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http://purl.uniprot.org/citations/2250705http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2250705http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2250705http://www.w3.org/2000/01/rdf-schema#comment"The t(14; 18) chromosomal translocation of human follicular B-cell lymphoma juxtaposes the bcl-2 gene with the immunoglobulin heavy chain locus. The bcl-2 immunoglobulin fusion gene is markedly deregulated resulting in inappropriately elevated levels of bcl-2 RNA and protein. Transgenic mice bearing a bcl-2 immunoglobulin minigene demonstrate a polyclonal expansion of resting yet responsive IgM-IgD B cells which display prolonged cell survival but no increase in cell cycling. Moreover, deregulated bcl-2 extends the survival of certain haematopoietic cell lines following growth-factor deprivation. By using immunolocalization studies we now demonstrate that Bcl-2 is an integral inner mitochondrial membrane protein of relative molecular mass 25,000 (25k). Overexpression of Bcl-2 blocks the apoptotic death of a pro-B-lymphocyte cell line. Thus, Bcl-2 is unique among proto-oncogenes, being localized to mitochondria and interfering with programmed cell death independent of promoting cell division."xsd:string
http://purl.uniprot.org/citations/2250705http://purl.org/dc/terms/identifier"doi:10.1038/348334a0"xsd:string
http://purl.uniprot.org/citations/2250705http://purl.org/dc/terms/identifier"doi:10.1038/348334a0"xsd:string
http://purl.uniprot.org/citations/2250705http://purl.uniprot.org/core/author"Nunez G."xsd:string
http://purl.uniprot.org/citations/2250705http://purl.uniprot.org/core/author"Nunez G."xsd:string
http://purl.uniprot.org/citations/2250705http://purl.uniprot.org/core/author"Milliman C."xsd:string
http://purl.uniprot.org/citations/2250705http://purl.uniprot.org/core/author"Milliman C."xsd:string
http://purl.uniprot.org/citations/2250705http://purl.uniprot.org/core/author"Korsmeyer S.J."xsd:string
http://purl.uniprot.org/citations/2250705http://purl.uniprot.org/core/author"Korsmeyer S.J."xsd:string
http://purl.uniprot.org/citations/2250705http://purl.uniprot.org/core/author"Schreiber R.D."xsd:string
http://purl.uniprot.org/citations/2250705http://purl.uniprot.org/core/author"Schreiber R.D."xsd:string
http://purl.uniprot.org/citations/2250705http://purl.uniprot.org/core/author"Hockenbery D."xsd:string
http://purl.uniprot.org/citations/2250705http://purl.uniprot.org/core/author"Hockenbery D."xsd:string
http://purl.uniprot.org/citations/2250705http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/2250705http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/2250705http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/2250705http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/2250705http://purl.uniprot.org/core/pages"334-336"xsd:string
http://purl.uniprot.org/citations/2250705http://purl.uniprot.org/core/pages"334-336"xsd:string
http://purl.uniprot.org/citations/2250705http://purl.uniprot.org/core/title"Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death."xsd:string
http://purl.uniprot.org/citations/2250705http://purl.uniprot.org/core/title"Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death."xsd:string
http://purl.uniprot.org/citations/2250705http://purl.uniprot.org/core/volume"348"xsd:string
http://purl.uniprot.org/citations/2250705http://purl.uniprot.org/core/volume"348"xsd:string