PubMed:19732724 JSONTXT

{"project":"LitCoin-PubTator-for-Tuning","denotations":[{"id":"2","span":{"begin":4,"end":12},"obj":"GeneOrGeneProduct"},{"id":"3","span":{"begin":69,"end":72},"obj":"GeneOrGeneProduct"},{"id":"24","span":{"begin":150,"end":161},"obj":"DiseaseOrPhenotypicFeature"},{"id":"25","span":{"begin":163,"end":176},"obj":"DiseaseOrPhenotypicFeature"},{"id":"26","span":{"begin":182,"end":190},"obj":"DiseaseOrPhenotypicFeature"},{"id":"27","span":{"begin":203,"end":211},"obj":"GeneOrGeneProduct"},{"id":"28","span":{"begin":373,"end":381},"obj":"GeneOrGeneProduct"},{"id":"29","span":{"begin":424,"end":427},"obj":"GeneOrGeneProduct"},{"id":"30","span":{"begin":429,"end":438},"obj":"ChemicalEntity"},{"id":"31","span":{"begin":498,"end":506},"obj":"GeneOrGeneProduct"},{"id":"32","span":{"begin":537,"end":546},"obj":"ChemicalEntity"},{"id":"33","span":{"begin":581,"end":586},"obj":"OrganismTaxon"},{"id":"34","span":{"begin":587,"end":600},"obj":"DiseaseOrPhenotypicFeature"},{"id":"35","span":{"begin":608,"end":616},"obj":"GeneOrGeneProduct"},{"id":"36","span":{"begin":617,"end":626},"obj":"ChemicalEntity"},{"id":"37","span":{"begin":651,"end":654},"obj":"GeneOrGeneProduct"},{"id":"38","span":{"begin":676,"end":690},"obj":"DiseaseOrPhenotypicFeature"},{"id":"39","span":{"begin":709,"end":719},"obj":"DiseaseOrPhenotypicFeature"},{"id":"40","span":{"begin":731,"end":736},"obj":"DiseaseOrPhenotypicFeature"},{"id":"41","span":{"begin":777,"end":785},"obj":"GeneOrGeneProduct"},{"id":"42","span":{"begin":793,"end":801},"obj":"GeneOrGeneProduct"},{"id":"43","span":{"begin":847,"end":850},"obj":"GeneOrGeneProduct"}],"attributes":[{"id":"A34","pred":"tao:has_database_id","subj":"34","obj":"MESH:D001943"},{"id":"A40","pred":"tao:has_database_id","subj":"40","obj":"MESH:D009369"},{"id":"A37","pred":"tao:has_database_id","subj":"37","obj":"Gene:20779"},{"id":"A42","pred":"tao:has_database_id","subj":"42","obj":"Gene:319939"},{"id":"A30","pred":"tao:has_database_id","subj":"30","obj":"MESH:D014443"},{"id":"A35","pred":"tao:has_database_id","subj":"35","obj":"Gene:319939"},{"id":"A41","pred":"tao:has_database_id","subj":"41","obj":"Gene:319939"},{"id":"A36","pred":"tao:has_database_id","subj":"36","obj":"MESH:D014443"},{"id":"A3","pred":"tao:has_database_id","subj":"3","obj":"Gene:20779"},{"id":"A38","pred":"tao:has_database_id","subj":"38","obj":"MESH:D009369"},{"id":"A24","pred":"tao:has_database_id","subj":"24","obj":"MESH:D008175"},{"id":"A27","pred":"tao:has_database_id","subj":"27","obj":"Gene:319939"},{"id":"A2","pred":"tao:has_database_id","subj":"2","obj":"Gene:319939"},{"id":"A28","pred":"tao:has_database_id","subj":"28","obj":"Gene:319939"},{"id":"A39","pred":"tao:has_database_id","subj":"39","obj":"MESH:D009362"},{"id":"A32","pred":"tao:has_database_id","subj":"32","obj":"MESH:D014443"},{"id":"A29","pred":"tao:has_database_id","subj":"29","obj":"Gene:20779"},{"id":"A25","pred":"tao:has_database_id","subj":"25","obj":"MESH:D001943"},{"id":"A33","pred":"tao:has_database_id","subj":"33","obj":"Tax:10090"},{"id":"A26","pred":"tao:has_database_id","subj":"26","obj":"MESH:D008545"},{"id":"A31","pred":"tao:has_database_id","subj":"31","obj":"Gene:319939"},{"id":"A43","pred":"tao:has_database_id","subj":"43","obj":"Gene:20779"}],"text":"The Tensin-3 protein, including its SH2 domain, is phosphorylated by Src and contributes to tumorigenesis and metastasis.