PMC:3585731 / 39990-41605 JSON TXT

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testone

2_test

{"project":"2_test","denotations":[{"id":"23469174-22037377-90505457","span":{"begin":105,"end":107},"obj":"22037377"},{"id":"23469174-20539307-90505458","span":{"begin":688,"end":690},"obj":"20539307"},{"id":"23469174-15131264-90505459","span":{"begin":694,"end":696},"obj":"15131264"},{"id":"23469174-22695613-90505460","span":{"begin":700,"end":702},"obj":"22695613"},{"id":"23469174-19118012-90505461","span":{"begin":1480,"end":1482},"obj":"19118012"}],"text":"Therefore, to examine the role of JNK, we switched to a more specific JNK inhibitor, JNK inhibitor VIII [43], and siRNAs against JNK1 and JNK2 (Fig. S10B–G). As expected, specific inhibition or knockdown of JNK1/2 allowed phosphorylation of Akt on Thr308 while inhibiting the phosphorylation of c-Jun at Ser63 (Fig. S10B,E), agreeing with our model. It did not, however, lead to a reduction in TNFα production or cell death (Fig. S10C,D,F,G), suggesting that earlier data with SP600125 protection (Fig. 2) could reflect off-target effects of this molecule, rather than JNK inhibition. Previous reports also suggested a critical role for c-Jun in necroptosis and autocrine TNFα synthesis [13], [14], [15] and we confirmed these conclusions using c-Jun siRNA knockdown (Fig. S10H–J). Notably, in this case, Thr308 phosphorylation was reduced after the induction of necroptosis. Thus, autocrine TNFα production, dependent on c-Jun, may create a feedback loop that contributes to the delayed activation of Akt. It is also important to note that we observed an overall increase in the protein level of c-Jun after treatment of L929 cells with zVAD.fmk or TNFα, which was both Akt and mTOR-dependent (Fig. 6E,F). These new data led us to an unexpected, but important conclusion that c-Jun is critical for necroptosis, while JNK activity may serve as a useful marker of pathway activation, but may be either redundant (e.g. phosphorylation of c-Jun on a site other than Ser63 may occur [44]) or dispensable functionally. In addition, researchers need to use caution when using SP600125 due to potantial off-target effects."}

pmc-enju-pas

bionlp-st-ge-2016-coref

{"project":"bionlp-st-ge-2016-coref","denotations":[{"id":"T18387","span":{"begin":1064,"end":1072},"obj":"Antecedent"},{"id":"T18386","span":{"begin":1156,"end":1161},"obj":"Anaphor"}],"relations":[{"id":"R12163","pred":"boundBy","subj":"T18386","obj":"T18387"}],"namespaces":[{"prefix":"_base","uri":"https://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"Therefore, to examine the role of JNK, we switched to a more specific JNK inhibitor, JNK inhibitor VIII [43], and siRNAs against JNK1 and JNK2 (Fig. S10B–G). As expected, specific inhibition or knockdown of JNK1/2 allowed phosphorylation of Akt on Thr308 while inhibiting the phosphorylation of c-Jun at Ser63 (Fig. S10B,E), agreeing with our model. It did not, however, lead to a reduction in TNFα production or cell death (Fig. S10C,D,F,G), suggesting that earlier data with SP600125 protection (Fig. 2) could reflect off-target effects of this molecule, rather than JNK inhibition. Previous reports also suggested a critical role for c-Jun in necroptosis and autocrine TNFα synthesis [13], [14], [15] and we confirmed these conclusions using c-Jun siRNA knockdown (Fig. S10H–J). Notably, in this case, Thr308 phosphorylation was reduced after the induction of necroptosis. Thus, autocrine TNFα production, dependent on c-Jun, may create a feedback loop that contributes to the delayed activation of Akt. It is also important to note that we observed an overall increase in the protein level of c-Jun after treatment of L929 cells with zVAD.fmk or TNFα, which was both Akt and mTOR-dependent (Fig. 6E,F). These new data led us to an unexpected, but important conclusion that c-Jun is critical for necroptosis, while JNK activity may serve as a useful marker of pathway activation, but may be either redundant (e.g. phosphorylation of c-Jun on a site other than Ser63 may occur [44]) or dispensable functionally. In addition, researchers need to use caution when using SP600125 due to potantial off-target effects."}

