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next investigated if the delayed RIP1 kinase-dependent increase in Akt Thr308 phosphorylation functionally contributes to the execution of necroptotic cell death. Firstly, PDGF/zVAD.fmk, which cannot induce necroptosis (Fig. 2A), triggered only the initial, rapid Akt and JNK phosphorylation changes and not the delayed activation (Fig. 4A), indicating that late, rather than early Akt phosphorylation correlates with necroptosis. Secondly, we saw that the ability of the Akt inhibitor to protect cells from necroptosis rapidly declined after 6 hrs of stimulation with zVAD.fmk, TNFα or bFGF/zVAD.fmk and no protection was observed when the inhibitor was added at 9 hrs (Fig. 4B,C). This time frame coincides with the timing of the secondary Akt Thr308 phosphorylation. Finally, we terminated the bFGF signal one hour after addition of bFGF by the addition of PD173074. This allowed us to retain early Akt activation, but to suppress the secondary increase (Fig. 4D). Both pre-addition and delayed addition of PD173074 fully prevented necroptosis (Fig. 4E). Overall, these data, while correlative, indicate that early Akt activation is insufficient to promote necroptosis and are strongly supportive of an important role for the delayed activation of Akt in the induction of necroptotic cell death."}

{"project":"bionlp-st-ge-2016-test-proteins","denotations":[{"id":"T8153","span":{"begin":839,"end":843},"obj":"Protein"},{"id":"T8152","span":{"begin":800,"end":804},"obj":"Protein"},{"id":"T8151","span":{"begin":590,"end":594},"obj":"Protein"},{"id":"T8150","span":{"begin":582,"end":586},"obj":"Protein"},{"id":"T8149","span":{"begin":36,"end":40},"obj":"Protein"}],"namespaces":[{"prefix":"_base","uri":"http://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"We next investigated if the delayed RIP1 kinase-dependent increase in Akt Thr308 phosphorylation functionally contributes to the execution of necroptotic cell death. Firstly, PDGF/zVAD.fmk, which cannot induce necroptosis (Fig. 2A), triggered only the initial, rapid Akt and JNK phosphorylation changes and not the delayed activation (Fig. 4A), indicating that late, rather than early Akt phosphorylation correlates with necroptosis. Secondly, we saw that the ability of the Akt inhibitor to protect cells from necroptosis rapidly declined after 6 hrs of stimulation with zVAD.fmk, TNFα or bFGF/zVAD.fmk and no protection was observed when the inhibitor was added at 9 hrs (Fig. 4B,C). This time frame coincides with the timing of the secondary Akt Thr308 phosphorylation. Finally, we terminated the bFGF signal one hour after addition of bFGF by the addition of PD173074. This allowed us to retain early Akt activation, but to suppress the secondary increase (Fig. 4D). Both pre-addition and delayed addition of PD173074 fully prevented necroptosis (Fig. 4E). Overall, these data, while correlative, indicate that early Akt activation is insufficient to promote necroptosis and are strongly supportive of an important role for the delayed activation of Akt in the induction of necroptotic cell death."}

{"project":"bionlp-st-ge-2016-uniprot","denotations":[{"id":"T8463","span":{"begin":839,"end":843},"obj":"http://www.uniprot.org/uniprot/Q788Q8"},{"id":"T8462","span":{"begin":800,"end":804},"obj":"http://www.uniprot.org/uniprot/Q788Q8"},{"id":"T8461","span":{"begin":590,"end":594},"obj":"http://www.uniprot.org/uniprot/Q788Q8"},{"id":"T8460","span":{"begin":582,"end":586},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T8459","span":{"begin":36,"end":40},"obj":"http://www.uniprot.org/uniprot/Q13546"},{"id":"T8458","span":{"begin":1254,"end":1257},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T8457","span":{"begin":1121,"end":1124},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T8456","span":{"begin":905,"end":908},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T8455","span":{"begin":745,"end":748},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T8454","span":{"begin":475,