http://purl.uniprot.org/citations/23159880 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/23159880 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/23159880 | http://www.w3.org/2000/01/rdf-schema#comment | "Lysosomal storage diseases are treated with human lysosomal enzymes produced in mammalian cells. Such enzyme therapeutics contain relatively low levels of mannose-6-phosphate, which is required to target them to the lysosomes of patient cells. Here we describe a method for increasing mannose-6-phosphate modification of lysosomal enzymes produced in yeast. We identified a glycosidase from C. cellulans that 'uncaps' N-glycans modified by yeast-type mannose-Pi-6-mannose to generate mammalian-type N-glycans with a mannose-6-phosphate substitution. Determination of the crystal structure of this glycosidase provided insight into its substrate specificity. We used this uncapping enzyme together with α-mannosidase to produce in yeast a form of the Pompe disease enzyme α-glucosidase rich in mannose-6-phosphate. Compared with the currently used therapeutic version, this form of α-glucosidase was more efficiently taken up by fibroblasts from Pompe disease patients, and it more effectively reduced cardiac muscular glycogen storage in a mouse model of the disease."xsd:string |
http://purl.uniprot.org/citations/23159880 | http://purl.org/dc/terms/identifier | "doi:10.1038/nbt.2427"xsd:string |
http://purl.uniprot.org/citations/23159880 | http://purl.org/dc/terms/identifier | "doi:10.1038/nbt.2427"xsd:string |
http://purl.uniprot.org/citations/23159880 | http://purl.uniprot.org/core/author | "Geysens S."xsd:string |
http://purl.uniprot.org/citations/23159880 | http://purl.uniprot.org/core/author | "Geysens S."xsd:string |
http://purl.uniprot.org/citations/23159880 | http://purl.uniprot.org/core/author | "Callewaert N."xsd:string |
http://purl.uniprot.org/citations/23159880 | http://purl.uniprot.org/core/author | "Callewaert N."xsd:string |
http://purl.uniprot.org/citations/23159880 | http://purl.uniprot.org/core/author | "Tiels P."xsd:string |
http://purl.uniprot.org/citations/23159880 | http://purl.uniprot.org/core/author | "Tiels P."xsd:string |
http://purl.uniprot.org/citations/23159880 | http://purl.uniprot.org/core/author | "Van Hecke A."xsd:string |
http://purl.uniprot.org/citations/23159880 | http://purl.uniprot.org/core/author | "Van Hecke A."xsd:string |
http://purl.uniprot.org/citations/23159880 | http://purl.uniprot.org/core/author | "Vervecken W."xsd:string |
http://purl.uniprot.org/citations/23159880 | http://purl.uniprot.org/core/author | "Vervecken W."xsd:string |
http://purl.uniprot.org/citations/23159880 | http://purl.uniprot.org/core/author | "Remaut H."xsd:string |
http://purl.uniprot.org/citations/23159880 | http://purl.uniprot.org/core/author | "Remaut H."xsd:string |
http://purl.uniprot.org/citations/23159880 | http://purl.uniprot.org/core/author | "Piens K."xsd:string |
http://purl.uniprot.org/citations/23159880 | http://purl.uniprot.org/core/author | "Piens K."xsd:string |
http://purl.uniprot.org/citations/23159880 | http://purl.uniprot.org/core/author | "Nerinckx W."xsd:string |
http://purl.uniprot.org/citations/23159880 | http://purl.uniprot.org/core/author | "Nerinckx W."xsd:string |
http://purl.uniprot.org/citations/23159880 | http://purl.uniprot.org/core/author | "Stout J."xsd:string |
http://purl.uniprot.org/citations/23159880 | http://purl.uniprot.org/core/author | "Stout J."xsd:string |
http://purl.uniprot.org/citations/23159880 | http://purl.uniprot.org/core/author | "Hulpiau P."xsd:string |
http://purl.uniprot.org/citations/23159880 | http://purl.uniprot.org/core/author | "Hulpiau P."xsd:string |