PubMed:11274152 JSONTXT

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":176},"obj":"Sentence"},{"id":"T2","span":{"begin":177,"end":321},"obj":"Sentence"},{"id":"T3","span":{"begin":322,"end":442},"obj":"Sentence"},{"id":"T4","span":{"begin":443,"end":665},"obj":"Sentence"},{"id":"T5","span":{"begin":666,"end":771},"obj":"Sentence"},{"id":"T6","span":{"begin":772,"end":904},"obj":"Sentence"},{"id":"T7","span":{"begin":905,"end":1032},"obj":"Sentence"},{"id":"T8","span":{"begin":1033,"end":1277},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Disruption of the interaction of mammalian protein synthesis eukaryotic initiation factor 4B with the poly(A)-binding protein by caspase- and viral protease-mediated cleavages.\nEukaryotic initiation factor (eIF) 4B interacts with several components of the initiation pathway and is targeted for cleavage during apoptosis. In a cell-free system, cleavage of eIF4B by caspase-3 coincides with a general inhibition of protein synthetic activity. Affinity chromatography demonstrates that mammalian eIF4B interacts with the poly(A)-binding protein and that a region consisting of the N-terminal 80 amino acids of eIF4B is both necessary and sufficient for such binding. This interaction is lost when eIF4B is cleaved by caspase-3, which removes the N-terminal 45 amino acids. Similarly, the association of eIF4B with the poly(A)-binding protein in vivo is reduced when cells are induced to undergo apoptosis. Cleavage of the poly(A)-binding protein itself, using human rhinovirus 3C protease, also eliminates the interaction with eIF4B. Thus, disruption of the association between mammalian eIF4B and the poly(A)-binding protein can occur during both apoptosis and picornaviral infection and is likely to contribute to the inhibition of translation observed under these conditions."}

{"project":"2015-BEL-Sample","denotations":[{"id":"T1","span":{"begin":322,"end":441},"obj":"cat(p(HGNC:CASP3)) increases deg(p(HGNC:EIF4B))"}],"text":"Disruption of the interaction of mammalian protein synthesis eukaryotic initiation factor 4B with the poly(A)-binding protein by caspase- and viral protease-mediated cleavages.\nEukaryotic initiation factor (eIF) 4B interacts with several components of the initiation pathway and is targeted for cleavage during apoptosis. In a cell-free system, cleavage of eIF4B by caspase-3 coincides with a general inhibition of protein synthetic activity. Affinity chromatography demonstrates that mammalian eIF4B interacts with the poly(A)-binding protein and that a region consisting of the N-terminal 80 amino acids of eIF4B is both necessary and sufficient for such binding. This interaction is lost when eIF4B is cleaved by caspase-3, which removes the N-terminal 45 amino acids. Similarly, the association of eIF4B with the poly(A)-binding protein in vivo is reduced when cells are induced to undergo apoptosis. Cleavage of the poly(A)-binding protein itself, using human rhinovirus 3C protease, also eliminates the interaction with eIF4B. Thus, disruption of the association between mammalian eIF4B and the poly(A)-binding protein can occur during both apoptosis and picornaviral infection and is likely to contribute to the inhibition of translation observed under these conditions."}

