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Furthermore, addition of TNFα led to comparable late activation of Akt p308 signal under both normal and serum free conditions (Fig. S4B, C), indicating that TNFα signaling to Akt Thr308 is growth factor-independent. In contrast, activation of JNK by TNFα followed different kinetics from zVAD.fmk-induced changes. TNFα treatment caused an early and robust increase in the phosphorylation of JNK and c-Jun. Nec-1 did not affect this early increase, however, it reduced levels of pJNK/Jun at the late, 9 hr time point (Fig. S4B, C). This again separated early RIP1-independent changes, which likely reflect the ability of additional upstream kinases, such as Ask1 to activate JNK [27], from the late RIP1 kinase-dependent necroptotic signaling."}

{"project":"bionlp-st-ge-2016-coref","denotations":[{"id":"T7430","span":{"begin":712,"end":720},"obj":"Antecedent"},{"id":"T7429","span":{"begin":783,"end":802},"obj":"Anaphor"}],"relations":[{"id":"R4799","pred":"boundBy","subj":"T7429","obj":"T7430"}],"namespaces":[{"prefix":"_base","uri":"https://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"TNFα Induces Delayed Akt Thr308 Phosphorylation and Necroptosis Independent of Growth Factor Stimulation\nConsistent with TNFα inducing necroptosis independently of growth factors (Fig. 1A), FGFR inhibitors did not attenuate TNFα-induced changes in Akt or JNK phosphorylation, while efficiently preventing these changes in response to zVAD.fmk (Fig. S4A). Furthermore, addition of TNFα led to comparable late activation of Akt p308 signal under both normal and serum free conditions (Fig. S4B, C), indicating that TNFα signaling to Akt Thr308 is growth factor-independent. In contrast, activation of JNK by TNFα followed different kinetics from zVAD.fmk-induced changes. TNFα treatment caused an early and robust increase in the phosphorylation of JNK and c-Jun. Nec-1 did not affect this early increase, however, it reduced levels of pJNK/Jun at the late, 9 hr time point (Fig. S4B, C). This again separated early RIP1-independent changes, which likely reflect the ability of additional upstream kinases, such as Ask1 to activate JNK [27], from the late RIP1 kinase-dependent necroptotic signaling."}

{"project":"bionlp-st-ge-2016-test-proteins","denotations":[{"id":"T7441","span":{"begin":1054,"end":1058},"obj":"Protein"},{"id":"T7440","span":{"begin":1013,"end":1017},"obj":"Protein"},{"id":"T7439","span":{"begin":914,"end":918},"obj":"Protein"},{"id":"T7438","span":{"begin":755,"end":760},"obj":"Protein"},{"id":"T7437","span":{"begin":670,"end":674},"obj":"Protein"},{"id":"T7436","span":{"begin":606,"end":610},"obj":"Protein"},{"id":"T7435","span":{"begin":513,"end":517},"obj":"Protein"},{"id":"T7434","span":{"begin":380,"end":384},"obj":"Protein"},{"id":"T7433","span":{"begin":224,"end":228},"obj":"Protein"},{"id":"T7432","span":{"begin":121,"end":125},"obj":"Protein"},{"id":"T7431","span":{"begin":0,"end":4},"obj":"Protein"}],"namespaces":[{"prefix":"_base","uri":"http://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"TNFα Induces Delayed Akt Thr308 Phosphorylation and Necroptosis Independent of Growth Factor Stimulation\nConsistent with TNFα inducing necroptosis independently of growth factors (Fig. 1A), FGFR inhibitors did not attenuate TNFα-induced changes in Akt or JNK phosphorylation, while efficiently preventing these changes in response to zVAD.fmk (Fig. S4A). Furthermore, addition of TNFα led to comparable late activation of Akt p308 signal under both normal and serum free conditions (Fig. S4B, C), indicating that TNFα signaling to Akt Thr308 is growth factor-independent. In contrast, activation of JNK by TNFα followed different kinetics from zVAD.fmk-induced changes. TNFα treatment caused an early and robust increase in the phosphorylation of JNK and c-Jun. Nec-1 did not affect this early increase, however, it reduced levels of pJNK/Jun at the late, 9 hr time point (Fig. S4B, C). This again separated early RIP1-independent changes, which likely reflect the ability of additional upstream kinases, such as Ask1 to activate JNK [27], from the late RIP1 kinase-dependent necroptotic signaling."}