bionlp-st-ge-2016-test-proteins

{"project":"bionlp-st-ge-2016-test-proteins","denotations":[{"id":"T18413","span":{"begin":1436,"end":1441},"obj":"Protein"},{"id":"T18412","span":{"begin":1277,"end":1282},"obj":"Protein"},{"id":"T18411","span":{"begin":1150,"end":1154},"obj":"Protein"},{"id":"T18410","span":{"begin":1097,"end":1102},"obj":"Protein"},{"id":"T18409","span":{"begin":922,"end":927},"obj":"Protein"},{"id":"T18408","span":{"begin":892,"end":896},"obj":"Protein"},{"id":"T18407","span":{"begin":745,"end":750},"obj":"Protein"},{"id":"T18406","span":{"begin":672,"end":676},"obj":"Protein"},{"id":"T18405","span":{"begin":637,"end":642},"obj":"Protein"},{"id":"T18404","span":{"begin":394,"end":398},"obj":"Protein"},{"id":"T18403","span":{"begin":295,"end":300},"obj":"Protein"},{"id":"T18402","span":{"begin":212,"end":213},"obj":"Protein"},{"id":"T18401","span":{"begin":207,"end":211},"obj":"Protein"},{"id":"T18400","span":{"begin":138,"end":142},"obj":"Protein"},{"id":"T18399","span":{"begin":129,"end":133},"obj":"Protein"}],"namespaces":[{"prefix":"_base","uri":"http://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"Therefore, to examine the role of JNK, we switched to a more specific JNK inhibitor, JNK inhibitor VIII [43], and siRNAs against JNK1 and JNK2 (Fig. S10B–G). As expected, specific inhibition or knockdown of JNK1/2 allowed phosphorylation of Akt on Thr308 while inhibiting the phosphorylation of c-Jun at Ser63 (Fig. S10B,E), agreeing with our model. It did not, however, lead to a reduction in TNFα production or cell death (Fig. S10C,D,F,G), suggesting that earlier data with SP600125 protection (Fig. 2) could reflect off-target effects of this molecule, rather than JNK inhibition. Previous reports also suggested a critical role for c-Jun in necroptosis and autocrine TNFα synthesis [13], [14], [15] and we confirmed these conclusions using c-Jun siRNA knockdown (Fig. S10H–J). Notably, in this case, Thr308 phosphorylation was reduced after the induction of necroptosis. Thus, autocrine TNFα production, dependent on c-Jun, may create a feedback loop that contributes to the delayed activation of Akt. It is also important to note that we observed an overall increase in the protein level of c-Jun after treatment of L929 cells with zVAD.fmk or TNFα, which was both Akt and mTOR-dependent (Fig. 6E,F). These new data led us to an unexpected, but important conclusion that c-Jun is critical for necroptosis, while JNK activity may serve as a useful marker of pathway activation, but may be either redundant (e.g. phosphorylation of c-Jun on a site other than Ser63 may occur [44]) or dispensable functionally. In addition, researchers need to use caution when using SP600125 due to potantial off-target effects."}

