PubMed:7471212 JSON TXT

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Test-Species-PubTator

Test-Species-PubDictionaries-PubMedBERT

{"project":"Test-Species-PubDictionaries-PubMedBERT","denotations":[{"id":"T1","span":{"begin":100,"end":103},"obj":"Species"},{"id":"T3","span":{"begin":133,"end":143},"obj":"Species"},{"id":"T4","span":{"begin":436,"end":439},"obj":"Species"},{"id":"T6","span":{"begin":482,"end":485},"obj":"Species"},{"id":"T8","span":{"begin":646,"end":650},"obj":"Species"},{"id":"T9","span":{"begin":677,"end":681},"obj":"Species"},{"id":"T10","span":{"begin":1406,"end":1410},"obj":"Species"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"85919"},{"id":"A2","pred":"db_id","subj":"T1","obj":"74730"},{"id":"A3","pred":"db_id","subj":"T3","obj":"58024"},{"id":"A4","pred":"db_id","subj":"T4","obj":"85919"},{"id":"A5","pred":"db_id","subj":"T4","obj":"74730"},{"id":"A6","pred":"db_id","subj":"T6","obj":"85919"},{"id":"A7","pred":"db_id","subj":"T6","obj":"74730"},{"id":"A8","pred":"db_id","subj":"T8","obj":"582003"},{"id":"A9","pred":"db_id","subj":"T9","obj":"582003"},{"id":"A10","pred":"db_id","subj":"T10","obj":"1369087"}],"text":"Studies on the galactose-binding site of ricin and the hybrid toxin Man6P-ricin.\nN-acetylimidazole (NAI) was used to O-acetylate the plant seed toxin ricin. O-acetylation of one to two tyrosine residues per molecule of ricin inhibited ricin binding to Sepharose 4B and decreased toxicity by 90% in a protein synthesis inhibition assay in HeLa cells. Lactose, known to block the binding site on the ricin B subunit, protected ricin from NAI modification of binding or toxicity. Thus NAI, under these conditions, can be a lactose site-specific inhibitor. The lactose site-specific modification of the hybrid toxin, Man6P-ricin, performed under the same conditions, exhibited the same 90% inhibition of Man6P receptor-mediated toxicity as the galactose-containing receptor-mediated toxicity of either Man6P-ricin or ricin. Thus the ricin B chain lactose-binding site appears to be essential for the high potency of Man6P-ricin via the new cell type-specific Man6P receptor. Treatment of fibroblasts with neuraminidase exposes galactose residues, thus increasing the sensitivity to ricin eight fold. The Man6P receptor-mediated toxicity of Man6P-ricin is not affected by this treatment, although the galactose-inhibited route is potentiated eight fold. The Man6P-ricin hybrid appears to require the ricin B chain galactose-binding site to enter the cytosol after initially binding to the Man6P receptor. These data provide some insights into the proper design of hybrid toxins. We discuss a number of possible models for hybrid toxin entry."}

GlyCosmos15-Glycan

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":350,"end":357},"obj":"Glycan"},{"id":"T2","span":{"begin":520,"end":527},"obj":"Glycan"},{"id":"T3","span":{"begin":557,"end":564},"obj":"Glycan"},{"id":"T4","span":{"begin":843,"end":850},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G15541SE"},{"id":"A5","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G15541SE"},{"id":"A6","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G15541SE"},{"id":"A7","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G15541SE"},{"id":"A8","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE"}],"text":"Studies on the galactose-binding site of ricin and the hybrid toxin Man6P-ricin.\nN-acetylimidazole (NAI) was used to O-acetylate the plant seed toxin ricin. O-acetylation of one to two tyrosine residues per molecule of ricin inhibited ricin binding to Sepharose 4B and decreased toxicity by 90% in a protein synthesis inhibition assay in HeLa cells. Lactose, known to block the binding site on the ricin B subunit, protected ricin from NAI modification of binding or toxicity. Thus NAI, under these conditions, can be a lactose site-specific inhibitor. The lactose site-specific modification of the hybrid toxin, Man6P-ricin, performed under the same conditions, exhibited the same 90% inhibition of Man6P receptor-mediated toxicity as the galactose-containing receptor-mediated toxicity of either Man6P-ricin or ricin. Thus the ricin B chain lactose-binding site appears to be essential for the high potency of Man6P-ricin via the new cell type-specific Man6P receptor. Treatment of fibroblasts with neuraminidase exposes galactose residues, thus increasing the sensitivity to ricin eight fold. The Man6P receptor-mediated toxicity of Man6P-ricin is not affected by this treatment, although the galactose-inhibited route is potentiated eight fold. The Man6P-ricin hybrid appears to require the ricin B chain galactose-binding site to enter the cytosol after initially binding to the Man6P receptor. These data provide some insights into the proper design of hybrid toxins. We discuss a number of possible models for hybrid toxin entry."}