\nIn cell lines from advanced lung cancer, breast cancer, and melanoma, endogenous tensin-3 contributes to cell migration, anchorage-independent growth, and tumorigenesis. Although SH2 domains have not been reported previously to be phosphorylated, the tensin-3 SH2 domain is a physiologic substrate for Src. Tyrosines in the SH2 domain contribute to the biological activity of tensin-3, and phosphorylation of these tyrosines can regulate ligand binding. In a mouse breast cancer model, tensin-3 tyrosines are phosphorylated in a Src-associated manner in primary tumors, and experimental metastases induced by tumor-derived cell lines depend on endogenous tensin-3. Thus, tensin-3 is implicated as an oncoprotein regulated by Src and possessing an SH2 domain with a previously undescribed mechanism for the regulation of ligand binding."}

{"project":"LitCoin-Disease-Tuning-1","denotations":[{"id":"T1","span":{"begin":92,"end":105},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T2","span":{"begin":110,"end":120},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T3","span":{"begin":150,"end":161},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T4","span":{"begin":163,"end":176},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T5","span":{"begin":182,"end":190},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T6","span":{"begin":277,"end":290},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T7","span":{"begin":587,"end":600},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T8","span":{"begin":684,"end":690},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T10","span":{"begin":709,"end":719},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T11","span":{"begin":731,"end":736},"obj":"DiseaseOrPhenotypicFeature"}],"attributes":[{"id":"A6","pred":"ID:","subj":"T6","obj":"D063646"},{"id":"A3","pred":"ID:","subj":"T3","obj":"D008175"},{"id":"A8","pred":"ID:","subj":"T8","obj":"DISEASE"},{"id":"A9","pred":"ID:","subj":"T8","obj":"D009369"},{"id":"A4","pred":"ID:","subj":"T4","obj":"D001943"},{"id":"A7","pred":"ID:","subj":"T7","obj":"D001943"},{"id":"A10","pred":"ID:","subj":"T10","obj":"D009362"},{"id":"A2","pred":"ID:","subj":"T2","obj":"D009362"},{"id":"A1","pred":"ID:","subj":"T1","obj":"D063646"},{"id":"A5","pred":"ID:","subj":"T5","obj":"D008545"},{"id":"A11","pred":"ID:","subj":"T11","obj":"D009369"}],"text":"The Tensin-3 protein, including its SH2 domain, is phosphorylated by Src and contributes to tumorigenesis and metastasis.\nIn cell lines from advanced lung cancer, breast cancer, and melanoma, endogenous tensin-3 contributes to cell migration, anchorage-independent growth, and tumorigenesis. Although SH2 domains have not been reported previously to be phosphorylated, the tensin-3 SH2 domain is a physiologic substrate for Src. Tyrosines in the SH2 domain contribute to the biological activity of tensin-3, and phosphorylation of these tyrosines can regulate ligand binding. In a mouse breast cancer model, tensin-3 tyrosines are phosphorylated in a Src-associated manner in primary tumors, and experimental metastases induced by tumor-derived cell lines depend on endogenous tensin-3. Thus, tensin-3 is implicated as an oncoprotein regulated by Src and possessing an SH2 domain with a previously undescribed mechanism for the regulation of ligand binding."}

{"project":"LitCoin-PubTator_CellLine","denotations":[{"id":"T1","span":{"begin":36,"end":39},"obj":"CellLine"},{"id":"T3","span":{"begin":301,"end":304},"obj":"CellLine"},{"id":"T5","span":{"begin":382,"end":385},"obj":"CellLine"},{"id":"T7","span":{"begin":446,"end":449},"obj":"CellLine"},{"id":"T9","span":{"begin":869,"end":872},"obj":"CellLine"}],"attributes":[{"id":"A1","pred":"cellosaurus_accession_id","subj":"T1","obj":"CVCL_C723"},{"id":"A2","pred":"cellosaurus_accession_id","subj":"T1","obj":"CVCL_M622"},{"id":"A7","pred":"cellosaurus_accession_id","subj":"T7","obj":"CVCL_C723"},{"id":"A8","pred":"cellosaurus_accession_id","subj":"T7","obj":"CVCL_M622"},{"id":"A3","pred":"cellosaurus_accession_id","subj":"T3","obj":"CVCL_C723"},{"id":"A4","pred":"cellosaurus_accession_id","subj":"T3","obj":"CVCL_M622"},{"id":"A9","pred":"cellosaurus_accession_id","subj":"T9","obj":"CVCL_C723"},{"id":"A10","pred":"cellosaurus_accession_id","subj":"T9","obj":"CVCL_M622"},{"id":"A5","pred":"cellosaurus_accession_id","subj":"T5","obj":"CVCL_C723"},{"id":"A6","pred":"cellosaurus_accession_id","subj":"T5","obj":"CVCL_M622"}],"text":"The