"end":478},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T8453","span":{"begin":385,"end":388},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T8452","span":{"begin":267,"end":270},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T8451","span":{"begin":70,"end":73},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T8449","span":{"begin":1254,"end":1257},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T8448","span":{"begin":1121,"end":1124},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T8447","span":{"begin":905,"end":908},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T8446","span":{"begin":745,"end":748},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T8445","span":{"begin":475,"end":478},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T8444","span":{"begin":385,"end":388},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T8443","span":{"begin":267,"end":270},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T8442","span":{"begin":70,"end":73},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T8440","span":{"begin":1254,"end":1257},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T8439","span":{"begin":1121,"end":1124},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T8438","span":{"begin":905,"end":908},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T8437","span":{"begin":745,"end":748},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T8436","span":{"begin":475,"end":478},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T8435","span":{"begin":385,"end":388},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T8434","span":{"begin":267,"end":270},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T8433","span":{"begin":70,"end":73},"obj":"http://www.uniprot.org/uniprot/P31749"}],"namespaces":[{"prefix":"_base","uri":"http://www.uniprot.org/uniprot/"}],"text":"We next investigated if the delayed RIP1 kinase-dependent increase in Akt Thr308 phosphorylation functionally contributes to the execution of necroptotic cell death. Firstly, PDGF/zVAD.fmk, which cannot induce necroptosis (Fig. 2A), triggered only the initial, rapid Akt and JNK phosphorylation changes and not the delayed activation (Fig. 4A), indicating that late, rather than early Akt phosphorylation correlates with necroptosis. Secondly, we saw that the ability of the Akt inhibitor to protect cells from necroptosis rapidly declined after 6 hrs of stimulation with zVAD.fmk, TNFα or bFGF/zVAD.fmk and no protection was observed when the inhibitor was added at 9 hrs (Fig. 4B,C). This time frame coincides with the timing of the secondary Akt Thr308 phosphorylation. Finally, we terminated the bFGF signal one hour after addition of bFGF by the addition of PD173074. This allowed us to retain early Akt activation, but to suppress the secondary increase (Fig. 4D). Both pre-addition and delayed addition of PD173074 fully prevented necroptosis (Fig. 4E). Overall, these data, while correlative, indicate that early Akt activation is insufficient to promote necroptosis and are strongly supportive of an important role for the delayed activation of Akt in the induction of necroptotic cell death."}

{"project":"GO-BP","denotations":[{"id":"T8176","span":{"begin":805,"end":811},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T8175","span":{"begin":275,"end":278},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T8174","span":{"begin":1163,"end":1174},"obj":"http://purl.obolibrary.org/obo/GO_0097528"},{"id":"T8173","span":{"begin":1038,"end":1049},"obj":"http://purl.obolibrary.org/obo/GO_0097528"},{"id":"T8172","span":{"begin":511,"end":522},"obj":"http://purl.obolibrary.org/obo/GO_0097528"},{"id":"T8171","span":{"begin":421,"end":432},"obj":"http://purl.obolibrary.org/obo/GO_0097528"},{"id":"T8170","span":{"begin":210,"end":221},"obj":"http://purl.obolibrary.org/obo/GO_0097528"},{"id":"T8169","span":{"begin":1163,"end":1174},"obj":"http://purl.obolibrary.org/obo/GO_0070266"},{"id":"T8168","span":{"begin":1038,"end":1049},"obj":"http://purl.obolibrary.org/obo/GO_0070266"},{"id":"T8167","span":{"begin":511,"end":522},"obj":"http://purl.obolibrary.org/obo/GO_0070266"},{"id":"T8166","span":{"begin":421,"end":432},"obj":"http://purl.obolibrary.org/obo/GO_0070266"},{"id":"T8165","span":{"begin":210,"end":221},"obj":"http://purl.obolibrary.org/obo/GO_0070266"},{"id":"T8164","span":{"begin":1295,"end":1300},"obj":"http://purl.obolibrary.org/obo/GO_0016265"},{"id":"T8163","span":{"begin":159,"end":164},"obj":"http://purl.obolibrary.org/obo/GO_0016265"},{"id":"T8161","span":{"begin":1290,"end":1300},"obj":"http://purl.obolibrary.org/obo/GO_0008219"},{"id":"T8160","span":{"begin":154,"end":164},"obj":"http://purl.obolibrary.org/obo/GO_0008219"},{"id":"T8158","span":{"begin":756,"end":771},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T8157","span":{"begin":389,"end":404},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T8156","span":{"begin":279,"end":294},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T8155","span":{"begin":81,"end":96},"obj":"http://purl.obolibrary.org/obo/GO_0016310"}],"text":"We next investigated if the delayed RIP1 kinase-dependent increase in Akt Thr308 phosphorylation functionally contributes to the execution of necroptotic cell death. Firstly, PDGF/zVAD.fmk, which cannot induce necroptosis (Fig. 2A), triggered only the initial, rapid Akt and JNK phosphorylation changes and not the delayed activation (Fig. 4A), indicating that late, rather than early Akt phosphorylation correlates with necroptosis. Secondly, we saw that the ability of the Akt inhibitor to protect cells from necroptosis rapidly declined after 6 hrs of stimulation with zVAD.fmk, TNFα or bFGF/zVAD.fmk and no protection was observed when the inhibitor was added at 9 hrs (Fig. 4B,C). This time frame coincides with the timing of the secondary Akt Thr308 phosphorylation. Finally, we terminated the bFGF signal one hour after addition of bFGF by the addition of PD173074. This allowed us to retain early Akt activation, but to suppress the secondary increase (Fig. 4D). Both pre-addition and delayed addition of PD173074 fully prevented necroptosis (Fig. 4E). Overall, these data, while correlative, indicate that early Akt activation is insufficient to promote necroptosis and are strongly supportive of an important role for the delayed activation of Akt in the induction of necroptotic cell death."}

{"project":"GO-MF","denotations":[{"id":"T8177","span":{"begin":175,"end":179},"obj":"http://purl.obolibrary.org/obo/GO_0005161"},{"id":"T8178","span":{"begin":275,"end":278},"obj":"http://purl.obolibrary.org/obo/GO_0004705"}],"text":"We next investigated if the delayed RIP1 kinase-dependent increase in Akt Thr308 phosphorylation functionally contributes to the execution of necroptotic cell death. Firstly, PDGF/zVAD.fmk, which cannot induce necroptosis (Fig. 2A), triggered only the initial, rapid Akt and JNK phosphorylation changes and not the delayed activation (Fig. 4A), indicating that late, rather than early Akt phosphorylation correlates with necroptosis. Secondly, we saw that the ability of the Akt inhibitor to protect cells from necroptosis rapidly declined after 6 hrs of stimulation with zVAD.fmk, TNFα or bFGF/zVAD.fmk and no protection was observed when the inhibitor was added at 9 hrs (Fig. 4B,C). This time frame coincides with the timing of the secondary Akt Thr308 phosphorylation. Finally, we terminated the bFGF signal one hour after addition of bFGF by the addition of PD173074. This allowed us to retain early Akt activation, but to suppress the secondary increase (Fig. 4D). Both pre-addition and delayed addition of PD173074 fully prevented necroptosis (Fig. 4E). Overall, these data, while correlative, indicate that early Akt activation is insufficient to promote necroptosis and are strongly supportive of an important role for the delayed activation of Akt in the induction of necroptotic cell death."}

