PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 31152486-2 2019 Tacrolimus (TAC) and rapamycin (Rapa) both bind to FK506-binding protein 12 (FKBP12). Tacrolimus 0-10 FKBP prolyl isomerase 1A Rattus norvegicus 51-75 31152486-2 2019 Tacrolimus (TAC) and rapamycin (Rapa) both bind to FK506-binding protein 12 (FKBP12). Tacrolimus 0-10 FKBP prolyl isomerase 1A Rattus norvegicus 77-83 31152486-2 2019 Tacrolimus (TAC) and rapamycin (Rapa) both bind to FK506-binding protein 12 (FKBP12). Tacrolimus 12-15 FKBP prolyl isomerase 1A Rattus norvegicus 51-75 31152486-2 2019 Tacrolimus (TAC) and rapamycin (Rapa) both bind to FK506-binding protein 12 (FKBP12). Tacrolimus 12-15 FKBP prolyl isomerase 1A Rattus norvegicus 77-83 31152486-10 2019 In silico docking and immunoprecipitation experiments confirmed that TAC can form a stable noncovalent interaction with FKBP12-mTOR. Tacrolimus 69-72 FKBP prolyl isomerase 1A Rattus norvegicus 120-126 29229832-3 2017 Calcineurin can be inhibited with Tacrolimus through the recruitment and inhibition of the 12-kDa cis-trans proline isomerase FK506-binding protein (FKBP12). Tacrolimus 34-44 FKBP prolyl isomerase 1A Rattus norvegicus 149-155 30476735-11 2019 FK506 inhibited NFAT translocation to the nucleus and disrupted the interaction of TRPC6 with FKBP12. Tacrolimus 0-5 FKBP prolyl isomerase 1A Rattus norvegicus 94-100 29229832-7 2017 Using a rat model of PD, partial elimination of the functional interaction between FKBP12 and calcineurin, with low doses of the Food and Drug Administration (FDA)-approved compound Tacrolimus, blocks calcineurin"s activity toward those proteins and protects against the toxic hallmarks of alpha-syn pathology. Tacrolimus 182-192 FKBP prolyl isomerase 1A Rattus norvegicus 83-89 24291098-6 2014 FK506-binding proteins 1a and 1b (FKBP1a/1b, also known as FKBP12/12.6) are immunophilin proteins that bind the immunosuppressant drugs FK506 and rapamycin. Tacrolimus 0-5 FKBP prolyl isomerase 1A Rattus norvegicus 59-65 21255728-3 2011 A variety of inhibitors of the PI activity of FKBP12, including FK506, rapamycin, and cycloheximide, increase steady-state palmitoylation. Tacrolimus 64-69 FKBP prolyl isomerase 1A Rattus norvegicus 46-52 23867624-3 2013 The best response was achieved with FK506 (tacrolimus), via a dual mechanism of action as a calcineurin inhibitor that also binds FK-binding protein-12 (FKBP12), a repressor of BMP signaling. Tacrolimus 36-41 FKBP prolyl isomerase 1A Rattus norvegicus 130-151 23867624-3 2013 The best response was achieved with FK506 (tacrolimus), via a dual mechanism of action as a calcineurin inhibitor that also binds FK-binding protein-12 (FKBP12), a repressor of BMP signaling. Tacrolimus 36-41 FKBP prolyl isomerase 1A Rattus norvegicus 153-159 23867624-3 2013 The best response was achieved with FK506 (tacrolimus), via a dual mechanism of action as a calcineurin inhibitor that also binds FK-binding protein-12 (FKBP12), a repressor of BMP signaling. Tacrolimus 43-53 FKBP prolyl isomerase 1A Rattus norvegicus 130-151 23867624-3 2013 The best response was achieved with FK506 (tacrolimus), via a dual mechanism of action as a calcineurin inhibitor that also binds FK-binding protein-12 (FKBP12), a repressor of BMP signaling. Tacrolimus 43-53 FKBP prolyl isomerase 1A Rattus norvegicus 153-159 23867624-4 2013 FK506 released FKBP12 from type I receptors activin receptor-like kinase 1 (ALK1), ALK2, and ALK3 and activated downstream SMAD1/5 and MAPK signaling and ID1 gene regulation in a manner superior to the calcineurin inhibitor cyclosporine and the FKBP12 ligand rapamycin. Tacrolimus 0-5 FKBP prolyl