PubMed:1310678 JSONTXT

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":92},"obj":"Sentence"},{"id":"T2","span":{"begin":93,"end":336},"obj":"Sentence"},{"id":"T3","span":{"begin":337,"end":544},"obj":"Sentence"},{"id":"T4","span":{"begin":545,"end":853},"obj":"Sentence"},{"id":"T5","span":{"begin":854,"end":1005},"obj":"Sentence"},{"id":"T6","span":{"begin":1006,"end":1167},"obj":"Sentence"},{"id":"T7","span":{"begin":1168,"end":1435},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":92},"obj":"Sentence"},{"id":"T2","span":{"begin":93,"end":336},"obj":"Sentence"},{"id":"T3","span":{"begin":337,"end":544},"obj":"Sentence"},{"id":"T4","span":{"begin":545,"end":853},"obj":"Sentence"},{"id":"T5","span":{"begin":854,"end":1005},"obj":"Sentence"},{"id":"T6","span":{"begin":1006,"end":1167},"obj":"Sentence"},{"id":"T7","span":{"begin":1168,"end":1435},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Reconstitution of the multiprotein complex of pp60src, hsp90, and p50 in a cell-free system.\nA rabbit reticulocyte lysate system that has been used to reconstitute functional complexes between steroid receptors and the 90-kDa heat shock protein (hsp90) has been used here to form complexes between the pp60src tyrosine kinase and hsp90. Reticulocyte lysate forms complexes between hsp90 and a temperature-sensitive mutant of Rous sarcoma virus pp60v-src, which is normally present in cytosol virtually entirely in the multiprotein complex form. In addition, hsp90 in the lysate complexes with wild-type pp60v-src, of which only a small portion is normally recovered in cytosol in the native multiprotein complex, and with the cellular homolog, pp60c-src, which has never been recovered in cytosol in the form of a native multiprotein complex with hsp90. Moreover, the reticulocyte lysate-reconstituted complex also contains the 50-kDa phosphoprotein component of the native pp60v-src multiprotein complex. The native and reconstituted pp60src-hsp90 complexes have similar thermal stability and, like steroid receptor heterocomplexes, they are stabilized by molybdate. As previously shown with reticulocyte lysate-reconstituted steroid receptor heteroprotein complexes, the reconstituted pp60src multiprotein complex contains hsp70, which is a major candidate for providing the protein unfoldase activity required for hsp90 association."}

{"project":"FSU-PRGE","denotations":[{"id":"T1","span":{"begin":46,"end":53},"obj":"protein"},{"id":"T2","span":{"begin":55,"end":60},"obj":"protein"},{"id":"T3","span":{"begin":193,"end":210},"obj":"protein"},{"id":"T4","span":{"begin":219,"end":244},"obj":"protein"},{"id":"T5","span":{"begin":246,"end":251},"obj":"protein"},{"id":"T6","span":{"begin":302,"end":309},"obj":"protein"},{"id":"T7","span":{"begin":310,"end":325},"obj":"protein"},{"id":"T8","span":{"begin":330,"end":335},"obj":"protein"},{"id":"T9","span":{"begin":381,"end":386},"obj":"protein"},{"id":"T10","span":{"begin":444,"end":453},"obj":"protein"},{"id":"T11","span":{"begin":558,"end":563},"obj":"protein"},{"id":"T12","span":{"begin":603,"end":612},"obj":"protein"},{"id":"T13","span":{"begin":744,"end":753},"obj":"protein"},{"id":"T14","span":{"begin":847,"end":852},"obj":"protein"},{"id":"T15","span":{"begin":974,"end":983},"obj":"protein"},{"id":"T16","span":{"begin":1035,"end":1042},"obj":"protein"},{"id":"T17","span":{"begin":1043,"end":1048},"obj":"protein"},{"id":"T18","span":{"begin":1100,"end":1116},"obj":"protein"},{"id":"T19","span":{"begin":1227,"end":1243},"obj":"protein"},{"id":"T20","span":{"begin":1287,"end":1294},"obj":"protein"},{"id":"T21","span":{"begin":1325,"end":1330},"obj":"protein"},{"id":"T22","span":{"begin":1417,"end":1422},"obj":"protein"}],"text":"Reconstitution of the multiprotein complex of pp60src, hsp90, and p50 in a cell-free system.