PMC:3585731 / 19907-21147 JSONTXT

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    testone

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    pmc-enju-pas

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next determined whether the necroptosis-associated increase in Thr308 phosphorylation results in an increase in Akt kinase activity. Under necroptotic conditions, we observed an increase in the phosphorylation of multiple known Akt substrates (Forkhead box class O (FoxO) proteins, GSK-3 kinases and mouse double minute 2 (MDM2)) as well as downstream molecules (p70 ribosomal protein S6 Kinase (p70S6K), S6) (Fig. 5A). In some cases (FoxO1, FoxO4, MDM2), a robust increase was observed. In other cases (FoxO3a, GSK-3α/β, p70S6K and its substrate S6), the changes were less pronounced (Fig. 5A). The timing of the phosphorylation changes paralleled the increase in Akt phosphorylation (Fig. 5B, S5A, B). In the case of pFoxO1 we occasionally observed a shift in migration rather than an increase in band intensity (e.g. comparing Fig. 5A and B), suggesting that phosphorylation events in addition to Thr24 take place during necroptosis. Notably, in all cases the necroptosis-associated increases in Akt substrates were abrogated by Nec-1 (Fig. 5A, Fig. S5A, B). Overall, these data suggested that a significant part of the “canonical” Akt signaling network is activated at the onset of necroptotic cell death in a RIP1 dependent fashion."}

    bionlp-st-ge-2016-coref

    {"project":"bionlp-st-ge-2016-coref","denotations":[{"id":"T9193","span":{"begin":525,"end":531},"obj":"Antecedent"},{"id":"T9192","span":{"begin":536,"end":539},"obj":"Anaphor"}],"relations":[{"id":"R5906","pred":"boundBy","subj":"T9192","obj":"T9193"}],"namespaces":[{"prefix":"_base","uri":"https://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"We next determined whether the necroptosis-associated increase in Thr308 phosphorylation results in an increase in Akt kinase activity. Under necroptotic conditions, we observed an increase in the phosphorylation of multiple known Akt substrates (Forkhead box class O (FoxO) proteins, GSK-3 kinases and mouse double minute 2 (MDM2)) as well as downstream molecules (p70 ribosomal protein S6 Kinase (p70S6K), S6) (Fig. 5A). In some cases (FoxO1, FoxO4, MDM2), a robust increase was observed. In other cases (FoxO3a, GSK-3α/β, p70S6K and its substrate S6), the changes were less pronounced (Fig. 5A). The timing of the phosphorylation changes paralleled the increase in Akt phosphorylation (Fig. 5B, S5A, B). In the case of pFoxO1 we occasionally observed a shift in migration rather than an increase in band intensity (e.g. comparing Fig. 5A and B), suggesting that phosphorylation events in addition to Thr24 take place during necroptosis. Notably, in all cases the necroptosis-associated increases in Akt substrates were abrogated by Nec-1 (Fig. 5A, Fig. S5A, B). Overall, these data suggested that a significant part of the “canonical” Akt signaling network is activated at the onset of necroptotic cell death in a RIP1 dependent fashion."}

