PMC:3585731 / 12399-13175 JSONTXT

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This time point was chosen because it reflects the early stage of cell death in our system (Fig. S3A, B). Following stimulation with either zVAD.fmk or TNFα we observed a robust increase in Akt phosphorylation at a known major activation site, Thr308 (Fig. 3A). Interestingly, we did not observe concomitant phosphorylation changes in the second major activation site of Akt, Ser473. We also observed an increase in the phosphorylation of both the p46 and p54 isoforms of JNK and its major substrate c-Jun (Fig. 3A). These data indicate that both Akt and JNK are activated under necroptotic conditions."}

{"project":"bionlp-st-ge-2016-test-proteins","denotations":[{"id":"T5382","span":{"begin":674,"end":679},"obj":"Protein"},{"id":"T5381","span":{"begin":630,"end":633},"obj":"Protein"},{"id":"T5380","span":{"begin":622,"end":625},"obj":"Protein"},{"id":"T5379","span":{"begin":326,"end":330},"obj":"Protein"},{"id":"T5378","span":{"begin":156,"end":160},"obj":"Protein"}],"namespaces":[{"prefix":"_base","uri":"http://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"To understand the activation of Akt and JNK under necroptotic conditions, we examined the changes in Akt and JNK phosphorylation at 9 hrs post zVAD.fmk and TNFα stimulation. This time point was chosen because it reflects the early stage of cell death in our system (Fig. S3A, B). Following stimulation with either zVAD.fmk or TNFα we observed a robust increase in Akt phosphorylation at a known major activation site, Thr308 (Fig. 3A). Interestingly, we did not observe concomitant phosphorylation changes in the second major activation site of Akt, Ser473. We also observed an increase in the phosphorylation of both the p46 and p54 isoforms of JNK and its major substrate c-Jun (Fig. 3A). These data indicate that both Akt and JNK are activated under necroptotic conditions."}

{"project":"bionlp-st-ge-2016-uniprot","denotations":[{"id":"T6532","span":{"begin":326,"end":330},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T6506","span":{"begin":721,"end":724},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T6505","span":{"begin":545,"end":548},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T6504","span":{"begin":364,"end":367},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T6503","span":{"begin":101,"end":104},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T6502","span":{"begin":32,"end":35},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T6478","span":{"begin":721,"end":724},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T6477","span":{"begin":545,"end":548},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T6476","span":{"begin":364,"end":367},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T6475","span":{"begin":101,"end":104},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T6474","span":{"begin":32,"end":35},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T6446","span":{"begin":32,"end":35},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T6450","span":{"begin":721,"end":724},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T6449","span":{"begin":545,"end":548},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T6448","span":{"begin":364,"end":367},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T6447","span":{"begin":101,"end":104},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T6531","span":{"begin":156,"end":160},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T6535","span":{"begin":674,"end":679},"obj":"http://www.uniprot.org/uniprot/P05412"},{"id":"T6534","span":{"begin":630,"end":633},"obj":"http://www.uniprot.org/uniprot/Q13451"}],"namespaces":[{"prefix":"_base","uri":"http://www.uniprot.org/uniprot/"}],"text":"To understand the activation of Akt and JNK under necroptotic conditions, we examined the changes in Akt and JNK phosphorylation at 9 hrs post zVAD.fmk and TNFα stimulation. This time point was chosen because it reflects the early stage of cell death in our system (Fig. S3A, B). Following stimulation with either zVAD.fmk or TNFα we observed a robust increase in Akt phosphorylation at a known major activation site, Thr308 (Fig. 3A). Interestingly, we did not observe concomitant phosphorylation changes in the second major activation site of Akt, Ser473. We also observed an increase in the phosphorylation of both the p46 and p54 isoforms of JNK and its major substrate c-Jun (Fig. 3A). These data indicate that both Akt and JNK are activated under necroptotic conditions."}

