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http://purl.uniprot.org/citations/19640993http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19640993http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19640993http://www.w3.org/2000/01/rdf-schema#comment"The severe acute respiratory syndrome coronavirus (SARS-CoV) generates 16 nonstructural proteins (nsp's) through proteolytic cleavage of a large precursor protein. Although several nsp's exhibit catalytic activities that are important for viral replication and transcription, other nsp's have less clearly defined roles during an infection. In order to gain a better understanding of their functions, we attempted to identify host proteins that interact with nsp's during SARS-CoV infections. For nsp2, we identified an interaction with two host proteins, prohibitin 1 (PHB1) and PHB2. Our results suggest that nsp2 may be involved in the disruption of intracellular host signaling during SARS-CoV infections."xsd:string
http://purl.uniprot.org/citations/19640993http://purl.org/dc/terms/identifier"doi:10.1128/jvi.00842-09"xsd:string
http://purl.uniprot.org/citations/19640993http://purl.org/dc/terms/identifier"doi:10.1128/jvi.00842-09"xsd:string
http://purl.uniprot.org/citations/19640993http://purl.uniprot.org/core/author"Kuhn P."xsd:string
http://purl.uniprot.org/citations/19640993http://purl.uniprot.org/core/author"Kuhn P."xsd:string
http://purl.uniprot.org/citations/19640993http://purl.uniprot.org/core/author"Yates J.R."xsd:string
http://purl.uniprot.org/citations/19640993http://purl.uniprot.org/core/author"Yates J.R."xsd:string
http://purl.uniprot.org/citations/19640993http://purl.uniprot.org/core/author"Liao L."xsd:string
http://purl.uniprot.org/citations/19640993http://purl.uniprot.org/core/author"Liao L."xsd:string
http://purl.uniprot.org/citations/19640993http://purl.uniprot.org/core/author"Buchmeier M.J."xsd:string
http://purl.uniprot.org/citations/19640993http://purl.uniprot.org/core/author"Buchmeier M.J."xsd:string
http://purl.uniprot.org/citations/19640993http://purl.uniprot.org/core/author"Cornillez-Ty C.T."xsd:string
http://purl.uniprot.org/citations/19640993http://purl.uniprot.org/core/author"Cornillez-Ty C.T."xsd:string
http://purl.uniprot.org/citations/19640993http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19640993http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19640993http://purl.uniprot.org/core/name"J. Virol."xsd:string
http://purl.uniprot.org/citations/19640993http://purl.uniprot.org/core/name"J. Virol."xsd:string
http://purl.uniprot.org/citations/19640993http://purl.uniprot.org/core/pages"10314-10318"xsd:string
http://purl.uniprot.org/citations/19640993http://purl.uniprot.org/core/pages"10314-10318"xsd:string
http://purl.uniprot.org/citations/19640993http://purl.uniprot.org/core/title"Severe acute respiratory syndrome coronavirus nonstructural protein 2 interacts with a host protein complex involved in mitochondrial biogenesis and intracellular signaling."xsd:string
http://purl.uniprot.org/citations/19640993http://purl.uniprot.org/core/title"Severe acute respiratory syndrome coronavirus nonstructural protein 2 interacts with a host protein complex involved in mitochondrial biogenesis and intracellular signaling."xsd:string
http://purl.uniprot.org/citations/19640993http://purl.uniprot.org/core/volume"83"xsd:string
http://purl.uniprot.org/citations/19640993http://purl.uniprot.org/core/volume"83"xsd:string