PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
33502189-0	2021	Phosphoproteomic Analysis and Protein-Protein Interaction of Rat Aorta GJA1 and Rat Heart FKBP1A after Secoiridoid Consumption from Virgin Olive Oil: A Functional Proteomic Approach.	Iridoids	103-114	FKBP prolyl isomerase 1A	Rattus norvegicus	90-96
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
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
31152486-2	2019	Tacrolimus (TAC) and rapamycin (Rapa) both bind to FK506-binding protein 12 (FKBP12).	Sirolimus	21-30	FKBP prolyl isomerase 1A	Rattus norvegicus	51-75
31152486-2	2019	Tacrolimus (TAC) and rapamycin (Rapa) both bind to FK506-binding protein 12 (FKBP12).	Sirolimus	21-30	FKBP prolyl isomerase 1A	Rattus norvegicus	77-83
31152486-2	2019	Tacrolimus (TAC) and rapamycin (Rapa) both bind to FK506-binding protein 12 (FKBP12).	Sirolimus	32-36	FKBP prolyl isomerase 1A	Rattus norvegicus	51-75
31152486-2	2019	Tacrolimus (TAC) and rapamycin (Rapa) both bind to FK506-binding protein 12 (FKBP12).	Sirolimus	32-36	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
31468006-5	2019	In skeletal muscle, statin treatment caused dissociation of the stabilizing protein FK506 binding protein (FKBP12) from the sarcoplasmic reticulum (SR) calcium (Ca2+) release channel, the ryanodine receptor 1, which was associated with pro-apoptotic signaling and reactive nitrogen species/reactive oxygen species (RNS/ROS)-dependent spontaneous SR Ca2+ release events (Ca2+ sparks).	Reactive Nitrogen Species	264-289	FKBP prolyl isomerase 1A	Rattus norvegicus	107-113
31468006-5	2019	In skeletal muscle, statin treatment caused dissociation of the stabilizing protein FK506 binding protein (FKBP12) from the sarcoplasmic reticulum (SR) calcium (Ca2+) release channel, the ryanodine receptor 1, which was associated with pro-apoptotic signaling and reactive nitrogen species/reactive oxygen species (RNS/ROS)-dependent spontaneous SR Ca2+ release events (Ca2+ sparks).	Reactive Oxygen Species	290-313	FKBP prolyl isomerase 1A	Rattus norvegicus	107-113
31468006-5	2019	In skeletal muscle, statin treatment caused dissociation of the stabilizing protein FK506 binding protein (FKBP12) from the sarcoplasmic reticulum (SR) calcium (Ca2+) release channel, the ryanodine receptor 1, which was associated with pro-apoptotic signaling and reactive nitrogen species/reactive oxygen species (RNS/ROS)-dependent spontaneous SR Ca2+ release events (Ca2+ sparks).	Radon	315-318	FKBP prolyl isomerase 1A	Rattus norvegicus	107-113
31468006-5	2019	In skeletal muscle, statin treatment caused dissociation of the stabilizing protein FK506 binding protein (FKBP12) from the sarcoplasmic reticulum (SR) calcium (Ca2+) release channel, the ryanodine receptor 1, which was associated with pro-apoptotic signaling and reactive nitrogen species/reactive oxygen species (RNS/ROS)-dependent spontaneous SR Ca2+ release events (Ca2+ sparks).	Reactive Oxygen Species	319-322	FKBP prolyl isomerase 1A	Rattus norvegicus	107-113
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
29229832-3	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
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
31916935-2	2020	Saturating concentrations (10 micromol/L) of either FKBP12 or 12.6 significantly reduced the frequency, spread, amplitude and Ca2+ spark mass relative to control, while the tomograms revealed both proteins shifted the tetramers into a largely side-by-side configuration.	Calcium	126-130	FKBP prolyl isomerase 1A	Rattus norvegicus	52-58
30999619-2	2019	Immunosuppresive macrolides have been shown to potentiate BMP-2 activity through FKBP12, but these have yet to translate to effective osteoinductive therapies.	Macrolides	17-27	FKBP prolyl isomerase 1A	Rattus norvegicus	81-87
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