bionlp-st-ge-2016-uniprot

{"project":"bionlp-st-ge-2016-uniprot","denotations":[{"id":"T19398","span":{"begin":1179,"end":1183},"obj":"http://www.uniprot.org/uniprot/P42345"},{"id":"T19397","span":{"begin":1436,"end":1441},"obj":"http://www.uniprot.org/uniprot/P05412"},{"id":"T19396","span":{"begin":1277,"end":1282},"obj":"http://www.uniprot.org/uniprot/P05412"},{"id":"T19395","span":{"begin":1097,"end":1102},"obj":"http://www.uniprot.org/uniprot/P05412"},{"id":"T19394","span":{"begin":922,"end":927},"obj":"http://www.uniprot.org/uniprot/P05412"},{"id":"T19393","span":{"begin":745,"end":750},"obj":"http://www.uniprot.org/uniprot/P05412"},{"id":"T19392","span":{"begin":637,"end":642},"obj":"http://www.uniprot.org/uniprot/P05412"},{"id":"T19391","span":{"begin":295,"end":300},"obj":"http://www.uniprot.org/uniprot/P05412"},{"id":"T19390","span":{"begin":1150,"end":1154},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T19389","span":{"begin":892,"end":896},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T19388","span":{"begin":672,"end":676},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T19387","span":{"begin":394,"end":398},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T19384","span":{"begin":1171,"end":1174},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T19383","span":{"begin":1002,"end":1005},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T19382","span":{"begin":241,"end":244},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T19362","span":{"begin":1171,"end":1174},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T19361","span":{"begin":1002,"end":1005},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T19340","span":{"begin":1171,"end":1174},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T19339","span":{"begin":1002,"end":1005},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T19338","span":{"begin":241,"end":244},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T19360","span":{"begin":241,"end":244},"obj":"http://www.uniprot.org/uniprot/P31751"}],"namespaces":[{"prefix":"_base","uri":"http://www.uniprot.org/uniprot/"}],"text":"Therefore, to examine the role of JNK, we switched to a more specific JNK inhibitor, JNK inhibitor VIII [43], and siRNAs against JNK1 and JNK2 (Fig. S10B–G). As expected, specific inhibition or knockdown of JNK1/2 allowed phosphorylation of Akt on Thr308 while inhibiting the phosphorylation of c-Jun at Ser63 (Fig. S10B,E), agreeing with our model. It did not, however, lead to a reduction in TNFα production or cell death (Fig. S10C,D,F,G), suggesting that earlier data with SP600125 protection (Fig. 2) could reflect off-target effects of this molecule, rather than JNK inhibition. Previous reports also suggested a critical role for c-Jun in necroptosis and autocrine TNFα synthesis [13], [14], [15] and we confirmed these conclusions using c-Jun siRNA knockdown (Fig. S10H–J). Notably, in this case, Thr308 phosphorylation was reduced after the induction of necroptosis. Thus, autocrine TNFα production, dependent on c-Jun, may create a feedback loop that contributes to the delayed activation of Akt. It is also important to note that we observed an overall increase in the protein level of c-Jun after treatment of L929 cells with zVAD.fmk or TNFα, which was both Akt and mTOR-dependent (Fig. 6E,F). These new data led us to an unexpected, but important conclusion that c-Jun is critical for necroptosis, while JNK activity may serve as a useful marker of pathway activation, but may be either redundant (e.g. phosphorylation of c-Jun on a site other than Ser63 may occur [44]) or dispensable functionally. In addition, researchers need to use caution when using SP600125 due to potantial off-target effects."}

