Evidence map›Paper›PMID 25886173›Full record

ReviewThe Biochemical journal2015

The multidrug transporter Pdr5 on the 25th anniversary of its discovery: an important model for the study of asymmetric ABC transporters.

John Golin, Suresh V Ambudkar

Open access · greenAbstract readReview
In one paragraph

Review in The Biochemical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.2field-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

32 citing papers in PubMed, 64 citations in OpenAlex.

  1. An ABC-B Transporter Helps ProtectJournal of fungi (Basel, Switzerland) · 2026
    Article
  2. Article
  3. Article
  4. Multidrug efflux pumps and innate azole resistance of Mucor lusitanicus.The Journal of antimicrobial chemotherapy · 2025
    Article
  5. Review
  6. Yeast Tools for Studying Type II Topoisomerases in Budding Yeast.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  7. An in vitro set-up to study Pdr5-mediated substrate translocation.Protein science : a publication of the Protein Society · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
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  15. Review
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  17. 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 2 institutions in 1 country.

John Golin*Department of Biology, The Catholic University of America, Washington, DC 20064, U.S.A.
Suresh V Ambudkar†The Laboratory of Cell Biology, Center for Cancer Research, NCI, NIH, Bethesda, MD 20892, U.S.A.
Center for Cancer Research · USUniversity of America · US

Funding

Biochemical Analysis of Multidrug Resistance-linked Transport ProteinsZIABC010030 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI AMBUDKAR, SURESH · 2009 to 2025
$21.6M
Molecular Genetic Analysis of Pdr5p, a Major Yeast Multidrug TransporterR15GM077211 · NIGMS · CATHOLIC UNIVERSITY OF AMERICA · PI GOLIN, JOHN · 2006 to 2017
$1.2M
Intramural NIH HHSNIGMS NIH HHS GM077211NIGMS NIH HHS R15 GM077211
6 · The paper itself

Abstract

Asymmetric ABC (ATP-binding cassette) transporters make up a significant proportion of this important superfamily of integral membrane proteins. These proteins contain one canonical (catalytic) ATP-binding site and a second atypical site with little enzymatic capability. The baker's yeast (Saccharomyces cerevisiae) Pdr5 multidrug transporter is the founding member of the Pdr subfamily of asymmetric ABC transporters, which exist only in fungi and slime moulds. Because these organisms are of considerable medical and agricultural significance, Pdr5 has been studied extensively, as has its medically important homologue Cdr1 from Candida albicans. Genetic and biochemical analyses of Pdr5 have contributed important observations that are likely to be applicable to mammalian asymmetric ABC multidrug transporter proteins, including the basis of transporter promiscuity, the function of the non-catalytic deviant ATP-binding site, the most complete description of an in vivo transmission interface, and the recent discovery that Pdr5 is a molecular diode (one-way gate). In the present review, we discuss the observations made with Pdr5 and compare them with findings from clinically important asymmetric ABC transporters, such as CFTR (cystic fibrosis transmembrane conductance regulator), Cdr1 and Tap1/Tap2.

Indexed as

Adenosine TriphosphatasesAnimalsATP-Binding Cassette TransportersBinding SitesDrug Resistance, MultipleFungal ProteinsHumansMembrane Transport ProteinsModels, BiologicalModels, MolecularMutationProtein Interaction Domains and MotifsProtein Structure, SecondarySaccharomyces cerevisiae ProteinsSignal TransductionAdenosine TriphosphatasesATP-Binding Cassette TransportersCDR1 protein, Candida albicansFungal ProteinsMembrane Transport ProteinsPDR5 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID25886173
PMCPMC4784962
OpenAlexW2411788789

What OpenQuestion holds

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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.