isomerase 1A Rattus norvegicus 15-21 23867624-4 2013 FK506 released FKBP12 from type I receptors activin receptor-like kinase 1 (ALK1), ALK2, and ALK3 and activated downstream SMAD1/5 and MAPK signaling and ID1 gene regulation in a manner superior to the calcineurin inhibitor cyclosporine and the FKBP12 ligand rapamycin. Tacrolimus 0-5 FKBP prolyl isomerase 1A Rattus norvegicus 245-251 18577426-4 2008 FK506 may exert neuroprotection via inhibition of calcineurin by binding the FKBP12, or by binding other immunophilins such as FKBP52, leading to modulation of heat shock proteins (Hsp) 90 and 70. Tacrolimus 0-5 FKBP prolyl isomerase 1A Rattus norvegicus 77-83 18635947-8 2008 FK506 and its derivatives with no immunosuppressive activities bind to the conserved active sites of the canonical FKBP members such as FKBP12, which shows PPIase activity. Tacrolimus 0-5 FKBP prolyl isomerase 1A Rattus norvegicus 136-142 15994335-6 2005 Binding of FKBP12, calcineurin, and calmodulin to TRPC6 channels is blocked by the following: 1) inhibition of PKC; 2) mutation of the PKC phosphorylation site (Ser(7168/714)) in the channels; or 3) pretreatment with FK506 or rapamycin, immunosuppressants that directly bind FKBP12. Tacrolimus 217-222 FKBP prolyl isomerase 1A Rattus norvegicus 11-17 17877381-1 2007 FKBP-12, a 12 kDa FK506-binding protein (neuroimmunophilin), acts as a receptor for the immunosuppressant drug FK506. Tacrolimus 18-23 FKBP prolyl isomerase 1A Rattus norvegicus 0-7 15780950-1 2005 FK506 is a commonly used immunosuppressant that mediates its action by exclusively interacting with the cytosolic immunophilin, FK506 binding protein 12 (FKBP12). Tacrolimus 0-5 FKBP prolyl isomerase 1A Rattus norvegicus 128-152 15780950-1 2005 FK506 is a commonly used immunosuppressant that mediates its action by exclusively interacting with the cytosolic immunophilin, FK506 binding protein 12 (FKBP12). Tacrolimus 0-5 FKBP prolyl isomerase 1A Rattus norvegicus 154-160 12494287-1 2002 To evaluate whether FK506 and other immunophilin ligands may have potential therapeutic efficacy for erectile function preservation after penile nerve injury, we demonstrated localizations of the immunophilin FK506 binding protein 12 (FKBP 12) in intact and injured rat penile nerves and correlated these findings with localizations of neuronal nitric oxide synthase (nNOS), which neuronally forms nitric oxide for mediation of penile erection, in response to systemically administered FK506. Tacrolimus 20-25 FKBP prolyl isomerase 1A Rattus norvegicus 235-242 12927209-5 2003 After 90 min of transient middle cerebral artery occlusion in male rats the expression of FKBP12, 52 and 65 was analyzed by Western blot in FK506-treated and control animals and the peptidyl-prolyl cis/trans isomerase activity was determined. Tacrolimus 140-145 FKBP prolyl isomerase 1A Rattus norvegicus 90-96 12927209-14 2003 It was shown for the first time that neuroprotection by FK506 also included the suppression of the cerebral peptidyl-prolyl cis/trans isomerase activity of FKBP in vivo whereas the expression levels of FKBP12, 52 and 65 following ischemia changed slightly and FK506 treatment does not suppress the expression patterns. Tacrolimus 56-61 FKBP prolyl isomerase 1A Rattus norvegicus 202-208 12494287-1 2002 To evaluate whether FK506 and other immunophilin ligands may have potential therapeutic efficacy for erectile function preservation after penile nerve injury, we demonstrated localizations of the immunophilin FK506 binding protein 12 (FKBP 12) in intact and injured rat penile nerves and correlated these findings with localizations of neuronal