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
16547004-3	2006	Here we show that neurotrophic FKBP ligands, such as GPI1046 and N-[methyl(ethoxycarbonyl)]cycloheximide, inhibit the calmodulin/Ca(2+) (CaM/Ca(2+))-regulated FKBP38 with up to 80-fold higher affinity than FKBP12.	GPI 1046	53-60	FKBP prolyl isomerase 1A	Rattus norvegicus	206-212
21293474-0	2011	Isoproterenol-induced FKBP12.6/12 downregulation is modulated by ETA and ETB receptors and reversed by argirhein, a derivative of rhein.	Isoproterenol	0-13	FKBP prolyl isomerase 1A	Rattus norvegicus	22-28
18570278-3	2008	Salvianolic acid B is expected to suppress life-threatening arrhythmias and to restore the abnormality of the RyR2-FKBP12.6 complex in rats.	salvianolic acid B	0-18	FKBP prolyl isomerase 1A	Rattus norvegicus	115-121
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
21255728-3	2011	A variety of inhibitors of the PI activity of FKBP12, including FK506, rapamycin, and cycloheximide, increase steady-state palmitoylation.	Sirolimus	71-80	FKBP prolyl isomerase 1A	Rattus norvegicus	46-52
21255728-3	2011	A variety of inhibitors of the PI activity of FKBP12, including FK506, rapamycin, and cycloheximide, increase steady-state palmitoylation.	Cycloheximide	86-99	FKBP prolyl isomerase 1A	Rattus norvegicus	46-52
19234362-6	2009	It seems that dissociation of FKBP12-RyR leads to conformational changes in RyR that make it difficult for ryanodine to access its binding site.	Ryanodine	107-116	FKBP prolyl isomerase 1A	Rattus norvegicus	30-36
19234362-7	2009	Rapamycin, which is commonly used as a pharmacological tool to disrupt the FKBP12-RyR complex, decreased phenylephrine-induced contractions in RVD epididymal halves.	Sirolimus	0-9	FKBP prolyl isomerase 1A	Rattus norvegicus	75-81
19234362-7	2009	Rapamycin, which is commonly used as a pharmacological tool to disrupt the FKBP12-RyR complex, decreased phenylephrine-induced contractions in RVD epididymal halves.	Phenylephrine	105-118	FKBP prolyl isomerase 1A	Rattus norvegicus	75-81
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
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
17877381-3	2007	In this report, we have utilized several analytical techniques, such as in situ hybridization, Western blotting, two-dimensional gel electrophoresis, and liquid chromatography electrospray tandem mass spectrometry to study the transcriptional expression as well as protein levels of FKBP-12 in the unilateral 6-hydroxydopamine (6-OHDA) rat model of Parkinson"s disease.	Oxidopamine	309-326	FKBP prolyl isomerase 1A	Rattus norvegicus	283-290
17877381-3	2007	In this report, we have utilized several analytical techniques, such as in situ hybridization, Western blotting, two-dimensional gel electrophoresis, and liquid chromatography electrospray tandem mass spectrometry to study the transcriptional expression as well as protein levels of FKBP-12 in the unilateral 6-hydroxydopamine (6-OHDA) rat model of Parkinson"s disease.	Oxidopamine	328-334	FKBP prolyl isomerase 1A	Rattus norvegicus	283-290
17877381-5	2007	We found increased levels of FKBP-12 mRNA and protein in the dorsal and middle part of the 6-OHDA lesioned striatum.	Oxidopamine	91-97	FKBP prolyl isomerase 1A	Rattus norvegicus	29-36
16547004-3	2006	Here we show that neurotrophic FKBP ligands, such as GPI1046 and N-[methyl(ethoxycarbonyl)]cycloheximide, inhibit the calmodulin/Ca(2+) (CaM/Ca(2+))-regulated FKBP38 with up to 80-fold higher affinity than FKBP12.	n-[methyl(ethoxycarbonyl)]cycloheximide	65-104	FKBP prolyl isomerase 1A	Rattus norvegicus	206-212
16547004-3	2006	Here we show that neurotrophic FKBP ligands, such as GPI1046 and N-[methyl(ethoxycarbonyl)]cycloheximide, inhibit the calmodulin/Ca(2+) (CaM/Ca(2+))-regulated FKBP38 with up to 80-fold higher affinity than FKBP12.	cafestol palmitate	137-140	FKBP prolyl isomerase 1A	Rattus norvegicus	206-212