    bionlp-st-ge-2016-test-proteins

    {"project":"bionlp-st-ge-2016-test-proteins","denotations":[{"id":"T9212","span":{"begin":1217,"end":1221},"obj":"Protein"},{"id":"T9211","span":{"begin":722,"end":728},"obj":"Protein"},{"id":"T9210","span":{"begin":550,"end":552},"obj":"Protein"},{"id":"T9209","span":{"begin":525,"end":531},"obj":"Protein"},{"id":"T9208","span":{"begin":522,"end":523},"obj":"Protein"},{"id":"T9207","span":{"begin":515,"end":521},"obj":"Protein"},{"id":"T9206","span":{"begin":507,"end":513},"obj":"Protein"},{"id":"T9205","span":{"begin":452,"end":456},"obj":"Protein"},{"id":"T9204","span":{"begin":445,"end":450},"obj":"Protein"},{"id":"T9203","span":{"begin":438,"end":443},"obj":"Protein"},{"id":"T9202","span":{"begin":408,"end":410},"obj":"Protein"},{"id":"T9201","span":{"begin":399,"end":405},"obj":"Protein"},{"id":"T9200","span":{"begin":366,"end":397},"obj":"Protein"},{"id":"T9199","span":{"begin":326,"end":330},"obj":"Protein"},{"id":"T9198","span":{"begin":309,"end":324},"obj":"Protein"}],"namespaces":[{"prefix":"_base","uri":"http://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"We next determined whether the necroptosis-associated increase in Thr308 phosphorylation results in an increase in Akt kinase activity. Under necroptotic conditions, we observed an increase in the phosphorylation of multiple known Akt substrates (Forkhead box class O (FoxO) proteins, GSK-3 kinases and mouse double minute 2 (MDM2)) as well as downstream molecules (p70 ribosomal protein S6 Kinase (p70S6K), S6) (Fig. 5A). In some cases (FoxO1, FoxO4, MDM2), a robust increase was observed. In other cases (FoxO3a, GSK-3α/β, p70S6K and its substrate S6), the changes were less pronounced (Fig. 5A). The timing of the phosphorylation changes paralleled the increase in Akt phosphorylation (Fig. 5B, S5A, B). In the case of pFoxO1 we occasionally observed a shift in migration rather than an increase in band intensity (e.g. comparing Fig. 5A and B), suggesting that phosphorylation events in addition to Thr24 take place during necroptosis. Notably, in all cases the necroptosis-associated increases in Akt substrates were abrogated by Nec-1 (Fig. 5A, Fig. S5A, B). Overall, these data suggested that a significant part of the “canonical” Akt signaling network is activated at the onset of necroptotic cell death in a RIP1 dependent fashion."}

    bionlp-st-ge-2016-uniprot

    {"project":"bionlp-st-ge-2016-uniprot","denotations":[{"id":"T10248","span":{"begin":115,"end":118},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T10266","span":{"begin":1138,"end":1141},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T10265","span":{"begin":1002,"end":1005},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T10264","span":{"begin":668,"end":671},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T10263","span":{"begin":231,"end":234},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T10262","span":{"begin":115,"end":118},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T10252","span":{"begin":1138,"end":1141},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T10251","span":{"begin":1002,"end":1005},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T10250","span":{"begin":668,"end":671},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T10249","span":{"begin":231,"end":234},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T10289","span":{"begin":1217,"end":1221},"obj":"http://www.uniprot.org/uniprot/Q13546"},{"id":"T10280","span":{"begin":1138,"end":1141},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T10279","span":{"begin":1002,"end":1005},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T10278","span":{"begin":668,"end":671},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T10277","span":{"begin":231,"end":234},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T10276","span":{"begin":115,"end":118},"obj":"http://www.uniprot.org/uniprot/Q9Y243"}],"namespaces":[{"prefix":"_base","uri":"http://www.uniprot.org/uniprot/"}],"text":"We next determined whether the necroptosis-associated increase in Thr308 phosphorylation results in an increase in Akt kinase activity. Under necroptotic conditions, we observed an increase in the phosphorylation of multiple known Akt substrates (Forkhead box class O (FoxO) proteins, GSK-3 kinases and mouse double minute 2 (MDM2)) as well as downstream molecules (p70 ribosomal protein S6 Kinase (p70S6K), S6) (Fig. 5A). In some cases (FoxO1, FoxO4, MDM2), a robust increase was observed. In other cases (FoxO3a, GSK-3α/β, p70S6K and its substrate S6), the changes were less pronounced (Fig. 5A). The timing of the phosphorylation changes paralleled the increase in Akt phosphorylation (Fig. 5B, S5A, B). In the case of pFoxO1 we occasionally observed a shift in migration rather than an increase in band intensity (e.g. comparing Fig. 5A and B), suggesting that phosphorylation events in addition to Thr24 take place during necroptosis. Notably, in all cases the necroptosis-associated increases in Akt substrates were abrogated by Nec-1 (Fig. 5A, Fig. S5A, B). Overall, these data suggested that a significant part of the “canonical” Akt signaling network is activated at the onset of necroptotic cell death in a RIP1 dependent fashion."}

