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http://purl.uniprot.org/citations/2204115http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2204115http://www.w3.org/2000/01/rdf-schema#comment"The post-translational processing of the yeast a-mating pheromone precursor, Ras proteins, nuclear lamins, and some subunits of trimeric G proteins requires a set of complex modifications at their carboxyl termini. This processing includes three steps: prenylation of a cysteine residue, proteolytic processing, and carboxymethylation. In the yeast Saccharomyces cerevisiae, the product of the DPR1-RAM1 gene participates in this type of processing. Through the use of an in vitro assay with peptide substrates modeled after a presumptive a-mating pheromone precursor, it was discovered that mutations in DPR1-RAM1 cause a defect in the prenylation reaction. It was further shown that DPR1-RAM1 encodes an essential and limiting component of a protein prenyltransferase. These studies also implied a fixed order of the three processing steps shared by prenylated proteins: prenylation, proteolysis, then carboxymethylation. Because the yeast protein prenyltransferase could also prenylate human H-ras p21 precursor, the human DPR1-RAM1 analogue may be a useful target for anticancer chemotherapy."xsd:string
http://purl.uniprot.org/citations/2204115http://purl.org/dc/terms/identifier"doi:10.1126/science.2204115"xsd:string
http://purl.uniprot.org/citations/2204115http://purl.uniprot.org/core/author"Kim S.H."xsd:string
http://purl.uniprot.org/citations/2204115http://purl.uniprot.org/core/author"Poulter C.D."xsd:string
http://purl.uniprot.org/citations/2204115http://purl.uniprot.org/core/author"Yang C.C."xsd:string
http://purl.uniprot.org/citations/2204115http://purl.uniprot.org/core/author"Rosenberg S."xsd:string
http://purl.uniprot.org/citations/2204115http://purl.uniprot.org/core/author"Rine J."xsd:string
http://purl.uniprot.org/citations/2204115http://purl.uniprot.org/core/author"Schafer W.R."xsd:string
http://purl.uniprot.org/citations/2204115http://purl.uniprot.org/core/author"Mayer M.P."xsd:string
http://purl.uniprot.org/citations/2204115http://purl.uniprot.org/core/author"Trueblood C.E."xsd:string
http://purl.uniprot.org/citations/2204115http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/2204115http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/2204115http://purl.uniprot.org/core/pages"1133-1139"xsd:string
http://purl.uniprot.org/citations/2204115http://purl.uniprot.org/core/title"Enzymatic coupling of cholesterol intermediates to a mating pheromone precursor and to the ras protein."xsd:string
http://purl.uniprot.org/citations/2204115http://purl.uniprot.org/core/volume"249"xsd:string
http://purl.uniprot.org/citations/2204115http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2204115
http://purl.uniprot.org/citations/2204115http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/2204115
http://purl.uniprot.org/uniprot/#_P22007-mappedCitation-2204115http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/2204115
http://purl.uniprot.org/uniprot/P22007http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/2204115