, Michigan State University, East Lansing, MI, U.S.A.
Dexin SuiDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, U.S.A.
Jian HuDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, U.S.A. hujian1@msu.edu.ORCID 0000-0001-6657-9826
Michigan State University · US

Funding

Zinc enrichment/zinc sensing mechanism through the extracellular domain of ZIP4R01GM115373 · NIGMS · MICHIGAN STATE UNIVERSITY · PI HU, JIAN · 2015 to 2019
$1.5M
Structural and Mechanistic Characterization of the ZIP Metal TransportersR01GM129004 · NIGMS · MICHIGAN STATE UNIVERSITY · PI HU, JIAN · 2018 to 2020
$593k
NIGMS NIH HHS R01 GM115373NIGMS NIH HHS R01 GM129004
6 · The paper itself

Abstract

The Zrt-/Irt-like protein (ZIP) family mediates zinc influx from extracellular space or intracellular vesicles/organelles, playing a central role in systemic and cellular zinc homeostasis. Out of the 14 family members encoded in human genome, ZIP4 is exclusively responsible for zinc uptake from dietary food and dysfunctional mutations of ZIP4 cause a life-threatening genetic disorder, Acrodermatitis Enteropathica (AE). About half of the missense AE-causing mutations occur within the large N-terminal extracellular domain (ECD), and our previous study has shown that ZIP4-ECD is crucial for optimal zinc uptake but the underlying mechanism has not been clarified. In this work, we examined zinc binding to the isolated ZIP4-ECD from

Indexed as

Mutation, MissenseAcrodermatitisAmino Acid SubstitutionBiological Transport, ActiveCation Transport ProteinsHEK293 CellsHumansProtein Structure, SecondaryStructure-Activity RelationshipZincCation Transport ProteinsSLC39A4 protein, humanZincAcrodermatitis Enteropathicahistidine-rich looptransporterzincZIP4Zrt-/Irt-like protein

Identifiers

PMID31164399
PMCPMC7661218
OpenAlexW2948100254

What OpenQuestion holds

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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.