{"project":"bionlp-st-ge-2016-uniprot","denotations":[{"id":"T7705","span":{"begin":1054,"end":1058},"obj":"http://www.uniprot.org/uniprot/Q13546"},{"id":"T7704","span":{"begin":914,"end":918},"obj":"http://www.uniprot.org/uniprot/Q13546"},{"id":"T7703","span":{"begin":755,"end":760},"obj":"http://www.uniprot.org/uniprot/P05412"},{"id":"T7702","span":{"begin":531,"end":534},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T7701","span":{"begin":422,"end":425},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T7700","span":{"begin":248,"end":251},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T7699","span":{"begin":21,"end":24},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T7698","span":{"begin":531,"end":534},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T7697","span":{"begin":422,"end":425},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T7696","span":{"begin":248,"end":251},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T7695","span":{"begin":21,"end":24},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T7694","span":{"begin":531,"end":534},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T7693","span":{"begin":422,"end":425},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T7692","span":{"begin":248,"end":251},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T7691","span":{"begin":21,"end":24},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T7690","span":{"begin":670,"end":674},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T7689","span":{"begin":606,"end":610},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T7688","span":{"begin":513,"end":517},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T7687","span":{"begin":380,"end":384},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T7686","span":{"begin":224,"end":228},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T7685","span":{"begin":121,"end":125},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T7684","span":{"begin":0,"end":4},"obj":"http://www.uniprot.org/uniprot/P01375"}],"namespaces":[{"prefix":"_base","uri":"http://www.uniprot.org/uniprot/"}],"text":"TNFα Induces Delayed Akt Thr308 Phosphorylation and Necroptosis Independent of Growth Factor Stimulation\nConsistent with TNFα inducing necroptosis independently of growth factors (Fig. 1A), FGFR inhibitors did not attenuate TNFα-induced changes in Akt or JNK phosphorylation, while efficiently preventing these changes in response to zVAD.fmk (Fig. S4A). Furthermore, addition of TNFα led to comparable late activation of Akt p308 signal under both normal and serum free conditions (Fig. S4B, C), indicating that TNFα signaling to Akt Thr308 is growth factor-independent. In contrast, activation of JNK by TNFα followed different kinetics from zVAD.fmk-induced changes. TNFα treatment caused an early and robust increase in the phosphorylation of JNK and c-Jun. Nec-1 did not affect this early increase, however, it reduced levels of pJNK/Jun at the late, 9 hr time point (Fig. S4B, C). This again separated early RIP1-independent changes, which likely reflect the ability of additional upstream kinases, such as Ask1 to activate JNK [27], from the late RIP1 kinase-dependent necroptotic signaling."}

{"project":"UBERON-AE","denotations":[{"id":"T7408","span":{"begin":460,"end":465},"obj":"http://purl.obolibrary.org/obo/UBERON_0001977"}],"text":"TNFα Induces Delayed Akt Thr308 Phosphorylation and Necroptosis Independent of Growth Factor Stimulation\nConsistent with TNFα inducing necroptosis independently of growth factors (Fig. 1A), FGFR inhibitors did not attenuate TNFα-induced changes in Akt or JNK phosphorylation, while efficiently preventing these changes in response to zVAD.fmk (Fig. S4A). Furthermore, addition of TNFα led to comparable late activation of Akt p308 signal under both normal and serum free conditions (Fig. S4B, C), indicating that TNFα signaling to Akt Thr308 is growth factor-independent. In contrast, activation of JNK by TNFα followed different kinetics from zVAD.fmk-induced changes. TNFα treatment caused an early and robust increase in the phosphorylation of JNK and c-Jun. Nec-1 did not affect this early increase, however, it reduced levels of pJNK/Jun at the late, 9 hr time point (Fig. S4B, C). This again separated early RIP1-independent changes, which likely reflect the ability of additional upstream kinases, such as Ask1 to activate JNK [27], from the late RIP1 kinase-dependent necroptotic signaling."}

