human
The task is to decide the Hallmarks of Cancer (HOC) taxonomy of the article based on its abstract. The input is an abstract text. There are 10 topics you will need to decide whether the article is related to. Topics: sustaining proliferative signaling, evading growth suppressors, resisting cell death, enabling replicative immortality, inducing angiogenesis, activating invasion and metastasis, genomic instability and mutation, tumor promoting inflammation, cellular energetics, avoiding immune destruction. The output should be topics from the above 10 topics, that are related to the input article. Please note one article can be related to multiple topics. Output format: provide a semicolon-separated list of relevant topics.
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    INPUT: Triggering tumor necrosis factor receptor-1 ( TNFR1 ) induces apoptosis in various cell lines . In contrast , stimulation of TNFR1 in L929sA leads to necrosis . Inhibition of HSP90 , a chaperone for many kinases , by geldanamycin or radicicol shifted the response of L929sA cells to TNF from necrosis to apoptosis . This shift was blocked by CrmA but not by BCL-2 overexpression , suggesting that it occurred through activation of procaspase-8 . Geldanamycin pretreatment led to a proteasome-dependent decrease in the levels of several TNFR1-interacting proteins including the kinases receptor-interacting protein , inhibitor of kappa B kinase-alpha , inhibitor of kappa B kinase-beta , and to a lesser extent the adaptors NF-kappaB essential modulator and tumor necrosis factor receptor-associated factor 2 . As a consequence , NF-kappa B , p38MAPK , and JNK activation were abolished . No significant decrease in the levels of mitogen-activated protein kinases , adaptor proteins TNFR-associated death domain and Fas-associated death domain , or caspase-3 , -8 , and -9 could be detected . These results suggest that HSP90 client proteins play a crucial role in necrotic signaling . We conclude that inhibition of HSP90 may alter the composition of the TNFR1 complex , favoring the caspase-8-dependent apoptotic pathway . In the absence of geldanamycin , certain HSP90 client proteins may be preferentially recruited to the TNFR1 complex , promoting necrosis . Thus , the availability of proteins such as receptor-interacting protein , Fas-associated death domain , and caspase-8 can determine whether TNFR1 activation will lead to apoptosis or to necrosis .
    OUTPUT:

agent
resisting cell death
The task is to decide the Hallmarks of Cancer (HOC) taxonomy of the article based on its abstract. The input is an abstract text. There are 10 topics you will need to decide whether the article is related to. Topics: sustaining proliferative signaling, evading growth suppressors, resisting cell death, enabling replicative immortality, inducing angiogenesis, activating invasion and metastasis, genomic instability and mutation, tumor promoting inflammation, cellular energetics, avoiding immune destruction. The output should be topics from the above 10 topics, that are related to the input article. Please note one article can be related to multiple topics. Output format: provide a semicolon-separated list of relevant topics.
    ###
    INPUT: Triggering tumor necrosis factor receptor-1 ( TNFR1 ) induces apoptosis in various cell lines . In contrast , stimulation of TNFR1 in L929sA leads to necrosis . Inhibition of HSP90 , a chaperone for many kinases , by geldanamycin or radicicol shifted the response of L929sA cells to TNF from necrosis to apoptosis . This shift was blocked by CrmA but not by BCL-2 overexpression , suggesting that it occurred through activation of procaspase-8 . Geldanamycin pretreatment led to a proteasome-dependent decrease in the levels of several TNFR1-interacting proteins including the kinases receptor-interacting protein , inhibitor of kappa B kinase-alpha , inhibitor of kappa B kinase-beta , and to a lesser extent the adaptors NF-kappaB essential modulator and tumor necrosis factor receptor-associated factor 2 . As a consequence , NF-kappa B , p38MAPK , and JNK activation were abolished . No significant decrease in the levels of mitogen-activated protein kinases , adaptor proteins TNFR-associated death domain and Fas-associated death domain , or caspase-3 , -8 , and -9 could be detected . These results suggest that HSP90 client proteins play a crucial role in necrotic signaling . We conclude that inhibition of HSP90 may alter the composition of the TNFR1 complex , favoring the caspase-8-dependent apoptotic pathway . In the absence of geldanamycin , certain HSP90 client proteins may be preferentially recruited to the TNFR1 complex , promoting necrosis . Thus , the availability of proteins such as receptor-interacting protein , Fas-associated death domain , and caspase-8 can determine whether TNFR1 activation will lead to apoptosis or to necrosis .
    OUTPUT:
