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CYLD has been shown to negatively regulate RANK signalling and osteoclastogenesis in mice [65]. Mice with a genetic deficiency of CYLD have aberrant osteoclast differentiation and develop severe osteoporosis. Osteoclast precursors of these mice are hyper-responsive to RANKL-induced differentiation and produce more and larger osteoclasts. CYLD expression is markedly upregulated under conditions of RANKL-induced osteoclastogenesis and is recruited to ubiquitinated TRAF6 via the ubiquitin-binding adaptor protein p62 (also known as sequestosome 1) [65], followed by the CYLD-mediated deubiquitination of TRAF6. In this context, it is worth mentioning that transgenic mice expressing a mutated form of p62 also display abnormal osteoclastogenesis and develop progressive bone loss [66]. These findings suggest that CYLD-mediated inhibi-tion of RANK-induced NF-κB signalling plays a key role in the negative regulation of osteoclastogenesis and indicate CYLD as a potential genetic factor involved in the pathology of bone disorders such as RA."}

{"project":"GO-BP","denotations":[{"id":"T14593","span":{"begin":923,"end":933},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T14592","span":{"begin":601,"end":617},"obj":"http://purl.obolibrary.org/obo/GO_0016579"},{"id":"T14591","span":{"begin":164,"end":190},"obj":"http://purl.obolibrary.org/obo/GO_0030316"},{"id":"T14589","span":{"begin":879,"end":889},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T14588","span":{"begin":63,"end":73},"obj":"http://purl.obolibrary.org/obo/GO_0023052"}],"text":"Interestingly, CYLD has been shown to negatively regulate RANK signalling and osteoclastogenesis in mice [65]. Mice with a genetic deficiency of CYLD have aberrant osteoclast differentiation and develop severe osteoporosis. Osteoclast precursors of these mice are hyper-responsive to RANKL-induced differentiation and produce more and larger osteoclasts. CYLD expression is markedly upregulated under conditions of RANKL-induced osteoclastogenesis and is recruited to ubiquitinated TRAF6 via the ubiquitin-binding adaptor protein p62 (also known as sequestosome 1) [65], followed by the CYLD-mediated deubiquitination of TRAF6. In this context, it is worth mentioning that transgenic mice expressing a mutated form of p62 also display abnormal osteoclastogenesis and develop progressive bone loss [66]. These findings suggest that CYLD-mediated inhibi-tion of RANK-induced NF-κB signalling plays a key role in the negative regulation of osteoclastogenesis and indicate CYLD as a potential genetic factor involved in the pathology of bone disorders such as RA."}

{"project":"GO-MF","denotations":[{"id":"T14599","span":{"begin":506,"end":513},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T14598","span":{"begin":496,"end":513},"obj":"http://purl.obolibrary.org/obo/GO_0043130"},{"id":"T14597","span":{"begin":496,"end":505},"obj":"http://purl.obolibrary.org/obo/GO_0031386"}],"text":"Interestingly, CYLD has been shown to negatively regulate RANK signalling and osteoclastogenesis in mice [65]. Mice with a genetic deficiency of CYLD have aberrant osteoclast differentiation and develop severe osteoporosis. Osteoclast precursors of these mice are hyper-responsive to RANKL-induced differentiation and produce more and larger osteoclasts. CYLD expression is markedly upregulated under conditions of RANKL-induced osteoclastogenesis and is recruited to ubiquitinated TRAF6 via the ubiquitin-binding adaptor protein p62 (also known as sequestosome 1) [65], followed by the CYLD-mediated deubiquitination of TRAF6. In this context, it is worth mentioning that transgenic mice expressing a mutated form of p62 also display abnormal osteoclastogenesis and develop progressive bone loss [66]. These findings suggest that CYLD-mediated inhibi-tion of RANK-induced NF-κB signalling plays a key role in the negative regulation of osteoclastogenesis and indicate CYLD as a potential genetic factor involved in the pathology of bone disorders such as RA."}