{"project":"GO-BP","denotations":[{"id":"T5466","span":{"begin":594,"end":609},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T5465","span":{"begin":482,"end":497},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T5464","span":{"begin":368,"end":383},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T5463","span":{"begin":113,"end":128},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T5450","span":{"begin":729,"end":732},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T5449","span":{"begin":646,"end":649},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T5448","span":{"begin":109,"end":112},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T5447","span":{"begin":40,"end":43},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T5443","span":{"begin":240,"end":250},"obj":"http://purl.obolibrary.org/obo/GO_0008219"},{"id":"T5434","span":{"begin":245,"end":250},"obj":"http://purl.obolibrary.org/obo/GO_0016265"}],"text":"To understand the activation of Akt and JNK under necroptotic conditions, we examined the changes in Akt and JNK phosphorylation at 9 hrs post zVAD.fmk and TNFα stimulation. This time point was chosen because it reflects the early stage of cell death in our system (Fig. S3A, B). Following stimulation with either zVAD.fmk or TNFα we observed a robust increase in Akt phosphorylation at a known major activation site, Thr308 (Fig. 3A). Interestingly, we did not observe concomitant phosphorylation changes in the second major activation site of Akt, Ser473. We also observed an increase in the phosphorylation of both the p46 and p54 isoforms of JNK and its major substrate c-Jun (Fig. 3A). These data indicate that both Akt and JNK are activated under necroptotic conditions."}

{"project":"GO-MF","denotations":[{"id":"T5498","span":{"begin":729,"end":732},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T5497","span":{"begin":646,"end":649},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T5496","span":{"begin":109,"end":112},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T5495","span":{"begin":40,"end":43},"obj":"http://purl.obolibrary.org/obo/GO_0004705"}],"text":"To understand the activation of Akt and JNK under necroptotic conditions, we examined the changes in Akt and JNK phosphorylation at 9 hrs post zVAD.fmk and TNFα stimulation. This time point was chosen because it reflects the early stage of cell death in our system (Fig. S3A, B). Following stimulation with either zVAD.fmk or TNFα we observed a robust increase in Akt phosphorylation at a known major activation site, Thr308 (Fig. 3A). Interestingly, we did not observe concomitant phosphorylation changes in the second major activation site of Akt, Ser473. We also observed an increase in the phosphorylation of both the p46 and p54 isoforms of JNK and its major substrate c-Jun (Fig. 3A). These data indicate that both Akt and JNK are activated under necroptotic conditions."}

{"project":"GO-CC","denotations":[{"id":"T5516","span":{"begin":240,"end":244},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"To understand the activation of Akt and JNK under necroptotic conditions, we examined the changes in Akt and JNK phosphorylation at 9 hrs post zVAD.fmk and TNFα stimulation. This time point was chosen because it reflects the early stage of cell death in our system (Fig. S3A, B). Following stimulation with either zVAD.fmk or TNFα we observed a robust increase in Akt phosphorylation at a known major activation site, Thr308 (Fig. 3A). Interestingly, we did not observe concomitant phosphorylation changes in the second major activation site of Akt, Ser473. We also observed an increase in the phosphorylation of both the p46 and p54 isoforms of JNK and its major substrate c-Jun (Fig. 3A). These data indicate that both Akt and JNK are activated under necroptotic conditions."}

{"project":"sentences","denotations":[{"id":"T5296","span":{"begin":691,"end":776},"obj":"Sentence"},{"id":"T5295","span":{"begin":558,"end":690},"obj":"Sentence"},{"id":"T5294","span":{"begin":436,"end":557},"obj":"Sentence"},{"id":"T5293","span":{"begin":280,"end":435},"obj":"Sentence"},{"id":"T5292","span":{"begin":174,"end":279},"obj":"Sentence"},{"id":"T5291","span":{"begin":0,"end":173},"obj":"Sentence"},{"id":"T80","span":{"begin":0,"end":173},"obj":"Sentence"},{"id":"T81","span":{"begin":174,"end":279},"obj":"Sentence"},{"id":"T82","span":{"begin":280,"end":435},"obj":"Sentence"},{"id":"T83","span":{"begin":436,"end":557},"obj":"Sentence"},{"id":"T84","span":{"begin":558,"end":690},"obj":"Sentence"},{"id":"T85","span":{"begin":691,"end":776},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"To understand the activation of Akt and JNK under necroptotic conditions, we examined the changes in Akt and JNK phosphorylation at 9 hrs post zVAD.fmk and TNFα stimulation. This time point was chosen because it reflects the early stage of cell death in our system (Fig. S3A, B). Following stimulation with either zVAD.fmk or TNFα we observed a robust increase in Akt phosphorylation at a known major activation site, Thr308 (Fig. 3A). Interestingly, we did not observe concomitant phosphorylation changes in the second major activation site of Akt, Ser473. We also observed an increase in the phosphorylation of both the p46 and p54 isoforms of JNK and its major substrate c-Jun (Fig. 3A). These data indicate that both Akt and JNK are activated under necroptotic conditions."}