{"project":"GO-CC","denotations":[{"id":"T8181","span":{"begin":1290,"end":1294},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T8180","span":{"begin":154,"end":158},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"We next investigated if the delayed RIP1 kinase-dependent increase in Akt Thr308 phosphorylation functionally contributes to the execution of necroptotic cell death. Firstly, PDGF/zVAD.fmk, which cannot induce necroptosis (Fig. 2A), triggered only the initial, rapid Akt and JNK phosphorylation changes and not the delayed activation (Fig. 4A), indicating that late, rather than early Akt phosphorylation correlates with necroptosis. Secondly, we saw that the ability of the Akt inhibitor to protect cells from necroptosis rapidly declined after 6 hrs of stimulation with zVAD.fmk, TNFα or bFGF/zVAD.fmk and no protection was observed when the inhibitor was added at 9 hrs (Fig. 4B,C). This time frame coincides with the timing of the secondary Akt Thr308 phosphorylation. Finally, we terminated the bFGF signal one hour after addition of bFGF by the addition of PD173074. This allowed us to retain early Akt activation, but to suppress the secondary increase (Fig. 4D). Both pre-addition and delayed addition of PD173074 fully prevented necroptosis (Fig. 4E). Overall, these data, while correlative, indicate that early Akt activation is insufficient to promote necroptosis and are strongly supportive of an important role for the delayed activation of Akt in the induction of necroptotic cell death."}

{"project":"sentences","denotations":[{"id":"T8142","span":{"begin":1061,"end":1301},"obj":"Sentence"},{"id":"T8141","span":{"begin":971,"end":1060},"obj":"Sentence"},{"id":"T8140","span":{"begin":873,"end":970},"obj":"Sentence"},{"id":"T8139","span":{"begin":773,"end":872},"obj":"Sentence"},{"id":"T8138","span":{"begin":686,"end":772},"obj":"Sentence"},{"id":"T8137","span":{"begin":434,"end":685},"obj":"Sentence"},{"id":"T8136","span":{"begin":166,"end":433},"obj":"Sentence"},{"id":"T8135","span":{"begin":0,"end":165},"obj":"Sentence"},{"id":"T110","span":{"begin":0,"end":165},"obj":"Sentence"},{"id":"T111","span":{"begin":166,"end":433},"obj":"Sentence"},{"id":"T112","span":{"begin":434,"end":685},"obj":"Sentence"},{"id":"T113","span":{"begin":686,"end":772},"obj":"Sentence"},{"id":"T114","span":{"begin":773,"end":872},"obj":"Sentence"},{"id":"T115","span":{"begin":873,"end":970},"obj":"Sentence"},{"id":"T116","span":{"begin":971,"end":1060},"obj":"Sentence"},{"id":"T117","span":{"begin":1061,"end":1301},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"We next investigated if the delayed RIP1 kinase-dependent increase in Akt Thr308 phosphorylation functionally contributes to the execution of necroptotic cell death. Firstly, PDGF/zVAD.fmk, which cannot induce necroptosis (Fig. 2A), triggered only the initial, rapid Akt and JNK phosphorylation changes and not the delayed activation (Fig. 4A), indicating that late, rather than early Akt phosphorylation correlates with necroptosis. Secondly, we saw that the ability of the Akt inhibitor to protect cells from necroptosis rapidly declined after 6 hrs of stimulation with zVAD.fmk, TNFα or bFGF/zVAD.fmk and no protection was observed when the inhibitor was added at 9 hrs (Fig. 4B,C). This time frame coincides with the timing of the secondary Akt Thr308 phosphorylation. Finally, we terminated the bFGF signal one hour after addition of bFGF by the addition of PD173074. This allowed us to retain early Akt activation, but to suppress the secondary increase (Fig. 4D). Both pre-addition and delayed addition of PD173074 fully prevented necroptosis (Fig. 4E). Overall, these data, while correlative, indicate that early Akt activation is insufficient to promote necroptosis and are strongly supportive of an important role for the delayed activation of Akt in the induction of necroptotic cell death."}

