PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31683063-4	2020	We show here that both an ATP-independent protein chaperone, Spy L32P, and the FK506 binding domain of a prolyl isomerase, FKBP-25 F145A/I223P, are disordered, yet exhibit structures that are distinct from chemically denatured unfolded states in solution, and that they undergo transitions to a more structured state upon ligand binding.	Tacrolimus	79-84	FKBP prolyl isomerase 3	Homo sapiens	123-130	
1375932-6	1992	The PPIase activity of FKBP25 was far more sensitive to inhibition by rapamycin (IC50 = 50 nM) than FK506 (IC50 = 400 nM).	Tacrolimus	100-105	FKBP prolyl isomerase 3	Homo sapiens	23-29	
1375932-7	1992	PPIase activity of 100 nM FKBP25 was almost completely inhibited by 150 nM rapamycin while only 90% inhibition was achieved by 4 microM FK506.	Tacrolimus	136-141	FKBP prolyl isomerase 3	Homo sapiens	26-32	
1375932-8	1992	These data demonstrate that FKBP25 has a higher affinity for rapamycin than for FK506 and suggest that this cellular receptor may be an important target molecule for immunosuppression by rapamycin.	Tacrolimus	80-85	FKBP prolyl isomerase 3	Homo sapiens	28-34	
31683063-7	2020	The protein-ligand systems studied here (the ATP-independent protein chaperone, Spy L32P, and the FK506 binding domain of a prolyl isomerase, FKBP-25 F145A/I223P) may serve as models for understanding ligand-induced disorder-to-order transitions in proteins.	Tacrolimus	98-103	FKBP prolyl isomerase 3	Homo sapiens	142-149	
26762975-4	2016	The FKBP25 structure revealed that the N-terminal helix-loop-helix (HLH) domain and C-terminal FK506-binding domain (FKBD) interact with each other and that both of the domains are involved in DNA binding.	Tacrolimus	95-100	FKBP prolyl isomerase 3	Homo sapiens	4-10	
26792730-6	2016	Treatment of Jurkat T cells with CsA plus FK506 led to a time-dependent conformational change in overexpressed human CrkII1-236 protein-containing FRET-based biosensor, supporting the accumulation of cis conformers of human CrkII1-236 in the presence of PPIase inhibitors.	Tacrolimus	42-47	FKBP prolyl isomerase 3	Homo sapiens	254-260	
26749369-0	2016	Crystal structure of the FK506 binding domain of human FKBP25 in complex with FK506.	Tacrolimus	25-30	FKBP prolyl isomerase 3	Homo sapiens	55-61	
26749369-0	2016	Crystal structure of the FK506 binding domain of human FKBP25 in complex with FK506.	Tacrolimus	78-83	FKBP prolyl isomerase 3	Homo sapiens	55-61	
26749369-2	2016	Similar to other FKBPs, FK506 binding domain (FKBD) of hFKBP25 also binds to immunosuppressive drugs such as rapamycin and FK506, albeit with a lower affinity for the latter.	Tacrolimus	24-29	FKBP prolyl isomerase 3	Homo sapiens	55-62	
26749369-2	2016	Similar to other FKBPs, FK506 binding domain (FKBD) of hFKBP25 also binds to immunosuppressive drugs such as rapamycin and FK506, albeit with a lower affinity for the latter.	Tacrolimus	123-128	FKBP prolyl isomerase 3	Homo sapiens	55-62	
26239116-9	2015	FK506 modified the pattern of association between FKBP25 and TRPCs as well as impaired OAG-evoked TRPC3 and TRPC6 coupling in both human and mouse platelets.	Tacrolimus	0-5	FKBP prolyl isomerase 3	Homo sapiens	50-56	
24998444-6	2014	Rapamycin or FK506 treatments of the polyribosomes isolated from porcine brain, HeLa and K568 cells caused a residual release of the endogenous FKBP25, which suggests that the immunophilin also binds to some proteins via its PPIase cavity.	Tacrolimus	13-18	FKBP prolyl isomerase 3	Homo sapiens	144-150	
24414276-1	2015	Human FKBP25, a nuclear protein, is a member of FK506 binding protein family (FKBP) and binds to immunosuppressive drugs such as FK506 and rapamycin.	Tacrolimus	48-53	FKBP prolyl isomerase 3	Homo sapiens	6-12	
24998444-6	2014	Rapamycin or FK506 treatments of the polyribosomes isolated from porcine brain, HeLa and K568 cells caused a residual release of the endogenous FKBP25, which suggests that the immunophilin also binds to some proteins via its PPIase cavity.	Tacrolimus	13-18	FKBP prolyl isomerase 3	Homo sapiens	225-231