![Logo](/assets/logo-d3f1fdf60522f0983e71f9fcc720cb7da5b55c0b748ed5bded3d2fbf81387bf0.png)
PMC:3585731 / 30780-31556
Annnotations
testone
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pmc-enju-pas
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kinase-dependent Thr308 phosphorylation of Myr-Akt during necroptosis increased Myr-Akt activity as it did with endogenous Akt (Fig. 5). Phosphorylation of many previously described Akt substrates was increased upon the expression of Myr-Akt, but not the K179M mutant, confirming that these molecules are Akt substrates in L929 cells (Fig. 7C). The effect of zVAD.fmk on their phosphorylation varied, likely due to the increased basal activity of Myr-Akt. Some substrates, including p70S6K, S6, GSK-3 and FoxO4, were fully phosphorylated even in the absence of zVAD.fmk. On the other hand, phosphorylation of FoxO1 and MDM2 was significantly increased in the presence of zVAD.fmk, indicating that necroptotic Thr308 phosphorylation of Myr-Akt still promoted its activity."}
bionlp-st-ge-2016-test-proteins
{"project":"bionlp-st-ge-2016-test-proteins","denotations":[{"id":"T13860","span":{"begin":740,"end":747},"obj":"Protein"},{"id":"T13859","span":{"begin":624,"end":628},"obj":"Protein"},{"id":"T13858","span":{"begin":614,"end":619},"obj":"Protein"},{"id":"T13857","span":{"begin":510,"end":515},"obj":"Protein"},{"id":"T13856","span":{"begin":496,"end":498},"obj":"Protein"},{"id":"T13855","span":{"begin":488,"end":494},"obj":"Protein"},{"id":"T13854","span":{"begin":452,"end":459},"obj":"Protein"},{"id":"T13853","span":{"begin":260,"end":265},"obj":"Protein"},{"id":"T13852","span":{"begin":239,"end":246},"obj":"Protein"},{"id":"T13851","span":{"begin":85,"end":92},"obj":"Protein"},{"id":"T13850","span":{"begin":48,"end":55},"obj":"Protein"}],"namespaces":[{"prefix":"_base","uri":"http://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"RIP1 kinase-dependent Thr308 phosphorylation of Myr-Akt during necroptosis increased Myr-Akt activity as it did with endogenous Akt (Fig. 5). Phosphorylation of many previously described Akt substrates was increased upon the expression of Myr-Akt, but not the K179M mutant, confirming that these molecules are Akt substrates in L929 cells (Fig. 7C). The effect of zVAD.fmk on their phosphorylation varied, likely due to the increased basal activity of Myr-Akt. Some substrates, including p70S6K, S6, GSK-3 and FoxO4, were fully phosphorylated even in the absence of zVAD.fmk. On the other hand, phosphorylation of FoxO1 and MDM2 was significantly increased in the presence of zVAD.fmk, indicating that necroptotic Thr308 phosphorylation of Myr-Akt still promoted its activity."}
bionlp-st-ge-2016-uniprot
{"project":"bionlp-st-ge-2016-uniprot","denotations":[{"id":"T15075","span":{"begin":310,"end":313},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T15074","span":{"begin":243,"end":246},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T15073","span":{"begin":187,"end":190},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T15072","span":{"begin":128,"end":131},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T15071","span":{"begin":89,"end":92},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T15070","span":{"begin":52,"end":55},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T15042","span":{"begin":744,"end":747},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T15041","span":{"begin":456,"end":459},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T15040","span":{"begin":310,"end":313},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