PubMed:9311830
Annnotations
jnlpba-st-training
{"project":"jnlpba-st-training","denotations":[{"id":"T1","span":{"begin":15,"end":20},"obj":"protein"},{"id":"T2","span":{"begin":206,"end":217},"obj":"cell_type"},{"id":"T3","span":{"begin":221,"end":241},"obj":"cell_type"},{"id":"T4","span":{"begin":404,"end":409},"obj":"protein"},{"id":"T5","span":{"begin":414,"end":464},"obj":"protein"},{"id":"T6","span":{"begin":490,"end":495},"obj":"protein"},{"id":"T7","span":{"begin":503,"end":525},"obj":"protein"},{"id":"T8","span":{"begin":541,"end":546},"obj":"protein"},{"id":"T9","span":{"begin":550,"end":563},"obj":"cell_line"},{"id":"T10","span":{"begin":614,"end":631},"obj":"protein"},{"id":"T11","span":{"begin":673,"end":678},"obj":"protein"},{"id":"T12","span":{"begin":784,"end":817},"obj":"cell_type"},{"id":"T13","span":{"begin":834,"end":839},"obj":"protein"},{"id":"T14","span":{"begin":851,"end":864},"obj":"cell_line"},{"id":"T15","span":{"begin":932,"end":937},"obj":"protein"},{"id":"T16","span":{"begin":942,"end":948},"obj":"protein"},{"id":"T17","span":{"begin":987,"end":992},"obj":"protein"},{"id":"T18","span":{"begin":1011,"end":1016},"obj":"protein"},{"id":"T19","span":{"begin":1021,"end":1027},"obj":"protein"},{"id":"T20","span":{"begin":1136,"end":1162},"obj":"protein"},{"id":"T21","span":{"begin":1167,"end":1182},"obj":"protein"},{"id":"T22","span":{"begin":1229,"end":1265},"obj":"protein"},{"id":"T23","span":{"begin":1290,"end":1295},"obj":"protein"},{"id":"T24","span":{"begin":1299,"end":1328},"obj":"cell_type"},{"id":"T25","span":{"begin":1488,"end":1493},"obj":"protein"},{"id":"T26","span":{"begin":1498,"end":1503},"obj":"protein"},{"id":"T27","span":{"begin":1509,"end":1520},"obj":"cell_line"},{"id":"T28","span":{"begin":1522,"end":1526},"obj":"cell_line"},{"id":"T29","span":{"begin":1624,"end":1643},"obj":"cell_type"},{"id":"T30","span":{"begin":1674,"end":1679},"obj":"protein"},{"id":"T31","span":{"begin":1716,"end":1721},"obj":"protein"}],"text":"The ability of BHRF1 to inhibit apoptosis is dependent on stimulus and cell type.\nThe development of resistance to host defense mechanisms such as tumor necrosis factor (TNF)- and Fas-mediated apoptosis of transformed or virus-infected cells may be a critical component in the development of disease. To find genes that protect cells from apoptosis, we used an expression cloning strategy and identified BHRF1, an Epstein-Barr virus (EBV) early-lytic-cycle protein with distant homology to Bcl-2, as an anti-apoptosis protein. Expression of BHRF1 in MCF-Fas cells conferred nearly complete resistance against both anti-Fas antibody and TNF-mediated apoptosis. In addition, BHRF1 protected these cells from monocyte-mediated killing but failed to protect them from killing mediated by lymphokine-activated killer cells. The ability of BHRF1 to protect MCF-Fas cells from apoptosis induced by various stimuli was identical to that of Bcl-2 and Bcl-xL. Moreover, the mechanism of action of BHRF1 resembled that of Bcl-2 and Bcl-xL as it inhibited TNF- and anti-Fas-induced activation of two enzymes participating in the apoptosis pathway, cytosolic phospholipase A2 and caspase-3/CPP32, but did not interfere with the activation of NF-kappaB-like transcription factors. A putative function of BHRF1 in EBV-infected epithelial cells may be to protect virus-infected cells from TNF- and/or anti-Fas-induced cell death in order to maximize virus production. Surprisingly, expression of neither BHRF1 nor Bcl-2 in a B-cell line, BJAB, protected the cells from anti-Fas-mediated apoptosis even though they increased the survival of serum-starved cells. Thus, the protective role of BHRF1 against apoptosis resembles that of Bcl-2 in being cell type specific and dependent on the apoptotic stimulus."}
pubmed-sentences-benchmark
{"project":"pubmed-sentences-benchmark","denotations":[{"id":"S1","span":{"begin":0,"end":81},"obj":"Sentence"},{"id":"S2","span":{"begin":82,"end":300},"obj":"Sentence"},{"id":"S3","span":{"begin":301,"end":526},"obj":"Sentence"},{"id":"S4","span":{"begin":527,"end":659},"obj":"Sentence"},{"id":"S5","span":{"begin":660,"end":818},"obj":"Sentence"},{"id":"S6","span":{"begin":819,"end":949},"obj":"Sentence"},{"id":"S7","span":{"begin":950,"end":1266},"obj":"Sentence"},{"id":"S8","span":{"begin":1267,"end":1451},"obj":"Sentence"},{"id":"S9","span":{"begin":1452,"end":1644},"obj":"Sentence"},{"id":"S10","span":{"begin":1645,"end":1790},"obj":"Sentence"}],"text":"The ability of BHRF1 to inhibit apoptosis is dependent on stimulus and cell type.\nThe development of resistance to host defense mechanisms such as tumor necrosis factor (TNF)- and Fas-mediated apoptosis of transformed or virus-infected cells may be a critical component in the development of disease. To find genes that protect cells from apoptosis, we used an expression cloning strategy and identified BHRF1, an Epstein-Barr virus (EBV) early-lytic-cycle protein with distant homology to Bcl-2, as an anti-apoptosis protein. Expression of BHRF1 in MCF-Fas cells conferred nearly complete resistance against both anti-Fas antibody and TNF-mediated apoptosis. In addition, BHRF1 protected these cells from monocyte-mediated killing but failed to protect them from killing mediated by lymphokine-activated killer cells. The ability of BHRF1 to protect MCF-Fas cells from apoptosis induced by various stimuli was identical to that of Bcl-2 and Bcl-xL. Moreover, the mechanism of action of BHRF1 resembled that of Bcl-2 and Bcl-xL as it inhibited TNF- and anti-Fas-induced activation of two enzymes participating in the apoptosis pathway, cytosolic phospholipase A2 and caspase-3/CPP32, but did not interfere with the activation of NF-kappaB-like transcription factors. A putative function of BHRF1 in EBV-infected epithelial cells may be to protect virus-infected cells from TNF- and/or anti-Fas-induced cell death in order to maximize virus production. Surprisingly, expression of neither BHRF1 nor Bcl-2 in a B-cell line, BJAB, protected the cells from anti-Fas-mediated apoptosis even though they increased the survival of serum-starved cells. Thus, the protective role of BHRF1 against apoptosis resembles that of Bcl-2 in being cell type specific and dependent on the apoptotic stimulus."}
genia-medco-coref
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A putative function of BHRF1 in EBV-infected epithelial cells may be to protect virus-infected cells from TNF- and/or anti-Fas-induced cell death in order to maximize virus production. Surprisingly, expression of neither BHRF1 nor Bcl-2 in a B-cell line, BJAB, protected the cells from anti-Fas-mediated apoptosis even though they increased the survival of serum-starved cells. Thus, the protective role of BHRF1 against apoptosis resembles that of Bcl-2 in being cell type specific and dependent on the apoptotic stimulus."}
GENIAcorpus
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