Evidence map›Paper›PMID 30370308›Full record

ReviewJournal of immunology research2018

Function, Structure, and Transport Aspects of ZIP and ZnT Zinc Transporters in Immune Cells.

Bum-Ho Bin, Juyeon Seo, Sung Tae Kim

Open access · goldAbstract readReview
In one paragraph

Review in Journal of immunology research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.8field-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

48 citing papers in PubMed, 92 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Metal Ions Within the Neuro-Immune-Tumor Axis.Journal of immunology research · 2026
    Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Modelling host-pathogen interactions:Microbiology (Reading, England) · 2025
    Article
  12. Biochemical Markers of Zinc Nutrition.Biological trace element research · 2024
    Review
  13. Article
  14. Review
  15. The ZnDevelopmental cell · 2024
    Article
  16. Zinc Toxicity: Understanding the Limits.Molecules (Basel, Switzerland) · 2024
    Review
  17. Article
  18. Article
  19. Review
  20. 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

3 authors at 3 institutions in 2 countries.

Bum-Ho BinDepartment of Molecular Science and Technology, College of Natural Sciences, Ajou University, Suwon 16499, Republic of Korea.ORCID 0000-0002-3312-702X
Juyeon SeoBasic Research & Innovation Division, AmorePacific R&D Unit, Yongin 17014, Republic of Korea.
Sung Tae KimDepartment of Pharmaceutical Engineering, Inje University, Gimhae 50834, Republic of Korea.ORCID 0000-0001-8852-0198
Amorepacific (South Korea) · KRInje University · KRShowa University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Zinc is an important trace metal in immune systems, and zinc transporters are involved in many immune responses. Recent advances have revealed the structural and biochemical bases for zinc transport across the cell membrane, with clinical implications for the regulation of zinc homeostasis in immune cells like dendritic cells, T cells, B cells, and mast cells. In this review, we discuss the function, structure, and transport aspects of two major mammalian zinc transporter types, importers and exporters. First, Zrt-/Irt-like proteins (ZIPs) mediate the zinc influx from the extracellular or luminal side into the cytoplasm. There are 14 ZIP family members in humans. They form a homo- or heterodimer with 8 transmembrane domains and extra-/intracellular domains of various lengths. Several ZIP members show specific extracellular domains composed of two subdomains, a helix-rich domain and proline-alanine-leucine (PAL) motif-containing domain. Second, ZnT (zinc transporter) was initially identified in early studies of zinc biology; it mediates zinc efflux as a counterpart of ZIPs in zinc homeostasis. Ten family members have been identified. They show a unique architecture characterized by a Y-shaped conformation and a large cytoplasmic domain. A precise, comprehensive understanding of the structures and transport mechanisms of ZIP and ZnT in combination with mice experiments would provide promising drug targets as well as a basis for identifying other transporters with therapeutic potential.

Indexed as

Immune SystemIon TransportAnimalsCarrier ProteinsCation Transport ProteinsHomeostasisHumansImmunity, CellularMiceMolecular StructureMolecular Targeted TherapyProtein ConformationRepressor ProteinsZincZinc Transporter 8Carrier ProteinsCation Transport ProteinsRepressor ProteinsZGPAT protein, humanZinczinc-binding proteinZinc Transporter 8

Identifiers

PMID30370308
PMCPMC6189677
OpenAlexW2895718781

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.