{"project":"simple1","denotations":[{"id":"T5535","span":{"begin":674,"end":679},"obj":"Protein"},{"id":"T5534","span":{"begin":630,"end":633},"obj":"Protein"},{"id":"T5533","span":{"begin":622,"end":625},"obj":"Protein"},{"id":"T5532","span":{"begin":326,"end":330},"obj":"Protein"},{"id":"T5531","span":{"begin":156,"end":160},"obj":"Protein"}],"text":"To understand the activation of Akt and JNK under necroptotic conditions, we examined the changes in Akt and JNK phosphorylation at 9 hrs post zVAD.fmk and TNFα stimulation. This time point was chosen because it reflects the early stage of cell death in our system (Fig. S3A, B). Following stimulation with either zVAD.fmk or TNFα we observed a robust increase in Akt phosphorylation at a known major activation site, Thr308 (Fig. 3A). Interestingly, we did not observe concomitant phosphorylation changes in the second major activation site of Akt, Ser473. We also observed an increase in the phosphorylation of both the p46 and p54 isoforms of JNK and its major substrate c-Jun (Fig. 3A). These data indicate that both Akt and JNK are activated under necroptotic conditions."}

{"project":"BioNLP16_DUT","denotations":[{"id":"T6416","span":{"begin":578,"end":586},"obj":"Positive_regulation"},{"id":"T6415","span":{"begin":594,"end":609},"obj":"Phosphorylation"},{"id":"T6394","span":{"begin":674,"end":679},"obj":"Protein"},{"id":"T6393","span":{"begin":630,"end":633},"obj":"Protein"},{"id":"T6392","span":{"begin":622,"end":625},"obj":"Protein"},{"id":"T6391","span":{"begin":326,"end":330},"obj":"Protein"},{"id":"T6390","span":{"begin":156,"end":160},"obj":"Protein"}],"relations":[{"id":"R4403","pred":"themeOf","subj":"T6392","obj":"T6415"},{"id":"R4404","pred":"themeOf","subj":"T6393","obj":"T6415"},{"id":"R4405","pred":"themeOf","subj":"T6394","obj":"T6415"},{"id":"R4406","pred":"themeOf","subj":"T6394","obj":"T6416"},{"id":"R4415","pred":"themeOf","subj":"T6415","obj":"T6416"},{"id":"R4416","pred":"themeOf","subj":"T6415","obj":"T6416"},{"id":"R4417","pred":"themeOf","subj":"T6415","obj":"T6416"}],"text":"To understand the activation of Akt and JNK under necroptotic conditions, we examined the changes in Akt and JNK phosphorylation at 9 hrs post zVAD.fmk and TNFα stimulation. This time point was chosen because it reflects the early stage of cell death in our system (Fig. S3A, B). Following stimulation with either zVAD.fmk or TNFα we observed a robust increase in Akt phosphorylation at a known major activation site, Thr308 (Fig. 3A). Interestingly, we did not observe concomitant phosphorylation changes in the second major activation site of Akt, Ser473. We also observed an increase in the phosphorylation of both the p46 and p54 isoforms of JNK and its major substrate c-Jun (Fig. 3A). These data indicate that both Akt and JNK are activated under necroptotic conditions."}

