Evidence map›Paper›PMID 25057462›Full record

ArticleInternational journal for parasitology. Drugs and drug resistance2014

Quantitative proteomic analysis of amphotericin B resistance in Leishmania infantum.

Marie-Christine Brotherton, Sylvie Bourassa, Danielle Légaré, Guy G Poirier, Arnaud Droit, Marc Ouellette

Open access · goldAbstract read
In one paragraph

Article in International journal for parasitology. Drugs and drug resistance, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
8.7field-weighted citation impact, top 2% 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

45 citing papers in PubMed, 89 citations in OpenAlex.

  1. Insights into the Structural and Proteomic Changes inAnimals : an open access journal from MDPI · 2025
    Article
  2. CRISPR-Cas13b mediated gene knockdowns in Leishmania infantum.International journal for parasitology. Drugs and drug resistance · 2025
    Article
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  10. ACS infectious diseases · 2023
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  15. Microbiology spectrum · 2021
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  16. Review
  17. Influence ofMolecules (Basel, Switzerland) · 2021
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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

6 authors at 2 institutions in 1 country.

Marie-Christine BrothertonCentre de Recherche en Infectiologie du Centre de Recherche du CHU de Québec, Pavillon CHUL, and Département de Microbiologie-Infectiologie et Immunologie, Faculté de Médecine, Université Laval, Québec, Canada.
Sylvie BourassaPlate-forme Protéomique du Centre de Génomique de Québec, CHU de Québec, Pavillon CHUL, Université Laval, Québec, Canada.
Danielle LégaréCentre de Recherche en Infectiologie du Centre de Recherche du CHU de Québec, Pavillon CHUL, and Département de Microbiologie-Infectiologie et Immunologie, Faculté de Médecine, Université Laval, Québec, Canada.
Guy G PoirierPlate-forme Protéomique du Centre de Génomique de Québec, CHU de Québec, Pavillon CHUL, Université Laval, Québec, Canada.
Arnaud DroitPlate-forme Protéomique du Centre de Génomique de Québec, CHU de Québec, Pavillon CHUL, Université Laval, Québec, Canada.
Marc OuelletteCentre de Recherche en Infectiologie du Centre de Recherche du CHU de Québec, Pavillon CHUL, and Département de Microbiologie-Infectiologie et Immunologie, Faculté de Médecine, Université Laval, Québec, Canada.
Centre hospitalier de l'Université Laval · CAUniversité Laval · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amphotericin B (AmB) in its liposomal form is now considered as either first- or second-line treatment against Leishmania infections in different part of the world. Few cases of AmB resistance have been reported and resistance mechanisms toward AmB are still poorly understood. This paper reports a large-scale comparative proteomic study in the context of AmB resistance. Quantitative proteomics using stable isotope labeling of amino acids in cell culture (SILAC) was used to better characterize cytoplasmic and membrane-enriched (ME) proteomes of the in vitro generated Leishmania infantum AmB resistant mutant AmB1000.1. In total, 97 individual proteins were found as differentially expressed between the mutant and its parental sensitive strain (WT). More than half of these proteins were either metabolic enzymes or involved in transcription or translation processes. Key energetic pathways such as glycolysis and TCA cycle were up-regulated in the mutant. Interestingly, many proteins involved in reactive oxygen species (ROS) scavenging and heat-shock proteins were also up-regulated in the resistant mutant. This work provides a basis for further investigations to understand the roles of proteins differentially expressed in relation with AmB resistance.

Indexed as

Amphotericin BDrug resistanceLeishmaniaQuantitative proteomicsStable isotope labeling of amino acids in cell culture (SILAC)

Identifiers

PMID25057462
PMCPMC4095042
OpenAlexW2079086346

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.