{"project":"simple1","denotations":[{"id":"T8186","span":{"begin":839,"end":843},"obj":"Protein"},{"id":"T8185","span":{"begin":800,"end":804},"obj":"Protein"},{"id":"T8184","span":{"begin":590,"end":594},"obj":"Protein"},{"id":"T8183","span":{"begin":582,"end":586},"obj":"Protein"},{"id":"T8182","span":{"begin":36,"end":40},"obj":"Protein"}],"text":"We next investigated if the delayed RIP1 kinase-dependent increase in Akt Thr308 phosphorylation functionally contributes to the execution of necroptotic cell death. Firstly, PDGF/zVAD.fmk, which cannot induce necroptosis (Fig. 2A), triggered only the initial, rapid Akt and JNK phosphorylation changes and not the delayed activation (Fig. 4A), indicating that late, rather than early Akt phosphorylation correlates with necroptosis. Secondly, we saw that the ability of the Akt inhibitor to protect cells from necroptosis rapidly declined after 6 hrs of stimulation with zVAD.fmk, TNFα or bFGF/zVAD.fmk and no protection was observed when the inhibitor was added at 9 hrs (Fig. 4B,C). This time frame coincides with the timing of the secondary Akt Thr308 phosphorylation. Finally, we terminated the bFGF signal one hour after addition of bFGF by the addition of PD173074. This allowed us to retain early Akt activation, but to suppress the secondary increase (Fig. 4D). Both pre-addition and delayed addition of PD173074 fully prevented necroptosis (Fig. 4E). Overall, these data, while correlative, indicate that early Akt activation is insufficient to promote necroptosis and are strongly supportive of an important role for the delayed activation of Akt in the induction of necroptotic cell death."}

{"project":"BioNLP16_DUT","denotations":[{"id":"T8431","span":{"begin":58,"end":66},"obj":"Positive_regulation"},{"id":"T8430","span":{"begin":839,"end":843},"obj":"Protein"},{"id":"T8429","span":{"begin":800,"end":804},"obj":"Protein"},{"id":"T8428","span":{"begin":590,"end":594},"obj":"Protein"},{"id":"T8427","span":{"begin":582,"end":586},"obj":"Protein"},{"id":"T8426","span":{"begin":36,"end":40},"obj":"Protein"}],"relations":[{"id":"R5493","pred":"themeOf","subj":"T8426","obj":"T8431"}],"text":"We next investigated if the delayed RIP1 kinase-dependent increase in Akt Thr308 phosphorylation functionally contributes to the execution of necroptotic cell death. Firstly, PDGF/zVAD.fmk, which cannot induce necroptosis (Fig. 2A), triggered only the initial, rapid Akt and JNK phosphorylation changes and not the delayed activation (Fig. 4A), indicating that late, rather than early Akt phosphorylation correlates with necroptosis. Secondly, we saw that the ability of the Akt inhibitor to protect cells from necroptosis rapidly declined after 6 hrs of stimulation with zVAD.fmk, TNFα or bFGF/zVAD.fmk and no protection was observed when the inhibitor was added at 9 hrs (Fig. 4B,C). This time frame coincides with the timing of the secondary Akt Thr308 phosphorylation. Finally, we terminated the bFGF signal one hour after addition of bFGF by the addition of PD173074. This allowed us to retain early Akt activation, but to suppress the secondary increase (Fig. 4D). Both pre-addition and delayed addition of PD173074 fully prevented necroptosis (Fig. 4E). Overall, these data, while correlative, indicate that early Akt activation is insufficient to promote necroptosis and are strongly supportive of an important role for the delayed activation of Akt in the induction of necroptotic cell death."}

{"project":"BioNLP16_Messiy","denotations":[{"id":"T8734","span":{"begin":58,"end":66},"obj":"Positive_regulation"},{"id":"T8733","span":{"begin":41,"end":57},"obj":"Regulation"},{"id":"T8732","span":{"begin":110,"end":121},"obj":"Positive_regulation"},{"id":"T8731","span":{"begin":839,"end":843},"obj":"Protein"},{"id":"T8730","span":{"begin":800,"end":804},"obj":"Protein"},{"id":"T8729","span":{"begin":590,"end":594},"obj":"Protein"},{"id":"T8728","span":{"begin":582,"end":586},"obj":"Protein"},{"id":"T8727","span":{"begin":36,"end":40},"obj":"Protein"}],"relations":[{"id":"R5748","pred":"themeOf","subj":"T8727","obj":"T8734"},{"id":"R5749","pred":"themeOf","subj":"T8734","obj":"T8732"},{"id":"R5750","pred":"themeOf","subj":"T8734","obj":"T8733"}],"text":"We next investigated if the delayed RIP1 kinase-dependent