PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
31792195-5	2019	FKBP12.6 induces a relaxation of the central domain that decouples it from the S6 bundle, stabilizing RyR2 in a closed state even in the presence of Ca2+ and PCB95.	2,2',3,5',6-pentachlorobiphenyl	158-163	FKBP prolyl isomerase 1B	Homo sapiens	0-8
30339815-16	2019	Matrine inhibited the disassociation of FKBP12.6 and RyR2, decreased the activity of RyR2, [Ca2+]i, apoptosis, expression levels of cytochrome c and active caspase3 in vivo and in vitro.	matrine	0-7	FKBP prolyl isomerase 1B	Homo sapiens	40-48
28077437-11	2017	The synergistic sensitization of RyRs by catecholaminergic signalling and FKBP12.6 dysfunction destabilized the CICR system, leading to chaotic Ca2+ waves and ventricular arrhythmias.	cicr	112-116	FKBP prolyl isomerase 1B	Homo sapiens	74-82
23747301-1	2013	BACKGROUND: This study was designed to determine whether the cardiac ryanodine receptor (RyR2) central domain, a region associated with catecholamine polymorphic ventricular tachycardia (CPVT) mutations, interacts with the RyR2 regulators, ATP and the FK506-binding protein 12.6 (FKBP12.6).	Catecholamines	136-149	FKBP prolyl isomerase 1B	Homo sapiens	252-278
25980334-5	2015	With Professor Triggle"s assistance, the relationship between an increase in ICa.L and other biological events including an enhancement of IKr and IKr currents, NADPH oxidase and endothelin receptor activation, down regulation of calcium modulating protein FKBP12.6, sarco/endoplasmic reticulum Ca(2+)ATPse (SERCA2A) and calsequens 2 (CASQ2), calcium leak at the diastole and endoplasmic reticulum stress, were evaluated and are discussed.	isocyanic acid	77-80	FKBP prolyl isomerase 1B	Homo sapiens	257-265
24598733-2	2014	With only a single previously reported X-ray structure of FKBP12.6, bound to the immunosuppressant rapamycin, structural inferences for this protein have been drawn from the more extensive studies of the homologous FKBP12.	Sirolimus	99-108	FKBP prolyl isomerase 1B	Homo sapiens	58-66
24598733-3	2014	X-ray structures at 1.70 and 1.90 A resolution from P21 and P3121 crystal forms are reported for an unligated cysteine-free variant of FKBP12.6 which exhibit a notable diversity of conformations.	Cysteine	110-118	FKBP prolyl isomerase 1B	Homo sapiens	135-143
24598733-7	2014	The NMR resonances for 21 backbone amides of FKBP12.6 are doubled, corresponding to a slow conformational transition centered near the tip of the 80s loop, as recently reported for 31 amides of FKBP12.	Amides	35-41	FKBP prolyl isomerase 1B	Homo sapiens	45-53
24598733-7	2014	The NMR resonances for 21 backbone amides of FKBP12.6 are doubled, corresponding to a slow conformational transition centered near the tip of the 80s loop, as recently reported for 31 amides of FKBP12.	Amides	184-190	FKBP prolyl isomerase 1B	Homo sapiens	45-53
28176839-4	2017	We found that a Cu2+ complex readily crosses the bacterial cell wall and inhibits SlyD, which is a molecular chaperone, cis/trans peptidyl prolyl isomerise (PPIase) and involved in various other metabolic pathways.	cupric ion	16-20	FKBP prolyl isomerase 1B	Homo sapiens	157-163
28176839-5	2017	The Cu2+ complex binds to the active sites of SlyD, which suppresses its PPIase and chaperone activities.	cupric ion	4-8	FKBP prolyl isomerase 1B	Homo sapiens	73-79