T15039","span":{"begin":243,"end":246},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T15038","span":{"begin":187,"end":190},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T15037","span":{"begin":128,"end":131},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T15036","span":{"begin":89,"end":92},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T15035","span":{"begin":52,"end":55},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T15007","span":{"begin":744,"end":747},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T15006","span":{"begin":456,"end":459},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T15005","span":{"begin":310,"end":313},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T15004","span":{"begin":243,"end":246},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T15003","span":{"begin":187,"end":190},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T15002","span":{"begin":128,"end":131},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T15001","span":{"begin":89,"end":92},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T15000","span":{"begin":52,"end":55},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T15099","span":{"begin":614,"end":619},"obj":"http://www.uniprot.org/uniprot/Q12778"},{"id":"T15077","span":{"begin":744,"end":747},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T15076","span":{"begin":456,"end":459},"obj":"http://www.uniprot.org/uniprot/Q9Y243"}],"namespaces":[{"prefix":"_base","uri":"http://www.uniprot.org/uniprot/"}],"text":"RIP1 kinase-dependent Thr308 phosphorylation of Myr-Akt during necroptosis increased Myr-Akt activity as it did with endogenous Akt (Fig. 5). Phosphorylation of many previously described Akt substrates was increased upon the expression of Myr-Akt, but not the K179M mutant, confirming that these molecules are Akt substrates in L929 cells (Fig. 7C). The effect of zVAD.fmk on their phosphorylation varied, likely due to the increased basal activity of Myr-Akt. Some substrates, including p70S6K, S6, GSK-3 and FoxO4, were fully phosphorylated even in the absence of zVAD.fmk. On the other hand, phosphorylation of FoxO1 and MDM2 was significantly increased in the presence of zVAD.fmk, indicating that necroptotic Thr308 phosphorylation of Myr-Akt still promoted its activity."}
GO-BP
{"project":"GO-BP","denotations":[{"id":"T13944","span":{"begin":500,"end":503},"obj":"http://purl.obolibrary.org/obo/GO_0050321"},{"id":"T13931","span":{"begin":721,"end":736},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T13930","span":{"begin":595,"end":610},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T13929","span":{"begin":382,"end":397},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T13900","span":{"begin":63,"end":74},"obj":"http://purl.obolibrary.org/obo/GO_0097528"},{"id":"T13886","span":{"begin":63,"end":74},"obj":"http://purl.obolibrary.org/obo/GO_0070266"}],"text":"RIP1 kinase-dependent Thr308 phosphorylation of Myr-Akt during necroptosis increased Myr-Akt activity as it did with endogenous Akt (Fig. 5). Phosphorylation of many previously described Akt substrates was increased upon the expression of Myr-Akt, but not the K179M mutant, confirming that these molecules are Akt substrates in L929 cells (Fig. 7C). The effect of zVAD.fmk on their phosphorylation varied, likely due to the increased basal activity of Myr-Akt. Some substrates, including p70S6K, S6, GSK-3 and FoxO4, were fully phosphorylated even in the absence of zVAD.fmk. On the other hand, phosphorylation of FoxO1 and MDM2 was significantly increased in the presence of zVAD.fmk, indicating that necroptotic Thr308 phosphorylation of Myr-Akt still promoted its activity."}
