Evidence map›Paper›PMID 32114317›Full record

ReviewCurrent opinion in chemical biology2020

Zinc homeostasis in the secretory pathway in yeast.

Amanda J Bird, Stevin Wilson

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

15 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Lysosome-related organelles contain an expansion compartment that mediates delivery of zinc transporters to promote homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Metalation and activation of ZnBiophysics reviews · 2023
    Review
  7. Article
  8. Review
  9. Nonsense-mediated mRNA decay and metal ion homeostasis and detoxification in Saccharomyces cerevisiae.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2022
    Review
  10. Article
  11. Article
  12. Review
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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 1 institution in 1 country.

Amanda J BirdDepartment of Molecular Genetics, The Ohio State University, Columbus, OH, 43210, USA; Department of Human Sciences, The Ohio State University, Columbus, OH, 43210, USA; Center for RNA Biology, The Ohio State University, Columbus, OH, 43210, USA. Electronic address: bird.96@osu.edu.
Stevin WilsonDepartment of Molecular Genetics, The Ohio State University, Columbus, OH, 43210, USA.
The Ohio State University · US

Funding

Zinc-dependent regulation of gene expressionR01GM105695 · NIGMS · OHIO STATE UNIVERSITY · PI BIRD, AMANDA JANE · 2014 to 2018
$1.4M
NIGMS NIH HHS R01 GM105695
6 · The paper itself

Abstract

It is estimated that up to 10% of proteins in eukaryotes require zinc for their function. Although the majority of these proteins are located in the nucleus and cytosol, a small subset is secreted from cells or is located within an intracellular compartment. As many of these compartmentalized metalloproteins fold to their native state and bind their zinc cofactor inside an organelle, cells require mechanisms to maintain supply of zinc to these compartments even under conditions of zinc deficiency. At the same time, intracellular compartments can also be the site for storing zinc ions, which then can be mobilized when needed. In this review, we highlight insight that has been obtained from yeast models about how zinc homeostasis is maintained in the secretory pathway and vacuole.

Indexed as

Amino AcidsBiological TransportCarrier ProteinsCytoplasmGene Expression Regulation, BacterialHomeostasisMetalloproteinsOrganellesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSecretory PathwayZincAmino AcidsCarrier ProteinsMetalloproteinsSaccharomyces cerevisiae ProteinsZinczinc-binding proteinmetalationorganelle zinc homeostasiszinc deficiencyzinc proteomezinc storage

Identifiers

PMID32114317
PMCPMC7237322
OpenAlexW3008367852

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.