PubMed:17339318 JSONTXT

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":84},"obj":"Sentence"},{"id":"T2","span":{"begin":85,"end":333},"obj":"Sentence"},{"id":"T3","span":{"begin":334,"end":599},"obj":"Sentence"},{"id":"T4","span":{"begin":600,"end":687},"obj":"Sentence"},{"id":"T5","span":{"begin":688,"end":782},"obj":"Sentence"},{"id":"T6","span":{"begin":783,"end":896},"obj":"Sentence"},{"id":"T7","span":{"begin":897,"end":1098},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Interaction of hydroxylated collagen IV with the von hippel-lindau tumor suppressor.\nThe von Hippel-Lindau tumor suppressor (pVHL) targets hydroxylated alpha-subunits of hypoxia-inducible factor (HIF) for ubiquitin-mediated proteasomal destruction through direct interaction with the hydroxyproline binding pocket in its beta-domain. Although disruption of this process may contribute to VHL-associated tumor predisposition by up-regulation of HIF target genes, genetic and biochemical analyses support the existence of additional functions, including a role in the assembly of extracellular matrix. In an attempt to delineate these pathways, we searched for novel pVHL-binding proteins. Here we report a direct, hydroxylation-dependent interaction with alpha-chains of collagen IV. Interaction with pVHL was also observed with fibrillar collagen chains, but not the folded collagen triple helix. The interaction was suppressed by a wide range of tumor-associated mutations, including those that do not disturb the regulation of HIF, supporting a role in HIF-independent tumor suppressor functions."}

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":107,"end":112},"obj":"HP_0002664"},{"id":"T2","span":{"begin":403,"end":408},"obj":"HP_0002664"},{"id":"T3","span":{"begin":947,"end":952},"obj":"HP_0002664"},{"id":"T4","span":{"begin":1071,"end":1076},"obj":"HP_0002664"}],"text":"Interaction of hydroxylated collagen IV with the von hippel-lindau tumor suppressor.\nThe von Hippel-Lindau tumor suppressor (pVHL) targets hydroxylated alpha-subunits of hypoxia-inducible factor (HIF) for ubiquitin-mediated proteasomal destruction through direct interaction with the hydroxyproline binding pocket in its beta-domain. Although disruption of this process may contribute to VHL-associated tumor predisposition by up-regulation of HIF target genes, genetic and biochemical analyses support the existence of additional functions, including a role in the assembly of extracellular matrix. In an attempt to delineate these pathways, we searched for novel pVHL-binding proteins. Here we report a direct, hydroxylation-dependent interaction with alpha-chains of collagen IV. Interaction with pVHL was also observed with fibrillar collagen chains, but not the folded collagen triple helix. The interaction was suppressed by a wide range of tumor-associated mutations, including those that do not disturb the regulation of HIF, supporting a role in HIF-independent tumor suppressor functions."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":67,"end":72},"obj":"Disease"},{"id":"T2","span":{"begin":107,"end":112},"obj":"Disease"},{"id":"T3","span":{"begin":388,"end":391},"obj":"Disease"},{"id":"T4","span":{"begin":403,"end":408},"obj":"Disease"},{"id":"T5","span":{"begin":947,"end":952},"obj":"Disease"},{"id":"T6","span":{"begin":1071,"end":1076},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005070"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0005070"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0008667"},{"id":"A4","pred":"mondo_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MONDO_0005070"},{"id":"A5","pred":"mondo_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MONDO_0005070"},{"id":"A6","pred":"mondo_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MONDO_0005070"}],"text":"Interaction of hydroxylated collagen IV with the von hippel-lindau tumor suppressor.\nThe von Hippel-Lindau tumor suppressor (pVHL) targets hydroxylated alpha-subunits of hypoxia-inducible factor (HIF) for ubiquitin-mediated proteasomal destruction through direct interaction with the hydroxyproline binding pocket in its beta-domain. Although disruption of this process may contribute to VHL-associated tumor predisposition by up-regulation of HIF target genes, genetic and biochemical analyses support the existence of additional functions, including a role in the assembly of extracellular matrix. In an attempt to delineate these pathways, we searched for novel pVHL-binding proteins. Here we report a direct, hydroxylation-dependent interaction with alpha-chains of collagen IV. Interaction with pVHL was also observed with fibrillar collagen chains, but not the folded collagen triple helix. The interaction was suppressed by a wide range of tumor-associated mutations, including those that do not disturb the regulation of HIF, supporting a role in HIF-independent tumor suppressor functions."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":578,"end":598},"obj":"Body_part"},{"id":"T2","span":{"begin":890,"end":895},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0031012"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0002488"}],"text":"Interaction of hydroxylated collagen IV with the von hippel-lindau tumor suppressor.\nThe von Hippel-Lindau tumor suppressor (pVHL) targets hydroxylated alpha-subunits of hypoxia-inducible factor (HIF) for ubiquitin-mediated proteasomal destruction through direct interaction with the hydroxyproline binding pocket in its beta-domain. Although disruption of this process may contribute to VHL-associated tumor predisposition by up-regulation of HIF target genes, genetic and biochemical analyses support the existence of additional functions, including a role in the assembly of extracellular matrix. In an attempt to delineate these pathways, we searched for novel pVHL-binding proteins. Here we report a direct, hydroxylation-dependent interaction with alpha-chains of collagen IV. Interaction with pVHL was also observed with fibrillar collagen chains, but not the folded collagen triple helix. The interaction was suppressed by a wide range of tumor-associated mutations, including those that do not disturb the regulation of HIF, supporting a role in HIF-independent tumor suppressor functions."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":67,"end":72},"obj":"Phenotype"},{"id":"T2","span":{"begin":107,"end":112},"obj":"Phenotype"},{"id":"T3","span":{"begin":170,"end":177},"obj":"Phenotype"},{"id":"T4","span":{"begin":403,"end":408},"obj":"Phenotype"},{"id":"T5","span":{"begin":947,"end":952},"obj":"Phenotype"},{"id":"T6","span":{"begin":1071,"end":1076},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0002664"},{"id":"A2","pred":"hp_id","subj":"T2","obj":"HP:0002664"},{"id":"A3","pred":"hp_id","subj":"T3","obj":"HP:0012418"},{"id":"A4","pred":"hp_id","subj":"T4","obj":"HP:0002664"},{"id":"A5","pred":"hp_id","subj":"T5","obj":"HP:0002664"},{"id":"A6","pred":"hp_id","subj":"T6","obj":"HP:0002664"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Interaction of hydroxylated collagen IV with the von hippel-lindau tumor suppressor.\nThe von Hippel-Lindau tumor suppressor (pVHL) targets hydroxylated alpha-subunits of hypoxia-inducible factor (HIF) for ubiquitin-mediated proteasomal destruction through direct interaction with the hydroxyproline binding pocket in its beta-domain. Although disruption of this process may contribute to VHL-associated tumor predisposition by up-regulation of HIF target genes, genetic and biochemical analyses support the existence of additional functions, including a role in the assembly of extracellular matrix. In an attempt to delineate these pathways, we searched for novel pVHL-binding proteins. Here we report a direct, hydroxylation-dependent interaction with alpha-chains of collagen IV. Interaction with pVHL was also observed with fibrillar collagen chains, but not the folded collagen triple helix. The interaction was suppressed by a wide range of tumor-associated mutations, including those that do not disturb the regulation of HIF, supporting a role in HIF-independent tumor suppressor functions."}