Tensin-3 protein, including its SH2 domain, is phosphorylated by Src and contributes to tumorigenesis and metastasis.\nIn cell lines from advanced lung cancer, breast cancer, and melanoma, endogenous tensin-3 contributes to cell migration, anchorage-independent growth, and tumorigenesis. Although SH2 domains have not been reported previously to be phosphorylated, the tensin-3 SH2 domain is a physiologic substrate for Src. Tyrosines in the SH2 domain contribute to the biological activity of tensin-3, and phosphorylation of these tyrosines can regulate ligand binding. In a mouse breast cancer model, tensin-3 tyrosines are phosphorylated in a Src-associated manner in primary tumors, and experimental metastases induced by tumor-derived cell lines depend on endogenous tensin-3. Thus, tensin-3 is implicated as an oncoprotein regulated by Src and possessing an SH2 domain with a previously undescribed mechanism for the regulation of ligand binding."}

{"project":"LitEisuke","denotations":[{"id":"T1","span":{"begin":92,"end":105},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T2","span":{"begin":150,"end":161},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T3","span":{"begin":163,"end":176},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T4","span":{"begin":182,"end":190},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T5","span":{"begin":277,"end":290},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T6","span":{"begin":587,"end":600},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T7","span":{"begin":684,"end":690},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T8","span":{"begin":709,"end":719},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T9","span":{"begin":731,"end":736},"obj":"DiseaseOrPhenotypicFeature"}],"attributes":[{"id":"A2","pred":"#label","subj":"T2","obj":"D008175"},{"id":"A7","pred":"#label","subj":"T7","obj":"D009369"},{"id":"A5","pred":"#label","subj":"T5","obj":"D063646"},{"id":"A4","pred":"#label","subj":"T4","obj":"D008545"},{"id":"A1","pred":"#label","subj":"T1","obj":"D063646"},{"id":"A9","pred":"#label","subj":"T9","obj":"D009369"},{"id":"A8","pred":"#label","subj":"T8","obj":"D009362"},{"id":"A6","pred":"#label","subj":"T6","obj":"D001943"},{"id":"A3","pred":"#label","subj":"T3","obj":"D001943"}],"text":"The Tensin-3 protein, including its SH2 domain, is phosphorylated by Src and contributes to tumorigenesis and metastasis.\nIn cell lines from advanced lung cancer, breast cancer, and melanoma, endogenous tensin-3 contributes to cell migration, anchorage-independent growth, and tumorigenesis. Although SH2 domains have not been reported previously to be phosphorylated, the tensin-3 SH2 domain is a physiologic substrate for Src. Tyrosines in the SH2 domain contribute to the biological activity of tensin-3, and phosphorylation of these tyrosines can regulate ligand binding. In a mouse breast cancer model, tensin-3 tyrosines are phosphorylated in a Src-associated manner in primary tumors, and experimental metastases induced by tumor-derived cell lines depend on endogenous tensin-3. Thus, tensin-3 is implicated as an oncoprotein regulated by Src and possessing an SH2 domain with a previously undescribed mechanism for the regulation of ligand binding."}

