PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8576111-9 1996 Furthermore, the binding of both forms of NFATp to calcineurin was inhibited by pretreatment of calcineurin with a complex of FK506 and its ligand FKBP12. Tacrolimus 126-131 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 147-153 8717522-3 1996 The FKBP12.FK506 complex specifically binds to and inhibits calcineurin, a signaling protein required for transcriptional activation of the interleukin (IL)-2 gene in response to T cell antigen receptor engagement. Tacrolimus 11-16 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 4-10 9371677-3 1997 METHODS: We investigated the relationship between the presence of anti-FKBP12 autoantibodies and rejection episodes in 47 patients treated with FK506 after living-related partial liver transplantation (LRLT). Tacrolimus 144-149 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 71-77 7592869-1 1995 FK506, an immunosuppressant that prolongs allograft survival, is a co-drug with its intracellular receptor, FKBP12. Tacrolimus 0-5 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 108-114 7592869-2 1995 The FKBP12.FK506 complex inhibits calcineurin, a critical signaling molecule during T-cell activation. Tacrolimus 11-16 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 4-10 7592869-3 1995 FKBP12 was, until recently, the sole FKBP known to mediate calcineurin inhibition at clinically relevant FK506 concentrations. Tacrolimus 105-110 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 0-6 7592869-7 1995 In transfected Jurkat cells, FKBP12.6 is equivalent to FKBP12 at mediating the inhibitory effects of FK506. Tacrolimus 101-106 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 29-35 7507662-0 1994 Catalytic and ligand binding properties of the FK506 binding protein FKBP12: effects of the single amino acid substitution of Tyr82 to Leu. Tacrolimus 47-52 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 69-75 9383417-3 1995 Rapamycin, ascomycin and FK506 have a common domain responsible for binding to FKBP12, their cellular receptor, and different effector domains that determine the target of the complex. Tacrolimus 25-30 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 79-85 9383417-7 1995 CONCLUSIONS: The designed rapamycin-based FKBP12 ligand exhibits powerful binding properties but, unlike rapamycin, shows no activity in IL-6 dependent B-cell proliferation and, in contrast to FK506, shows no activity in the IL-2 reporter assay. Tacrolimus 193-198 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 42-48 7521210-7 1994 To gain insight into the mechanism of FK506"s regulation of PR action, we questioned whether calcineurin is involved, because it has been shown that FK506 is a specific inhibitor of calcineurin, a Ca(2+)- and calmodulin-regulated phosphatase, through the formation of an FKBP12-FK506-calcineurin-calmodulin complex. Tacrolimus 149-154 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 271-277 7521210-7 1994 To gain insight into the mechanism of FK506"s regulation of PR action, we questioned whether calcineurin is involved, because it has been shown that FK506 is a specific inhibitor of calcineurin, a Ca(2+)- and calmodulin-regulated phosphatase, through the formation of an FKBP12-FK506-calcineurin-calmodulin complex. Tacrolimus 149-154 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 271-277 8008069-1 1994 The structurally related natural products rapamycin and FK506 bind to the same intracellular receptor, FKBP12, yet the resulting complexes interfere with distinct signalling pathways. Tacrolimus 56-61 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 103-109 7512379-1 1994 Backbone dynamics of the ligand- (FK506-) bound protein FKBP-12 (107 amino acids) have been examined using 15N relaxation data derived from inverse-detected two-dimensional 1H-15N NMR spectra. Tacrolimus 34-39 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 56-63 7518356-1 1994 The immunosuppressants rapamycin and FK506 bind to the same intracellular protein, the immunophilin FKBP12. Tacrolimus 37-42 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 100-106 7507662-1 1994 The binding of FK506 and rapamycin to their cytosolic receptor FKBP12 is an intermediate step in the paths leading to their potent immunosuppressive properties. Tacrolimus 15-20 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 63-69 11437371-4 2001 Ascomycin, an FK506 analogue, was identified for the first time as a drug which can disrupt the FKBP12-RyR1 complex. Tacrolimus 14-19 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 96-102 7690248-1 1993 Backbone dynamics of the major tacrolimus (FK506) binding protein (FKBP-12, 107 amino acids) have been studied using 15N relaxation data derived from proton-detected two-dimensional 1H-15N NMR spectroscopy. Tacrolimus 31-41 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 67-74 7690248-1 1993 Backbone dynamics of the major tacrolimus (FK506) binding protein (FKBP-12, 107 amino acids) have been studied using 15N relaxation data derived from proton-detected two-dimensional 1H-15N NMR spectroscopy. Tacrolimus 43-48 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 67-74 8325502-8 1993 The single immunoblot-positive allele was found to contain a mutation altering a specific residue (Tyr89) which is conserved among the known FKBPs, and which, based on the solution and x-ray structures of human FKBP12, has been proposed to be part of a hydrophobic drug-binding pocket for FK506 and Rm. Tacrolimus 289-294 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 211-217 30707421-3 2019 One potential antifungal drug, FK506, establishes a ternary complex between the phosphatase, calcineurin, and the 12-kDa peptidyl-prolyl isomerase FK506-binding protein, FKBP12. Tacrolimus 31-36 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 170-176 26366742-3 2015 FK506-binding proteins (FKBPs) form