{"project":"sentences","denotations":[{"id":"T14151","span":{"begin":803,"end":1059},"obj":"Sentence"},{"id":"T14150","span":{"begin":628,"end":802},"obj":"Sentence"},{"id":"T14149","span":{"begin":355,"end":627},"obj":"Sentence"},{"id":"T14148","span":{"begin":224,"end":354},"obj":"Sentence"},{"id":"T14147","span":{"begin":111,"end":223},"obj":"Sentence"},{"id":"T14146","span":{"begin":0,"end":110},"obj":"Sentence"},{"id":"T146","span":{"begin":0,"end":110},"obj":"Sentence"},{"id":"T147","span":{"begin":111,"end":223},"obj":"Sentence"},{"id":"T148","span":{"begin":224,"end":354},"obj":"Sentence"},{"id":"T149","span":{"begin":355,"end":627},"obj":"Sentence"},{"id":"T150","span":{"begin":628,"end":802},"obj":"Sentence"},{"id":"T151","span":{"begin":803,"end":1059},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Interestingly, CYLD has been shown to negatively regulate RANK signalling and osteoclastogenesis in mice [65]. Mice with a genetic deficiency of CYLD have aberrant osteoclast differentiation and develop severe osteoporosis. Osteoclast precursors of these mice are hyper-responsive to RANKL-induced differentiation and produce more and larger osteoclasts. CYLD expression is markedly upregulated under conditions of RANKL-induced osteoclastogenesis and is recruited to ubiquitinated TRAF6 via the ubiquitin-binding adaptor protein p62 (also known as sequestosome 1) [65], followed by the CYLD-mediated deubiquitination of TRAF6. In this context, it is worth mentioning that transgenic mice expressing a mutated form of p62 also display abnormal osteoclastogenesis and develop progressive bone loss [66]. These findings suggest that CYLD-mediated inhibi-tion of RANK-induced NF-κB signalling plays a key role in the negative regulation of osteoclastogenesis and indicate CYLD as a potential genetic factor involved in the pathology of bone disorders such as RA."}

{"project":"ICD10","denotations":[{"id":"T14595","span":{"begin":1033,"end":1047},"obj":"http://purl.bioontology.org/ontology/ICD10/M89.9"},{"id":"T14594","span":{"begin":210,"end":222},"obj":"http://purl.bioontology.org/ontology/ICD10/M81.9"}],"text":"Interestingly, CYLD has been shown to negatively regulate RANK signalling and osteoclastogenesis in mice [65]. Mice with a genetic deficiency of CYLD have aberrant osteoclast differentiation and develop severe osteoporosis. Osteoclast precursors of these mice are hyper-responsive to RANKL-induced differentiation and produce more and larger osteoclasts. CYLD expression is markedly upregulated under conditions of RANKL-induced osteoclastogenesis and is recruited to ubiquitinated TRAF6 via the ubiquitin-binding adaptor protein p62 (also known as sequestosome 1) [65], followed by the CYLD-mediated deubiquitination of TRAF6. In this context, it is worth mentioning that transgenic mice expressing a mutated form of p62 also display abnormal osteoclastogenesis and develop progressive bone loss [66]. These findings suggest that CYLD-mediated inhibi-tion of RANK-induced NF-κB signalling plays a key role in the negative regulation of osteoclastogenesis and indicate CYLD as a potential genetic factor involved in the pathology of bone disorders such as RA."}

