Evidence map›Paper›PMID 21645130›Full record

ArticleMolecular microbiology2011

Functional characterization of the ferroxidase, permease high-affinity iron transport complex from Candida albicans.

Lynn Ziegler, Alaina Terzulli, Ruchi Gaur, Ryan McCarthy, Daniel J Kosman

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.3field-weighted citation impact, top 14% 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

26 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Multicopper Oxidases inJournal of fungi (Basel, Switzerland) · 2020
    Review
  15. Article
  16. Pathogens (Basel, Switzerland) · 2019
    Review
  17. Article
  18. Iron at the Centre ofFrontiers in cellular and infection microbiology · 2018
    Review
  19. Fungal Strategies to Evade the Host Immune Recognition.Journal of fungi (Basel, Switzerland) · 2017
    Review
  20. Iron acquisition in fungal pathogens of humans.Metallomics : integrated biometal science · 2017
    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

5 authors at 1 institution in 1 country.

Lynn ZieglerDepartment of Biochemistry, School of Medicine and Biomedical Sciences, State University of New York at Buffalo, Buffalo, NY 14214, USA.
Alaina Terzulli
Ruchi Gaur
Ryan McCarthy
Daniel J Kosman
University at Buffalo, State University of New York · US

Funding

Managing ionic iron: ferri-reduction, ferro-oxidation and iron permeationR01DK053820 · NIDDK · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI KOSMAN, DANIEL J. · 1999 to 2016
$4.0M
Managing Ionic Iron: Molecular Architecture and Mechanism of Cell Iron MetabolismR01DK077826 · NIDDK · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI KOSMAN, DANIEL J. · 2007 to 2010
$1.2M
Managing ionic iron: ferri-reduction, ferro-oxidation and iron permeationR56DK053820 · NIDDK · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI KOSMAN, DANIEL J. · 2013 to 2013
$155k
NIDDK NIH HHS DK053820NIDDK NIH HHS DK077826NIDDK NIH HHS R01 DK053820NIDDK NIH HHS R01 DK077826NIDDK NIH HHS R56 DK053820
6 · The paper itself

Abstract

Saccharomyces cerevisiae expresses two proteins that together support high-affinity Fe-uptake. These are a multicopper oxidase, Fet3p, with specificity towards Fe²⁺ and a ferric iron permease, Ftr1p, which supports Fe-accumulation. Homologues of the genes encoding these two proteins are found in all fungal genomes including those for the pathogens, Candida albicans and Cryptococcus neoformans. At least one of these loci represents a virulence factor for each pathogen suggesting that this complex would be an appropriate pharmacologic target. However, the mechanism by which this protein pair supports Fe-uptake in any fungal pathogen has not been elucidated. Taking advantage of the robust molecular genetics available in S. cerevisiae, we identify the two of five candidate ferroxidases likely involved in high-affinity Fe-uptake in C. albicans, Fet31 and Fet34. Both localize to the yeast plasma membrane and both support Fe-uptake along with an Ftr1 protein, either from C. albicans or from S. cerevisiae. We express and characterize Fet34, demonstrating that it is functionally homologous to ScFet3p. Using S. cerevisiae as host for the functional expression of the C. albicans Fe-uptake proteins, we demonstrate that they support a mechanism of Fe-trafficking that involves channelling of the CaFet34-generated Fe³⁺ directly to CaFtr1 for transport into the cytoplasm.

Indexed as

Candida albicansCell MembraneCeruloplasminCryptococcus neoformansFungal ProteinsIronMembrane Transport ProteinsModels, BiologicalModels, MolecularSaccharomyces cerevisiaeCeruloplasminFTR1 protein, Candida albicansFungal ProteinsIronMembrane Transport Proteins

Identifiers

PMID21645130
PMCPMC3133879
OpenAlexW1919708403

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.