GO-MF
{"project":"GO-MF","denotations":[{"id":"T13960","span":{"begin":500,"end":503},"obj":"http://purl.obolibrary.org/obo/GO_0050321"}],"text":"RIP1 kinase-dependent Thr308 phosphorylation of Myr-Akt during necroptosis increased Myr-Akt activity as it did with endogenous Akt (Fig. 5). Phosphorylation of many previously described Akt substrates was increased upon the expression of Myr-Akt, but not the K179M mutant, confirming that these molecules are Akt substrates in L929 cells (Fig. 7C). The effect of zVAD.fmk on their phosphorylation varied, likely due to the increased basal activity of Myr-Akt. Some substrates, including p70S6K, S6, GSK-3 and FoxO4, were fully phosphorylated even in the absence of zVAD.fmk. On the other hand, phosphorylation of FoxO1 and MDM2 was significantly increased in the presence of zVAD.fmk, indicating that necroptotic Thr308 phosphorylation of Myr-Akt still promoted its activity."}
GO-CC
{"project":"GO-CC","denotations":[{"id":"T13967","span":{"begin":333,"end":338},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"RIP1 kinase-dependent Thr308 phosphorylation of Myr-Akt during necroptosis increased Myr-Akt activity as it did with endogenous Akt (Fig. 5). Phosphorylation of many previously described Akt substrates was increased upon the expression of Myr-Akt, but not the K179M mutant, confirming that these molecules are Akt substrates in L929 cells (Fig. 7C). The effect of zVAD.fmk on their phosphorylation varied, likely due to the increased basal activity of Myr-Akt. Some substrates, including p70S6K, S6, GSK-3 and FoxO4, were fully phosphorylated even in the absence of zVAD.fmk. On the other hand, phosphorylation of FoxO1 and MDM2 was significantly increased in the presence of zVAD.fmk, indicating that necroptotic Thr308 phosphorylation of Myr-Akt still promoted its activity."}
sentences
{"project":"sentences","denotations":[{"id":"T13709","span":{"begin":576,"end":776},"obj":"Sentence"},{"id":"T13708","span":{"begin":350,"end":575},"obj":"Sentence"},{"id":"T13707","span":{"begin":142,"end":349},"obj":"Sentence"},{"id":"T193","span":{"begin":0,"end":141},"obj":"Sentence"},{"id":"T194","span":{"begin":142,"end":349},"obj":"Sentence"},{"id":"T195","span":{"begin":350,"end":460},"obj":"Sentence"},{"id":"T196","span":{"begin":461,"end":575},"obj":"Sentence"},{"id":"T197","span":{"begin":576,"end":776},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"RIP1 kinase-dependent Thr308 phosphorylation of Myr-Akt during necroptosis increased Myr-Akt activity as it did with endogenous Akt (Fig. 5). Phosphorylation of many previously described Akt substrates was increased upon the expression of Myr-Akt, but not the K179M mutant, confirming that these molecules are Akt substrates in L929 cells (Fig. 7C). The effect of zVAD.fmk on their phosphorylation varied, likely due to the increased basal activity of Myr-Akt. Some substrates, including p70S6K, S6, GSK-3 and FoxO4, were fully phosphorylated even in the absence of zVAD.fmk. On the other hand, phosphorylation of FoxO1 and MDM2 was significantly increased in the presence of zVAD.fmk, indicating that necroptotic Thr308 phosphorylation of Myr-Akt still promoted its activity."}
simple1