{"project":"2015-BEL-Sample-2","denotations":[{"id":"BEL:20000284","span":{"begin":772,"end":903},"obj":"bp(GOBP:\"apoptotic process\") decreases complex(p(HGNC:EIF4B),p(HGNC:PABPN1))"},{"id":"BEL:20000286","span":{"begin":322,"end":441},"obj":"cat(p(HGNC:CASP3)) increases deg(p(HGNC:EIF4B))"},{"id":"BEL:20000282","span":{"begin":177,"end":320},"obj":"bp(GOBP:\"apoptotic process\") increases deg(p(HGNC:EIF4B))"},{"id":"BEL:20000284","span":{"begin":772,"end":903},"obj":"bp(GOBP:\"apoptotic process\") decreases complex(p(HGNC:EIF4B),p(HGNC:PABPN1))"},{"id":"BEL:20000286","span":{"begin":322,"end":441},"obj":"cat(p(HGNC:CASP3)) increases deg(p(HGNC:EIF4B))"},{"id":"BEL:20029108","span":{"begin":177,"end":441},"obj":"bp(GOBP:\"apoptotic process\") increases deg(p(HGNC:EIF4B))"},{"id":"BEL:20029476","span":{"begin":177,"end":441},"obj":"cat(p(HGNC:CASP3)) increases deg(p(HGNC:EIF4B))"}],"text":"Disruption of the interaction of mammalian protein synthesis eukaryotic initiation factor 4B with the poly(A)-binding protein by caspase- and viral protease-mediated cleavages.\nEukaryotic initiation factor (eIF) 4B interacts with several components of the initiation pathway and is targeted for cleavage during apoptosis. In a cell-free system, cleavage of eIF4B by caspase-3 coincides with a general inhibition of protein synthetic activity. Affinity chromatography demonstrates that mammalian eIF4B interacts with the poly(A)-binding protein and that a region consisting of the N-terminal 80 amino acids of eIF4B is both necessary and sufficient for such binding. This interaction is lost when eIF4B is cleaved by caspase-3, which removes the N-terminal 45 amino acids. Similarly, the association of eIF4B with the poly(A)-binding protein in vivo is reduced when cells are induced to undergo apoptosis. Cleavage of the poly(A)-binding protein itself, using human rhinovirus 3C protease, also eliminates the interaction with eIF4B. Thus, disruption of the association between mammalian eIF4B and the poly(A)-binding protein can occur during both apoptosis and picornaviral infection and is likely to contribute to the inhibition of translation observed under these conditions."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":1174,"end":1183},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"}],"text":"Disruption of the interaction of mammalian protein synthesis eukaryotic initiation factor 4B with the poly(A)-binding protein by caspase- and viral protease-mediated cleavages.\nEukaryotic initiation factor (eIF) 4B interacts with several components of the initiation pathway and is targeted for cleavage during apoptosis. In a cell-free system, cleavage of eIF4B by caspase-3 coincides with a general inhibition of protein synthetic activity. Affinity chromatography demonstrates that mammalian eIF4B interacts with the poly(A)-binding protein and that a region consisting of the N-terminal 80 amino acids of eIF4B is both necessary and sufficient for such binding. This interaction is lost when eIF4B is cleaved by caspase-3, which removes the N-terminal 45 amino acids. Similarly, the association of eIF4B with the poly(A)-binding protein in vivo is reduced when cells are induced to undergo apoptosis. Cleavage of the poly(A)-binding protein itself, using human rhinovirus 3C protease, also eliminates the interaction with eIF4B. Thus, disruption of the association between mammalian eIF4B and the poly(A)-binding protein can occur during both apoptosis and picornaviral infection and is likely to contribute to the inhibition of translation observed under these conditions."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":959,"end":964},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"}],"text":"Disruption of the interaction of mammalian protein synthesis eukaryotic initiation factor 4B with the poly(A)-binding protein by caspase- and viral protease-mediated cleavages.\nEukaryotic initiation factor (eIF) 4B interacts with several components of the initiation pathway and is targeted for cleavage during apoptosis. In a cell-free system, cleavage of eIF4B by caspase-3 coincides with a general inhibition of protein synthetic activity. Affinity chromatography demonstrates that mammalian eIF4B interacts with the poly(A)-binding protein and that a region consisting of the N-terminal 80 amino acids of eIF4B is both necessary and sufficient for such binding. This interaction is lost when eIF4B is cleaved by caspase-3, which removes the N-terminal 45 amino acids. Similarly, the association of eIF4B with the poly(A)-binding protein in vivo is reduced when cells are induced to undergo apoptosis. Cleavage of the poly(A)-binding protein itself, using human rhinovirus 3C protease, also eliminates the interaction with eIF4B. Thus, disruption of the association between mammalian eIF4B and the poly(A)-binding protein can occur during both apoptosis and picornaviral infection and is likely to contribute to the inhibition of translation observed under these conditions."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":102,"end":106},"obj":"Cell"},{"id":"T3","span":{"begin":520,"end":524},"obj":"Cell"},{"id":"T5","span":{"begin":817,"end":821},"obj":"Cell"},{"id":"T7","span":{"begin":921,"end":925},"obj":"Cell"},{"id":"T9","span":{"begin":1101,"end":1105},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A2","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A4","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A6","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A7","pred":"cl_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A8","pred":"cl_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL:0000775"},{"id":"A9","pred":"cl_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A10","pred":"cl_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/CL:0000775"}],"text":"Disruption of the interaction of mammalian protein synthesis eukaryotic initiation factor 4B with the poly(A)-binding protein by caspase- and viral protease-mediated cleavages.\nEukaryotic initiation factor (eIF) 4B interacts with several components of the initiation pathway and is targeted for cleavage during apoptosis. In a cell-free system, cleavage of eIF4B by caspase-3 coincides with a general inhibition of protein synthetic activity. Affinity chromatography demonstrates that mammalian eIF4B interacts with the poly(A)-binding protein and that a region consisting of the N-terminal 80 amino acids of eIF4B is both necessary and sufficient for such binding. This interaction is lost when eIF4B is cleaved by caspase-3, which removes the N-terminal 45 amino acids. Similarly, the association of eIF4B with the poly(A)-binding protein in vivo is reduced when cells are induced to undergo apoptosis. Cleavage of the poly(A)-binding protein itself, using human rhinovirus 3C protease, also eliminates the interaction with eIF4B. Thus, disruption of the association between mammalian eIF4B and the poly(A)-binding protein can occur during both apoptosis and picornaviral infection and is likely to contribute to the inhibition of translation observed under these conditions."}