{"project":"simple1","denotations":[{"id":"T14638","span":{"begin":969,"end":973},"obj":"Protein"},{"id":"T14637","span":{"begin":860,"end":864},"obj":"Protein"},{"id":"T14636","span":{"begin":831,"end":835},"obj":"Protein"},{"id":"T14635","span":{"begin":718,"end":721},"obj":"Protein"},{"id":"T14634","span":{"begin":621,"end":626},"obj":"Protein"},{"id":"T14633","span":{"begin":587,"end":591},"obj":"Protein"},{"id":"T14632","span":{"begin":549,"end":563},"obj":"Protein"},{"id":"T14631","span":{"begin":530,"end":533},"obj":"Protein"},{"id":"T14630","span":{"begin":496,"end":505},"obj":"Protein"},{"id":"T14629","span":{"begin":482,"end":487},"obj":"Protein"},{"id":"T14628","span":{"begin":415,"end":420},"obj":"Protein"},{"id":"T14627","span":{"begin":355,"end":359},"obj":"Protein"},{"id":"T14626","span":{"begin":284,"end":289},"obj":"Protein"},{"id":"T14625","span":{"begin":145,"end":149},"obj":"Protein"},{"id":"T14624","span":{"begin":58,"end":62},"obj":"Protein"},{"id":"T14623","span":{"begin":15,"end":19},"obj":"Protein"}],"text":"Interestingly, CYLD has been shown to negatively regulate RANK signalling and osteoclastogenesis in mice [65]. Mice with a genetic deficiency of CYLD have aberrant osteoclast differentiation and develop severe osteoporosis. Osteoclast precursors of these mice are hyper-responsive to RANKL-induced differentiation and produce more and larger osteoclasts. CYLD expression is markedly upregulated under conditions of RANKL-induced osteoclastogenesis and is recruited to ubiquitinated TRAF6 via the ubiquitin-binding adaptor protein p62 (also known as sequestosome 1) [65], followed by the CYLD-mediated deubiquitination of TRAF6. In this context, it is worth mentioning that transgenic mice expressing a mutated form of p62 also display abnormal osteoclastogenesis and develop progressive bone loss [66]. These findings suggest that CYLD-mediated inhibi-tion of RANK-induced NF-κB signalling plays a key role in the negative regulation of osteoclastogenesis and indicate CYLD as a potential genetic factor involved in the pathology of bone disorders such as RA."}

{"project":"BioNLP16_DUT","denotations":[{"id":"T15301","span":{"begin":689,"end":699},"obj":"Gene_expression"},{"id":"T15300","span":{"begin":360,"end":370},"obj":"Gene_expression"},{"id":"T15299","span":{"begin":506,"end":513},"obj":"Binding"},{"id":"T15298","span":{"begin":601,"end":617},"obj":"Negative_regulation"},{"id":"T15297","span":{"begin":383,"end":394},"obj":"Positive_regulation"},{"id":"T15296","span":{"begin":131,"end":141},"obj":"Negative_regulation"},{"id":"T15293","span":{"begin":969,"end":973},"obj":"Protein"},{"id":"T15292","span":{"begin":860,"end":864},"obj":"Protein"},{"id":"T15291","span":{"begin":831,"end":835},"obj":"Protein"},{"id":"T15290","span":{"begin":718,"end":721},"obj":"Protein"},{"id":"T15289","span":{"begin":621,"end":626},"obj":"Protein"},{"id":"T15288","span":{"begin":587,"end":591},"obj":"Protein"},{"id":"T15287","span":{"begin":549,"end":563},"obj":"Protein"},{"id":"T15286","span":{"begin":530,"end":533},"obj":"Protein"},{"id":"T15285","span":{"begin":496,"end":505},"obj":"Protein"},{"id":"T15284","span":{"begin":482,"end":487},"obj":"Protein"},{"id":"T15283","span":{"begin":415,"end":420},"obj":"Protein"},{"id":"T15282","span":{"begin":355,"end":359},"obj":"Protein"},{"id":"T15281","span":{"begin":284,"end":289},"obj":"Protein"},{"id":"T15280","span":{"begin":145,"end":149},"obj":"Protein"},{"id":"T15279","span":{"begin":58,"end":62},"obj":"Protein"},{"id":"T15278","span":{"begin":15,"end":19},"obj":"Protein"}],"relations":[{"id":"R10135","pred":"themeOf","subj":"T15280","obj":"T15296"},{"id":"R10136","pred":"themeOf","subj":"T15282","obj":"T15300"},{"id":"R10137","pred":"themeOf","subj":"T15285","obj":"T15299"},{"id":"R10138","pred":"themeOf","subj":"T15286","obj":"T15299"},{"id":"R10139","pred":"themeOf","subj":"T15286","obj":"T15300"},{"id":"R10140","pred":"themeOf","subj":"T15289","obj":"T15298"},{"id":"R10141","pred":"themeOf","subj":"T15290","obj":"T15301"},{"id":"R10142","pred":"themeOf","subj":"T15300","obj":"T15297"},{"id":"R10143","pred":"themeOf","subj":"T15300","obj":"T15297"}],"text":"Interestingly, CYLD