    GO-BP

    {"project":"GO-BP","denotations":[{"id":"T9297","span":{"begin":1206,"end":1211},"obj":"http://purl.obolibrary.org/obo/GO_0016265"},{"id":"T9295","span":{"begin":1201,"end":1211},"obj":"http://purl.obolibrary.org/obo/GO_0008219"},{"id":"T9293","span":{"begin":1142,"end":1151},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T9291","span":{"begin":515,"end":518},"obj":"http://purl.obolibrary.org/obo/GO_0050321"},{"id":"T9290","span":{"begin":285,"end":288},"obj":"http://purl.obolibrary.org/obo/GO_0050321"},{"id":"T9289","span":{"begin":119,"end":134},"obj":"http://purl.obolibrary.org/obo/GO_0016301"},{"id":"T9287","span":{"begin":865,"end":880},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T9286","span":{"begin":672,"end":687},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T9285","span":{"begin":617,"end":632},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T9284","span":{"begin":197,"end":212},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T9283","span":{"begin":73,"end":88},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T9266","span":{"begin":966,"end":977},"obj":"http://purl.obolibrary.org/obo/GO_0097528"},{"id":"T9265","span":{"begin":927,"end":938},"obj":"http://purl.obolibrary.org/obo/GO_0097528"},{"id":"T9264","span":{"begin":31,"end":42},"obj":"http://purl.obolibrary.org/obo/GO_0097528"},{"id":"T9245","span":{"begin":966,"end":977},"obj":"http://purl.obolibrary.org/obo/GO_0070266"},{"id":"T9244","span":{"begin":927,"end":938},"obj":"http://purl.obolibrary.org/obo/GO_0070266"},{"id":"T9243","span":{"begin":31,"end":42},"obj":"http://purl.obolibrary.org/obo/GO_0070266"}],"text":"We next determined whether the necroptosis-associated increase in Thr308 phosphorylation results in an increase in Akt kinase activity. Under necroptotic conditions, we observed an increase in the phosphorylation of multiple known Akt substrates (Forkhead box class O (FoxO) proteins, GSK-3 kinases and mouse double minute 2 (MDM2)) as well as downstream molecules (p70 ribosomal protein S6 Kinase (p70S6K), S6) (Fig. 5A). In some cases (FoxO1, FoxO4, MDM2), a robust increase was observed. In other cases (FoxO3a, GSK-3α/β, p70S6K and its substrate S6), the changes were less pronounced (Fig. 5A). The timing of the phosphorylation changes paralleled the increase in Akt phosphorylation (Fig. 5B, S5A, B). In the case of pFoxO1 we occasionally observed a shift in migration rather than an increase in band intensity (e.g. comparing Fig. 5A and B), suggesting that phosphorylation events in addition to Thr24 take place during necroptosis. Notably, in all cases the necroptosis-associated increases in Akt substrates were abrogated by Nec-1 (Fig. 5A, Fig. S5A, B). Overall, these data suggested that a significant part of the “canonical” Akt signaling network is activated at the onset of necroptotic cell death in a RIP1 dependent fashion."}

    GO-MF

    {"project":"GO-MF","denotations":[{"id":"T9317","span":{"begin":370,"end":387},"obj":"http://purl.obolibrary.org/obo/GO_0003735"},{"id":"T9315","span":{"begin":515,"end":518},"obj":"http://purl.obolibrary.org/obo/GO_0050321"},{"id":"T9314","span":{"begin":285,"end":288},"obj":"http://purl.obolibrary.org/obo/GO_0050321"},{"id":"T9313","span":{"begin":119,"end":134},"obj":"http://purl.obolibrary.org/obo/GO_0016301"}],"text":"We next determined whether the necroptosis-associated increase in Thr308 phosphorylation results in an increase in Akt kinase activity. Under necroptotic conditions, we observed an increase in the phosphorylation of multiple known Akt substrates (Forkhead box class O (FoxO) proteins, GSK-3 kinases and mouse double minute 2 (MDM2)) as well as downstream molecules (p70 ribosomal protein S6 Kinase (p70S6K), S6) (Fig. 5A). In some cases (FoxO1, FoxO4, MDM2), a robust increase was observed. In other cases (FoxO3a, GSK-3α/β, p70S6K and its substrate S6), the changes were less pronounced (Fig. 5A). The timing of the phosphorylation changes paralleled the increase in Akt phosphorylation (Fig. 5B, S5A, B). In the case of pFoxO1 we occasionally observed a shift in migration rather than an increase in band intensity (e.g. comparing Fig. 5A and B), suggesting that phosphorylation events in addition to Thr24 take place during necroptosis. Notably, in all cases the necroptosis-associated increases in Akt substrates were abrogated by Nec-1 (Fig. 5A, Fig. S5A, B). Overall, these data suggested that a significant part of the “canonical” Akt signaling network is activated at the onset of necroptotic cell death in a RIP1 dependent fashion."}