{"project":"BioNLP16_Messiy","denotations":[{"id":"T6700","span":{"begin":578,"end":586},"obj":"Positive_regulation"},{"id":"T6699","span":{"begin":594,"end":609},"obj":"Phosphorylation"},{"id":"T6673","span":{"begin":622,"end":625},"obj":"Protein"},{"id":"T6672","span":{"begin":326,"end":330},"obj":"Protein"},{"id":"T6671","span":{"begin":156,"end":160},"obj":"Protein"},{"id":"T6675","span":{"begin":674,"end":679},"obj":"Protein"},{"id":"T6674","span":{"begin":630,"end":633},"obj":"Protein"}],"relations":[{"id":"R4484","pred":"themeOf","subj":"T6673","obj":"T6699"},{"id":"R4485","pred":"themeOf","subj":"T6674","obj":"T6699"},{"id":"R4486","pred":"themeOf","subj":"T6675","obj":"T6699"},{"id":"R4492","pred":"themeOf","subj":"T6699","obj":"T6700"},{"id":"R4493","pred":"themeOf","subj":"T6699","obj":"T6700"},{"id":"R4494","pred":"themeOf","subj":"T6699","obj":"T6700"}],"text":"To understand the activation of Akt and JNK under necroptotic conditions, we examined the changes in Akt and JNK phosphorylation at 9 hrs post zVAD.fmk and TNFα stimulation. This time point was chosen because it reflects the early stage of cell death in our system (Fig. S3A, B). Following stimulation with either zVAD.fmk or TNFα we observed a robust increase in Akt phosphorylation at a known major activation site, Thr308 (Fig. 3A). Interestingly, we did not observe concomitant phosphorylation changes in the second major activation site of Akt, Ser473. We also observed an increase in the phosphorylation of both the p46 and p54 isoforms of JNK and its major substrate c-Jun (Fig. 3A). These data indicate that both Akt and JNK are activated under necroptotic conditions."}

{"project":"DLUT931","denotations":[{"id":"T6580","span":{"begin":578,"end":586},"obj":"Positive_regulation"},{"id":"T6579","span":{"begin":594,"end":609},"obj":"Phosphorylation"},{"id":"T6578","span":{"begin":314,"end":322},"obj":"Positive_regulation"},{"id":"T6555","span":{"begin":674,"end":679},"obj":"Protein"},{"id":"T6554","span":{"begin":630,"end":633},"obj":"Protein"},{"id":"T6553","span":{"begin":622,"end":625},"obj":"Protein"},{"id":"T6552","span":{"begin":326,"end":330},"obj":"Protein"},{"id":"T6551","span":{"begin":156,"end":160},"obj":"Protein"}],"relations":[{"id":"R4428","pred":"themeOf","subj":"T6552","obj":"T6578"},{"id":"R4429","pred":"themeOf","subj":"T6553","obj":"T6579"},{"id":"R4430","pred":"themeOf","subj":"T6554","obj":"T6579"},{"id":"R4431","pred":"themeOf","subj":"T6555","obj":"T6579"},{"id":"R4444","pred":"themeOf","subj":"T6579","obj":"T6580"},{"id":"R4445","pred":"themeOf","subj":"T6579","obj":"T6580"},{"id":"R4446","pred":"themeOf","subj":"T6579","obj":"T6580"}],"text":"To understand the activation of Akt and JNK under necroptotic conditions, we examined the changes in Akt and JNK phosphorylation at 9 hrs post zVAD.fmk and TNFα stimulation. This time point was chosen because it reflects the early stage of cell death in our system (Fig. S3A, B). Following stimulation with either zVAD.fmk or TNFα we observed a robust increase in Akt phosphorylation at a known major activation site, Thr308 (Fig. 3A). Interestingly, we did not observe concomitant phosphorylation changes in the second major activation site of Akt, Ser473. We also observed an increase in the phosphorylation of both the p46 and p54 isoforms of JNK and its major substrate c-Jun (Fig. 3A). These data indicate that both Akt and JNK are activated under necroptotic conditions."}

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