PubMed:7538907 JSONTXT

{"project":"AIMed","denotations":[{"id":"T1","span":{"begin":0,"end":4},"obj":"protein"},{"id":"T2","span":{"begin":82,"end":85},"obj":"protein"},{"id":"T3","span":{"begin":143,"end":146},"obj":"protein"},{"id":"T4","span":{"begin":227,"end":231},"obj":"protein"},{"id":"T5","span":{"begin":245,"end":248},"obj":"protein"},{"id":"T6","span":{"begin":253,"end":256},"obj":"protein"},{"id":"T7","span":{"begin":257,"end":260},"obj":"protein"},{"id":"T8","span":{"begin":274,"end":277},"obj":"protein"},{"id":"T9","span":{"begin":358,"end":361},"obj":"protein"},{"id":"T10","span":{"begin":362,"end":365},"obj":"protein"},{"id":"T11","span":{"begin":370,"end":373},"obj":"protein"},{"id":"T12","span":{"begin":374,"end":377},"obj":"protein"},{"id":"T13","span":{"begin":379,"end":383},"obj":"protein"},{"id":"T14","span":{"begin":443,"end":446},"obj":"protein"},{"id":"T15","span":{"begin":451,"end":457},"obj":"protein"},{"id":"T16","span":{"begin":479,"end":483},"obj":"protein"},{"id":"T17","span":{"begin":518,"end":521},"obj":"protein"},{"id":"T18","span":{"begin":553,"end":556},"obj":"protein"},{"id":"T19","span":{"begin":631,"end":635},"obj":"protein"},{"id":"T20","span":{"begin":690,"end":693},"obj":"protein"},{"id":"T21","span":{"begin":727,"end":731},"obj":"protein"},{"id":"T22","span":{"begin":761,"end":797},"obj":"protein"},{"id":"T23","span":{"begin":827,"end":831},"obj":"protein"},{"id":"T24","span":{"begin":898,"end":901},"obj":"protein"}],"text":"FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis.\nUsing the cytoplasmic domain of Fas in the yeast two-hybrid system, we have identified a novel interacting protein, FADD, which binds Fas and Fas-FD5, a mutant of Fas possessing enhanced killing activity, but not the functionally inactive mutants Fas-LPR and Fas-FD8. FADD contains a death domain homologous to the death domains of Fas and TNFR-1. A point mutation in FADD, analogous to the lpr mutation of Fas, abolishes its ability to bind Fas, suggesting a death domain to death domain interaction. Overexpression of FADD in MCF7 and BJAB cells induces apoptosis, which, like Fas-induced apoptosis, is blocked by CrmA, a specific inhibitor of the interleukin-1 beta-converting enzyme. These findings suggest that FADD may play an important role in the proximal signal transduction of Fas."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":866,"end":874},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000491"}],"text":"FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis.\nUsing the cytoplasmic domain of Fas in the yeast two-hybrid system, we have identified a novel interacting protein, FADD, which binds Fas and Fas-FD5, a mutant of Fas possessing enhanced killing activity, but not the functionally inactive mutants Fas-LPR and Fas-FD8. FADD contains a death domain homologous to the death domains of Fas and TNFR-1. A point mutation in FADD, analogous to the lpr mutation of Fas, abolishes its ability to bind Fas, suggesting a death domain to death domain interaction. Overexpression of FADD in MCF7 and BJAB cells induces apoptosis, which, like Fas-induced apoptosis, is blocked by CrmA, a specific inhibitor of the interleukin-1 beta-converting enzyme. These findings suggest that FADD may play an important role in the proximal signal transduction of Fas."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":121,"end":132},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0005737"}],"text":"FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis.\nUsing the cytoplasmic domain of Fas in the yeast two-hybrid system, we have identified a novel interacting protein, FADD, which binds Fas and Fas-FD5, a mutant of Fas possessing enhanced killing activity, but not the functionally inactive mutants Fas-LPR and Fas-FD8. FADD contains a death domain homologous to the death domains of Fas and TNFR-1. A point mutation in FADD, analogous to the lpr mutation of Fas, abolishes its ability to bind Fas, suggesting a death domain to death domain interaction. Overexpression of FADD in MCF7 and BJAB cells induces apoptosis, which, like Fas-induced apoptosis, is blocked by CrmA, a specific inhibitor of the interleukin-1 beta-converting enzyme. These findings suggest that FADD may play an important role in the proximal signal transduction of Fas."}