{"project":"GO-BP","denotations":[{"id":"T7459","span":{"begin":1088,"end":1097},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T7458","span":{"begin":518,"end":527},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T7457","span":{"begin":431,"end":437},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T7456","span":{"begin":1030,"end":1033},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T7455","span":{"begin":747,"end":750},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T7454","span":{"begin":599,"end":602},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T7453","span":{"begin":255,"end":258},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T7452","span":{"begin":190,"end":194},"obj":"http://purl.obolibrary.org/obo/GO_0005007"},{"id":"T7451","span":{"begin":545,"end":551},"obj":"http://purl.obolibrary.org/obo/GO_0040007"},{"id":"T7450","span":{"begin":164,"end":170},"obj":"http://purl.obolibrary.org/obo/GO_0040007"},{"id":"T7449","span":{"begin":79,"end":85},"obj":"http://purl.obolibrary.org/obo/GO_0040007"},{"id":"T7448","span":{"begin":135,"end":146},"obj":"http://purl.obolibrary.org/obo/GO_0097528"},{"id":"T7447","span":{"begin":52,"end":63},"obj":"http://purl.obolibrary.org/obo/GO_0097528"},{"id":"T7446","span":{"begin":135,"end":146},"obj":"http://purl.obolibrary.org/obo/GO_0070266"},{"id":"T7445","span":{"begin":52,"end":63},"obj":"http://purl.obolibrary.org/obo/GO_0070266"},{"id":"T7444","span":{"begin":728,"end":743},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T7443","span":{"begin":259,"end":274},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T7442","span":{"begin":32,"end":47},"obj":"http://purl.obolibrary.org/obo/GO_0016310"}],"text":"TNFα Induces Delayed Akt Thr308 Phosphorylation and Necroptosis Independent of Growth Factor Stimulation\nConsistent with TNFα inducing necroptosis independently of growth factors (Fig. 1A), FGFR inhibitors did not attenuate TNFα-induced changes in Akt or JNK phosphorylation, while efficiently preventing these changes in response to zVAD.fmk (Fig. S4A). Furthermore, addition of TNFα led to comparable late activation of Akt p308 signal under both normal and serum free conditions (Fig. S4B, C), indicating that TNFα signaling to Akt Thr308 is growth factor-independent. In contrast, activation of JNK by TNFα followed different kinetics from zVAD.fmk-induced changes. TNFα treatment caused an early and robust increase in the phosphorylation of JNK and c-Jun. Nec-1 did not affect this early increase, however, it reduced levels of pJNK/Jun at the late, 9 hr time point (Fig. S4B, C). This again separated early RIP1-independent changes, which likely reflect the ability of additional upstream kinases, such as Ask1 to activate JNK [27], from the late RIP1 kinase-dependent necroptotic signaling."}

