Essential role for vacuolar acidification in Candida albicans virulence. - Wikidata - wikimedia - TriplyDB

Essential role for vacuolar acidification in Candida albicans virulence.

Essential role for vacuolar acidification in Candida albicans virulence.

http://www.wikidata.org/entity/Q37151114

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Advances in targeting the vacuolar proton-translocating ATPase (V-ATPase) for anti-fungal therapy Components of the calcium-calcineurin signaling pathway in fungal cells and their potential as antifungal targets Synergistic Effect of Fluconazole and Calcium Channel Blockers against Resistant Candida albicans In Vivo Indicators of Cytoplasmic, Vacuolar, and Extracellular pH Using pHluorin2 in Candida albicans.The contribution of Candida albicans vacuolar ATPase subunit V₁B, encoded by VMA2, to stress response, autophagy, and virulence is independent of environmental pH.Quinacrine inhibits Candida albicans growth and filamentation at neutral pH.ERG2 and ERG24 Are Required for Normal Vacuolar Physiology as Well as Candida albicans Pathogenicity in a Murine Model of Disseminated but Not Vaginal Candidiasis.Antagonism of Fluconazole and a Proton Pump Inhibitor against Candida albicans.Saccharomyces cerevisiae vacuolar H+-ATPase regulation by disassembly and reassembly: one structure and multiple signals.Attenuation of Candida albicans virulence with focus on disruption of its vacuole functions Proton Transport and pH Control in Fungi.pH-Dependant Antifungal Activity of Valproic Acid against the Human Fungal Pathogen Candida albicans.How alkalinization drives fungal pathogenicity.FcRav2, a gene with a ROGDI domain involved in Fusarium head blight and crown rot on durum wheat caused by Fusarium culmorum.Promising Antifungal Targets Against Based on Ion Homeostasis

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Essential role for vacuolar acidification in Candida albicans virulence.

http://www.wikidata.org/entity/Q37151114

description

article científic

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article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

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scientific article published on 24 July 2013

@en

vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

@da

vědecký článek

@cs

name

Essential role for vacuolar acidification in Candida albicans virulence.

@en

Essential role for vacuolar acidification in Candida albicans virulence.

@nl

type

label

Essential role for vacuolar acidification in Candida albicans virulence.

@en

Essential role for vacuolar acidification in Candida albicans virulence.

@nl

prefLabel

Essential role for vacuolar acidification in Candida albicans virulence.

@en

Essential role for vacuolar acidification in Candida albicans virulence.

@nl

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JBC.M113.494815

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Journal of Biological Chemistry

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Essential role for vacuolar acidification in Candida albicans virulence.

@en

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Brendan Cormack

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Cassandra Patenaude

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Julia Köhler

http://www.w3.org/2001/XMLSchema#string

Rajini Rao

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Yongqiang Zhang

http://www.w3.org/2001/XMLSchema#string

P2860

Characterization of yeast V-ATPase mutants lacking Vph1p or Stv1p and the effect on endocytosis.

Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-subunit differ in coupling efficiency and in vivo dissociation.

vph6 mutants of Saccharomyces cerevisiae require calcineurin for growth and are defective in vacuolar H(+)-ATPase assembly.

STV1 gene encodes functional homologue of 95-kDa yeast vacuolar H(+)-ATPase subunit Vph1p.

The yeast endosomal Na+K+/H+ exchanger Nhx1 regulates cellular pH to control vesicle trafficking

The VPH1 gene encodes a 95-kDa integral membrane polypeptide required for in vivo assembly and activity of the yeast vacuolar H(+)-ATPase.

Requirement for ergosterol in V-ATPase function underlies antifungal activity of azole drugs

Mucosal damage and neutropenia are required for Candida albicans dissemination

Identification of inhibitors of vacuolar proton-translocating ATPase pumps in yeast by high-throughput screening flow cytometry.

Yeasts in the gut: from commensals to infectious agents.

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26256-26264

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scholarly article

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10.1074/JBC.M113.494815

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36

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2013-07-24T00:00:00Z

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251878273

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23884420

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3764829

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