Evidence map›Paper›PMID 30874431›Full record

ArticleBiochemistry2019

Quantifying the Oligomeric State of hZIP4 on the Surface of Cells.

Meghan E Ahern, Elizabeth M Bafaro, Ann Cowan, Robert E Dempski

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

8 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
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  7. Transcription factors and transporters in zinc homeostasis: lessons learned from fungi.Critical reviews in biochemistry and molecular biology · 2020
    Review
  8. Review
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 2 institutions in 1 country.

Meghan E AhernDepartment of Chemistry and Biochemistry , Worcester Polytechnic Institute , Worcester , Massachusetts 01609-2247 , United States.
Elizabeth M BafaroDepartment of Chemistry and Biochemistry , Worcester Polytechnic Institute , Worcester , Massachusetts 01609-2247 , United States.
Ann CowanDepartment of Molecular Biology and Biophysics and Center for Cell Analysis and Modeling , University of Connecticut Health Center , Farmington , Connecticut 06030 , United States.
Robert E DempskiDepartment of Chemistry and Biochemistry , Worcester Polytechnic Institute , Worcester , Massachusetts 01609-2247 , United States.ORCID 0000-0002-7751-1613
Worcester Polytechnic Institute · USUConn Health · US

Funding

The molecular determinants of zinc uptake mediated by hZIP4R01GM105964 · NIGMS · WORCESTER POLYTECHNIC INSTITUTE · PI DEMPSKI, ROBERT EDWARD · 2014 to 2018
$1.4M
NIGMS NIH HHS R01 GM105964
6 · The paper itself

Abstract

The human (h) zinc transporter ZIP4 is expressed on the plasma membrane and functions to increase cytosolic zinc levels. Mutations in hZIP4 cause the disease acrodermatitis enteropathica. Dysfunction in the regulation of hZIP4 has also been indicated in solid tissue cancers, including pancreatic and prostate cancer. Although structural studies of the extracellular domain and computational modeling of the membrane domain suggest hZIP4 exists as a dimer, the oligomerization status of hZIP4 in the plasma membrane of mammalian cells has not been directly quantified in vivo. Here, the oligomeric state of hZIP4 expressed in HEK293 cells was quantified using fluorescence correlation spectroscopy. hZIP4 was tagged with eGFP, and by comparing brightness values (ε) of monomer and tandem eGFP constructs to that of an hZIP4/eGFP, we show that hZIP4 is a dimer. Determining that hZIP4 is a dimer is an important step toward understanding the function and processing of the protein, which can provide more insight into how diseases affected by hZIP4 occur and can be managed.

Indexed as

Cation Transport ProteinsCell MembraneHEK293 CellsHumansModels, MolecularProtein DomainsProtein MultimerizationSpectrometry, FluorescenceCation Transport ProteinsSLC39A4 protein, human

Identifiers

PMID30874431
PMCPMC7163800
OpenAlexW2920952320

What OpenQuestion holds

Textmetadata
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.