increase in Akt Thr308 phosphorylation functionally contributes to the execution of necroptotic cell death. Firstly, PDGF/zVAD.fmk, which cannot induce necroptosis (Fig. 2A), triggered only the initial, rapid Akt and JNK phosphorylation changes and not the delayed activation (Fig. 4A), indicating that late, rather than early Akt phosphorylation correlates with necroptosis. Secondly, we saw that the ability of the Akt inhibitor to protect cells from necroptosis rapidly declined after 6 hrs of stimulation with zVAD.fmk, TNFα or bFGF/zVAD.fmk and no protection was observed when the inhibitor was added at 9 hrs (Fig. 4B,C). This time frame coincides with the timing of the secondary Akt Thr308 phosphorylation. Finally, we terminated the bFGF signal one hour after addition of bFGF by the addition of PD173074. This allowed us to retain early Akt activation, but to suppress the secondary increase (Fig. 4D). Both pre-addition and delayed addition of PD173074 fully prevented necroptosis (Fig. 4E). Overall, these data, while correlative, indicate that early Akt activation is insufficient to promote necroptosis and are strongly supportive of an important role for the delayed activation of Akt in the induction of necroptotic cell death."}

{"project":"DLUT931","denotations":[{"id":"T8713","span":{"begin":572,"end":580},"obj":"Positive_regulation"},{"id":"T8712","span":{"begin":41,"end":57},"obj":"Positive_regulation"},{"id":"T8711","span":{"begin":28,"end":35},"obj":"Positive_regulation"},{"id":"T8710","span":{"begin":110,"end":121},"obj":"Positive_regulation"},{"id":"T8709","span":{"begin":58,"end":66},"obj":"Positive_regulation"},{"id":"T8708","span":{"begin":839,"end":843},"obj":"Protein"},{"id":"T8707","span":{"begin":800,"end":804},"obj":"Protein"},{"id":"T8706","span":{"begin":590,"end":594},"obj":"Protein"},{"id":"T8705","span":{"begin":582,"end":586},"obj":"Protein"},{"id":"T8704","span":{"begin":36,"end":40},"obj":"Protein"}],"relations":[{"id":"R5728","pred":"themeOf","subj":"T8704","obj":"T8709"},{"id":"R5729","pred":"themeOf","subj":"T8705","obj":"T8713"},{"id":"R5730","pred":"themeOf","subj":"T8706","obj":"T8713"},{"id":"R5731","pred":"themeOf","subj":"T8709","obj":"T8710"},{"id":"R5732","pred":"themeOf","subj":"T8709","obj":"T8711"},{"id":"R5733","pred":"themeOf","subj":"T8709","obj":"T8712"},{"id":"R5734","pred":"themeOf","subj":"T8711","obj":"T8709"}],"text":"We next investigated if the delayed RIP1 kinase-dependent increase in Akt Thr308 phosphorylation functionally contributes to the execution of necroptotic cell death. Firstly, PDGF/zVAD.fmk, which cannot induce necroptosis (Fig. 2A), triggered only the initial, rapid Akt and JNK phosphorylation changes and not the delayed activation (Fig. 4A), indicating that late, rather than early Akt phosphorylation correlates with necroptosis. Secondly, we saw that the ability of the Akt inhibitor to protect cells from necroptosis rapidly declined after 6 hrs of stimulation with zVAD.fmk, TNFα or bFGF/zVAD.fmk and no protection was observed when the inhibitor was added at 9 hrs (Fig. 4B,C). This time frame coincides with the timing of the secondary Akt Thr308 phosphorylation. Finally, we terminated the bFGF signal one hour after addition of bFGF by the addition of PD173074. This allowed us to retain early Akt activation, but to suppress the secondary increase (Fig. 4D). Both pre-addition and delayed addition of PD173074 fully prevented necroptosis (Fig. 4E). Overall, these data, while correlative, indicate that early Akt activation is insufficient to promote necroptosis and are strongly supportive of an important role for the delayed activation of Akt in the induction of necroptotic cell death."}