    GO-CC

    {"project":"GO-CC","denotations":[{"id":"T9322","span":{"begin":1201,"end":1205},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"We next determined whether the necroptosis-associated increase in Thr308 phosphorylation results in an increase in Akt kinase activity. Under necroptotic conditions, we observed an increase in the phosphorylation of multiple known Akt substrates (Forkhead box class O (FoxO) proteins, GSK-3 kinases and mouse double minute 2 (MDM2)) as well as downstream molecules (p70 ribosomal protein S6 Kinase (p70S6K), S6) (Fig. 5A). In some cases (FoxO1, FoxO4, MDM2), a robust increase was observed. In other cases (FoxO3a, GSK-3α/β, p70S6K and its substrate S6), the changes were less pronounced (Fig. 5A). The timing of the phosphorylation changes paralleled the increase in Akt phosphorylation (Fig. 5B, S5A, B). In the case of pFoxO1 we occasionally observed a shift in migration rather than an increase in band intensity (e.g. comparing Fig. 5A and B), suggesting that phosphorylation events in addition to Thr24 take place during necroptosis. Notably, in all cases the necroptosis-associated increases in Akt substrates were abrogated by Nec-1 (Fig. 5A, Fig. S5A, B). Overall, these data suggested that a significant part of the “canonical” Akt signaling network is activated at the onset of necroptotic cell death in a RIP1 dependent fashion."}

    sentences

    {"project":"sentences","denotations":[{"id":"T9093","span":{"begin":1065,"end":1240},"obj":"Sentence"},{"id":"T9092","span":{"begin":940,"end":1064},"obj":"Sentence"},{"id":"T9091","span":{"begin":707,"end":939},"obj":"Sentence"},{"id":"T9090","span":{"begin":599,"end":706},"obj":"Sentence"},{"id":"T9089","span":{"begin":491,"end":598},"obj":"Sentence"},{"id":"T9088","span":{"begin":423,"end":490},"obj":"Sentence"},{"id":"T9087","span":{"begin":136,"end":422},"obj":"Sentence"},{"id":"T9086","span":{"begin":0,"end":135},"obj":"Sentence"},{"id":"T127","span":{"begin":0,"end":135},"obj":"Sentence"},{"id":"T128","span":{"begin":136,"end":422},"obj":"Sentence"},{"id":"T129","span":{"begin":423,"end":490},"obj":"Sentence"},{"id":"T130","span":{"begin":491,"end":598},"obj":"Sentence"},{"id":"T131","span":{"begin":599,"end":706},"obj":"Sentence"},{"id":"T132","span":{"begin":707,"end":939},"obj":"Sentence"},{"id":"T133","span":{"begin":940,"end":1064},"obj":"Sentence"},{"id":"T134","span":{"begin":1065,"end":1240},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"We next determined whether the necroptosis-associated increase in Thr308 phosphorylation results in an increase in Akt kinase activity. Under necroptotic conditions, we observed an increase in the phosphorylation of multiple known Akt substrates (Forkhead box class O (FoxO) proteins, GSK-3 kinases and mouse double minute 2 (MDM2)) as well as downstream molecules (p70 ribosomal protein S6 Kinase (p70S6K), S6) (Fig. 5A). In some cases (FoxO1, FoxO4, MDM2), a robust increase was observed. In other cases (FoxO3a, GSK-3α/β, p70S6K and its substrate S6), the changes were less pronounced (Fig. 5A). The timing of the phosphorylation changes paralleled the increase in Akt phosphorylation (Fig. 5B, S5A, B). In the case of pFoxO1 we occasionally observed a shift in migration rather than an increase in band intensity (e.g. comparing Fig. 5A and B), suggesting that phosphorylation events in addition to Thr24 take place during necroptosis. Notably, in all cases the necroptosis-associated increases in Akt substrates were abrogated by Nec-1 (Fig. 5A, Fig. S5A, B). Overall, these data suggested that a significant part of the “canonical” Akt signaling network is activated at the onset of necroptotic cell death in a RIP1 dependent fashion."}