has been shown to negatively regulate RANK signalling and osteoclastogenesis in mice [65]. Mice with a genetic deficiency of CYLD have aberrant osteoclast differentiation and develop severe osteoporosis. Osteoclast precursors of these mice are hyper-responsive to RANKL-induced differentiation and produce more and larger osteoclasts. CYLD expression is markedly upregulated under conditions of RANKL-induced osteoclastogenesis and is recruited to ubiquitinated TRAF6 via the ubiquitin-binding adaptor protein p62 (also known as sequestosome 1) [65], followed by the CYLD-mediated deubiquitination of TRAF6. In this context, it is worth mentioning that transgenic mice expressing a mutated form of p62 also display abnormal osteoclastogenesis and develop progressive bone loss [66]. These findings suggest that CYLD-mediated inhibi-tion of RANK-induced NF-κB signalling plays a key role in the negative regulation of osteoclastogenesis and indicate CYLD as a potential genetic factor involved in the pathology of bone disorders such as RA."}

{"project":"BioNLP16_Messiy","denotations":[{"id":"T15071","span":{"begin":689,"end":699},"obj":"Gene_expression"},{"id":"T15069","span":{"begin":383,"end":394},"obj":"Positive_regulation"},{"id":"T15068","span":{"begin":455,"end":464},"obj":"Binding"},{"id":"T15067","span":{"begin":601,"end":617},"obj":"Negative_regulation"},{"id":"T15066","span":{"begin":360,"end":370},"obj":"Gene_expression"},{"id":"T15065","span":{"begin":290,"end":297},"obj":"Positive_regulation"},{"id":"T15064","span":{"begin":131,"end":141},"obj":"Negative_regulation"},{"id":"T15062","span":{"begin":969,"end":973},"obj":"Protein"},{"id":"T15061","span":{"begin":860,"end":864},"obj":"Protein"},{"id":"T15060","span":{"begin":831,"end":835},"obj":"Protein"},{"id":"T15059","span":{"begin":718,"end":721},"obj":"Protein"},{"id":"T15058","span":{"begin":621,"end":626},"obj":"Protein"},{"id":"T15057","span":{"begin":587,"end":591},"obj":"Protein"},{"id":"T15056","span":{"begin":549,"end":563},"obj":"Protein"},{"id":"T15055","span":{"begin":530,"end":533},"obj":"Protein"},{"id":"T15054","span":{"begin":496,"end":505},"obj":"Protein"},{"id":"T15053","span":{"begin":482,"end":487},"obj":"Protein"},{"id":"T15052","span":{"begin":415,"end":420},"obj":"Protein"},{"id":"T15051","span":{"begin":355,"end":359},"obj":"Protein"},{"id":"T15050","span":{"begin":284,"end":289},"obj":"Protein"},{"id":"T15049","span":{"begin":145,"end":149},"obj":"Protein"},{"id":"T15048","span":{"begin":58,"end":62},"obj":"Protein"},{"id":"T15047","span":{"begin":15,"end":19},"obj":"Protein"},{"id":"T15070","span":{"begin":506,"end":513},"obj":"Binding"}],"relations":[{"id":"R10042","pred":"themeOf","subj":"T15049","obj":"T15064"},{"id":"R10043","pred":"themeOf","subj":"T15050","obj":"T15065"},{"id":"R10044","pred":"themeOf","subj":"T15051","obj":"T15066"},{"id":"R10045","pred":"themeOf","subj":"T15054","obj":"T15070"},{"id":"R10046","pred":"themeOf","subj":"T15055","obj":"T15068"},{"id":"R10047","pred":"themeOf","subj":"T15055","obj":"T15070"},{"id":"R10048","pred":"themeOf","subj":"T15058","obj":"T15067"},{"id":"R10049","pred":"themeOf","subj":"T15059","obj":"T15071"},{"id":"R10050","pred":"themeOf","subj":"T15066","obj":"T15069"}],"text":"Interestingly, CYLD