Glycan-GlyCosmos

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":350,"end":357},"obj":"Glycan"},{"id":"T2","span":{"begin":520,"end":527},"obj":"Glycan"},{"id":"T3","span":{"begin":557,"end":564},"obj":"Glycan"},{"id":"T4","span":{"begin":843,"end":850},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G15541SE"},{"id":"A5","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G15541SE"},{"id":"A6","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G15541SE"},{"id":"A7","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G15541SE"},{"id":"A8","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE"}],"text":"Studies on the galactose-binding site of ricin and the hybrid toxin Man6P-ricin.\nN-acetylimidazole (NAI) was used to O-acetylate the plant seed toxin ricin. O-acetylation of one to two tyrosine residues per molecule of ricin inhibited ricin binding to Sepharose 4B and decreased toxicity by 90% in a protein synthesis inhibition assay in HeLa cells. Lactose, known to block the binding site on the ricin B subunit, protected ricin from NAI modification of binding or toxicity. Thus NAI, under these conditions, can be a lactose site-specific inhibitor. The lactose site-specific modification of the hybrid toxin, Man6P-ricin, performed under the same conditions, exhibited the same 90% inhibition of Man6P receptor-mediated toxicity as the galactose-containing receptor-mediated toxicity of either Man6P-ricin or ricin. Thus the ricin B chain lactose-binding site appears to be essential for the high potency of Man6P-ricin via the new cell type-specific Man6P receptor. Treatment of fibroblasts with neuraminidase exposes galactose residues, thus increasing the sensitivity to ricin eight fold. The Man6P receptor-mediated toxicity of Man6P-ricin is not affected by this treatment, although the galactose-inhibited route is potentiated eight fold. The Man6P-ricin hybrid appears to require the ricin B chain galactose-binding site to enter the cytosol after initially binding to the Man6P receptor. These data provide some insights into the proper design of hybrid toxins. We discuss a number of possible models for hybrid toxin entry."}

GlyCosmos15-CL

{"project":"GlyCosmos15-CL","denotations":[{"id":"T1","span":{"begin":984,"end":995},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000057"}],"text":"Studies on the galactose-binding site of ricin and the hybrid toxin Man6P-ricin.\nN-acetylimidazole (NAI) was used to O-acetylate the plant seed toxin ricin. O-acetylation of one to two tyrosine residues per molecule of ricin inhibited ricin binding to Sepharose 4B and decreased toxicity by 90% in a protein synthesis inhibition assay in HeLa cells. Lactose, known to block the binding site on the ricin B subunit, protected ricin from NAI modification of binding or toxicity. Thus NAI, under these conditions, can be a lactose site-specific inhibitor. The lactose site-specific modification of the hybrid toxin, Man6P-ricin, performed under the same conditions, exhibited the same 90% inhibition of Man6P receptor-mediated toxicity as the galactose-containing receptor-mediated toxicity of either Man6P-ricin or ricin. Thus the ricin B chain lactose-binding site appears to be essential for the high potency of Man6P-ricin via the new cell type-specific Man6P receptor. Treatment of fibroblasts with neuraminidase exposes galactose residues, thus increasing the sensitivity to ricin eight fold. The Man6P receptor-mediated toxicity of Man6P-ricin is not affected by this treatment, although the galactose-inhibited route is potentiated eight fold. The Man6P-ricin hybrid appears to require the ricin B chain galactose-binding site to enter the cytosol after initially binding to the Man6P receptor. These data provide some insights into the proper design of hybrid toxins. We discuss a number of possible models for hybrid toxin entry."}