nitric oxide synthase (nNOS), which neuronally forms nitric oxide for mediation of penile erection, in response to systemically administered FK506. Tacrolimus 209-214 FKBP prolyl isomerase 1A Rattus norvegicus 235-242 12183690-1 2002 The polyketides FK506 (tacrolimus) and FK520 (ascomycin) are potent immunosuppressants that function by inhibiting calcineurin phosphatase through formation of an FKBP12-FK506/520-calcineurin ternary complex. Tacrolimus 16-21 FKBP prolyl isomerase 1A Rattus norvegicus 163-169 12183690-1 2002 The polyketides FK506 (tacrolimus) and FK520 (ascomycin) are potent immunosuppressants that function by inhibiting calcineurin phosphatase through formation of an FKBP12-FK506/520-calcineurin ternary complex. Tacrolimus 23-33 FKBP prolyl isomerase 1A Rattus norvegicus 163-169 12183690-3 2002 Based on the crystal structure of the FKBP12-FK506-calcineurin complex, we deduced that the 13- and 15-methoxy groups of FK506 or FK520 are important for inhibition of calcineurin phosphatase but not for binding to FKBP12. Tacrolimus 45-50 FKBP prolyl isomerase 1A Rattus norvegicus 38-44 12183690-3 2002 Based on the crystal structure of the FKBP12-FK506-calcineurin complex, we deduced that the 13- and 15-methoxy groups of FK506 or FK520 are important for inhibition of calcineurin phosphatase but not for binding to FKBP12. Tacrolimus 45-50 FKBP prolyl isomerase 1A Rattus norvegicus 215-221 12183690-3 2002 Based on the crystal structure of the FKBP12-FK506-calcineurin complex, we deduced that the 13- and 15-methoxy groups of FK506 or FK520 are important for inhibition of calcineurin phosphatase but not for binding to FKBP12. Tacrolimus 121-126 FKBP prolyl isomerase 1A Rattus norvegicus 38-44 12183690-3 2002 Based on the crystal structure of the FKBP12-FK506-calcineurin complex, we deduced that the 13- and 15-methoxy groups of FK506 or FK520 are important for inhibition of calcineurin phosphatase but not for binding to FKBP12. Tacrolimus 121-126 FKBP prolyl isomerase 1A Rattus norvegicus 215-221 10566134-15 1999 FK 506 promotes axonal regeneration through binding to FKBP-12, thus activating GAP-43 (growth associated protein) and the TGF beta 1-pathway (transforming growth factor). Tacrolimus 0-6 FKBP prolyl isomerase 1A Rattus norvegicus 55-62 11041285-10 2000 A strong immunostaining for FKBP-12, a tacrolimus-binding protein, was observed in the medulla of the kidneys of rats treated with tacrolimus either with or without furosemide. Tacrolimus 39-49 FKBP prolyl isomerase 1A Rattus norvegicus 28-35 12671210-15 2000 FK 506 promotes axonal regeneration through binding to FKBP-12. Tacrolimus 0-6 FKBP prolyl isomerase 1A Rattus norvegicus 55-62 11772413-6 2002 The effects of FKBP12 were reversed by FK506. Tacrolimus 39-44 FKBP prolyl isomerase 1A Rattus norvegicus 15-21 11359520-1 2001 Immunosuppressant drugs, like FK506, and nonimmunosuppressant compounds like, GPI1046 and L685818, are immunophilin ligands that specifically bind to immunophilins, like FK506 binding protein 12 (FKBP12). Tacrolimus 30-35 FKBP prolyl isomerase 1A Rattus norvegicus 170-194 11359520-1 2001 Immunosuppressant drugs, like FK506, and nonimmunosuppressant compounds like, GPI1046 and L685818, are immunophilin ligands that specifically bind to immunophilins, like FK506 binding protein 12 (FKBP12). Tacrolimus 30-35 FKBP prolyl isomerase 1A Rattus norvegicus 196-202 10752948-5 2000 By gavage, animals were given 5 mg/kg per day of the FKBP12 ligand FK506 in sterile phosphate-buffered saline (PBS) or in PBS alone. Tacrolimus 67-72 FKBP prolyl isomerase 1A Rattus norvegicus 53-59 10752948-11 2000 In addition, the