has been shown to negatively regulate RANK signalling and osteoclastogenesis in mice [65]. Mice with a genetic deficiency of CYLD have aberrant osteoclast differentiation and develop severe osteoporosis. Osteoclast precursors of these mice are hyper-responsive to RANKL-induced differentiation and produce more and larger osteoclasts. CYLD expression is markedly upregulated under conditions of RANKL-induced osteoclastogenesis and is recruited to ubiquitinated TRAF6 via the ubiquitin-binding adaptor protein p62 (also known as sequestosome 1) [65], followed by the CYLD-mediated deubiquitination of TRAF6. In this context, it is worth mentioning that transgenic mice expressing a mutated form of p62 also display abnormal osteoclastogenesis and develop progressive bone loss [66]. These findings suggest that CYLD-mediated inhibi-tion of RANK-induced NF-κB signalling plays a key role in the negative regulation of osteoclastogenesis and indicate CYLD as a potential genetic factor involved in the pathology of bone disorders such as RA."}

{"project":"bionlp-st-ge-2016-test-ihmc","denotations":[{"id":"T15367","span":{"begin":468,"end":487},"obj":"Ubiquitination"},{"id":"T15365","span":{"begin":0,"end":109},"obj":"Regulation"},{"id":"T15362","span":{"begin":580,"end":626},"obj":"Regulation"},{"id":"T15361","span":{"begin":355,"end":370},"obj":"Gene_expression"},{"id":"T15357","span":{"begin":415,"end":428},"obj":"Protein"},{"id":"T15356","span":{"begin":831,"end":844},"obj":"Protein"},{"id":"T15353","span":{"begin":715,"end":721},"obj":"Protein"},{"id":"T15352","span":{"begin":224,"end":259},"obj":"Entity"},{"id":"T15351","span":{"begin":1033,"end":1058},"obj":"Protein"},{"id":"T15346","span":{"begin":969,"end":973},"obj":"Protein"},{"id":"T15345","span":{"begin":58,"end":109},"obj":"Protein"},{"id":"T15343","span":{"begin":15,"end":19},"obj":"Protein"},{"id":"T15341","span":{"begin":549,"end":563},"obj":"Protein"},{"id":"T15337","span":{"begin":142,"end":149},"obj":"Protein"},{"id":"T15334","span":{"begin":618,"end":626},"obj":"Protein"},{"id":"T15330","span":{"begin":468,"end":487},"obj":"Protein"},{"id":"T15327","span":{"begin":860,"end":889},"obj":"Protein"},{"id":"T15326","span":{"begin":335,"end":353},"obj":"Entity"},{"id":"T15325","span":{"begin":514,"end":533},"obj":"Protein"},{"id":"T15323","span":{"begin":111,"end":149},"obj":"Protein"},{"id":"T15322","span":{"begin":860,"end":872},"obj":"Protein"},{"id":"T15320","span":{"begin":514,"end":533},"obj":"Protein"},{"id":"T15318","span":{"begin":492,"end":513},"obj":"Protein"},{"id":"T15314","span":{"begin":355,"end":359},"obj":"Protein"},{"id":"T15312","span":{"begin":587,"end":600},"obj":"Protein"},{"id":"T15311","span":{"begin":284,"end":289},"obj":"Protein"},{"id":"T15303","span":{"begin":100,"end":109},"obj":"Protein"}],"relations":[{"id":"R10148","pred":"causeOf","subj":"T15312","obj":"T15362"},{"id":"R10149","pred":"themeOf","subj":"T15314","obj":"T15361"},{"id":"R10151","pred":"themeOf","subj":"T15330","obj":"T15367"},{"id":"R10153","pred":"causeOf","subj":"T15343","obj":"T15365"},{"id":"R10154","pred":"themeOf","subj":"T15345","obj":"T15365"}],"text":"Interestingly, CYLD has been shown to negatively regulate RANK signalling and osteoclastogenesis in mice [65]. Mice with a genetic deficiency of CYLD have aberrant osteoclast differentiation and develop severe osteoporosis. Osteoclast precursors of these mice are hyper-responsive to RANKL-induced differentiation and produce more and larger osteoclasts. CYLD