\nA rabbit reticulocyte lysate system that has been used to reconstitute functional complexes between steroid receptors and the 90-kDa heat shock protein (hsp90) has been used here to form complexes between the pp60src tyrosine kinase and hsp90. Reticulocyte lysate forms complexes between hsp90 and a temperature-sensitive mutant of Rous sarcoma virus pp60v-src, which is normally present in cytosol virtually entirely in the multiprotein complex form. In addition, hsp90 in the lysate complexes with wild-type pp60v-src, of which only a small portion is normally recovered in cytosol in the native multiprotein complex, and with the cellular homolog, pp60c-src, which has never been recovered in cytosol in the form of a native multiprotein complex with hsp90. Moreover, the reticulocyte lysate-reconstituted complex also contains the 50-kDa phosphoprotein component of the native pp60v-src multiprotein complex. The native and reconstituted pp60src-hsp90 complexes have similar thermal stability and, like steroid receptor heterocomplexes, they are stabilized by molybdate. As previously shown with reticulocyte lysate-reconstituted steroid receptor heteroprotein complexes, the reconstituted pp60src multiprotein complex contains hsp70, which is a major candidate for providing the protein unfoldase activity required for hsp90 association."}

{"project":"AIMed","denotations":[{"id":"T1","span":{"begin":46,"end":53},"obj":"protein"},{"id":"T2","span":{"begin":55,"end":60},"obj":"protein"},{"id":"T3","span":{"begin":66,"end":69},"obj":"protein"},{"id":"T4","span":{"begin":246,"end":251},"obj":"protein"},{"id":"T5","span":{"begin":302,"end":309},"obj":"protein"},{"id":"T6","span":{"begin":330,"end":335},"obj":"protein"},{"id":"T7","span":{"begin":381,"end":386},"obj":"protein"},{"id":"T8","span":{"begin":444,"end":453},"obj":"protein"},{"id":"T9","span":{"begin":558,"end":563},"obj":"protein"},{"id":"T10","span":{"begin":603,"end":612},"obj":"protein"},{"id":"T11","span":{"begin":744,"end":753},"obj":"protein"},{"id":"T12","span":{"begin":847,"end":852},"obj":"protein"},{"id":"T13","span":{"begin":974,"end":983},"obj":"protein"},{"id":"T14","span":{"begin":1035,"end":1042},"obj":"protein"},{"id":"T15","span":{"begin":1043,"end":1048},"obj":"protein"},{"id":"T16","span":{"begin":1287,"end":1294},"obj":"protein"},{"id":"T17","span":{"begin":1325,"end":1330},"obj":"protein"},{"id":"T18","span":{"begin":1417,"end":1422},"obj":"protein"}],"text":"Reconstitution of the multiprotein complex of pp60src, hsp90, and p50 in a cell-free system.\nA rabbit reticulocyte lysate system that has been used to reconstitute functional complexes between steroid receptors and the 90-kDa heat shock protein (hsp90) has been used here to form complexes between the pp60src tyrosine kinase and hsp90. Reticulocyte lysate forms complexes between hsp90 and a temperature-sensitive mutant of Rous sarcoma virus pp60v-src, which is normally present in cytosol virtually entirely in the multiprotein complex form. In addition, hsp90 in the lysate complexes with wild-type pp60v-src, of which only a small portion is normally recovered in cytosol in the native multiprotein complex, and with the cellular homolog, pp60c-src, which has never been recovered in cytosol in the form of a native multiprotein complex with hsp90. Moreover, the reticulocyte lysate-reconstituted complex also contains the 50-kDa phosphoprotein component of the native pp60v-src multiprotein complex. The native and reconstituted pp60src-hsp90 complexes have similar thermal stability and, like steroid receptor heterocomplexes, they are stabilized by molybdate. As previously shown with reticulocyte lysate-reconstituted steroid receptor heteroprotein complexes, the reconstituted pp60src multiprotein complex contains hsp70, which is a major candidate for providing the protein unfoldase activity required for hsp90 association."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":425,"end":437},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0025382"}],"text":"Reconstitution of the multiprotein complex of pp60src, hsp90, and p50 in a cell-free system.