GO-BP

{"project":"GO-BP","denotations":[{"id":"T18468","span":{"begin":677,"end":686},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T18466","span":{"begin":418,"end":423},"obj":"http://purl.obolibrary.org/obo/GO_0016265"},{"id":"T18462","span":{"begin":413,"end":423},"obj":"http://purl.obolibrary.org/obo/GO_0008219"},{"id":"T18453","span":{"begin":1417,"end":1432},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T18452","span":{"begin":812,"end":827},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T18451","span":{"begin":276,"end":291},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T18450","span":{"begin":222,"end":237},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T18442","span":{"begin":1299,"end":1310},"obj":"http://purl.obolibrary.org/obo/GO_0097528"},{"id":"T18441","span":{"begin":863,"end":874},"obj":"http://purl.obolibrary.org/obo/GO_0097528"},{"id":"T18440","span":{"begin":646,"end":657},"obj":"http://purl.obolibrary.org/obo/GO_0097528"},{"id":"T18434","span":{"begin":850,"end":874},"obj":"http://purl.obolibrary.org/obo/GO_0070266"},{"id":"T18432","span":{"begin":863,"end":874},"obj":"http://purl.obolibrary.org/obo/GO_0070266"},{"id":"T18431","span":{"begin":646,"end":657},"obj":"http://purl.obolibrary.org/obo/GO_0070266"},{"id":"T18421","span":{"begin":1318,"end":1321},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T18420","span":{"begin":569,"end":572},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T18419","span":{"begin":85,"end":88},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T18418","span":{"begin":70,"end":73},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T18417","span":{"begin":34,"end":37},"obj":"http://purl.obolibrary.org/obo/GO_0004705"}],"text":"Therefore, to examine the role of JNK, we switched to a more specific JNK inhibitor, JNK inhibitor VIII [43], and siRNAs against JNK1 and JNK2 (Fig. S10B–G). As expected, specific inhibition or knockdown of JNK1/2 allowed phosphorylation of Akt on Thr308 while inhibiting the phosphorylation of c-Jun at Ser63 (Fig. S10B,E), agreeing with our model. It did not, however, lead to a reduction in TNFα production or cell death (Fig. S10C,D,F,G), suggesting that earlier data with SP600125 protection (Fig. 2) could reflect off-target effects of this molecule, rather than JNK inhibition. Previous reports also suggested a critical role for c-Jun in necroptosis and autocrine TNFα synthesis [13], [14], [15] and we confirmed these conclusions using c-Jun siRNA knockdown (Fig. S10H–J). Notably, in this case, Thr308 phosphorylation was reduced after the induction of necroptosis. Thus, autocrine TNFα production, dependent on c-Jun, may create a feedback loop that contributes to the delayed activation of Akt. It is also important to note that we observed an overall increase in the protein level of c-Jun after treatment of L929 cells with zVAD.fmk or TNFα, which was both Akt and mTOR-dependent (Fig. 6E,F). These new data led us to an unexpected, but important conclusion that c-Jun is critical for necroptosis, while JNK activity may serve as a useful marker of pathway activation, but may be either redundant (e.g. phosphorylation of c-Jun on a site other than Ser63 may occur [44]) or dispensable functionally. In addition, researchers need to use caution when using SP600125 due to potantial off-target effects."}

GO-MF

{"project":"GO-MF","denotations":[{"id":"T18478","span":{"begin":1318,"end":1321},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T18477","span":{"begin":569,"end":572},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T18476","span":{"begin":85,"end":88},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T18475","span":{"begin":70,"end":73},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T18474","span":{"begin":34,"end":37},"obj":"http://purl.obolibrary.org/obo/GO_0004705"}],"text":"Therefore, to examine the role of JNK, we switched to a more specific JNK inhibitor, JNK inhibitor VIII [43], and siRNAs against JNK1 and JNK2 (Fig. S10B–G). As expected, specific inhibition or knockdown of JNK1/2 allowed phosphorylation of Akt on Thr308 while inhibiting the phosphorylation of c-Jun at Ser63 (Fig. S10B,E), agreeing with our model. It did not, however, lead to a reduction in TNFα production or cell death (Fig. S10C,D,F,G), suggesting that earlier data with SP600125 protection (Fig. 2) could reflect off-target effects of this molecule, rather than JNK inhibition. Previous reports also suggested a critical role for c-Jun in necroptosis and autocrine TNFα synthesis [13], [14], [15] and we confirmed these conclusions using c-Jun siRNA knockdown (Fig. S10H–J). Notably, in this case, Thr308 phosphorylation was reduced after the induction of necroptosis. Thus, autocrine TNFα production, dependent on c-Jun, may create a feedback loop that contributes to the delayed activation of Akt. It is also important to note that we observed an overall increase in the protein level of c-Jun after treatment of L929 cells with zVAD.fmk or TNFα, which was both Akt and mTOR-dependent (Fig. 6E,F). These new data led us to an unexpected, but important conclusion that c-Jun is critical for necroptosis, while JNK activity may serve as a useful marker of pathway activation, but may be either redundant (e.g. phosphorylation of c-Jun on a site other than Ser63 may occur [44]) or dispensable functionally. In addition, researchers need to use caution when using SP600125 due to potantial off-target effects."}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T18486","span":{"begin":1127,"end":1132},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Therefore, to examine the role of JNK, we switched to a more specific JNK inhibitor, JNK inhibitor VIII [43], and siRNAs against JNK1 and JNK2 (Fig. S10B–G). As expected, specific inhibition or knockdown of JNK1/2 allowed phosphorylation of Akt on Thr308 while inhibiting the phosphorylation of c-Jun at Ser63 (Fig. S10B,E), agreeing with our model. It did not, however, lead to a reduction in TNFα production or cell death (Fig. S10C,D,F,G), suggesting that earlier data with SP600125 protection (Fig. 2) could reflect off-target effects of this molecule, rather than JNK inhibition. Previous reports also suggested a critical role for c-Jun in necroptosis and autocrine TNFα synthesis [13], [14], [15] and we confirmed these conclusions using c-Jun siRNA knockdown (Fig. S10H–J). Notably, in this case, Thr308 phosphorylation was reduced after the induction of necroptosis. Thus, autocrine TNFα production, dependent on c-Jun, may create a feedback loop that contributes to the delayed activation of Akt. It is also important to note that we observed an overall increase in the protein level of c-Jun after treatment of L929 cells with zVAD.fmk or TNFα, which was both Akt and mTOR-dependent (Fig. 6E,F). These new data led us to an unexpected, but important conclusion that c-Jun is critical for necroptosis, while JNK activity may serve as a useful marker of pathway activation, but may be either redundant (e.g. phosphorylation of c-Jun on a site other than Ser63 may occur [44]) or dispensable functionally. In addition, researchers need to use caution when using SP600125 due to potantial off-target effects."}