{"project":"simple1","denotations":[{"id":"T14041","span":{"begin":614,"end":619},"obj":"Protein"},{"id":"T14040","span":{"begin":510,"end":515},"obj":"Protein"},{"id":"T14039","span":{"begin":496,"end":498},"obj":"Protein"},{"id":"T14038","span":{"begin":488,"end":494},"obj":"Protein"},{"id":"T14037","span":{"begin":452,"end":459},"obj":"Protein"},{"id":"T14036","span":{"begin":260,"end":265},"obj":"Protein"},{"id":"T14035","span":{"begin":239,"end":246},"obj":"Protein"},{"id":"T14034","span":{"begin":85,"end":92},"obj":"Protein"},{"id":"T14033","span":{"begin":48,"end":55},"obj":"Protein"},{"id":"T14043","span":{"begin":740,"end":747},"obj":"Protein"},{"id":"T14042","span":{"begin":624,"end":628},"obj":"Protein"}],"text":"RIP1 kinase-dependent Thr308 phosphorylation of Myr-Akt during necroptosis increased Myr-Akt activity as it did with endogenous Akt (Fig. 5). Phosphorylation of many previously described Akt substrates was increased upon the expression of Myr-Akt, but not the K179M mutant, confirming that these molecules are Akt substrates in L929 cells (Fig. 7C). The effect of zVAD.fmk on their phosphorylation varied, likely due to the increased basal activity of Myr-Akt. Some substrates, including p70S6K, S6, GSK-3 and FoxO4, were fully phosphorylated even in the absence of zVAD.fmk. On the other hand, phosphorylation of FoxO1 and MDM2 was significantly increased in the presence of zVAD.fmk, indicating that necroptotic Thr308 phosphorylation of Myr-Akt still promoted its activity."}
BioNLP16_DUT
{"project":"BioNLP16_DUT","denotations":[{"id":"T14970","span":{"begin":721,"end":736},"obj":"Phosphorylation"},{"id":"T14969","span":{"begin":595,"end":610},"obj":"Phosphorylation"},{"id":"T14968","span":{"begin":647,"end":656},"obj":"Positive_regulation"},{"id":"T14967","span":{"begin":528,"end":542},"obj":"Phosphorylation"},{"id":"T14966","span":{"begin":424,"end":433},"obj":"Positive_regulation"},{"id":"T14965","span":{"begin":206,"end":215},"obj":"Positive_regulation"},{"id":"T14964","span":{"begin":225,"end":235},"obj":"Gene_expression"},{"id":"T14961","span":{"begin":75,"end":84},"obj":"Positive_regulation"},{"id":"T14939","span":{"begin":740,"end":747},"obj":"Protein"},{"id":"T14938","span":{"begin":624,"end":628},"obj":"Protein"},{"id":"T14937","span":{"begin":614,"end":619},"obj":"Protein"},{"id":"T14936","span":{"begin":510,"end":515},"obj":"Protein"},{"id":"T14935","span":{"begin":496,"end":498},"obj":"Protein"},{"id":"T14934","span":{"begin":488,"end":494},"obj":"Protein"},{"id":"T14933","span":{"begin":452,"end":459},"obj":"Protein"},{"id":"T14932","span":{"begin":260,"end":265},"obj":"Protein"},{"id":"T14931","span":{"begin":239,"end":246},"obj":"Protein"},{"id":"T14930","span":{"begin":85,"end":92},"obj":"Protein"},{"id":"T14929","span":{"begin":48,"end":55},"obj":"Protein"}],"relations":[{"id":"R9919","pred":"themeOf","subj":"T14930","obj":"T14961"},{"id":"R9920","pred":"themeOf","subj":"T14931","obj":"T14964"},{"id":"R9921","pred":"themeOf","subj":"T14932","obj":"T14964"},{"id":"R9922","pred":"themeOf","subj":"T14933","obj":"T14966"},{"id":"R9923","pred":"themeOf","subj":"T14934","obj":"T14967"},{"id":"R9924","pred":"themeOf","subj":"T14935","obj":"T14967"},{"id":"R9925","pred":"themeOf","subj":"T14936","obj":"T14967"},{"id":"R9926","pred":"themeOf","subj":"T14937","obj":"T14969"},{"id":"R9927","pred":"themeOf","subj":"T14938","obj":"T14969"},{"id":"R9928","pred":"themeOf","subj":"T14939","obj":"T14970"},{"id":"R9943","pred":"themeOf","subj":"T14964","obj":"T14965"},{"id":"R9944","pred":"themeOf","subj":"T14964","obj":"T14965"},{"id":"R9945","pred":"themeOf","subj":"T14969","obj":"T14968"},{"id":"R9946","pred":"themeOf","subj":"T14969","obj":"T14968"}],"text":"RIP1 kinase-dependent Thr308 phosphorylation of Myr-Akt during necroptosis increased Myr-Akt