    simple1

    {"project":"simple1","denotations":[{"id":"T9348","span":{"begin":1217,"end":1221},"obj":"Protein"},{"id":"T9347","span":{"begin":722,"end":728},"obj":"Protein"},{"id":"T9346","span":{"begin":550,"end":552},"obj":"Protein"},{"id":"T9345","span":{"begin":525,"end":531},"obj":"Protein"},{"id":"T9344","span":{"begin":522,"end":523},"obj":"Protein"},{"id":"T9343","span":{"begin":515,"end":521},"obj":"Protein"},{"id":"T9342","span":{"begin":507,"end":513},"obj":"Protein"},{"id":"T9341","span":{"begin":452,"end":456},"obj":"Protein"},{"id":"T9340","span":{"begin":445,"end":450},"obj":"Protein"},{"id":"T9339","span":{"begin":438,"end":443},"obj":"Protein"},{"id":"T9338","span":{"begin":408,"end":410},"obj":"Protein"},{"id":"T9337","span":{"begin":399,"end":405},"obj":"Protein"},{"id":"T9336","span":{"begin":366,"end":397},"obj":"Protein"},{"id":"T9335","span":{"begin":326,"end":330},"obj":"Protein"},{"id":"T9334","span":{"begin":309,"end":324},"obj":"Protein"}],"text":"We next determined whether the necroptosis-associated increase in Thr308 phosphorylation results in an increase in Akt kinase activity. Under necroptotic conditions, we observed an increase in the phosphorylation of multiple known Akt substrates (Forkhead box class O (FoxO) proteins, GSK-3 kinases and mouse double minute 2 (MDM2)) as well as downstream molecules (p70 ribosomal protein S6 Kinase (p70S6K), S6) (Fig. 5A). In some cases (FoxO1, FoxO4, MDM2), a robust increase was observed. In other cases (FoxO3a, GSK-3α/β, p70S6K and its substrate S6), the changes were less pronounced (Fig. 5A). The timing of the phosphorylation changes paralleled the increase in Akt phosphorylation (Fig. 5B, S5A, B). In the case of pFoxO1 we occasionally observed a shift in migration rather than an increase in band intensity (e.g. comparing Fig. 5A and B), suggesting that phosphorylation events in addition to Thr24 take place during necroptosis. Notably, in all cases the necroptosis-associated increases in Akt substrates were abrogated by Nec-1 (Fig. 5A, Fig. S5A, B). Overall, these data suggested that a significant part of the “canonical” Akt signaling network is activated at the onset of necroptotic cell death in a RIP1 dependent fashion."}