\nA rabbit reticulocyte lysate system that has been used to reconstitute functional complexes between steroid receptors and the 90-kDa heat shock protein (hsp90) has been used here to form complexes between the pp60src tyrosine kinase and hsp90. Reticulocyte lysate forms complexes between hsp90 and a temperature-sensitive mutant of Rous sarcoma virus pp60v-src, which is normally present in cytosol virtually entirely in the multiprotein complex form. In addition, hsp90 in the lysate complexes with wild-type pp60v-src, of which only a small portion is normally recovered in cytosol in the native multiprotein complex, and with the cellular homolog, pp60c-src, which has never been recovered in cytosol in the form of a native multiprotein complex with hsp90. Moreover, the reticulocyte lysate-reconstituted complex also contains the 50-kDa phosphoprotein component of the native pp60v-src multiprotein complex. The native and reconstituted pp60src-hsp90 complexes have similar thermal stability and, like steroid receptor heterocomplexes, they are stabilized by molybdate. As previously shown with reticulocyte lysate-reconstituted steroid receptor heteroprotein complexes, the reconstituted pp60src multiprotein complex contains hsp70, which is a major candidate for providing the protein unfoldase activity required for hsp90 association."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":231,"end":236},"obj":"Phenotype"},{"id":"T2","span":{"begin":430,"end":437},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0031273"},{"id":"A2","pred":"hp_id","subj":"T2","obj":"HP:0100242"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Reconstitution of the multiprotein complex of pp60src, hsp90, and p50 in a cell-free system.\nA rabbit reticulocyte lysate system that has been used to reconstitute functional complexes between steroid receptors and the 90-kDa heat shock protein (hsp90) has been used here to form complexes between the pp60src tyrosine kinase and hsp90. Reticulocyte lysate forms complexes between hsp90 and a temperature-sensitive mutant of Rous sarcoma virus pp60v-src, which is normally present in cytosol virtually entirely in the multiprotein complex form. In addition, hsp90 in the lysate complexes with wild-type pp60v-src, of which only a small portion is normally recovered in cytosol in the native multiprotein complex, and with the cellular homolog, pp60c-src, which has never been recovered in cytosol in the form of a native multiprotein complex with hsp90. Moreover, the reticulocyte lysate-reconstituted complex also contains the 50-kDa phosphoprotein component of the native pp60v-src multiprotein complex. The native and reconstituted pp60src-hsp90 complexes have similar thermal stability and, like steroid receptor heterocomplexes, they are stabilized by molybdate. As previously shown with reticulocyte lysate-reconstituted steroid receptor heteroprotein complexes, the reconstituted pp60src multiprotein complex contains hsp70, which is a major candidate for providing the protein unfoldase activity required for hsp90 association."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":425,"end":443},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"11886"}],"text":"Reconstitution of the multiprotein complex of pp60src, hsp90, and p50 in a cell-free system.\nA rabbit reticulocyte lysate system that has been used to reconstitute functional complexes between steroid receptors and the 90-kDa heat shock protein (hsp90) has been used here to form complexes between the pp60src tyrosine kinase and hsp90. Reticulocyte lysate forms complexes between hsp90 and a temperature-sensitive mutant of Rous sarcoma virus pp60v-src, which is normally present in cytosol virtually entirely in the multiprotein complex form. In addition, hsp90 in the lysate complexes with wild-type pp60v-src, of which only a small portion is normally recovered in cytosol in the native multiprotein complex, and with the cellular homolog, pp60c-src, which has never been recovered in cytosol in the form of a native multiprotein complex with hsp90. Moreover, the reticulocyte lysate-reconstituted complex also contains the 50-kDa phosphoprotein component of the native pp60v-src multiprotein complex. The native and reconstituted pp60src-hsp90 complexes have similar thermal stability and, like steroid receptor heterocomplexes, they are stabilized by molybdate. As previously shown with reticulocyte lysate-reconstituted steroid receptor heteroprotein complexes, the reconstituted pp60src multiprotein complex contains hsp70, which is a major candidate for providing the protein unfoldase activity required for hsp90 association."