FKBP12 ligand FK506 confers neuroprotection on RGCs after optic nerve crush. Tacrolimus 31-36 FKBP prolyl isomerase 1A Rattus norvegicus 17-23 9918571-3 1999 Drugs binding to FKBP12 and inhibiting calcineurin, such as FK506 and SDZ ASM 981, dose dependently reduced the infarct volumes, determined 48 h after MCAO by both magnetic resonance imaging and triphenyltetrazolium chloride staining but only in the transient MCAO model. Tacrolimus 60-65 FKBP prolyl isomerase 1A Rattus norvegicus 17-23 9457703-2 1997 FK506 is inactive by itself and requires binding to an FK506 binding protein-12 (FKBP-12), or immunophilin, for activation. Tacrolimus 0-5 FKBP prolyl isomerase 1A Rattus norvegicus 55-79 9653668-1 1998 Since FK506 binding protein (FKBP12) inhibits dose-dependently the immunosuppressive activity of FK506 in vitro, plasma FKBP12 levels were measured after rat small bowel transplantation (SBTx). Tacrolimus 6-11 FKBP prolyl isomerase 1A Rattus norvegicus 29-35 9653668-5 1998 Therefore, the plasma FKBP12 level should be considered as one of the parameters related to the immunosuppressive activity of FK506 in SBTx. Tacrolimus 126-131 FKBP prolyl isomerase 1A Rattus norvegicus 22-28 9555045-5 1998 These results suggest that modulation of the activity of the Ca2+-dependent K+ channel by FK506 and rapamycin is directly through association of immunosuppressants with FKBP12. Tacrolimus 90-95 FKBP prolyl isomerase 1A Rattus norvegicus 169-175 9457703-2 1997 FK506 is inactive by itself and requires binding to an FK506 binding protein-12 (FKBP-12), or immunophilin, for activation. Tacrolimus 0-5 FKBP prolyl isomerase 1A Rattus norvegicus 81-88 9457703-9 1997 The nerve regenerative property of this class of agents is separate from their immunosuppressant action because FK506-related compounds that bind to FKBP-12 but do not inhibit calcineurin are also able to increase nerve regeneration. Tacrolimus 112-117 FKBP prolyl isomerase 1A Rattus norvegicus 149-156 1380976-6 1992 Recently, it was found that the complex of FKBP-12 with FK-506, but not with RAP, inhibits the phosphatase activity of calcineurin. Tacrolimus 56-62 FKBP prolyl isomerase 1A Rattus norvegicus 43-50 9344552-1 1997 The immunosuppressant drugs FK506 and cyclosporin A inhibit T-cell proliferation via a common mechanism: calcineurin inhibition following binding to their respective binding proteins, the peptidyl prolyl isomerases FKBP-12 and cyclophilin A. Tacrolimus 28-33 FKBP prolyl isomerase 1A Rattus norvegicus 215-222 8623162-1 1996 FK506 blocks T cell activation by preventing the transcription of lymphokine genes through binding to the intracellular protein FKBP12 and formation of complex that inhibits the phosphatase activity of calcineurin. Tacrolimus 0-5 FKBP prolyl isomerase 1A Rattus norvegicus 128-134 7539960-10 1995 Thus, as in the case with NF-AT in T cells, these findings point to the reduction of unidentified nuclear factors for insulin mRNA transcription caused by the binding of FK506 to FKBP-12 and a subsequent inhibition of calcineurin in the beta-cells. Tacrolimus 170-175 FKBP prolyl isomerase 1A Rattus norvegicus 179-186 1380976-4 1992 FK-506 is known to interact with FK-binding protein-12 (FKBP-12), an abundant cytosolic protein with cis-trans peptidyl-prolyl isomerase activity (PPIase) activity. Tacrolimus 0-6 FKBP prolyl isomerase 1A Rattus norvegicus 33-54 1380976-4 1992 FK-506 is known to interact with FK-binding protein-12 (FKBP-12), an abundant cytosolic protein with cis-trans peptidyl-prolyl isomerase activity (PPIase) activity. Tacrolimus 0-6 FKBP prolyl isomerase 1A Rattus norvegicus 56-63