    BioNLP16_DUT

    {"project":"BioNLP16_DUT","denotations":[{"id":"T10217","span":{"begin":790,"end":798},"obj":"Positive_regulation"},{"id":"T10216","span":{"begin":468,"end":476},"obj":"Positive_regulation"},{"id":"T10215","span":{"begin":181,"end":189},"obj":"Positive_regulation"},{"id":"T10214","span":{"begin":197,"end":212},"obj":"Phosphorylation"},{"id":"T10186","span":{"begin":1217,"end":1221},"obj":"Protein"},{"id":"T10185","span":{"begin":722,"end":728},"obj":"Protein"},{"id":"T10184","span":{"begin":507,"end":513},"obj":"Protein"},{"id":"T10183","span":{"begin":550,"end":552},"obj":"Protein"},{"id":"T10182","span":{"begin":525,"end":531},"obj":"Protein"},{"id":"T10181","span":{"begin":522,"end":523},"obj":"Protein"},{"id":"T10180","span":{"begin":515,"end":521},"obj":"Protein"},{"id":"T10179","span":{"begin":452,"end":456},"obj":"Protein"},{"id":"T10178","span":{"begin":445,"end":450},"obj":"Protein"},{"id":"T10177","span":{"begin":438,"end":443},"obj":"Protein"},{"id":"T10176","span":{"begin":408,"end":410},"obj":"Protein"},{"id":"T10175","span":{"begin":399,"end":405},"obj":"Protein"},{"id":"T10174","span":{"begin":366,"end":397},"obj":"Protein"},{"id":"T10173","span":{"begin":326,"end":330},"obj":"Protein"},{"id":"T10172","span":{"begin":309,"end":324},"obj":"Protein"}],"relations":[{"id":"R6659","pred":"themeOf","subj":"T10172","obj":"T10214"},{"id":"R6660","pred":"themeOf","subj":"T10173","obj":"T10214"},{"id":"R6661","pred":"themeOf","subj":"T10174","obj":"T10214"},{"id":"R6662","pred":"themeOf","subj":"T10175","obj":"T10214"},{"id":"R6663","pred":"themeOf","subj":"T10176","obj":"T10214"},{"id":"R6664","pred":"themeOf","subj":"T10178","obj":"T10216"},{"id":"R6665","pred":"themeOf","subj":"T10185","obj":"T10217"},{"id":"R6687","pred":"themeOf","subj":"T10214","obj":"T10215"},{"id":"R6688","pred":"themeOf","subj":"T10214","obj":"T10215"},{"id":"R6689","pred":"themeOf","subj":"T10214","obj":"T10215"},{"id":"R6690","pred":"themeOf","subj":"T10214","obj":"T10215"},{"id":"R6691","pred":"themeOf","subj":"T10214","obj":"T10215"}],"text":"We next determined whether the necroptosis-associated increase in Thr308 phosphorylation results in an increase in Akt kinase activity. Under necroptotic conditions, we observed an increase in the phosphorylation of multiple known Akt substrates (Forkhead box class O (FoxO) proteins, GSK-3 kinases and mouse double minute 2 (MDM2)) as well as downstream molecules (p70 ribosomal protein S6 Kinase (p70S6K), S6) (Fig. 5A). In some cases (FoxO1, FoxO4, MDM2), a robust increase was observed. In other cases (FoxO3a, GSK-3α/β, p70S6K and its substrate S6), the changes were less pronounced (Fig. 5A). The timing of the phosphorylation changes paralleled the increase in Akt phosphorylation (Fig. 5B, S5A, B). In the case of pFoxO1 we occasionally observed a shift in migration rather than an increase in band intensity (e.g. comparing Fig. 5A and B), suggesting that phosphorylation events in addition to Thr24 take place during necroptosis. Notably, in all cases the necroptosis-associated increases in Akt substrates were abrogated by Nec-1 (Fig. 5A, Fig. S5A, B). Overall, these data suggested that a significant part of the “canonical” Akt signaling network is activated at the onset of necroptotic cell death in a RIP1 dependent fashion."}