activity as it did with endogenous Akt (Fig. 5). Phosphorylation of many previously described Akt substrates was increased upon the expression of Myr-Akt, but not the K179M mutant, confirming that these molecules are Akt substrates in L929 cells (Fig. 7C). The effect of zVAD.fmk on their phosphorylation varied, likely due to the increased basal activity of Myr-Akt. Some substrates, including p70S6K, S6, GSK-3 and FoxO4, were fully phosphorylated even in the absence of zVAD.fmk. On the other hand, phosphorylation of FoxO1 and MDM2 was significantly increased in the presence of zVAD.fmk, indicating that necroptotic Thr308 phosphorylation of Myr-Akt still promoted its activity."}
BioNLP16_Messiy
{"project":"BioNLP16_Messiy","denotations":[{"id":"T15283","span":{"begin":647,"end":656},"obj":"Positive_regulation"},{"id":"T15282","span":{"begin":595,"end":610},"obj":"Phosphorylation"},{"id":"T15281","span":{"begin":721,"end":736},"obj":"Phosphorylation"},{"id":"T15280","span":{"begin":528,"end":542},"obj":"Phosphorylation"},{"id":"T15279","span":{"begin":225,"end":235},"obj":"Gene_expression"},{"id":"T15278","span":{"begin":206,"end":215},"obj":"Positive_regulation"},{"id":"T15276","span":{"begin":75,"end":84},"obj":"Positive_regulation"},{"id":"T15246","span":{"begin":260,"end":265},"obj":"Protein"},{"id":"T15245","span":{"begin":239,"end":246},"obj":"Protein"},{"id":"T15244","span":{"begin":85,"end":92},"obj":"Protein"},{"id":"T15243","span":{"begin":48,"end":55},"obj":"Protein"},{"id":"T15253","span":{"begin":740,"end":747},"obj":"Protein"},{"id":"T15252","span":{"begin":624,"end":628},"obj":"Protein"},{"id":"T15251","span":{"begin":614,"end":619},"obj":"Protein"},{"id":"T15250","span":{"begin":510,"end":515},"obj":"Protein"},{"id":"T15249","span":{"begin":496,"end":498},"obj":"Protein"},{"id":"T15248","span":{"begin":488,"end":494},"obj":"Protein"},{"id":"T15247","span":{"begin":452,"end":459},"obj":"Protein"}],"relations":[{"id":"R10017","pred":"themeOf","subj":"T15245","obj":"T15279"},{"id":"R10018","pred":"themeOf","subj":"T15248","obj":"T15280"},{"id":"R10019","pred":"themeOf","subj":"T15249","obj":"T15280"},{"id":"R10020","pred":"themeOf","subj":"T15250","obj":"T15280"},{"id":"R10021","pred":"themeOf","subj":"T15251","obj":"T15282"},{"id":"R10022","pred":"themeOf","subj":"T15252","obj":"T15282"},{"id":"R10023","pred":"themeOf","subj":"T15253","obj":"T15281"},{"id":"R10037","pred":"themeOf","subj":"T15279","obj":"T15278"},{"id":"R10038","pred":"themeOf","subj":"T15282","obj":"T15283"},{"id":"R10039","pred":"themeOf","subj":"T15282","obj":"T15283"}],"text":"RIP1 kinase-dependent Thr308 phosphorylation of Myr-Akt during necroptosis increased Myr-Akt activity as it did with endogenous Akt (Fig. 5). Phosphorylation of many previously described Akt substrates was increased upon the expression of Myr-Akt, but not the K179M mutant, confirming that these molecules are Akt substrates in L929 cells (Fig. 7C). The effect of zVAD.fmk on their phosphorylation varied, likely due to the increased basal activity of Myr-Akt. Some substrates, including p70S6K, S6, GSK-3 and FoxO4, were fully phosphorylated even in the absence of zVAD.fmk. On the other hand, phosphorylation of FoxO1 and MDM2 was significantly increased in the presence of zVAD.fmk, indicating that necroptotic Thr308 phosphorylation of Myr-Akt still promoted its activity."}
DLUT931
