Nanopublications LDF server

Matches in Nanopublications for { ?s ?p "The rapamycin-sensitive component in the 4E-BP1 phosphorylation pathway is FRAP/mTOR (FKBP12-rapamycin associated protein/mammalian target of rapamycin), also known as RAFT1 (rapamycin and 12-kD FK506 binding protein target 1), a member of the PIK (phosphoinositide kinase-related) family of kinases. (from full text) A recombinant FRAP/mTOR protein and a FRAP/mTOR immunoprecipitate were utilized in in vitro kinase assays to phosphorylate 4E-BP1. Phosphopeptide mapping of the in vitro-labeled protein yielded two 4E-BP1 phosphopeptides that comigrated with phosphopeptides produced in vivo. Mass spectrometry analysis indicated that these peptides contain phosphorylated Thr-37 and Thr-46. Thr-37 and Thr-46 are efficiently phosphorylated in vitro by FRAP/mTOR when 4E-BP1 is bound to eIF4E." ?g. }

• _7 value "The rapamycin-sensitive component in the 4E-BP1 phosphorylation pathway is FRAP/mTOR (FKBP12-rapamycin associated protein/mammalian target of rapamycin), also known as RAFT1 (rapamycin and 12-kD FK506 binding protein target 1), a member of the PIK (phosphoinositide kinase-related) family of kinases. (from full text) A recombinant FRAP/mTOR protein and a FRAP/mTOR immunoprecipitate were utilized in in vitro kinase assays to phosphorylate 4E-BP1. Phosphopeptide mapping of the in vitro-labeled protein yielded two 4E-BP1 phosphopeptides that comigrated with phosphopeptides produced in vivo. Mass spectrometry analysis indicated that these peptides contain phosphorylated Thr-37 and Thr-46. Thr-37 and Thr-46 are efficiently phosphorylated in vitro by FRAP/mTOR when 4E-BP1 is bound to eIF4E." provenance.
• _5 value "The rapamycin-sensitive component in the 4E-BP1 phosphorylation pathway is FRAP/mTOR (FKBP12-rapamycin associated protein/mammalian target of rapamycin), also known as RAFT1 (rapamycin and 12-kD FK506 binding protein target 1), a member of the PIK (phosphoinositide kinase-related) family of kinases. (from full text) A recombinant FRAP/mTOR protein and a FRAP/mTOR immunoprecipitate were utilized in in vitro kinase assays to phosphorylate 4E-BP1. Phosphopeptide mapping of the in vitro-labeled protein yielded two 4E-BP1 phosphopeptides that comigrated with phosphopeptides produced in vivo. Mass spectrometry analysis indicated that these peptides contain phosphorylated Thr-37 and Thr-46. Thr-37 and Thr-46 are efficiently phosphorylated in vitro by FRAP/mTOR when 4E-BP1 is bound to eIF4E." provenance.
• _7 value "The rapamycin-sensitive component in the 4E-BP1 phosphorylation pathway is FRAP/mTOR (FKBP12-rapamycin associated protein/mammalian target of rapamycin), also known as RAFT1 (rapamycin and 12-kD FK506 binding protein target 1), a member of the PIK (phosphoinositide kinase-related) family of kinases. (from full text) A recombinant FRAP/mTOR protein and a FRAP/mTOR immunoprecipitate were utilized in in vitro kinase assays to phosphorylate 4E-BP1. Phosphopeptide mapping of the in vitro-labeled protein yielded two 4E-BP1 phosphopeptides that comigrated with phosphopeptides produced in vivo. Mass spectrometry analysis indicated that these peptides contain phosphorylated Thr-37 and Thr-46. Thr-37 and Thr-46 are efficiently phosphorylated in vitro by FRAP/mTOR when 4E-BP1 is bound to eIF4E." provenance.
• _5 value "The rapamycin-sensitive component in the 4E-BP1 phosphorylation pathway is FRAP/mTOR (FKBP12-rapamycin associated protein/mammalian target of rapamycin), also known as RAFT1 (rapamycin and 12-kD FK506 binding protein target 1), a member of the PIK (phosphoinositide kinase-related) family of kinases. (from full text) A recombinant FRAP/mTOR protein and a FRAP/mTOR immunoprecipitate were utilized in in vitro kinase assays to phosphorylate 4E-BP1. Phosphopeptide mapping of the in vitro-labeled protein yielded two 4E-BP1 phosphopeptides that comigrated with phosphopeptides produced in vivo. Mass spectrometry analysis indicated that these peptides contain phosphorylated Thr-37 and Thr-46. Thr-37 and Thr-46 are efficiently phosphorylated in vitro by FRAP/mTOR when 4E-BP1 is bound to eIF4E." provenance.