    BioNLP16_Messiy

    {"project":"BioNLP16_Messiy","denotations":[{"id":"T10473","span":{"begin":1217,"end":1221},"obj":"Protein"},{"id":"T10472","span":{"begin":722,"end":728},"obj":"Protein"},{"id":"T10471","span":{"begin":507,"end":513},"obj":"Protein"},{"id":"T10470","span":{"begin":550,"end":552},"obj":"Protein"},{"id":"T10469","span":{"begin":525,"end":531},"obj":"Protein"},{"id":"T10468","span":{"begin":522,"end":523},"obj":"Protein"},{"id":"T10467","span":{"begin":515,"end":521},"obj":"Protein"},{"id":"T10466","span":{"begin":452,"end":456},"obj":"Protein"},{"id":"T10465","span":{"begin":445,"end":450},"obj":"Protein"},{"id":"T10464","span":{"begin":438,"end":443},"obj":"Protein"},{"id":"T10463","span":{"begin":408,"end":410},"obj":"Protein"},{"id":"T10462","span":{"begin":399,"end":405},"obj":"Protein"},{"id":"T10461","span":{"begin":366,"end":397},"obj":"Protein"},{"id":"T10460","span":{"begin":326,"end":330},"obj":"Protein"},{"id":"T10459","span":{"begin":309,"end":324},"obj":"Protein"},{"id":"T10503","span":{"begin":790,"end":798},"obj":"Positive_regulation"},{"id":"T10502","span":{"begin":181,"end":189},"obj":"Positive_regulation"},{"id":"T10501","span":{"begin":197,"end":212},"obj":"Phosphorylation"}],"relations":[{"id":"R6777","pred":"themeOf","subj":"T10459","obj":"T10501"},{"id":"R6778","pred":"themeOf","subj":"T10460","obj":"T10501"},{"id":"R6779","pred":"themeOf","subj":"T10461","obj":"T10501"},{"id":"R6780","pred":"themeOf","subj":"T10462","obj":"T10501"},{"id":"R6781","pred":"themeOf","subj":"T10463","obj":"T10501"},{"id":"R6782","pred":"themeOf","subj":"T10472","obj":"T10503"},{"id":"R6802","pred":"themeOf","subj":"T10501","obj":"T10502"},{"id":"R6803","pred":"themeOf","subj":"T10501","obj":"T10502"},{"id":"R6804","pred":"themeOf","subj":"T10501","obj":"T10502"},{"id":"R6805","pred":"themeOf","subj":"T10501","obj":"T10502"},{"id":"R6806","pred":"themeOf","subj":"T10501","obj":"T10502"}],"text":"We next determined whether the necroptosis-associated increase in Thr308 phosphorylation results in an increase in Akt kinase activity. Under necroptotic conditions, we observed an increase in the phosphorylation of multiple known Akt substrates (Forkhead box class O (FoxO) proteins, GSK-3 kinases and mouse double minute 2 (MDM2)) as well as downstream molecules (p70 ribosomal protein S6 Kinase (p70S6K), S6) (Fig. 5A). In some cases (FoxO1, FoxO4, MDM2), a robust increase was observed. In other cases (FoxO3a, GSK-3α/β, p70S6K and its substrate S6), the changes were less pronounced (Fig. 5A). The timing of the phosphorylation changes paralleled the increase in Akt phosphorylation (Fig. 5B, S5A, B). In the case of pFoxO1 we occasionally observed a shift in migration rather than an increase in band intensity (e.g. comparing Fig. 5A and B), suggesting that phosphorylation events in addition to Thr24 take place during necroptosis. Notably, in all cases the necroptosis-associated increases in Akt substrates were abrogated by Nec-1 (Fig. 5A, Fig. S5A, B). Overall, these data suggested that a significant part of the “canonical” Akt signaling network is activated at the onset of necroptotic cell death in a RIP1 dependent fashion."}

    DLUT931

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    bionlp-st-ge-2016-test-ihmc

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next determined whether the necroptosis-associated increase in Thr308 phosphorylation results in an increase in Akt kinase activity. Under necroptotic conditions, we observed an increase in the phosphorylation of multiple known Akt substrates (Forkhead box class O (FoxO) proteins, GSK-3 kinases and mouse double minute 2 (MDM2)) as well as downstream molecules (p70 ribosomal protein S6 Kinase (p70S6K), S6) (Fig. 5A). In some cases (FoxO1, FoxO4, MDM2), a robust increase was observed. In other cases (FoxO3a, GSK-3α/β, p70S6K and its substrate S6), the changes were less pronounced (Fig. 5A). The timing of the phosphorylation changes paralleled the increase in Akt phosphorylation (Fig. 5B, S5A, B). In the case of pFoxO1 we occasionally observed a shift in migration rather than an increase in band intensity (e.g. comparing Fig. 5A and B), suggesting that phosphorylation events in addition to Thr24 take place during necroptosis. Notably, in all cases the necroptosis-associated increases in Akt substrates were abrogated by Nec-1 (Fig. 5A, Fig. S5A, B). Overall, these data suggested that a significant part of the “canonical” Akt signaling network is activated at the onset of necroptotic cell death in a RIP1 dependent fashion."}

