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http://purl.uniprot.org/citations/18413721http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18413721http://www.w3.org/2000/01/rdf-schema#comment"Misfolded or aggregated proteins have two fates: they are either refolded with the help of chaperones or degraded by the proteasome. Cells also have an alternative pathway that involves intracellular "storage bins" for misfolded intracellular proteins known as aggresomes. Aggresomes recruit motor proteins that transport misfolded or aggregated proteins to chaperones and proteasomes for subsequent destruction. There is emerging evidence that inhibiting the aggresome pathway leads to accumulation of misfolded proteins and apoptosis in tumor cells through autophagy. We discuss the role of aggresomes in cancer and the potential to target this pathway for therapy."xsd:string
http://purl.uniprot.org/citations/18413721http://purl.org/dc/terms/identifier"doi:10.1158/0008-5472.can-07-5989"xsd:string
http://purl.uniprot.org/citations/18413721http://purl.uniprot.org/core/author"Lin T."xsd:string
http://purl.uniprot.org/citations/18413721http://purl.uniprot.org/core/author"Fu C."xsd:string
http://purl.uniprot.org/citations/18413721http://purl.uniprot.org/core/author"Sakamoto K.M."xsd:string
http://purl.uniprot.org/citations/18413721http://purl.uniprot.org/core/author"Rodriguez-Gonzalez A."xsd:string
http://purl.uniprot.org/citations/18413721http://purl.uniprot.org/core/author"Ikeda A.K."xsd:string
http://purl.uniprot.org/citations/18413721http://purl.uniprot.org/core/author"Simms-Waldrip T."xsd:string
http://purl.uniprot.org/citations/18413721http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18413721http://purl.uniprot.org/core/name"Cancer Res"xsd:string
http://purl.uniprot.org/citations/18413721http://purl.uniprot.org/core/pages"2557-2560"xsd:string
http://purl.uniprot.org/citations/18413721http://purl.uniprot.org/core/title"Role of the aggresome pathway in cancer: targeting histone deacetylase 6-dependent protein degradation."xsd:string
http://purl.uniprot.org/citations/18413721http://purl.uniprot.org/core/volume"68"xsd:string
http://purl.uniprot.org/citations/18413721http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18413721
http://purl.uniprot.org/citations/18413721http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18413721
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http://purl.uniprot.org/uniprot/#_B3KNA1-mappedCitation-18413721http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18413721
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http://purl.uniprot.org/uniprot/#_B4DJ18-mappedCitation-18413721http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18413721
http://purl.uniprot.org/uniprot/#_Q9NZS3-mappedCitation-18413721http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18413721