Evidence map›Paper›PMID 25066473›Full record

ArticleBiochimica et biophysica acta2014

Phosphatidylinositol binding of Saccharomyces cerevisiae Pdr16p represents an essential feature of this lipid transfer protein to provide protection against azole antifungals.

Roman Holič, Zuzana Simová, Tim Ashlin, Vladimír Pevala, Katarína Poloncová, Dana Tahotná, Eva Kutejová, Shamshad Cockcroft, Peter Griač

Open access · hybridAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

12 citing papers in PubMed, 27 citations in OpenAlex.

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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

9 authors at 2 institutions in 2 countries.

Roman HoličDepartment of Membrane Biochemistry, Institute of Animal Biochemistry and Genetics, Slovak Academy of Sciences, 900 28 Ivanka pri Dunaji, Slovakia.
Zuzana SimováDepartment of Membrane Biochemistry, Institute of Animal Biochemistry and Genetics, Slovak Academy of Sciences, 900 28 Ivanka pri Dunaji, Slovakia.
Tim AshlinDepartment of Neuroscience, Physiology and Pharmacology, Division of Biosciences, University College London, London WC1E 6JJ, United Kingdom.
Vladimír PevalaDepartment of Biochemistry and Structural Biology, Institute of Molecular Biology, Slovak Academy of Sciences, 845 51 Bratislava, Slovakia.
Katarína PoloncováDepartment of Membrane Biochemistry, Institute of Animal Biochemistry and Genetics, Slovak Academy of Sciences, 900 28 Ivanka pri Dunaji, Slovakia.
Dana TahotnáDepartment of Membrane Biochemistry, Institute of Animal Biochemistry and Genetics, Slovak Academy of Sciences, 900 28 Ivanka pri Dunaji, Slovakia.
Eva KutejováDepartment of Biochemistry and Structural Biology, Institute of Molecular Biology, Slovak Academy of Sciences, 845 51 Bratislava, Slovakia.
Shamshad CockcroftDepartment of Neuroscience, Physiology and Pharmacology, Division of Biosciences, University College London, London WC1E 6JJ, United Kingdom.
Peter GriačDepartment of Membrane Biochemistry, Institute of Animal Biochemistry and Genetics, Slovak Academy of Sciences, 900 28 Ivanka pri Dunaji, Slovakia. Electronic address: Peter.Griac@savba.sk.
Slovak Academy of Sciences · SKUniversity College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pdr16p is considered a factor of clinical azole resistance in fungal pathogens. The most distinct phenotype of yeast cells lacking Pdr16p is their increased susceptibility to azole and morpholine antifungals. Pdr16p (also known as Sfh3p) of Saccharomyces cerevisiae belongs to the Sec14 family of phosphatidylinositol transfer proteins. It facilitates transfer of phosphatidylinositol (PI) between membrane compartments in in vitro systems. We generated Pdr16p(E235A, K267A) mutant defective in PI binding. This PI binding deficient mutant is not able to fulfill the role of Pdr16p in protection against azole and morpholine antifungals, providing evidence that PI binding is critical for Pdr16 function in modulation of sterol metabolism in response to these two types of antifungal drugs. A novel feature of Pdr16p, and especially of Pdr16p(E235A, K267A) mutant, to bind sterol molecules, is observed.

Indexed as

Azole resistanceLipid bindingSaccharomyces cerevisiaeSFH3Sterol metabolism

Identifiers

PMID25066473
PMCPMC4331669
OpenAlexW2000903293

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.