Evidence map›Paper›PMID 25971965›Full record

ArticleThe Journal of biological chemistry2015

Computation and Functional Studies Provide a Model for the Structure of the Zinc Transporter hZIP4.

Sagar Antala, Sergey Ovchinnikov, Hetunandan Kamisetty, David Baker, Robert E Dempski

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
7.6field-weighted citation impact, top 2% 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

38 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. The Molecular Basis for Zinc Bioavailability.International journal of molecular sciences · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Transcription factors and transporters in zinc homeostasis: lessons learned from fungi.Critical reviews in biochemistry and molecular biology · 2020
    Review
  14. Elucidating the HInternational journal of molecular sciences · 2020
    Article
  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. Article
  17. Article
  18. Article
  19. Article
  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

5 authors at 3 institutions in 1 country.

Sagar AntalaDepartment of Chemistry and Biochemistry, Worcester Polytechnic Institute, Worcester, Massachusetts 01609.
Sergey OvchinnikovHoward Hughes Medical Institute, University of Washington, Seattle, Washington 98195; Department of Biochemistry, University of Washington, Seattle, Washington 98195; Molecular and Cellular Biology Program, University of Washington, Seattle, Washington 98195.
Hetunandan KamisettyHoward Hughes Medical Institute, University of Washington, Seattle, Washington 98195; Department of Biochemistry, University of Washington, Seattle, Washington 98195.
David BakerHoward Hughes Medical Institute, University of Washington, Seattle, Washington 98195; Department of Biochemistry, University of Washington, Seattle, Washington 98195.
Robert E DempskiDepartment of Chemistry and Biochemistry, Worcester Polytechnic Institute, Worcester, Massachusetts 01609. Electronic address: rdempski@wpi.edu.
University of Washington · USWorcester Polytechnic Institute · USHoward Hughes Medical Institute · US

Funding

TRAINING IN MOLECULAR AND CELLULAR BIOLOGYT32GM007270 · NIGMS · UNIVERSITY OF WASHINGTON · PI RAIBLE, DAVID W · 1985 to 2020
$21.0M
High resolution structure modeling with RosettaR01GM092802 · NIGMS · UNIVERSITY OF WASHINGTON · PI BAKER, DAVID · 2010 to 2017
$2.3M
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 GM092802NIGMS NIH HHS GM105964NIGMS NIH HHS R01 GM092802NIGMS NIH HHS R01 GM105964NIGMS NIH HHS T32 GM007270
6 · The paper itself

Abstract

Members of the Zrt and Irt protein (ZIP) family are a central participant in transition metal homeostasis as they function to increase the cytosolic concentration of zinc and/or iron. However, the lack of a crystal structure hinders elucidation of the molecular mechanism of ZIP proteins. Here, we employed GREMLIN, a co-evolution-based contact prediction approach in conjunction with the Rosetta structure prediction program to construct a structural model of the human (h) ZIP4 transporter. The predicted contact data are best fit by modeling hZIP4 as a dimer. Mutagenesis of residues that comprise a central putative hZIP4 transmembrane transition metal coordination site in the structural model alter the kinetics and specificity of hZIP4. Comparison of the hZIP4 dimer model to all known membrane protein structures identifies the 12-transmembrane monomeric Piriformospora indica phosphate transporter (PiPT), a member of the major facilitator superfamily (MFS), as a likely structural homolog.

Indexed as

AnimalsCations, DivalentCation Transport ProteinsCells, CulturedCrystallography, X-RayHumansIronModels, MolecularProtein MultimerizationXenopusZincCations, DivalentCation Transport ProteinsIronSLC39A4 protein, humanZinccomputer modelingmembrane biophysicsmembrane proteinmetal homeostasismetal ion-protein interactionprotein evolutiontransportertransport metalzinc

Identifiers

PMID25971965
PMCPMC4505028
OpenAlexW1509744189

What OpenQuestion holds

Textmetadata
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.