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next investigated if the delayed RIP1 kinase-dependent increase in Akt Thr308 phosphorylation functionally contributes to the execution of necroptotic cell death. Firstly, PDGF/zVAD.fmk, which cannot induce necroptosis (Fig. 2A), triggered only the initial, rapid Akt and JNK phosphorylation changes and not the delayed activation (Fig. 4A), indicating that late, rather than early Akt phosphorylation correlates with necroptosis. Secondly, we saw that the ability of the Akt inhibitor to protect cells from necroptosis rapidly declined after 6 hrs of stimulation with zVAD.fmk, TNFα or bFGF/zVAD.fmk and no protection was observed when the inhibitor was added at 9 hrs (Fig. 4B,C). This time frame coincides with the timing of the secondary Akt Thr308 phosphorylation. Finally, we terminated the bFGF signal one hour after addition of bFGF by the addition of PD173074. This allowed us to retain early Akt activation, but to suppress the secondary increase (Fig. 4D). Both pre-addition and delayed addition of PD173074 fully prevented necroptosis (Fig. 4E). Overall, these data, while correlative, indicate that early Akt activation is insufficient to promote necroptosis and are strongly supportive of an important role for the delayed activation of Akt in the induction of necroptotic cell death."}

{"project":"bionlp-st-ge-2016-test-tees","denotations":[{"id":"T8763","span":{"begin":1240,"end":1250},"obj":"Positive_regulation"},{"id":"T8762","span":{"begin":1125,"end":1135},"obj":"Positive_regulation"},{"id":"T8761","span":{"begin":1254,"end":1257},"obj":"Protein"},{"id":"T8760","span":{"begin":1121,"end":1124},"obj":"Protein"},{"id":"T8759","span":{"begin":909,"end":919},"obj":"Positive_regulation"},{"id":"T8758","span":{"begin":905,"end":908},"obj":"Protein"},{"id":"T8757","span":{"begin":863,"end":871},"obj":"Protein"},{"id":"T8756","span":{"begin":839,"end":843},"obj":"Protein"},{"id":"T8755","span":{"begin":800,"end":804},"obj":"Protein"},{"id":"T8754","span":{"begin":756,"end":771},"obj":"Phosphorylation"},{"id":"T8753","span":{"begin":749,"end":755},"obj":"Protein"},{"id":"T8752","span":{"begin":479,"end":488},"obj":"Negative_regulation"},{"id":"T8751","span":{"begin":590,"end":603},"obj":"Protein"},{"id":"T8750","span":{"begin":582,"end":586},"obj":"Protein"},{"id":"T8749","span":{"begin":572,"end":580},"obj":"Protein"},{"id":"T8748","span":{"begin":475,"end":478},"obj":"Protein"},{"id":"T8747","span":{"begin":233,"end":242},"obj":"Positive_regulation"},{"id":"T8746","span":{"begin":323,"end":333},"obj":"Positive_regulation"},{"id":"T8745","span":{"begin":279,"end":294},"obj":"Phosphorylation"},{"id":"T8744","span":{"begin":233,"end":242},"obj":"Positive_regulation"},{"id":"T8743","span":{"begin":275,"end":278},"obj":"Protein"},{"id":"T8742","span":{"begin":175,"end":188},"obj":"Protein"},{"id":"T8741","span":{"begin":58,"end":66},"obj":"Positive_regulation"},{"id":"T8740","span":{"begin":58,"end":66},"obj":"Positive_regulation"},{"id":"T8739","span":{"begin":81,"end":96},"obj":"Phosphorylation"},{"id":"T8738","span":{"begin":81,"end":96},"obj":"Phosphorylation"},{"id":"T8737","span":{"begin":74,"end":80},"obj":"Protein"},{"id":"T8736","span":{"begin":70,"end":73},"obj":"Protein"},{"id":"T8735","span":{"begin":36,"end":47},"obj":"Protein"}],"relations":[{"id":"R5751","pred":"themeOf","subj":"T8736","obj":"T8738"},{"id":"R5752","pred":"themeOf","subj":"T8737","obj":"T8739"},{"id":"R5753","pred":"themeOf","subj":"T8738","obj":"T8740"},{"id":"R5754","pred":"themeOf","subj":"T8739","obj":"T8741"},{"id":"R5755","pred":"causeOf","subj":"T8742","obj":"T8744"},{"id":"R5756","pred":"causeOf","subj":"T8742","obj":"T8747"},{"id":"R5757","pred":"themeOf","subj":"T8743","obj":"T8744"},{"id":"R5758","pred":"themeOf","subj":"T8743","obj":"T8745"},{"id":"R5759","pred":"themeOf","subj":"T8745","obj":"T8746"},{"id":"R5760","pred":"themeOf","subj":"T8745","obj":"T8747"},{"id":"R5761","pred":"themeOf","subj":"T8748","obj":"T8752"},{"id":"R5762","pred":"themeOf","subj":"T8753","obj":"T8754"},{"id":"R5763","pred":"themeOf","subj":"T8758","obj":"T8759"},{"id":"R5764","pred":"themeOf","subj":"T8760","obj":"T8762"},{"id":"R5765","pred":"themeOf","subj":"T8761","obj":"T8763"}],"text":"We next investigated if the delayed RIP1 kinase-dependent increase in Akt Thr308 