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":102,"end":114},"obj":"Body_part"},{"id":"T2","span":{"begin":337,"end":349},"obj":"Body_part"},{"id":"T3","span":{"begin":484,"end":491},"obj":"Body_part"},{"id":"T4","span":{"begin":669,"end":676},"obj":"Body_part"},{"id":"T5","span":{"begin":789,"end":796},"obj":"Body_part"},{"id":"T6","span":{"begin":868,"end":880},"obj":"Body_part"},{"id":"T7","span":{"begin":1193,"end":1205},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000558"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000558"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/GO_0005829"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/GO_0005829"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/GO_0005829"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL_0000558"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL_0000558"}],"text":"Reconstitution of the multiprotein complex of pp60src, hsp90, and p50 in a cell-free system.\nA rabbit reticulocyte lysate system that has been used to reconstitute functional complexes between steroid receptors and the 90-kDa heat shock protein (hsp90) has been used here to form complexes between the pp60src tyrosine kinase and hsp90. Reticulocyte lysate forms complexes between hsp90 and a temperature-sensitive mutant of Rous sarcoma virus pp60v-src, which is normally present in cytosol virtually entirely in the multiprotein complex form. In addition, hsp90 in the lysate complexes with wild-type pp60v-src, of which only a small portion is normally recovered in cytosol in the native multiprotein complex, and with the cellular homolog, pp60c-src, which has never been recovered in cytosol in the form of a native multiprotein complex with hsp90. Moreover, the reticulocyte lysate-reconstituted complex also contains the 50-kDa phosphoprotein component of the native pp60v-src multiprotein complex. The native and reconstituted pp60src-hsp90 complexes have similar thermal stability and, like steroid receptor heterocomplexes, they are stabilized by molybdate. As previously shown with reticulocyte lysate-reconstituted steroid receptor heteroprotein complexes, the reconstituted pp60src multiprotein complex contains hsp70, which is a major candidate for providing the protein unfoldase activity required for hsp90 association."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":102,"end":114},"obj":"Cell"},{"id":"T2","span":{"begin":337,"end":349},"obj":"Cell"},{"id":"T3","span":{"begin":868,"end":880},"obj":"Cell"},{"id":"T4","span":{"begin":1193,"end":1205},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000558"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000558"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000558"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000558"}],"text":"Reconstitution of the multiprotein complex of pp60src, hsp90, and p50 in a cell-free system.\nA rabbit reticulocyte lysate system that has been used to reconstitute functional complexes between steroid receptors and the 90-kDa heat shock protein (hsp90) has been used here to form complexes between the pp60src tyrosine kinase and hsp90. Reticulocyte lysate forms complexes between hsp90 and a temperature-sensitive mutant of Rous sarcoma virus pp60v-src, which is normally present in cytosol virtually entirely in the multiprotein complex form. In addition, hsp90 in the lysate complexes with wild-type pp60v-src, of which only a small portion is normally recovered in cytosol in the native multiprotein complex, and with the cellular homolog, pp60c-src, which has never been recovered in cytosol in the form of a native multiprotein complex with hsp90. Moreover, the reticulocyte lysate-reconstituted complex also contains the 50-kDa phosphoprotein component of the native pp60v-src multiprotein complex. The native and reconstituted pp60src-hsp90 complexes have similar thermal stability and, like steroid receptor heterocomplexes, they are stabilized by molybdate. As previously shown with reticulocyte lysate-reconstituted steroid receptor heteroprotein complexes, the reconstituted pp60src multiprotein complex contains hsp70, which is a major candidate for providing the protein unfoldase activity required for hsp90 association."}