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http://purl.uniprot.org/citations/7628016http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7628016http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7628016http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/7628016http://www.w3.org/2000/01/rdf-schema#comment"Multiple sulfatase deficiency (MSD) is a lysosomal storage disorder characterized by a decreased activity of all known sulfatases. The deficiency of sulfatases was proposed to result from the lack of a co- or posttranslational modification that is common to all sulfatases and required for their catalytic activity. Structural analysis of two catalytically active sulfatases revealed that a cysteine residue that is predicted from the cDNA sequence and conserved among all known sulfatases is replaced by a 2-amino-3-oxopropionic acid residue, while in sulfatases derived from MSD cells, this cysteine residue is retained. It is proposed that the co- or posttranslational conversion of a cysteine to 2-amino-3-oxopropionic acid is required for generating catalytically active sulfatases and that deficiency of this protein modification is the cause of MSD."xsd:string
http://purl.uniprot.org/citations/7628016http://purl.org/dc/terms/identifier"doi:10.1016/0092-8674(95)90314-3"xsd:string
http://purl.uniprot.org/citations/7628016http://purl.org/dc/terms/identifier"doi:10.1016/0092-8674(95)90314-3"xsd:string
http://purl.uniprot.org/citations/7628016http://purl.uniprot.org/core/author"Schmidt B."xsd:string
http://purl.uniprot.org/citations/7628016http://purl.uniprot.org/core/author"Schmidt B."xsd:string
http://purl.uniprot.org/citations/7628016http://purl.uniprot.org/core/author"Selmer T."xsd:string
http://purl.uniprot.org/citations/7628016http://purl.uniprot.org/core/author"Selmer T."xsd:string
http://purl.uniprot.org/citations/7628016http://purl.uniprot.org/core/author"von Figura K."xsd:string
http://purl.uniprot.org/citations/7628016http://purl.uniprot.org/core/author"von Figura K."xsd:string
http://purl.uniprot.org/citations/7628016http://purl.uniprot.org/core/author"Ingendoh A."xsd:string
http://purl.uniprot.org/citations/7628016http://purl.uniprot.org/core/author"Ingendoh A."xsd:string
http://purl.uniprot.org/citations/7628016http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7628016http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7628016http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/7628016http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/7628016http://purl.uniprot.org/core/pages"271-278"xsd:string
http://purl.uniprot.org/citations/7628016http://purl.uniprot.org/core/pages"271-278"xsd:string
http://purl.uniprot.org/citations/7628016http://purl.uniprot.org/core/title"A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency."xsd:string
http://purl.uniprot.org/citations/7628016http://purl.uniprot.org/core/title"A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency."xsd:string
http://purl.uniprot.org/citations/7628016http://purl.uniprot.org/core/volume"82"xsd:string
http://purl.uniprot.org/citations/7628016http://purl.uniprot.org/core/volume"82"xsd:string
http://purl.uniprot.org/citations/7628016http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7628016