GlyCosmos15-UBERON

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":984,"end":995},"obj":"Body_part"},{"id":"T2","span":{"begin":1345,"end":1352},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000057"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/GO_0005829"}],"text":"Studies on the galactose-binding site of ricin and the hybrid toxin Man6P-ricin.\nN-acetylimidazole (NAI) was used to O-acetylate the plant seed toxin ricin. O-acetylation of one to two tyrosine residues per molecule of ricin inhibited ricin binding to Sepharose 4B and decreased toxicity by 90% in a protein synthesis inhibition assay in HeLa cells. Lactose, known to block the binding site on the ricin B subunit, protected ricin from NAI modification of binding or toxicity. Thus NAI, under these conditions, can be a lactose site-specific inhibitor. The lactose site-specific modification of the hybrid toxin, Man6P-ricin, performed under the same conditions, exhibited the same 90% inhibition of Man6P receptor-mediated toxicity as the galactose-containing receptor-mediated toxicity of either Man6P-ricin or ricin. Thus the ricin B chain lactose-binding site appears to be essential for the high potency of Man6P-ricin via the new cell type-specific Man6P receptor. Treatment of fibroblasts with neuraminidase exposes galactose residues, thus increasing the sensitivity to ricin eight fold. The Man6P receptor-mediated toxicity of Man6P-ricin is not affected by this treatment, although the galactose-inhibited route is potentiated eight fold. The Man6P-ricin hybrid appears to require the ricin B chain galactose-binding site to enter the cytosol after initially binding to the Man6P receptor. These data provide some insights into the proper design of hybrid toxins. We discuss a number of possible models for hybrid toxin entry."}

GlyCosmos15-Sentences

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":80},"obj":"Sentence"},{"id":"T2","span":{"begin":81,"end":156},"obj":"Sentence"},{"id":"T3","span":{"begin":157,"end":349},"obj":"Sentence"},{"id":"T4","span":{"begin":350,"end":476},"obj":"Sentence"},{"id":"T5","span":{"begin":477,"end":552},"obj":"Sentence"},{"id":"T6","span":{"begin":553,"end":819},"obj":"Sentence"},{"id":"T7","span":{"begin":820,"end":970},"obj":"Sentence"},{"id":"T8","span":{"begin":971,"end":1095},"obj":"Sentence"},{"id":"T9","span":{"begin":1096,"end":1248},"obj":"Sentence"},{"id":"T10","span":{"begin":1249,"end":1399},"obj":"Sentence"},{"id":"T11","span":{"begin":1400,"end":1473},"obj":"Sentence"},{"id":"T12","span":{"begin":1474,"end":1536},"obj":"Sentence"}],"text":"Studies on the galactose-binding site of ricin and the hybrid toxin Man6P-ricin.\nN-acetylimidazole (NAI) was used to O-acetylate the plant seed toxin ricin. O-acetylation of one to two tyrosine residues per molecule of ricin inhibited ricin binding to Sepharose 4B and decreased toxicity by 90% in a protein synthesis inhibition assay in HeLa cells. Lactose, known to block the binding site on the ricin B subunit, protected ricin from NAI modification of binding or toxicity. Thus NAI, under these conditions, can be a lactose site-specific inhibitor. The lactose site-specific modification of the hybrid toxin, Man6P-ricin, performed under the same conditions, exhibited the same 90% inhibition of Man6P receptor-mediated toxicity as the galactose-containing receptor-mediated toxicity of either Man6P-ricin or ricin. Thus the ricin B chain lactose-binding site appears to be essential for the high potency of Man6P-ricin via the new cell type-specific Man6P receptor. Treatment of fibroblasts with neuraminidase exposes galactose residues, thus increasing the sensitivity to ricin eight fold. The Man6P receptor-mediated toxicity of Man6P-ricin is not affected by this treatment, although the galactose-inhibited route is potentiated eight fold. The Man6P-ricin hybrid appears to require the ricin B chain galactose-binding site to enter the cytosol after initially binding to the Man6P receptor. These data provide some insights into the proper design of hybrid toxins. We discuss a number of possible models for hybrid toxin entry."}

