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http://purl.uniprot.org/citations/11259440http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11259440http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11259440http://www.w3.org/2000/01/rdf-schema#comment"Bax is a proapoptotic member of the Bcl-2 protein family that commits the cell to undergo programmed cell death in response to apoptotic stimuli. To gain further insights into Bax mechanisms, we have identified a novel Bax-binding protein, termed Bif-1, by using a yeast two-hybrid cloning technique. Bif-1 is an evolutionarily conserved cytoplasmic protein that contains a predicted Src homology 3 (SH3) domain located near its C terminus but shares no significant homology with members of the Bcl-2 family. A Northern blot analysis indicates that Bif-1 is expressed in most tissues with abundant expression in heart and skeletal muscle. Bif-1 is capable of interacting with Bax as demonstrated by yeast two-hybrid, coimmunoprecipitation, and immunofluorescence studies. Induction of apoptosis in murine pre-B hematopoietic cells FL5.12 by interleukin-3 withdrawal results in increased association of Bax with Bif-1, which is accompanied by a conformational change in the Bax protein. Overexpression of Bif-1 promotes Bax conformational change, caspase activation, and apoptotic cell death in FL5.12 cells following interleukin-3 deprivation. Bif-1 thus represents a new type of regulator of Bax-mediated signaling pathways for apoptosis."xsd:string
http://purl.uniprot.org/citations/11259440http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m101527200"xsd:string
http://purl.uniprot.org/citations/11259440http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m101527200"xsd:string
http://purl.uniprot.org/citations/11259440http://purl.uniprot.org/core/author"Komatsu K."xsd:string
http://purl.uniprot.org/citations/11259440http://purl.uniprot.org/core/author"Komatsu K."xsd:string
http://purl.uniprot.org/citations/11259440http://purl.uniprot.org/core/author"Singh S."xsd:string
http://purl.uniprot.org/citations/11259440http://purl.uniprot.org/core/author"Singh S."xsd:string
http://purl.uniprot.org/citations/11259440http://purl.uniprot.org/core/author"Yamada M."xsd:string
http://purl.uniprot.org/citations/11259440http://purl.uniprot.org/core/author"Yamada M."xsd:string
http://purl.uniprot.org/citations/11259440http://purl.uniprot.org/core/author"Wu C."xsd:string
http://purl.uniprot.org/citations/11259440http://purl.uniprot.org/core/author"Wu C."xsd:string
http://purl.uniprot.org/citations/11259440http://purl.uniprot.org/core/author"Yamaguchi H."xsd:string
http://purl.uniprot.org/citations/11259440http://purl.uniprot.org/core/author"Yamaguchi H."xsd:string
http://purl.uniprot.org/citations/11259440http://purl.uniprot.org/core/author"Wang H.-G."xsd:string
http://purl.uniprot.org/citations/11259440http://purl.uniprot.org/core/author"Wang H.-G."xsd:string
http://purl.uniprot.org/citations/11259440http://purl.uniprot.org/core/author"Miyashita T."xsd:string
http://purl.uniprot.org/citations/11259440http://purl.uniprot.org/core/author"Miyashita T."xsd:string
http://purl.uniprot.org/citations/11259440http://purl.uniprot.org/core/author"Cuddeback S.M."xsd:string
http://purl.uniprot.org/citations/11259440http://purl.uniprot.org/core/author"Cuddeback S.M."xsd:string
http://purl.uniprot.org/citations/11259440http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11259440http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11259440http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11259440http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string