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http://purl.uniprot.org/citations/36206736http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/36206736http://www.w3.org/2000/01/rdf-schema#comment"In this issue of Structure, Armstrong and colleagues probe the structure of human fucosidase FucA1. Their work resolves an ongoing debate around the enzyme's catalytic mechanism and provides a valid structural template to guide the design of drugs alleviating the rare, yet severe, lysosomal storage disease fucosidosis."xsd:string
http://purl.uniprot.org/citations/36206736http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2022.09.002"xsd:string
http://purl.uniprot.org/citations/36206736http://purl.uniprot.org/core/author"Sulzenbacher G."xsd:string
http://purl.uniprot.org/citations/36206736http://purl.uniprot.org/core/author"Barelier S."xsd:string
http://purl.uniprot.org/citations/36206736http://purl.uniprot.org/core/date"2022"xsd:gYear
http://purl.uniprot.org/citations/36206736http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/36206736http://purl.uniprot.org/core/pages"1369-1371"xsd:string
http://purl.uniprot.org/citations/36206736http://purl.uniprot.org/core/title"The long-awaited structure of human fucosidase FucA1 opens novel avenues for the treatment of fucosidosis."xsd:string
http://purl.uniprot.org/citations/36206736http://purl.uniprot.org/core/volume"30"xsd:string
http://purl.uniprot.org/citations/36206736http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/36206736
http://purl.uniprot.org/citations/36206736http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/36206736
http://purl.uniprot.org/uniprot/#_B5MDC5-mappedCitation-36206736http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/36206736
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