    bionlp-st-ge-2016-test-tees

    {"project":"bionlp-st-ge-2016-test-tees","denotations":[{"id":"T10564","span":{"begin":1217,"end":1221},"obj":"Protein"},{"id":"T10563","span":{"begin":1138,"end":1141},"obj":"Protein"},{"id":"T10562","span":{"begin":1022,"end":1031},"obj":"Negative_regulation"},{"id":"T10561","span":{"begin":1022,"end":1031},"obj":"Negative_regulation"},{"id":"T10560","span":{"begin":989,"end":998},"obj":"Positive_regulation"},{"id":"T10559","span":{"begin":1056,"end":1059},"obj":"Protein"},{"id":"T10558","span":{"begin":1051,"end":1054},"obj":"Protein"},{"id":"T10537","span":{"begin":303,"end":324},"obj":"Protein"},{"id":"T10536","span":{"begin":285,"end":298},"obj":"Protein"},{"id":"T10535","span":{"begin":247,"end":283},"obj":"Protein"},{"id":"T10534","span":{"begin":231,"end":234},"obj":"Protein"},{"id":"T10533","span":{"begin":103,"end":111},"obj":"Positive_regulation"},{"id":"T10532","span":{"begin":115,"end":125},"obj":"Protein"},{"id":"T10557","span":{"begin":1042,"end":1049},"obj":"Protein"},{"id":"T10556","span":{"begin":1035,"end":1040},"obj":"Protein"},{"id":"T10555","span":{"begin":1002,"end":1005},"obj":"Protein"},{"id":"T10554","span":{"begin":656,"end":664},"obj":"Positive_regulation"},{"id":"T10553","span":{"begin":672,"end":687},"obj":"Phosphorylation"},{"id":"T10552","span":{"begin":617,"end":632},"obj":"Phosphorylation"},{"id":"T10551","span":{"begin":617,"end":632},"obj":"Phosphorylation"},{"id":"T10550","span":{"begin":698,"end":701},"obj":"Protein"},{"id":"T10549","span":{"begin":689,"end":696},"obj":"Protein"},{"id":"T10548","span":{"begin":668,"end":671},"obj":"Protein"},{"id":"T10547","span":{"begin":515,"end":531},"obj":"Protein"},{"id":"T10546","span":{"begin":507,"end":513},"obj":"Protein"},{"id":"T10545","span":{"begin":468,"end":476},"obj":"Positive_regulation"},{"id":"T10544","span":{"begin":452,"end":456},"obj":"Protein"},{"id":"T10543","span":{"begin":445,"end":450},"obj":"Protein"},{"id":"T10542","span":{"begin":438,"end":443},"obj":"Protein"},{"id":"T10541","span":{"begin":399,"end":405},"obj":"Protein"},{"id":"T10540","span":{"begin":388,"end":397},"obj":"Protein"},{"id":"T10539","span":{"begin":366,"end":387},"obj":"Protein"},{"id":"T10538","span":{"begin":326,"end":330},"obj":"Protein"}],"relations":[{"id":"R6816","pred":"themeOf","subj":"T10532","obj":"T10533"},{"id":"R6817","pred":"themeOf","subj":"T10542","obj":"T10545"},{"id":"R6818","pred":"themeOf","subj":"T10548","obj":"T10553"},{"id":"R6819","pred":"themeOf","subj":"T10549","obj":"T10551"},{"id":"R6820","pred":"themeOf","subj":"T10550","obj":"T10552"},{"id":"R6821","pred":"themeOf","subj":"T10553","obj":"T10554"},{"id":"R6822","pred":"themeOf","subj":"T10555","obj":"T10560"},{"id":"R6823","pred":"causeOf","subj":"T10556","obj":"T10561"},{"id":"R6824","pred":"causeOf","subj":"T10556","obj":"T10562"},{"id":"R6825","pred":"themeOf","subj":"T10557","obj":"T10561"},{"id":"R6826","pred":"themeOf","subj":"T10560","obj":"T10562"}],"text":"We next determined whether the necroptosis-associated increase in Thr308 phosphorylation results in an increase in Akt kinase activity. Under necroptotic conditions, we observed an increase in the phosphorylation of multiple known Akt substrates (Forkhead box class O (FoxO) proteins, GSK-3 kinases and mouse double minute 2 (MDM2)) as well as downstream molecules (p70 ribosomal protein S6 Kinase (p70S6K), S6) (Fig. 5A). In some cases (FoxO1, FoxO4, MDM2), a robust increase was observed. In other cases (FoxO3a, GSK-3α/β, p70S6K and its substrate S6), the changes were less pronounced (Fig. 5A). The timing of the phosphorylation changes paralleled the increase in Akt phosphorylation (Fig. 5B, S5A, B). In the case of pFoxO1 we occasionally observed a shift in migration rather than an increase in band intensity (e.g. comparing Fig. 5A and B), suggesting that phosphorylation events in addition to Thr24 take place during necroptosis. Notably, in all cases the necroptosis-associated increases in Akt substrates were abrogated by Nec-1 (Fig. 5A, Fig. S5A, B). Overall, these data suggested that a significant part of the “canonical” Akt signaling network is activated at the onset of necroptotic cell death in a RIP1 dependent fashion."}

    test3

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