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http://purl.uniprot.org/citations/18800175http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18800175http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18800175http://www.w3.org/2000/01/rdf-schema#comment"Fluorescein efflux from S. cerevisiae cells was measured to study the peculiarities of fluorescein transport system, which is important for yeast resistance to certain drugs and weak organic acid preservatives. Glucose-independent and glucose-stimulated fluorescein effluxes were characterized using iodoacetate, cyanide and orthovanadate, inhibitors of glycolysis, electron transport chain, and ATPases, respectively. It is supposed that in glucose-free medium fluorescein extrusion is ATP-dependent and the energy for this efflux is mainly provided by respiration. In glucose-containing medium, glycolysis plays a critical role for extrusion of fluorescein. The results indicate that acetic acid inhibits the fluorescein efflux from yeast cells. The inhibition constant of glucose-stimulated fluorescein efflux is significantly lower in parental strain than in two mutants defective in PDR12 (ABC-transporter Pdr12p) or WAR1 (transcription factor of Pdr12p). It can be suggested that the membrane protein Pdr12 is involved in fluorescein extrusion from the yeast cells, but component(s) other than Pdr12p is (are) also important."xsd:string
http://purl.uniprot.org/citations/18800175http://purl.uniprot.org/core/author"Miedzobrodzki J."xsd:string
http://purl.uniprot.org/citations/18800175http://purl.uniprot.org/core/author"Miedzobrodzki J."xsd:string
http://purl.uniprot.org/citations/18800175http://purl.uniprot.org/core/author"Abrat O."xsd:string
http://purl.uniprot.org/citations/18800175http://purl.uniprot.org/core/author"Abrat O."xsd:string
http://purl.uniprot.org/citations/18800175http://purl.uniprot.org/core/author"Lushchak V."xsd:string
http://purl.uniprot.org/citations/18800175http://purl.uniprot.org/core/author"Lushchak V."xsd:string
http://purl.uniprot.org/citations/18800175http://purl.uniprot.org/core/author"Semchyshyn H."xsd:string
http://purl.uniprot.org/citations/18800175http://purl.uniprot.org/core/author"Semchyshyn H."xsd:string
http://purl.uniprot.org/citations/18800175http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18800175http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18800175http://purl.uniprot.org/core/name"Acta Biochim. Pol."xsd:string
http://purl.uniprot.org/citations/18800175http://purl.uniprot.org/core/name"Acta Biochim. Pol."xsd:string
http://purl.uniprot.org/citations/18800175http://purl.uniprot.org/core/pages"595-601"xsd:string
http://purl.uniprot.org/citations/18800175http://purl.uniprot.org/core/pages"595-601"xsd:string
http://purl.uniprot.org/citations/18800175http://purl.uniprot.org/core/title"Pdr12p-dependent and -independent fluorescein extrusion from baker's yeast cells."xsd:string
http://purl.uniprot.org/citations/18800175http://purl.uniprot.org/core/title"Pdr12p-dependent and -independent fluorescein extrusion from baker's yeast cells."xsd:string
http://purl.uniprot.org/citations/18800175http://purl.uniprot.org/core/volume"55"xsd:string
http://purl.uniprot.org/citations/18800175http://purl.uniprot.org/core/volume"55"xsd:string
http://purl.uniprot.org/citations/18800175http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18800175
http://purl.uniprot.org/citations/18800175http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18800175
http://purl.uniprot.org/citations/18800175http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18800175
http://purl.uniprot.org/citations/18800175http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18800175