GlyCosmos15-FMA

{"project":"GlyCosmos15-FMA","denotations":[{"id":"T1","span":{"begin":984,"end":995},"obj":"Body_part"},{"id":"T2","span":{"begin":1345,"end":1352},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"FMA:63877"},{"id":"A2","pred":"db_id","subj":"T2","obj":"FMA:66836"}],"namespaces":[{"prefix":"FMA","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Studies on the galactose-binding site of ricin and the hybrid toxin Man6P-ricin.\nN-acetylimidazole (NAI) was used to O-acetylate the plant seed toxin ricin. O-acetylation of one to two tyrosine residues per molecule of ricin inhibited ricin binding to Sepharose 4B and decreased toxicity by 90% in a protein synthesis inhibition assay in HeLa cells. Lactose, known to block the binding site on the ricin B subunit, protected ricin from NAI modification of binding or toxicity. Thus NAI, under these conditions, can be a lactose site-specific inhibitor. The lactose site-specific modification of the hybrid toxin, Man6P-ricin, performed under the same conditions, exhibited the same 90% inhibition of Man6P receptor-mediated toxicity as the galactose-containing receptor-mediated toxicity of either Man6P-ricin or ricin. Thus the ricin B chain lactose-binding site appears to be essential for the high potency of Man6P-ricin via the new cell type-specific Man6P receptor. Treatment of fibroblasts with neuraminidase exposes galactose residues, thus increasing the sensitivity to ricin eight fold. The Man6P receptor-mediated toxicity of Man6P-ricin is not affected by this treatment, although the galactose-inhibited route is potentiated eight fold. The Man6P-ricin hybrid appears to require the ricin B chain galactose-binding site to enter the cytosol after initially binding to the Man6P receptor. These data provide some insights into the proper design of hybrid toxins. We discuss a number of possible models for hybrid toxin entry."}

Anatomy-UBERON

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":984,"end":995},"obj":"Body_part"},{"id":"T2","span":{"begin":1345,"end":1352},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000057"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/GO_0005829"}],"text":"Studies on the galactose-binding site of ricin and the hybrid toxin Man6P-ricin.\nN-acetylimidazole (NAI) was used to O-acetylate the plant seed toxin ricin. O-acetylation of one to two tyrosine residues per molecule of ricin inhibited ricin binding to Sepharose 4B and decreased toxicity by 90% in a protein synthesis inhibition assay in HeLa cells. Lactose, known to block the binding site on the ricin B subunit, protected ricin from NAI modification of binding or toxicity. Thus NAI, under these conditions, can be a lactose site-specific inhibitor. The lactose site-specific modification of the hybrid toxin, Man6P-ricin, performed under the same conditions, exhibited the same 90% inhibition of Man6P receptor-mediated toxicity as the galactose-containing receptor-mediated toxicity of either Man6P-ricin or ricin. Thus the ricin B chain lactose-binding site appears to be essential for the high potency of Man6P-ricin via the new cell type-specific Man6P receptor. Treatment of fibroblasts with neuraminidase exposes galactose residues, thus increasing the sensitivity to ricin eight fold. The Man6P receptor-mediated toxicity of Man6P-ricin is not affected by this treatment, although the galactose-inhibited route is potentiated eight fold. The Man6P-ricin hybrid appears to require the ricin B chain galactose-binding site to enter the cytosol after initially binding to the Man6P receptor. These data provide some insights into the proper design of hybrid toxins. We discuss a number of possible models for hybrid toxin entry."}

CL-cell

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":984,"end":995},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000057"}],"text":"Studies on the galactose-binding site of ricin and the hybrid toxin Man6P-ricin.\nN-acetylimidazole (NAI) was used to O-acetylate the plant seed toxin ricin. O-acetylation of one to two tyrosine residues per molecule of ricin inhibited ricin binding to Sepharose 4B and decreased toxicity by 90% in a protein synthesis inhibition assay in HeLa cells. Lactose, known to block the binding site on the ricin B subunit, protected ricin from NAI modification of binding or toxicity. Thus NAI, under these conditions, can be a lactose site-specific inhibitor. The lactose site-specific modification of the hybrid toxin, Man6P-ricin, performed under the same conditions, exhibited the same 90% inhibition of Man6P receptor-mediated toxicity as the galactose-containing receptor-mediated toxicity of either Man6P-ricin or ricin. Thus the ricin B chain lactose-binding site appears to be essential for the high potency of Man6P-ricin via the new cell type-specific Man6P receptor. Treatment of fibroblasts with neuraminidase exposes galactose residues, thus increasing the sensitivity to ricin eight fold. The Man6P receptor-mediated toxicity of Man6P-ricin is not affected by this treatment, although the galactose-inhibited route is potentiated eight fold. The Man6P-ricin hybrid appears to require the ricin B chain galactose-binding site to enter the cytosol after initially binding to the Man6P receptor. These data provide some insights into the proper design of hybrid toxins. We discuss a number of possible models for hybrid toxin entry."}