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http://purl.uniprot.org/citations/21420397http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21420397http://www.w3.org/2000/01/rdf-schema#comment"Hydrophilins are a group of proteins that are present in all organisms and that have been defined as being highly hydrophilic and rich in glycine. They are assumed to play important roles in cellular dehydration tolerance. There are 12 genes in the yeast Saccharomyces cerevisiae that encode hydrophilins and most of these genes are stress responsive. However, the functional role of yeast hydrophilins, especially in desiccation and freezing tolerance, is largely unknown. Here, we selected six candidate hydrophilins for further analysis. All six proteins were predicted to be intrinsically disordered, i.e. to have no stable structure in solution. The contribution of these proteins to the desiccation and freezing tolerance of yeast was investigated in the respective knock-out strains. Only the disruption of the genes YJL144W and YMR175W (SIP18) resulted in significantly reduced desiccation tolerance, while none of the strains was affected in its freezing tolerance under our experimental conditions. Complementation experiments showed that yeast cells overexpressing these two genes were both more desiccation and freezing tolerant, confirming the role of these two hydrophilins in yeast dehydration stress tolerance."xsd:string
http://purl.uniprot.org/citations/21420397http://purl.org/dc/terms/identifier"doi:10.1016/j.cryobiol.2011.03.002"xsd:string
http://purl.uniprot.org/citations/21420397http://purl.uniprot.org/core/author"Hincha D.K."xsd:string
http://purl.uniprot.org/citations/21420397http://purl.uniprot.org/core/author"Dang N.X."xsd:string
http://purl.uniprot.org/citations/21420397http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21420397http://purl.uniprot.org/core/name"Cryobiology"xsd:string
http://purl.uniprot.org/citations/21420397http://purl.uniprot.org/core/pages"188-193"xsd:string
http://purl.uniprot.org/citations/21420397http://purl.uniprot.org/core/title"Identification of two hydrophilins that contribute to the desiccation and freezing tolerance of yeast (Saccharomyces cerevisiae) cells."xsd:string
http://purl.uniprot.org/citations/21420397http://purl.uniprot.org/core/volume"62"xsd:string
http://purl.uniprot.org/citations/21420397http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21420397
http://purl.uniprot.org/citations/21420397http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21420397
http://purl.uniprot.org/uniprot/P50263#attribution-B2ADA68D6680046B4996222AF902C885http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/21420397
http://purl.uniprot.org/uniprot/P47009#attribution-B2ADA68D6680046B4996222AF902C885http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/21420397
http://purl.uniprot.org/uniprot/#_P47009-mappedCitation-21420397http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21420397
http://purl.uniprot.org/uniprot/#_P50263-mappedCitation-21420397http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21420397
http://purl.uniprot.org/uniprot/P50263http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21420397
http://purl.uniprot.org/uniprot/P47009http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21420397