phosphorylation functionally contributes to the execution of necroptotic cell death. Firstly, PDGF/zVAD.fmk, which cannot induce necroptosis (Fig. 2A), triggered only the initial, rapid Akt and JNK phosphorylation changes and not the delayed activation (Fig. 4A), indicating that late, rather than early Akt phosphorylation correlates with necroptosis. Secondly, we saw that the ability of the Akt inhibitor to protect cells from necroptosis rapidly declined after 6 hrs of stimulation with zVAD.fmk, TNFα or bFGF/zVAD.fmk and no protection was observed when the inhibitor was added at 9 hrs (Fig. 4B,C). This time frame coincides with the timing of the secondary Akt Thr308 phosphorylation. Finally, we terminated the bFGF signal one hour after addition of bFGF by the addition of PD173074. This allowed us to retain early Akt activation, but to suppress the secondary increase (Fig. 4D). Both pre-addition and delayed addition of PD173074 fully prevented necroptosis (Fig. 4E). Overall, these data, while correlative, indicate that early Akt activation is insufficient to promote necroptosis and are strongly supportive of an important role for the delayed activation of Akt in the induction of necroptotic cell death."}

{"project":"test3","denotations":[{"id":"T8133","span":{"begin":1240,"end":1250},"obj":"Positive_regulation"},{"id":"T8132","span":{"begin":1125,"end":1135},"obj":"Positive_regulation"},{"id":"T8131","span":{"begin":909,"end":919},"obj":"Positive_regulation"},{"id":"T8130","span":{"begin":839,"end":843},"obj":"Protein"},{"id":"T8129","span":{"begin":800,"end":804},"obj":"Protein"},{"id":"T8128","span":{"begin":756,"end":771},"obj":"Phosphorylation"},{"id":"T8127","span":{"begin":644,"end":653},"obj":"Negative_regulation"},{"id":"T8126","span":{"begin":590,"end":594},"obj":"Protein"},{"id":"T8125","span":{"begin":582,"end":586},"obj":"Protein"},{"id":"T8124","span":{"begin":479,"end":488},"obj":"Negative_regulation"},{"id":"T8123","span":{"begin":389,"end":404},"obj":"Phosphorylation"},{"id":"T8122","span":{"begin":279,"end":294},"obj":"Phosphorylation"},{"id":"T8121","span":{"begin":81,"end":96},"obj":"Phosphorylation"},{"id":"T8120","span":{"begin":58,"end":66},"obj":"Positive_regulation"},{"id":"T8119","span":{"begin":36,"end":40},"obj":"Protein"},{"id":"T8116","span":{"begin":839,"end":843},"obj":"Protein"},{"id":"T8115","span":{"begin":800,"end":804},"obj":"Protein"},{"id":"T8114","span":{"begin":590,"end":594},"obj":"Protein"},{"id":"T8113","span":{"begin":582,"end":586},"obj":"Protein"},{"id":"T8112","span":{"begin":36,"end":40},"obj":"Protein"}],"relations":[{"id":"R5256","pred":"themeOf","subj":"T8121","obj":"T8120"},{"id":"R5257","pred":"themeOf","subj":"T8129","obj":"T8130"}],"text":"We next investigated if the delayed RIP1 kinase-dependent increase in Akt Thr308 phosphorylation functionally contributes to the execution of necroptotic cell death. Firstly, PDGF/zVAD.fmk, which cannot induce necroptosis (Fig. 2A), triggered only the initial, rapid Akt and JNK phosphorylation changes and not the delayed activation (Fig. 4A), indicating that late, rather than early Akt phosphorylation correlates with necroptosis. Secondly, we saw that the ability of the Akt inhibitor to protect cells from necroptosis rapidly declined after 6 hrs of stimulation with zVAD.fmk, TNFα or bFGF/zVAD.fmk and no protection was observed when the inhibitor was added at 9 hrs (Fig. 4B,C). This time frame coincides with the timing of the secondary Akt Thr308 phosphorylation. Finally, we terminated the bFGF signal one hour after addition of bFGF by the addition of PD173074. This allowed us to retain early Akt activation, but to suppress the secondary increase (Fig. 4D). Both pre-addition and delayed addition of PD173074 fully prevented necroptosis (Fig. 4E). Overall, these data, while correlative, indicate that early Akt activation is insufficient to promote necroptosis and are strongly supportive of an important role for the delayed activation of Akt in the induction of necroptotic cell death."}