PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10200280-2	1999	Depriving cells of amino acids or treating them with the small molecule rapamycin inhibits FRAP and results in rapid dephosphorylation and inactivation of the translational regulators 4E-BP1(eukaryotic initiation factor 4E-binding protein 1) and p70(s6k) (the 70-kDa S6 kinase).	Sirolimus	72-81	ribosomal protein S6 kinase B1	Homo sapiens	246-253	
10200280-5	1999	A calyculin A-sensitive phosphatase is required for the rapamycin- or amino acid deprivation-induced dephosphorylation of p70(s6k), and treatment of Jurkat I cells with rapamycin increases the activity of the protein phosphatase 2A (PP2A) toward 4E-BP1.	Sirolimus	56-65	ribosomal protein S6 kinase B1	Homo sapiens	122-129	
10200280-7	1999	FRAP also is shown to phosphorylate PP2A in vitro, consistent with a model in which phosphorylation of PP2A by FRAP prevents the dephosphorylation of 4E-BP1 and p70(s6k), whereas amino acid deprivation or rapamycin treatment inhibits FRAP"s ability to restrain the phosphatase.	Sirolimus	205-214	ribosomal protein S6 kinase B1	Homo sapiens	161-168