15780950-4	2005	RT-PCR, immunolocalisation and Western blotting studies were employed to identify and characterise FKBP12 in rat primary osteoblasts and osteoblast-like osteosarcoma ROS 17/2.8 cells.	ros	166-169	FKBP prolyl isomerase 1A	Rattus norvegicus	99-105
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.	Serine	161-164	FKBP prolyl isomerase 1A	Rattus norvegicus	11-17
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.	Serine	161-164	FKBP prolyl isomerase 1A	Rattus norvegicus	275-281
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
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.	Sirolimus	226-235	FKBP prolyl isomerase 1A	Rattus norvegicus	11-17
15780950-0	2005	Characterisation of cytosolic FK506 binding protein 12 and its role in modulating expression of Cbfa1 and osterix in ROS 17/2.8 cells.	ros	117-120	FKBP prolyl isomerase 1A	Rattus norvegicus	30-54
15780950-6	2005	The transient exposure of ROS 17/2.8 cells to H2O2 (100 microM) was found to elevate FKBP12 mRNA after 10 min and protein expression after 24 h. Both PTH (10(-9) M) and 1,25 (OH)2D3 (Vitamin D3) (10(-7) M) suppressed FKBP12 protein expression.	ros	26-29	FKBP prolyl isomerase 1A	Rattus norvegicus	85-91
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
15780950-6	2005	The transient exposure of ROS 17/2.8 cells to H2O2 (100 microM) was found to elevate FKBP12 mRNA after 10 min and protein expression after 24 h. Both PTH (10(-9) M) and 1,25 (OH)2D3 (Vitamin D3) (10(-7) M) suppressed FKBP12 protein expression.	ros	26-29	FKBP prolyl isomerase 1A	Rattus norvegicus	217-223
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
15780950-6	2005	The transient exposure of ROS 17/2.8 cells to H2O2 (100 microM) was found to elevate FKBP12 mRNA after 10 min and protein expression after 24 h. Both PTH (10(-9) M) and 1,25 (OH)2D3 (Vitamin D3) (10(-7) M) suppressed FKBP12 protein expression.	Hydrogen Peroxide	46-50	FKBP prolyl isomerase 1A	Rattus norvegicus	85-91
15780950-6	2005	The transient exposure of ROS 17/2.8 cells to H2O2 (100 microM) was found to elevate FKBP12 mRNA after 10 min and protein expression after 24 h. Both PTH (10(-9) M) and 1,25 (OH)2D3 (Vitamin D3) (10(-7) M) suppressed FKBP12 protein expression.	Hydrogen Peroxide	46-50	FKBP prolyl isomerase 1A	Rattus norvegicus	217-223
12871169-5	2003	FKBP12 is associated with IP3 and ryanodine receptors present on the endoplasmic reticulum and plays a role in stabilizing calcium release.	Inositol 1,4,5-Trisphosphate	26-29	FKBP prolyl isomerase 1A	Rattus norvegicus	0-6
12871169-5	2003	FKBP12 is associated with IP3 and ryanodine receptors present on the endoplasmic reticulum and plays a role in stabilizing calcium release.	Calcium	123-130	FKBP prolyl isomerase 1A	Rattus norvegicus	0-6
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.	Polyketides	4-15	FKBP prolyl isomerase 1A	Rattus norvegicus	163-169
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
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.	Nitric Oxide	345-357	FKBP prolyl isomerase 1A	Rattus norvegicus	235-242
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.	immunomycin	39-44	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.	immunomycin	46-55	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
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.	immunomycin	130-135	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.	immunomycin	130-135	FKBP prolyl isomerase 1A	Rattus norvegicus	215-221
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
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
12183690-1	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
