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http://purl.uniprot.org/citations/18321989http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18321989http://www.w3.org/2000/01/rdf-schema#comment"Over the last decade, yeast has been used successfully as a model system for studying the molecular mechanism of apoptotic cell death. Here, we report that Mcd1, the yeast homology of human cohesin Rad21, plays an important role in hydrogen peroxide-induced apoptosis in yeast. On induction of cell death, Mcd1 is cleaved and the C-terminal fragment is translocated from nucleus into mitochondria, causing the decrease of mitochondrial membrane potential and the amplification of cell death in a cytochrome c-dependent manner. We further demonstrate that the caspase-like protease Esp1 has dual functions and that it is responsible for the cleavage of Mcd1 during the hydrogen peroxide-induced apoptosis. When apoptosis is induced, Esp1 is released from the anaphase inhibitor Pds1. The activated Esp1 acts as caspase-like protease for the cleavage of Mcd1, which enhances the cell death via its translocation from nucleus to mitochondria."xsd:string
http://purl.uniprot.org/citations/18321989http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e07-11-1113"xsd:string
http://purl.uniprot.org/citations/18321989http://purl.uniprot.org/core/author"Ren Q."xsd:string
http://purl.uniprot.org/citations/18321989http://purl.uniprot.org/core/author"Zhang Z."xsd:string
http://purl.uniprot.org/citations/18321989http://purl.uniprot.org/core/author"Yang H."xsd:string
http://purl.uniprot.org/citations/18321989http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18321989http://purl.uniprot.org/core/name"Mol Biol Cell"xsd:string
http://purl.uniprot.org/citations/18321989http://purl.uniprot.org/core/pages"2127-2134"xsd:string
http://purl.uniprot.org/citations/18321989http://purl.uniprot.org/core/title"Cleavage of Mcd1 by caspase-like protease Esp1 promotes apoptosis in budding yeast."xsd:string
http://purl.uniprot.org/citations/18321989http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/18321989http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18321989
http://purl.uniprot.org/citations/18321989http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18321989
http://purl.uniprot.org/uniprot/Q03018#attribution-8E3A0883174160F3D812F8BBAAA180AEhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18321989
http://purl.uniprot.org/uniprot/Q12158#attribution-11AD76E5873B420F78AC3426EE1F0286http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18321989
http://purl.uniprot.org/uniprot/Q12158#attribution-8E3A0883174160F3D812F8BBAAA180AEhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18321989
http://purl.uniprot.org/uniprot/#_A0A8H4FA12-mappedCitation-18321989http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18321989
http://purl.uniprot.org/uniprot/#_A0A8H8UMR9-mappedCitation-18321989http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18321989
http://purl.uniprot.org/uniprot/#_Q12158-mappedCitation-18321989http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18321989
http://purl.uniprot.org/uniprot/#_Q03018-mappedCitation-18321989http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18321989
http://purl.uniprot.org/uniprot/A0A8H4FA12http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18321989
http://purl.uniprot.org/uniprot/Q03018http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18321989
http://purl.uniprot.org/uniprot/A0A8H8UMR9http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18321989
http://purl.uniprot.org/uniprot/Q12158http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18321989