26092277-5	2015	We used fluorescent CaM, FKBP12.6, and domain-peptide biosensor (F-DPc10) to measure, directly in cardiac myocytes, (1) RyR2 activation by hydrogen peroxide (H2O2)-induced oxidation, (2) RyR2 conformation change caused by oxidation, (3) CaM-RyR2 and FK506-binding protein (FKBP12.6)-RyR2 interaction upon oxidation, and (4) whether dantrolene affects 1-3.	Hydrogen Peroxide	158-162	FKBP prolyl isomerase 1B	Homo sapiens	25-33
26092277-5	2015	We used fluorescent CaM, FKBP12.6, and domain-peptide biosensor (F-DPc10) to measure, directly in cardiac myocytes, (1) RyR2 activation by hydrogen peroxide (H2O2)-induced oxidation, (2) RyR2 conformation change caused by oxidation, (3) CaM-RyR2 and FK506-binding protein (FKBP12.6)-RyR2 interaction upon oxidation, and (4) whether dantrolene affects 1-3.	Hydrogen Peroxide	158-162	FKBP prolyl isomerase 1B	Homo sapiens	273-281
23747301-1	2013	BACKGROUND: This study was designed to determine whether the cardiac ryanodine receptor (RyR2) central domain, a region associated with catecholamine polymorphic ventricular tachycardia (CPVT) mutations, interacts with the RyR2 regulators, ATP and the FK506-binding protein 12.6 (FKBP12.6).	Catecholamines	136-149	FKBP prolyl isomerase 1B	Homo sapiens	280-288
22349148-4	2012	Knockdown of the cellular FK506-binding proteins FKBP1A and FKBP1B in CaCo2 cells prevented replication of HCoV-NL63, suggesting the requirement of these members of the immunophilin family for virus growth.	caco2	70-75	FKBP prolyl isomerase 1B	Homo sapiens	60-66
22618235-7	2012	The general patterns of FKBP12 and FKBP12.6 mRNA expression showed upregulation after hypoxia, downregulation after ischemia and normalization after reperfusion, which was partially attenuated if ROS was added during HEDA.	ros	196-199	FKBP prolyl isomerase 1B	Homo sapiens	35-43
22618235-12	2012	Furthermore, we could demonstrate disturbances of calcium handling in the sarcoplasmic reticulum as well as alterations in the expressions of the calcium handling proteins FKBP12 and FKBP12.6, why this model may be suitable for further studies on ischemia and reperfusion with respect to calcium handling of the sarcoplasmic reticulum.	Calcium	146-153	FKBP prolyl isomerase 1B	Homo sapiens	183-191
22618235-12	2012	Furthermore, we could demonstrate disturbances of calcium handling in the sarcoplasmic reticulum as well as alterations in the expressions of the calcium handling proteins FKBP12 and FKBP12.6, why this model may be suitable for further studies on ischemia and reperfusion with respect to calcium handling of the sarcoplasmic reticulum.	Calcium	146-153	FKBP prolyl isomerase 1B	Homo sapiens	183-191
20518593-0	2011	Hypoxia induces intracellular Ca2+ release by causing reactive oxygen species-mediated dissociation of FK506-binding protein 12.6 from ryanodine receptor 2 in pulmonary artery myocytes.	Reactive Oxygen Species	54-77	FKBP prolyl isomerase 1B	Homo sapiens	103-129
22900083-3	2012	TbPin1 was identified as a novel class of Pin1-type parvulins from Trypanosoma brucei, containing a unique PPIase domain, which can catalyze the isomerization of phosphorylated Ser/Thr-Pro peptide bond.	Serine	177-180	FKBP prolyl isomerase 1B	Homo sapiens	107-113
22900083-3	2012	TbPin1 was identified as a novel class of Pin1-type parvulins from Trypanosoma brucei, containing a unique PPIase domain, which can catalyze the isomerization of phosphorylated Ser/Thr-Pro peptide bond.	Threonine	181-184	FKBP prolyl isomerase 1B	Homo sapiens	107-113