11208908-1	2001	ortho-Substituted PCBs mobilize Ca2+ from isolated brain microsomes by interaction with FKBP12/RyR complexes.	Polychlorinated Biphenyls	18-22	FKBP prolyl isomerase 1A	Rattus norvegicus	88-94
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
11772413-5	2002	In the presence of ATP, FKBP12 can also induce co-ordinated gating with neighbouring receptors.	Adenosine Triphosphate	19-22	FKBP prolyl isomerase 1A	Rattus norvegicus	24-30
11772413-6	2002	The effects of FKBP12 were reversed by FK506.	Tacrolimus	39-44	FKBP prolyl isomerase 1A	Rattus norvegicus	15-21
11208908-8	2001	These results revealed that PCB95 disrupts intracellular Ca2+ signaling in PC12 cells by interaction with the FKBP12/RyR complex that in turn accelerated cellular metabolism, possibly affecting signaling between ER and mitochondria.	2,2',3,5',6-pentachlorobiphenyl	28-33	FKBP prolyl isomerase 1A	Rattus norvegicus	110-116
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.	Furosemide	165-175	FKBP prolyl isomerase 1A	Rattus norvegicus	28-35
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
11113532-2	2000	On the other hand, the major physiological role of the immunophilin FK506-binding protein-12 (FKBP12) is a modulation of intracellular calcium flux.	Calcium	135-142	FKBP prolyl isomerase 1A	Rattus norvegicus	94-100
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
9852316-8	1999	Midecamycin (cis, 10-30 microM) activated three of four single native channels, six of eight control-incubated channels and six of seven FKBP12-stripped channels.	midecamycin	0-11	FKBP prolyl isomerase 1A	Rattus norvegicus	137-143
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
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.	Sulfadiazine	70-73	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.	triphenyltetrazolium	195-224	FKBP prolyl isomerase 1A	Rattus norvegicus	17-23
12671210-15	2000	FK 506 promotes axonal regeneration through binding to FKBP-12.	Tacrolimus	0-6	FKBP prolyl isomerase 1A	Rattus norvegicus	55-62
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
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
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
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
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
7822316-5	1995	In the presence of rapamycin, immobilized GST-FKBP12 specifically precipitates similar high molecular mass proteins from both rat brain and murine T-lymphoma cell extracts.	Sirolimus	19-28	FKBP prolyl isomerase 1A	Rattus norvegicus	46-52
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
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
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.	Cyclosporine	38-51	FKBP prolyl isomerase 1A	Rattus norvegicus	215-222
8917502-5	1996	Yeast expressing fusion proteins of the hormone binding domain of the rat glucocorticoid receptor fused to the LexA DNA-binding domain and FKBP12 fused to a transcriptional activation domain activated reporter genes when plated on medium containing the dexamethasone-FK506 heterodimer.	Dexamethasone	253-266	FKBP prolyl isomerase 1A	Rattus norvegicus	139-145
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
1380976-5	1992	Because rapamycin (RAP) similarly binds to FKBP-12, although it acts in a manner different from FK-506, by inhibiting T cell responses to lymphokines, such an interaction with FKBP-12 is not sufficient to mediate immunosuppression.	Sirolimus	8-17	FKBP prolyl isomerase 1A	Rattus norvegicus	43-50
1380976-5	1992	Because rapamycin (RAP) similarly binds to FKBP-12, although it acts in a manner different from FK-506, by inhibiting T cell responses to lymphokines, such an interaction with FKBP-12 is not sufficient to mediate immunosuppression.	Sirolimus	8-17	FKBP prolyl isomerase 1A	Rattus norvegicus	176-183
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