{"project":"DLUT931","denotations":[{"id":"T15157","span":{"begin":721,"end":736},"obj":"Phosphorylation"},{"id":"T15156","span":{"begin":647,"end":656},"obj":"Positive_regulation"},{"id":"T15155","span":{"begin":595,"end":610},"obj":"Phosphorylation"},{"id":"T15154","span":{"begin":528,"end":542},"obj":"Phosphorylation"},{"id":"T15153","span":{"begin":424,"end":433},"obj":"Positive_regulation"},{"id":"T15152","span":{"begin":206,"end":215},"obj":"Positive_regulation"},{"id":"T15151","span":{"begin":225,"end":235},"obj":"Gene_expression"},{"id":"T15126","span":{"begin":740,"end":747},"obj":"Protein"},{"id":"T15125","span":{"begin":624,"end":628},"obj":"Protein"},{"id":"T15124","span":{"begin":614,"end":619},"obj":"Protein"},{"id":"T15123","span":{"begin":510,"end":515},"obj":"Protein"},{"id":"T15122","span":{"begin":496,"end":498},"obj":"Protein"},{"id":"T15121","span":{"begin":488,"end":494},"obj":"Protein"},{"id":"T15120","span":{"begin":452,"end":459},"obj":"Protein"},{"id":"T15119","span":{"begin":260,"end":265},"obj":"Protein"},{"id":"T15118","span":{"begin":239,"end":246},"obj":"Protein"},{"id":"T15117","span":{"begin":85,"end":92},"obj":"Protein"},{"id":"T15116","span":{"begin":48,"end":55},"obj":"Protein"}],"relations":[{"id":"R9957","pred":"themeOf","subj":"T15118","obj":"T15151"},{"id":"R9958","pred":"themeOf","subj":"T15119","obj":"T15151"},{"id":"R9959","pred":"themeOf","subj":"T15120","obj":"T15153"},{"id":"R9960","pred":"themeOf","subj":"T15121","obj":"T15154"},{"id":"R9961","pred":"themeOf","subj":"T15122","obj":"T15154"},{"id":"R9962","pred":"themeOf","subj":"T15123","obj":"T15154"},{"id":"R9963","pred":"themeOf","subj":"T15124","obj":"T15155"},{"id":"R9964","pred":"themeOf","subj":"T15125","obj":"T15155"},{"id":"R9965","pred":"themeOf","subj":"T15126","obj":"T15157"},{"id":"R9987","pred":"themeOf","subj":"T15151","obj":"T15152"},{"id":"R9988","pred":"themeOf","subj":"T15151","obj":"T15152"},{"id":"R9989","pred":"themeOf","subj":"T15155","obj":"T15156"},{"id":"R9990","pred":"themeOf","subj":"T15155","obj":"T15156"}],"text":"RIP1 kinase-dependent Thr308 phosphorylation of Myr-Akt during necroptosis increased Myr-Akt activity as it did with endogenous Akt (Fig. 5). Phosphorylation of many previously described Akt substrates was increased upon the expression of Myr-Akt, but not the K179M mutant, confirming that these molecules are Akt substrates in L929 cells (Fig. 7C). The effect of zVAD.fmk on their phosphorylation varied, likely due to the increased basal activity of Myr-Akt. Some substrates, including p70S6K, S6, GSK-3 and FoxO4, were fully phosphorylated even in the absence of zVAD.fmk. On the other hand, phosphorylation of FoxO1 and MDM2 was significantly increased in the presence of zVAD.fmk, indicating that necroptotic Thr308 phosphorylation of Myr-Akt still promoted its activity."}
bionlp-st-ge-2016-test-ihmc
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bionlp-st-ge-2016-spacy-parsed
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Phosphorylation of many previously described Akt substrates was increased upon the expression of Myr-Akt, but not the K179M mutant, confirming that these molecules are Akt substrates in L929 cells (Fig. 7C). The effect of zVAD.fmk on their phosphorylation varied, likely due to the increased basal activity of Myr-Akt. Some substrates, including p70S6K, S6, GSK-3 and FoxO4, were fully phosphorylated even in the absence of zVAD.fmk. On the other hand, phosphorylation of FoxO1 and MDM2 was significantly increased in the presence of zVAD.fmk, indicating that necroptotic Thr308 phosphorylation of Myr-Akt still promoted its activity."}
bionlp-st-ge-2016-test-tees
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test3
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