{"project":"GO-MF","denotations":[{"id":"T7464","span":{"begin":1030,"end":1033},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T7463","span":{"begin":747,"end":750},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T7462","span":{"begin":599,"end":602},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T7461","span":{"begin":255,"end":258},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T7460","span":{"begin":190,"end":194},"obj":"http://purl.obolibrary.org/obo/GO_0005007"}],"text":"TNFα Induces Delayed Akt Thr308 Phosphorylation and Necroptosis Independent of Growth Factor Stimulation\nConsistent with TNFα inducing necroptosis independently of growth factors (Fig. 1A), FGFR inhibitors did not attenuate TNFα-induced changes in Akt or JNK phosphorylation, while efficiently preventing these changes in response to zVAD.fmk (Fig. S4A). Furthermore, addition of TNFα led to comparable late activation of Akt p308 signal under both normal and serum free conditions (Fig. S4B, C), indicating that TNFα signaling to Akt Thr308 is growth factor-independent. In contrast, activation of JNK by TNFα followed different kinetics from zVAD.fmk-induced changes. TNFα treatment caused an early and robust increase in the phosphorylation of JNK and c-Jun. Nec-1 did not affect this early increase, however, it reduced levels of pJNK/Jun at the late, 9 hr time point (Fig. S4B, C). This again separated early RIP1-independent changes, which likely reflect the ability of additional upstream kinases, such as Ask1 to activate JNK [27], from the late RIP1 kinase-dependent necroptotic signaling."}

{"project":"sentences","denotations":[{"id":"T7414","span":{"begin":887,"end":1098},"obj":"Sentence"},{"id":"T7413","span":{"begin":670,"end":886},"obj":"Sentence"},{"id":"T7412","span":{"begin":572,"end":669},"obj":"Sentence"},{"id":"T7411","span":{"begin":355,"end":571},"obj":"Sentence"},{"id":"T7410","span":{"begin":105,"end":354},"obj":"Sentence"},{"id":"T7409","span":{"begin":0,"end":104},"obj":"Sentence"},{"id":"T102","span":{"begin":0,"end":104},"obj":"Sentence"},{"id":"T103","span":{"begin":105,"end":354},"obj":"Sentence"},{"id":"T104","span":{"begin":355,"end":571},"obj":"Sentence"},{"id":"T105","span":{"begin":572,"end":669},"obj":"Sentence"},{"id":"T106","span":{"begin":670,"end":761},"obj":"Sentence"},{"id":"T107","span":{"begin":762,"end":886},"obj":"Sentence"},{"id":"T108","span":{"begin":887,"end":1098},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"TNFα Induces Delayed Akt Thr308 Phosphorylation and Necroptosis Independent of Growth Factor Stimulation\nConsistent with TNFα inducing necroptosis independently of growth factors (Fig. 1A), FGFR inhibitors did not attenuate TNFα-induced changes in Akt or JNK phosphorylation, while efficiently preventing these changes in response to zVAD.fmk (Fig. S4A). Furthermore, addition of TNFα led to comparable late activation of Akt p308 signal under both normal and serum free conditions (Fig. S4B, C), indicating that TNFα signaling to Akt Thr308 is growth factor-independent. In contrast, activation of JNK by TNFα followed different kinetics from zVAD.fmk-induced changes. TNFα treatment caused an early and robust increase in the phosphorylation of JNK and c-Jun. Nec-1 did not affect this early increase, however, it reduced levels of pJNK/Jun at the late, 9 hr time point (Fig. S4B, C). This again separated early RIP1-independent changes, which likely reflect the ability of additional upstream kinases, such as Ask1 to activate JNK [27], from the late RIP1 kinase-dependent necroptotic signaling."}