expression is markedly upregulated under conditions of RANKL-induced osteoclastogenesis and is recruited to ubiquitinated TRAF6 via the ubiquitin-binding adaptor protein p62 (also known as sequestosome 1) [65], followed by the CYLD-mediated deubiquitination of TRAF6. In this context, it is worth mentioning that transgenic mice expressing a mutated form of p62 also display abnormal osteoclastogenesis and develop progressive bone loss [66]. These findings suggest that CYLD-mediated inhibi-tion of RANK-induced NF-κB signalling plays a key role in the negative regulation of osteoclastogenesis and indicate CYLD as a potential genetic factor involved in the pathology of bone disorders such as RA."}

{"project":"bionlp-st-ge-2016-test-tees","denotations":[{"id":"T15167","span":{"begin":969,"end":973},"obj":"Protein"},{"id":"T15166","span":{"begin":873,"end":878},"obj":"Protein"},{"id":"T15165","span":{"begin":860,"end":864},"obj":"Protein"},{"id":"T15164","span":{"begin":689,"end":699},"obj":"Gene_expression"},{"id":"T15163","span":{"begin":718,"end":721},"obj":"Protein"},{"id":"T15162","span":{"begin":455,"end":464},"obj":"Negative_regulation"},{"id":"T15161","span":{"begin":383,"end":394},"obj":"Positive_regulation"},{"id":"T15160","span":{"begin":360,"end":370},"obj":"Gene_expression"},{"id":"T15159","span":{"begin":621,"end":626},"obj":"Protein"},{"id":"T15158","span":{"begin":530,"end":533},"obj":"Protein"},{"id":"T15157","span":{"begin":496,"end":505},"obj":"Protein"},{"id":"T15156","span":{"begin":468,"end":487},"obj":"Protein"},{"id":"T15155","span":{"begin":415,"end":420},"obj":"Protein"},{"id":"T15154","span":{"begin":355,"end":359},"obj":"Protein"},{"id":"T15153","span":{"begin":284,"end":289},"obj":"Protein"},{"id":"T15152","span":{"begin":131,"end":141},"obj":"Negative_regulation"},{"id":"T15151","span":{"begin":145,"end":149},"obj":"Protein"},{"id":"T15150","span":{"begin":49,"end":57},"obj":"Regulation"},{"id":"T15149","span":{"begin":58,"end":62},"obj":"Protein"},{"id":"T15148","span":{"begin":15,"end":19},"obj":"Protein"}],"relations":[{"id":"R10087","pred":"themeOf","subj":"T15149","obj":"T15150"},{"id":"R10088","pred":"Cause","subj":"T15150","obj":"T15148"},{"id":"R10089","pred":"themeOf","subj":"T15151","obj":"T15152"},{"id":"R10090","pred":"themeOf","subj":"T15154","obj":"T15160"},{"id":"R10091","pred":"themeOf","subj":"T15160","obj":"T15161"},{"id":"R10092","pred":"themeOf","subj":"T15160","obj":"T15162"},{"id":"R10093","pred":"themeOf","subj":"T15163","obj":"T15164"}],"text":"Interestingly, CYLD has been shown to negatively regulate RANK signalling and osteoclastogenesis in mice [65]. Mice with a genetic deficiency of CYLD have aberrant osteoclast differentiation and develop severe osteoporosis. Osteoclast precursors of these mice are hyper-responsive to RANKL-induced differentiation and produce more and larger osteoclasts. CYLD expression is markedly upregulated under conditions of RANKL-induced osteoclastogenesis and is recruited to ubiquitinated TRAF6 via the ubiquitin-binding adaptor protein p62 (also known as sequestosome 1) [65], followed by the CYLD-mediated deubiquitination of TRAF6. In this context, it is worth mentioning that transgenic mice expressing a mutated form of p62 also display abnormal osteoclastogenesis and develop progressive bone loss [66]. These findings suggest that CYLD-mediated inhibi-tion of RANK-induced NF-κB signalling plays a key role in the negative regulation of osteoclastogenesis and indicate CYLD as a potential genetic factor involved in the pathology of bone disorders such as RA."}

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