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http://purl.uniprot.org/citations/24265594http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24265594http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24265594http://www.w3.org/2000/01/rdf-schema#comment"Several myopathies are associated with defects in autophagic and lysosomal degradation of glycogen, but it remains unclear how glycogen is targeted to the lysosome and what significance this process has for muscle cells. We have established a Drosophila melanogaster model to study glycogen autophagy in skeletal muscles, using chloroquine (CQ) to simulate a vacuolar myopathy that is completely dependent on the core autophagy genes. We show that autophagy is required for the most efficient degradation of glycogen in response to starvation. Furthermore, we show that CQ-induced myopathy can be improved by reduction of either autophagy or glycogen synthesis, the latter possibly due to a direct role of Glycogen Synthase in regulating autophagy through its interaction with Atg8."xsd:string
http://purl.uniprot.org/citations/24265594http://purl.org/dc/terms/identifier"doi:10.1371/journal.pbio.1001708"xsd:string
http://purl.uniprot.org/citations/24265594http://purl.org/dc/terms/identifier"doi:10.1371/journal.pbio.1001708"xsd:string
http://purl.uniprot.org/citations/24265594http://purl.uniprot.org/core/author"Perrimon N."xsd:string
http://purl.uniprot.org/citations/24265594http://purl.uniprot.org/core/author"Perrimon N."xsd:string
http://purl.uniprot.org/citations/24265594http://purl.uniprot.org/core/author"Nieuwenhuis J."xsd:string
http://purl.uniprot.org/citations/24265594http://purl.uniprot.org/core/author"Nieuwenhuis J."xsd:string
http://purl.uniprot.org/citations/24265594http://purl.uniprot.org/core/author"Zirin J."xsd:string
http://purl.uniprot.org/citations/24265594http://purl.uniprot.org/core/author"Zirin J."xsd:string
http://purl.uniprot.org/citations/24265594http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/24265594http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/24265594http://purl.uniprot.org/core/name"PLoS Biol."xsd:string
http://purl.uniprot.org/citations/24265594http://purl.uniprot.org/core/name"PLoS Biol."xsd:string
http://purl.uniprot.org/citations/24265594http://purl.uniprot.org/core/pages"E1001708"xsd:string
http://purl.uniprot.org/citations/24265594http://purl.uniprot.org/core/pages"E1001708"xsd:string
http://purl.uniprot.org/citations/24265594http://purl.uniprot.org/core/title"Role of autophagy in glycogen breakdown and its relevance to chloroquine myopathy."xsd:string
http://purl.uniprot.org/citations/24265594http://purl.uniprot.org/core/title"Role of autophagy in glycogen breakdown and its relevance to chloroquine myopathy."xsd:string
http://purl.uniprot.org/citations/24265594http://purl.uniprot.org/core/volume"11"xsd:string
http://purl.uniprot.org/citations/24265594http://purl.uniprot.org/core/volume"11"xsd:string
http://purl.uniprot.org/citations/24265594http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24265594
http://purl.uniprot.org/citations/24265594http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24265594
http://purl.uniprot.org/citations/24265594http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24265594
http://purl.uniprot.org/citations/24265594http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24265594