Evidence map›Paper›PMID 9811853›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

Chloride is an allosteric effector of copper assembly for the yeast multicopper oxidase Fet3p: an unexpected role for intracellular chloride channels.

S R Davis-Kaplan, C C Askwith, A C Bengtzen, D Radisky, J Kaplan

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

27 citing papers in PubMed, 119 citations in OpenAlex.

  1. A Defense Strategy inMolecules (Basel, Switzerland) · 2026
    Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Copper Acquisition and Utilization in Fungi.Annual review of microbiology · 2017
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. The removal of a disulfide bridge in CotA-laccase changes the slower motion dynamics involved in copper binding but has no effect on the thermodynamic stability.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011
    Article
  13. Article
  14. Article
  15. Review
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  18. Review
  19. Article
  20. Copper incorporation into recombinant CotA laccase from Bacillus subtilis: characterization of fully copper loaded enzymes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2008
    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 2 institutions in 2 countries.

S R Davis-KaplanDivision of Immunology and Cell Biology, Department of Pathology, School of Medicine, University of Utah, Salt Lake City, UT 84132, USA. kaplan@bioscience.biology.utah.edu
C C Askwith
A C Bengtzen
D Radisky
J Kaplan
University of Utah · USBipar · FR

Funding

UTAH REGIONAL CANCER CENTERP30CA042014 · NCI · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Jared P Rutter · 1986 to 2026
$72.6M
FACTORS REGULATING THE CELLULAR UPTAKE OF IRONR37DK030534 · NIDDK · UNIVERSITY OF UTAH · PI KAPLAN, JERRY · 2000 to 2009
$3.3M
FACTORS REGULATING THE CELLULAR UPTAKE OF IRONR01DK030534 · NIDDK · UNIVERSITY OF UTAH · PI WARD, DIANE MCVEY · 1986 to 2018
$2.7M
ROLE OF BETA-2 INTEGRINS IN LEUKOCYTE ADHESION AND SIGNALINGP50DK049219 · NIDDK · UNIVERSITY OF UTAH · PI SPANGRUDE, GERALD J · 1994 to 2000
$75k
NCI NIH HHS 5 P30 CA 42014NCI NIH HHS P30 CA042014NIDDK NIH HHS DK 30534NIDDK NIH HHS DK 49219NIDDK NIH HHS R01 DK030534NIDDK NIH HHS R37 DK030534
6 · The paper itself

Abstract

GEF1 is a gene in Saccharomyces cerevisiae, which encodes a putative voltage-regulated chloride channel. gef1 mutants have a defect in the high-affinity iron transport system, which relies on the cell surface multicopper oxidase Fet3p. The defect is due to an inability to transfer Cu+ to apoFet3p within the secretory apparatus. We demonstrate that the insertion of Cu into apoFet3p is dependent on the presence of Cl-. Cu-loading of apoFet3p is favored at acidic pH, but in the absence of Cl- there is very little Cu-loading at any pH. Cl- has a positive allosteric effect on Cu-loading of apoFet3p. Kinetic studies suggest that Cl- may also bind to Fet3p and that Cu+ has an allosteric effect on the binding of Cl- to the enzyme. Thus, Cl- may be required for the metal loading of proteins within the secretory apparatus. These results may have implications in mammalian physiology, as mutations in human intracellular chloride channels result in disease.

Indexed as

Allosteric RegulationCeruloplasminChloride ChannelsChloridesCopperHumansSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCeruloplasminChloride ChannelsChloridesCopperFET3 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID9811853
PMCPMC24872
OpenAlexW2106392025

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.