{"project":"DisGeNET","denotations":[{"id":"T0","span":{"begin":4,"end":12},"obj":"gene:64759"},{"id":"T1","span":{"begin":92,"end":105},"obj":"disease:C0596263"},{"id":"T2","span":{"begin":4,"end":12},"obj":"gene:64759"},{"id":"T3","span":{"begin":110,"end":120},"obj":"disease:C0027627"},{"id":"T4","span":{"begin":4,"end":12},"obj":"gene:64759"},{"id":"T5","span":{"begin":110,"end":120},"obj":"disease:C2939420"},{"id":"T6","span":{"begin":203,"end":211},"obj":"gene:64759"},{"id":"T7","span":{"begin":277,"end":290},"obj":"disease:C0596263"}],"relations":[{"id":"R1","pred":"associated_with","subj":"T0","obj":"T1"},{"id":"R2","pred":"associated_with","subj":"T2","obj":"T3"},{"id":"R3","pred":"associated_with","subj":"T4","obj":"T5"},{"id":"R4","pred":"associated_with","subj":"T6","obj":"T7"}],"namespaces":[{"prefix":"gene","uri":"http://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"disease","uri":"http://purl.bioontology.org/ontology/MEDLINEPLUS/"}],"text":"The Tensin-3 protein, including its SH2 domain, is phosphorylated by Src and contributes to tumorigenesis and metastasis.\nIn cell lines from advanced lung cancer, breast cancer, and melanoma, endogenous tensin-3 contributes to cell migration, anchorage-independent growth, and tumorigenesis. Although SH2 domains have not been reported previously to be phosphorylated, the tensin-3 SH2 domain is a physiologic substrate for Src. Tyrosines in the SH2 domain contribute to the biological activity of tensin-3, and phosphorylation of these tyrosines can regulate ligand binding. In a mouse breast cancer model, tensin-3 tyrosines are phosphorylated in a Src-associated manner in primary tumors, and experimental metastases induced by tumor-derived cell lines depend on endogenous tensin-3. Thus, tensin-3 is implicated as an oncoprotein regulated by Src and possessing an SH2 domain with a previously undescribed mechanism for the regulation of ligand binding."}

{"project":"DisGeNET5_gene_disease","denotations":[{"id":"19732724-0#4#12#gene64759","span":{"begin":4,"end":12},"obj":"gene64759"},{"id":"19732724-0#110#120#diseaseC0027627","span":{"begin":110,"end":120},"obj":"diseaseC0027627"},{"id":"19732724-0#92#105#diseaseC0596263","span":{"begin":92,"end":105},"obj":"diseaseC0596263"}],"relations":[{"id":"4#12#gene64759110#120#diseaseC0027627","pred":"associated_with","subj":"19732724-0#4#12#gene64759","obj":"19732724-0#110#120#diseaseC0027627"},{"id":"4#12#gene6475992#105#diseaseC0596263","pred":"associated_with","subj":"19732724-0#4#12#gene64759","obj":"19732724-0#92#105#diseaseC0596263"}],"text":"The Tensin-3 protein, including its SH2 domain, is phosphorylated by Src and contributes to tumorigenesis and metastasis.\nIn cell lines from advanced lung cancer, breast cancer, and melanoma, endogenous tensin-3 contributes to cell migration, anchorage-independent growth, and tumorigenesis. Although SH2 domains have not been reported previously to be phosphorylated, the tensin-3 SH2 domain is a physiologic substrate for Src. Tyrosines in the SH2 domain contribute to the biological activity of tensin-3, and phosphorylation of these tyrosines can regulate ligand binding. In a mouse breast cancer model, tensin-3 tyrosines are phosphorylated in a Src-associated manner in primary tumors, and experimental metastases induced by tumor-derived cell lines depend on endogenous tensin-3. Thus, tensin-3 is implicated as an oncoprotein regulated by Src and possessing an SH2 domain with a previously undescribed mechanism for the regulation of ligand binding."}