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http://purl.uniprot.org/citations/18655794http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18655794http://www.w3.org/2000/01/rdf-schema#comment"Tyrosinase is a rate-limiting enzyme in mammalian melanogenesis, and is known as a glycoprotein. Post-translational processing of mammalian tyrosinase is required for its folding, sorting, and for enzymatic activity. Here we show for the first time that the mammalian tyrosinase has beta1,6-branched N-glycan structure that can be recognized by binding with specific lectin Leukoagglutinating phytohematoagglutinin (L-PHA). Further, this specific glycoconjugate structure has been shown to have a function relationship in melanin synthesis."xsd:string
http://purl.uniprot.org/citations/18655794http://purl.org/dc/terms/identifier"doi:10.1016/j.lfs.2008.06.012"xsd:string
http://purl.uniprot.org/citations/18655794http://purl.uniprot.org/core/author"Chakraborty A.K."xsd:string
http://purl.uniprot.org/citations/18655794http://purl.uniprot.org/core/author"Chakraborty D."xsd:string
http://purl.uniprot.org/citations/18655794http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18655794http://purl.uniprot.org/core/name"Life Sci"xsd:string
http://purl.uniprot.org/citations/18655794http://purl.uniprot.org/core/pages"260-263"xsd:string
http://purl.uniprot.org/citations/18655794http://purl.uniprot.org/core/title"Evidence for tyrosinase as a beta1,6 branch containing glycoprotein: substrate of GnT-V."xsd:string
http://purl.uniprot.org/citations/18655794http://purl.uniprot.org/core/volume"83"xsd:string
http://purl.uniprot.org/citations/18655794http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18655794
http://purl.uniprot.org/citations/18655794http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18655794
http://purl.uniprot.org/uniprot/#_Q91XK0-mappedCitation-18655794http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18655794
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http://purl.uniprot.org/uniprot/#_Q3UFR6-mappedCitation-18655794http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18655794
http://purl.uniprot.org/uniprot/#_P11344-mappedCitation-18655794http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18655794
http://purl.uniprot.org/uniprot/#_Q64ID7-mappedCitation-18655794http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18655794
http://purl.uniprot.org/uniprot/#_Q3UFK9-mappedCitation-18655794http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18655794
http://purl.uniprot.org/uniprot/#_Q99NK7-mappedCitation-18655794http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18655794
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http://purl.uniprot.org/uniprot/Q99NK7http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18655794
http://purl.uniprot.org/uniprot/Q64ID7http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18655794
http://purl.uniprot.org/uniprot/Q3UFR6http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18655794