Evidence map›Paper›PMID 21841123›Full record

ArticleEukaryotic cell2011

Unexpected role for a serine/threonine-rich domain in the Candida albicans Iff protein family.

Anita Boisramé, Amandine Cornu, Grégory Da Costa, Mathias L Richard

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

28 citing papers in PubMed, 44 citations in OpenAlex.

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  11. Virulence · 2022
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  14. Using Genomics to Shape the Definition of the Agglutinin-Like Sequence (Frontiers in cellular and infection microbiology · 2021
    Article
  15. Review
  16. Article
  17. Agglutinin-Like Sequence (Frontiers in microbiology · 2019
    Article
  18. Article
  19. Biological Roles of Protein-Coding Tandem Repeats in the YeastJournal of fungi (Basel, Switzerland) · 2018
    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

4 authors at 1 institution in 1 country.

Anita BoisraméINRA, UMR1319 Micalis, F-78350 Jouy-en-Josas, France. anita.boisrame@grignon.inra.fr
Amandine Cornu
Grégory Da Costa
Mathias L Richard
Microbiologie de l’alimentation au service de la santé · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosylphosphatidylinositol (GPI)-anchored proteins are an important class of cell wall proteins in Candida albicans because of their localization and their function, even if more than half of them have no characterized homolog in the databases. In this study, we focused on the IFF protein family, investigating their exposure on the cell surface and the sequences that determine their subcellular localization. Protein localization and surface exposure were monitored by the addition of a V5 tag on all members of the family. The data obtained using the complete proteins showed for Iff3 (or -9), Iff5, Iff6, and Iff8 a covalent linkage to the β-1,6-glucan network but, remarkably, showed that Iff2/Hyr3 was linked through disulfide bridges or NaOH-labile bonds. However, since some proteins of the Iff family were undetectable, we designed chimeric constructions using the last 60 amino acids of these proteins to test the localization signal. These constructions showed a β-1,6-glucan linkage for Iff1/Rbr3, Iff2/Hyr3, Iff4 and Iff7/Hyr4 C-terminal-Iff5 fusion proteins, and a membrane localization for the Iff10/Flo9 C terminus-Iff5 fusion protein. Immunofluorescence analyses coupled to these cell fraction data confirmed the importance of the length of the central serine/threonine-rich region for cell surface exposure. Further analysis of the Iff2/Hyr3 linkage to the cell surface showed for the first time that a serine/threonine central region of a GPI-anchored protein may be responsible for the disulfide and the NaOH bonds to the glucan and glycoproteins network and may also override the signal of the proximal ω site region.

Indexed as

Multigene FamilyAmino Acid SequenceCandida albicansFungal ProteinsMolecular Sequence DataProtein Structure, TertiarySequence AlignmentFungal Proteins

Identifiers

PMID21841123
PMCPMC3187068
OpenAlexW2105375915

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.