a complex with calcineurin in the presence of FK506 (FKBP12-FK506) and inhibit calcineurin activity. Tacrolimus 0-5 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 89-95 26366742-3 2015 FK506-binding proteins (FKBPs) form a complex with calcineurin in the presence of FK506 (FKBP12-FK506) and inhibit calcineurin activity. Tacrolimus 82-87 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 89-95 26366742-6 2015 Deletional analysis of the four genes revealed that the Deltafkbp12-1 strain was resistant to FK506, indicating FKBP12-1 as the key mediator of FK506-binding to calcineurin. Tacrolimus 144-149 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 112-118 26366742-7 2015 The endogenously expressed FKBP12-1-EGFP fusion protein localized to the cytoplasm and nuclei under normal growth conditions but also to the hyphal septa following FK506 treatment, revealing its interaction with calcineurin. Tacrolimus 164-169 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 27-33 26366742-11 2015 Together, these results indicate that while only FKBP12-1 is the bona fide binding partner of FK506, leading to the inhibition of calcineurin in A. fumigatus, FKBP12-4 may play a role in basal growth and the caspofungin-mediated paradoxical growth response. Tacrolimus 94-99 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 49-55 26366742-12 2015 Exploitation of differences between A. fumigatus FKBP12-1 and human FKBP12 will be critical for the generation of fungal-specific FK506 analogs to inhibit fungal calcineurin and treat invasive fungal disease. Tacrolimus 130-135 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 49-55 26366742-12 2015 Exploitation of differences between A. fumigatus FKBP12-1 and human FKBP12 will be critical for the generation of fungal-specific FK506 analogs to inhibit fungal calcineurin and treat invasive fungal disease. Tacrolimus 130-135 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 68-74 30707421-4 2019 It has been well established that calcineurin, highly conserved from yeast to mammals, is necessary for invasive fungal disease and is inhibited when in complex with FK506/FKBP12. Tacrolimus 166-171 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 172-178 30707421-7 2019 Here we report the backbone and sidechain NMR assignments of recombinant FKBP12 proteins from the pathogenic fungi Mucor circinelloides and Aspergillus fumigatus in the apo form and compare these to the backbone assignments of the FK506 bound form. Tacrolimus 231-236 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 73-79 30707421-8 2019 In addition, we report the backbone assignments of the apo and FK506 bound forms of the Homo sapiens FKBP12 protein for evaluation against the fungal forms. Tacrolimus 63-68 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 101-107 30707421-9 2019 These data are the first steps towards defining, at a residue specific level, the impacts of FK506 binding to fungal and mammalian FKBP12 proteins. Tacrolimus 93-98 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 131-137 30879170-2 2019 Human FKBP12 is a prototype of this family and it is involved in many diseases due to its interaction with the immunosuppressive drugs FK506 and rapamycin. Tacrolimus 135-140 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 6-12 24499793-8 2014 This FKBP12-overexpression-induced effect was reverted by FK506. Tacrolimus 58-63 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 5-11 15077060-3 2004 FKBP12 is the mediator of immunosuppressive action of FK506. Tacrolimus 54-59 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 0-6 11335722-1 2001 FKBP12 is a ubiquitous and a highly conserved prolyl isomerase that binds the immunosuppressive drugs FK506 and rapamycin. Tacrolimus 102-107 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 0-6 10551814-7 1999 These actions of B10 were produced only on the cytoplasmic face of the channel, were selectively eliminated by pretreatment of channels with FK506 or rapamycin, and were reconstituted by human recombinant FKBP12. Tacrolimus 141-146 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 205-211 10593895-2 1999 Calcineurin is the target of the immunosuppressive drugs cyclosporin A and FK506 complexed with their cytoplasmic receptors cyclophilin and FKBP12, respectively. Tacrolimus 75-80 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 140-146 9743407-2 1998 The immunosuppressants FK506 and rapamycin both bind to FKBP12 and in turn dissociate the protein from the ryanodine receptor. Tacrolimus 23-28 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 56-62 9831660-10 1998 In this TcFK, 9 out of 15 amino acid residues forming the FK506 binding pocket of human FKBP12 were found. Tacrolimus 58-63 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 88-94 10049913-1 1999 The immunosuppressive drugs FK506 and rapamycin bind to the cellular protein FKBP12, and the resulting FKBP12-drug complexes inhibit signal transduction. Tacrolimus 28-33 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 77-83 10049913-1 1999 The immunosuppressive drugs FK506 and rapamycin bind to the cellular protein FKBP12, and the resulting FKBP12-drug complexes inhibit signal transduction. Tacrolimus 28-33 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 103-109 10049913-9 1999 Because HMG1/2 proteins are conserved from yeast to humans, our findings suggest that FKBP12-HMG1/2 interactions could represent the first conserved function of FKBP12 other than mediating FK506 and rapamycin actions. Tacrolimus 189-194 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 86-92 10049913-9 1999 Because HMG1/2 proteins are conserved from yeast to humans, our findings suggest that FKBP12-HMG1/2 interactions could represent the first conserved function of FKBP12 other than mediating FK506 and rapamycin actions. Tacrolimus 189-194 FKBP prolyl isomerase 1A pseudogene 1 Homo sapiens 161-167