{"project":"simple1","denotations":[{"id":"T7475","span":{"begin":1054,"end":1058},"obj":"Protein"},{"id":"T7474","span":{"begin":1013,"end":1017},"obj":"Protein"},{"id":"T7473","span":{"begin":914,"end":918},"obj":"Protein"},{"id":"T7472","span":{"begin":755,"end":760},"obj":"Protein"},{"id":"T7471","span":{"begin":670,"end":674},"obj":"Protein"},{"id":"T7470","span":{"begin":606,"end":610},"obj":"Protein"},{"id":"T7469","span":{"begin":513,"end":517},"obj":"Protein"},{"id":"T7468","span":{"begin":380,"end":384},"obj":"Protein"},{"id":"T7467","span":{"begin":224,"end":228},"obj":"Protein"},{"id":"T7466","span":{"begin":121,"end":125},"obj":"Protein"},{"id":"T7465","span":{"begin":0,"end":4},"obj":"Protein"}],"text":"TNFα Induces Delayed Akt Thr308 Phosphorylation and Necroptosis Independent of Growth Factor Stimulation\nConsistent with TNFα inducing necroptosis independently of growth factors (Fig. 1A), FGFR inhibitors did not attenuate TNFα-induced changes in Akt or JNK phosphorylation, while efficiently preventing these changes in response to zVAD.fmk (Fig. S4A). Furthermore, addition of TNFα led to comparable late activation of Akt p308 signal under both normal and serum free conditions (Fig. S4B, C), indicating that TNFα signaling to Akt Thr308 is growth factor-independent. In contrast, activation of JNK by TNFα followed different kinetics from zVAD.fmk-induced changes. TNFα treatment caused an early and robust increase in the phosphorylation of JNK and c-Jun. Nec-1 did not affect this early increase, however, it reduced levels of pJNK/Jun at the late, 9 hr time point (Fig. S4B, C). This again separated early RIP1-independent changes, which likely reflect the ability of additional upstream kinases, such as Ask1 to activate JNK [27], from the late RIP1 kinase-dependent necroptotic signaling."}

{"project":"BioNLP16_DUT","denotations":[{"id":"T7681","span":{"begin":229,"end":236},"obj":"Positive_regulation"},{"id":"T7680","span":{"begin":914,"end":918},"obj":"Protein"},{"id":"T7679","span":{"begin":1054,"end":1058},"obj":"Protein"},{"id":"T7678","span":{"begin":1013,"end":1017},"obj":"Protein"},{"id":"T7677","span":{"begin":755,"end":760},"obj":"Protein"},{"id":"T7676","span":{"begin":670,"end":674},"obj":"Protein"},{"id":"T7675","span":{"begin":606,"end":610},"obj":"Protein"},{"id":"T7674","span":{"begin":513,"end":517},"obj":"Protein"},{"id":"T7673","span":{"begin":380,"end":384},"obj":"Protein"},{"id":"T7672","span":{"begin":224,"end":228},"obj":"Protein"},{"id":"T7671","span":{"begin":121,"end":125},"obj":"Protein"},{"id":"T7670","span":{"begin":0,"end":4},"obj":"Protein"},{"id":"T7683","span":{"begin":712,"end":720},"obj":"Positive_regulation"},{"id":"T7682","span":{"begin":728,"end":743},"obj":"Phosphorylation"}],"relations":[{"id":"R4988","pred":"themeOf","subj":"T7672","obj":"T7681"},{"id":"R4989","pred":"themeOf","subj":"T7677","obj":"T7682"},{"id":"R4990","pred":"themeOf","subj":"T7682","obj":"T7683"}],"text":"TNFα Induces Delayed Akt Thr308 Phosphorylation and Necroptosis Independent of Growth Factor Stimulation\nConsistent with TNFα inducing necroptosis independently of growth factors (Fig. 1A), FGFR inhibitors did not attenuate TNFα-induced changes in Akt or JNK phosphorylation, while efficiently preventing these changes in response to zVAD.fmk (Fig. S4A). Furthermore, addition of TNFα led to comparable late activation of Akt p308 signal under both normal and serum free conditions (Fig. S4B, C), indicating that TNFα signaling to Akt Thr308 is growth factor-independent. In contrast, activation of JNK by TNFα followed different kinetics from zVAD.fmk-induced changes. TNFα treatment caused an early and robust increase in the phosphorylation of JNK and c-Jun. Nec-1 did not affect this early increase, however, it reduced levels of pJNK/Jun at the late, 9 hr time point (Fig. S4B, C). This again separated early RIP1-independent changes, which likely reflect the ability of additional upstream kinases, such as Ask1 to activate JNK [27], from the late RIP1 kinase-dependent necroptotic signaling."}

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