sentences

{"project":"sentences","denotations":[{"id":"T18334","span":{"begin":1514,"end":1615},"obj":"Sentence"},{"id":"T18333","span":{"begin":1207,"end":1513},"obj":"Sentence"},{"id":"T18332","span":{"begin":876,"end":1206},"obj":"Sentence"},{"id":"T18331","span":{"begin":782,"end":875},"obj":"Sentence"},{"id":"T18330","span":{"begin":585,"end":781},"obj":"Sentence"},{"id":"T18329","span":{"begin":350,"end":584},"obj":"Sentence"},{"id":"T18328","span":{"begin":158,"end":349},"obj":"Sentence"},{"id":"T18327","span":{"begin":0,"end":157},"obj":"Sentence"},{"id":"T248","span":{"begin":0,"end":157},"obj":"Sentence"},{"id":"T249","span":{"begin":158,"end":349},"obj":"Sentence"},{"id":"T250","span":{"begin":350,"end":584},"obj":"Sentence"},{"id":"T251","span":{"begin":585,"end":781},"obj":"Sentence"},{"id":"T252","span":{"begin":782,"end":875},"obj":"Sentence"},{"id":"T253","span":{"begin":876,"end":1006},"obj":"Sentence"},{"id":"T254","span":{"begin":1007,"end":1206},"obj":"Sentence"},{"id":"T255","span":{"begin":1207,"end":1513},"obj":"Sentence"},{"id":"T256","span":{"begin":1514,"end":1615},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Therefore, to examine the role of JNK, we switched to a more specific JNK inhibitor, JNK inhibitor VIII [43], and siRNAs against JNK1 and JNK2 (Fig. S10B–G). As expected, specific inhibition or knockdown of JNK1/2 allowed phosphorylation of Akt on Thr308 while inhibiting the phosphorylation of c-Jun at Ser63 (Fig. S10B,E), agreeing with our model. It did not, however, lead to a reduction in TNFα production or cell death (Fig. S10C,D,F,G), suggesting that earlier data with SP600125 protection (Fig. 2) could reflect off-target effects of this molecule, rather than JNK inhibition. Previous reports also suggested a critical role for c-Jun in necroptosis and autocrine TNFα synthesis [13], [14], [15] and we confirmed these conclusions using c-Jun siRNA knockdown (Fig. S10H–J). Notably, in this case, Thr308 phosphorylation was reduced after the induction of necroptosis. Thus, autocrine TNFα production, dependent on c-Jun, may create a feedback loop that contributes to the delayed activation of Akt. It is also important to note that we observed an overall increase in the protein level of c-Jun after treatment of L929 cells with zVAD.fmk or TNFα, which was both Akt and mTOR-dependent (Fig. 6E,F). These new data led us to an unexpected, but important conclusion that c-Jun is critical for necroptosis, while JNK activity may serve as a useful marker of pathway activation, but may be either redundant (e.g. phosphorylation of c-Jun on a site other than Ser63 may occur [44]) or dispensable functionally. In addition, researchers need to use caution when using SP600125 due to potantial off-target effects."}

