PubMed:7834747 JSONTXT

{"project":"AIMed","denotations":[{"id":"T1","span":{"begin":35,"end":40},"obj":"protein"},{"id":"T2","span":{"begin":50,"end":71},"obj":"protein"},{"id":"T3","span":{"begin":190,"end":211},"obj":"protein"},{"id":"T4","span":{"begin":220,"end":225},"obj":"protein"},{"id":"T5","span":{"begin":231,"end":236},"obj":"protein"},{"id":"T6","span":{"begin":281,"end":286},"obj":"protein"},{"id":"T7","span":{"begin":296,"end":301},"obj":"protein"},{"id":"T8","span":{"begin":445,"end":450},"obj":"protein"},{"id":"T9","span":{"begin":455,"end":460},"obj":"protein"},{"id":"T10","span":{"begin":688,"end":693},"obj":"protein"},{"id":"T11","span":{"begin":697,"end":702},"obj":"protein"},{"id":"T12","span":{"begin":718,"end":721},"obj":"protein"},{"id":"T13","span":{"begin":981,"end":986},"obj":"protein"},{"id":"T14","span":{"begin":1058,"end":1063},"obj":"protein"},{"id":"T15","span":{"begin":1068,"end":1073},"obj":"protein"}],"text":"Cloning and functional analysis of BAG-1: a novel Bcl-2-binding protein with anti-cell death activity.\nUsing a protein interaction cloning technique, we identified cDNAs that encode a novel Bcl-2-binding protein, termed BAG-1. The BAG-1 protein shares no significant homology with Bcl-2 or other Bcl-2 family proteins, which can form homo- and heterodimers. In gene transfer experiments using a human lymphoid cell line, Jurkat, coexpression of BAG-1 and Bcl-2 provided markedly increased protection from cell death induced by several stimuli, including staurosporine, anti-Fas antibody, and cytolytic T cells, relative to cells that contained gene transfer-mediated elevations in either BAG-1 or Bcl-2 protein alone. BAG-transfected 3T3 fibroblasts also exhibited prolonged cell survival in response to an apoptotic stimulus. The findings indicate that bag-1 represents a new type of anti-cell death gene and suggest that some routes of apoptosis induction previously ascribed to Bcl-2-independent pathways may instead reflect a need for the combination of Bcl-2 and BAG-1."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":334,"end":338},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":395,"end":400},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9605"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"}],"text":"Cloning and functional analysis of BAG-1: a novel Bcl-2-binding protein with anti-cell death activity.\nUsing a protein interaction cloning technique, we identified cDNAs that encode a novel Bcl-2-binding protein, termed BAG-1. The BAG-1 protein shares no significant homology with Bcl-2 or other Bcl-2 family proteins, which can form homo- and heterodimers. In gene transfer experiments using a human lymphoid cell line, Jurkat, coexpression of BAG-1 and Bcl-2 provided markedly increased protection from cell death induced by several stimuli, including staurosporine, anti-Fas antibody, and cytolytic T cells, relative to cells that contained gene transfer-mediated elevations in either BAG-1 or Bcl-2 protein alone. BAG-transfected 3T3 fibroblasts also exhibited prolonged cell survival in response to an apoptotic stimulus. The findings indicate that bag-1 represents a new type of anti-cell death gene and suggest that some routes of apoptosis induction previously ascribed to Bcl-2-independent pathways may instead reflect a need for the combination of Bcl-2 and BAG-1."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":738,"end":749},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000057"}],"text":"Cloning and functional analysis of BAG-1: a novel Bcl-2-binding protein with anti-cell death activity.\nUsing a protein interaction cloning technique, we identified cDNAs that encode a novel Bcl-2-binding protein, termed BAG-1. The BAG-1 protein shares no significant homology with Bcl-2 or other Bcl-2 family proteins, which can form homo- and heterodimers. In gene transfer experiments using a human lymphoid cell line, Jurkat, coexpression of BAG-1 and Bcl-2 provided markedly increased protection from cell death induced by several stimuli, including staurosporine, anti-Fas antibody, and cytolytic T cells, relative to cells that contained gene transfer-mediated elevations in either BAG-1 or Bcl-2 protein alone. BAG-transfected 3T3 fibroblasts also exhibited prolonged cell survival in response to an apoptotic stimulus. The findings indicate that bag-1 represents a new type of anti-cell death gene and suggest that some routes of apoptosis induction previously ascribed to Bcl-2-independent pathways may instead reflect a need for the combination of Bcl-2 and BAG-1."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":602,"end":609},"obj":"Cell"},{"id":"T2","span":{"begin":738,"end":749},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000084"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000057"}],"text":"Cloning and functional analysis of BAG-1: a novel Bcl-2-binding protein with anti-cell death activity.\nUsing a protein interaction cloning technique, we identified cDNAs that encode a novel Bcl-2-binding protein, termed BAG-1. The BAG-1 protein shares no significant homology with Bcl-2 or other Bcl-2 family proteins, which can form homo- and heterodimers. In gene transfer experiments using a human lymphoid cell line, Jurkat, coexpression of BAG-1 and Bcl-2 provided markedly increased protection from cell death induced by several stimuli, including staurosporine, anti-Fas antibody, and cytolytic T cells, relative to cells that contained gene transfer-mediated elevations in either BAG-1 or Bcl-2 protein alone. BAG-transfected 3T3 fibroblasts also exhibited prolonged cell survival in response to an apoptotic stimulus. The findings indicate that bag-1 represents a new type of anti-cell death gene and suggest that some routes of apoptosis induction previously ascribed to Bcl-2-independent pathways may instead reflect a need for the combination of Bcl-2 and BAG-1."}