PubMed:24035784 / 1454-1870 JSONTXT

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    PubMed_Structured_Abstracts

    {"project":"PubMed_Structured_Abstracts","denotations":[{"id":"T3","span":{"begin":0,"end":416},"obj":"RESULTS"}],"text":"HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase."}

    NGLY1-deficiency

    {"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T7","span":{"begin":198,"end":204},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T8","span":{"begin":349,"end":355},"obj":"chem:24139"}],"namespaces":[{"prefix":"hgnc","uri":"https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:"},{"prefix":"omim","uri":"https://www.omim.org/entry/"},{"prefix":"chem","uri":"https://pubchem.ncbi.nlm.nih.gov/compound/"}],"text":"HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase."}

    Glycan-GlyCosmos

    {"project":"Glycan-GlyCosmos","denotations":[{"id":"T5","span":{"begin":196,"end":204},"obj":"Glycan"},{"id":"T6","span":{"begin":347,"end":355},"obj":"Glycan"}],"attributes":[{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A11","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G49108TO"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A12","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G49108TO"}],"text":"HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase."}

    GlyCosmos15-Sentences

    {"project":"GlyCosmos15-Sentences","blocks":[{"id":"T13","span":{"begin":118,"end":214},"obj":"Sentence"},{"id":"T14","span":{"begin":215,"end":303},"obj":"Sentence"},{"id":"T15","span":{"begin":304,"end":416},"obj":"Sentence"}],"text":"HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase."}

    GlyCosmos15-Glycan

    {"project":"GlyCosmos15-Glycan","denotations":[{"id":"T5","span":{"begin":196,"end":204},"obj":"Glycan"},{"id":"T6","span":{"begin":347,"end":355},"obj":"Glycan"}],"attributes":[{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A11","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G49108TO"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A12","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G49108TO"}],"text":"HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase."}

    GlyCosmos15-GlycoEpitope

    {"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T5","span":{"begin":196,"end":204},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":347,"end":355},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0004"}],"text":"HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase."}

    GlyCosmos-GlycoEpitope

    {"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T5","span":{"begin":196,"end":204},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":347,"end":355},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0004"}],"text":"HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase."}