simple1

{"project":"simple1","denotations":[{"id":"T18516","span":{"begin":1436,"end":1441},"obj":"Protein"},{"id":"T18515","span":{"begin":1277,"end":1282},"obj":"Protein"},{"id":"T18514","span":{"begin":1150,"end":1154},"obj":"Protein"},{"id":"T18513","span":{"begin":1097,"end":1102},"obj":"Protein"},{"id":"T18512","span":{"begin":922,"end":927},"obj":"Protein"},{"id":"T18511","span":{"begin":892,"end":896},"obj":"Protein"},{"id":"T18510","span":{"begin":745,"end":750},"obj":"Protein"},{"id":"T18509","span":{"begin":672,"end":676},"obj":"Protein"},{"id":"T18508","span":{"begin":637,"end":642},"obj":"Protein"},{"id":"T18507","span":{"begin":394,"end":398},"obj":"Protein"},{"id":"T18506","span":{"begin":295,"end":300},"obj":"Protein"},{"id":"T18505","span":{"begin":212,"end":213},"obj":"Protein"},{"id":"T18504","span":{"begin":207,"end":211},"obj":"Protein"},{"id":"T18503","span":{"begin":138,"end":142},"obj":"Protein"},{"id":"T18502","span":{"begin":129,"end":133},"obj":"Protein"}],"text":"Therefore, to examine the role of JNK, we switched to a more specific JNK inhibitor, JNK inhibitor VIII [43], and siRNAs against JNK1 and JNK2 (Fig. S10B–G). As expected, specific inhibition or knockdown of JNK1/2 allowed phosphorylation of Akt on Thr308 while inhibiting the phosphorylation of c-Jun at Ser63 (Fig. S10B,E), agreeing with our model. It did not, however, lead to a reduction in TNFα production or cell death (Fig. S10C,D,F,G), suggesting that earlier data with SP600125 protection (Fig. 2) could reflect off-target effects of this molecule, rather than JNK inhibition. Previous reports also suggested a critical role for c-Jun in necroptosis and autocrine TNFα synthesis [13], [14], [15] and we confirmed these conclusions using c-Jun siRNA knockdown (Fig. S10H–J). Notably, in this case, Thr308 phosphorylation was reduced after the induction of necroptosis. Thus, autocrine TNFα production, dependent on c-Jun, may create a feedback loop that contributes to the delayed activation of Akt. It is also important to note that we observed an overall increase in the protein level of c-Jun after treatment of L929 cells with zVAD.fmk or TNFα, which was both Akt and mTOR-dependent (Fig. 6E,F). These new data led us to an unexpected, but important conclusion that c-Jun is critical for necroptosis, while JNK activity may serve as a useful marker of pathway activation, but may be either redundant (e.g. phosphorylation of c-Jun on a site other than Ser63 may occur [44]) or dispensable functionally. In addition, researchers need to use caution when using SP600125 due to potantial off-target effects."}

BioNLP16_DUT

BioNLP16_Messiy

DLUT931

bionlp-st-ge-2016-test-ihmc

bionlp-st-ge-2016-spacy-parsed

bionlp-st-ge-2016-test-tees

test3

PMC:3585731 / 39990-41605 JSONTXT

Annnotations TAB JSON ListView MergeView

PMC:3585731 / 39990-41605 JSON TXT