| http://purl.uniprot.org/citations/11800270 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11800270 | http://www.w3.org/2000/01/rdf-schema#comment | "O-Glycosylation in many fungal species is initiated in the endoplasmic reticulum by protein mannosyltransferases (Pmt-proteins), which transfer mannose to serine or threonine residues, and it is completed by mannosyltransferases (Mnt-proteins) in the Golgi. In this review, some recent results on O-glycosylation in the human fungal pathogen Candida albicans are discussed and compared to the corresponding knowledge in the non-pathogenic yeast Saccharomyces cerevisiae. The Pmt-family in C. albicans comprises five isoforms, of which Pmt1p and Pmt6p have been studied in detail. Surprisingly, O-glycosylation mediated by Pmt-proteins is required not only for the modification of several secreted and cell-wall proteins, but also affects yeast-hyphal morphogenesis (dimorphism) and resistance to several antifungal compounds. Furthermore, Pmt1- and Pmt6p-activities maximize adherence to host cells and determine or contribute to virulence in models of systemic infection. Thus, O-glycosylation processes directly and/or indirectly affect several virulence traits of C. albicans and can be considered as potential antifungal targets."xsd:string |
| http://purl.uniprot.org/citations/11800270 | http://purl.org/dc/terms/identifier | "doi:10.1080/mmy.39.1.67.74"xsd:string |
| http://purl.uniprot.org/citations/11800270 | http://purl.uniprot.org/core/author | "Ernst J.F."xsd:string |
| http://purl.uniprot.org/citations/11800270 | http://purl.uniprot.org/core/author | "Prill S.K."xsd:string |
| http://purl.uniprot.org/citations/11800270 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11800270 | http://purl.uniprot.org/core/name | "Med Mycol 39 Suppl"xsd:string |
| http://purl.uniprot.org/citations/11800270 | http://purl.uniprot.org/core/pages | "67-74"xsd:string |
| http://purl.uniprot.org/citations/11800270 | http://purl.uniprot.org/core/title | "O-glycosylation."xsd:string |
| http://purl.uniprot.org/citations/11800270 | http://purl.uniprot.org/core/volume | "1"xsd:string |
| http://purl.uniprot.org/citations/11800270 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11800270 |
| http://purl.uniprot.org/citations/11800270 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11800270 |
| http://purl.uniprot.org/uniprot/#_P42934-mappedCitation-11800270 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11800270 |
| http://purl.uniprot.org/uniprot/#_P33775-mappedCitation-11800270 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11800270 |
| http://purl.uniprot.org/uniprot/P42934 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/11800270 |
| http://purl.uniprot.org/uniprot/P33775 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/11800270 |