21659649-8	2011	cAMP-dependent protein kinase-phosphorylated RyR2-G230C channels exhibited a significantly higher open probability at diastolic Ca(2+) concentrations, associated with a depletion of calstabin2.	Cyclic AMP	0-4	FKBP prolyl isomerase 1B	Homo sapiens	182-192
22900083-3	2012	TbPin1 was identified as a novel class of Pin1-type parvulins from Trypanosoma brucei, containing a unique PPIase domain, which can catalyze the isomerization of phosphorylated Ser/Thr-Pro peptide bond.	Proline	185-188	FKBP prolyl isomerase 1B	Homo sapiens	107-113
21262961-4	2011	Insertion of GFP after residue Arg-626 abolished the binding of a bulky GST- or cyan fluorescent protein-tagged FKBP12.6 but not the binding of a smaller, nontagged FKBP12.6, suggesting that residue Arg-626 and the dantrolene-binding sequence are located near the FKBP12.6-binding site.	Arginine	31-34	FKBP prolyl isomerase 1B	Homo sapiens	112-120
21262961-4	2011	Insertion of GFP after residue Arg-626 abolished the binding of a bulky GST- or cyan fluorescent protein-tagged FKBP12.6 but not the binding of a smaller, nontagged FKBP12.6, suggesting that residue Arg-626 and the dantrolene-binding sequence are located near the FKBP12.6-binding site.	Dantrolene	215-225	FKBP prolyl isomerase 1B	Homo sapiens	112-120
21262961-5	2011	Using cryo-EM, we have mapped the three-dimensional location of Tyr-846-GFP to domain 9, which is also adjacent to the FKBP12.6-binding site.	Tyrosine	64-67	FKBP prolyl isomerase 1B	Homo sapiens	119-127
21262961-7	2011	Based on the FRET efficiencies of these FRET pairs and the corresponding distance relationships, we mapped the three-dimensional location of Arg-626-GFP or -cyan fluorescent protein, hence the dantrolene-binding sequence, to domain 9 near the FKBP12.6-binding site but distant to the central region around residue Ser-2367.	Arginine	141-144	FKBP prolyl isomerase 1B	Homo sapiens	243-251
21262961-7	2011	Based on the FRET efficiencies of these FRET pairs and the corresponding distance relationships, we mapped the three-dimensional location of Arg-626-GFP or -cyan fluorescent protein, hence the dantrolene-binding sequence, to domain 9 near the FKBP12.6-binding site but distant to the central region around residue Ser-2367.	Dantrolene	193-203	FKBP prolyl isomerase 1B	Homo sapiens	243-251
20518593-1	2011	Here we attempted to test a novel hypothesis that hypoxia may induce Ca(2+) release through reactive oxygen species (ROS)-mediated dissociation of FK506-binding protein 12.6 (FKBP12.6) from ryanodine receptors (RyRs) on the sarcoplasmic reticulum (SR) in pulmonary artery smooth muscle cells (PASMCs).	Reactive Oxygen Species	92-115	FKBP prolyl isomerase 1B	Homo sapiens	147-173
20518593-1	2011	Here we attempted to test a novel hypothesis that hypoxia may induce Ca(2+) release through reactive oxygen species (ROS)-mediated dissociation of FK506-binding protein 12.6 (FKBP12.6) from ryanodine receptors (RyRs) on the sarcoplasmic reticulum (SR) in pulmonary artery smooth muscle cells (PASMCs).	Reactive Oxygen Species	92-115	FKBP prolyl isomerase 1B	Homo sapiens	175-183
20518593-1	2011	Here we attempted to test a novel hypothesis that hypoxia may induce Ca(2+) release through reactive oxygen species (ROS)-mediated dissociation of FK506-binding protein 12.6 (FKBP12.6) from ryanodine receptors (RyRs) on the sarcoplasmic reticulum (SR) in pulmonary artery smooth muscle cells (PASMCs).	Reactive Oxygen Species	117-120	FKBP prolyl isomerase 1B	Homo sapiens	147-173
20518593-1	2011	Here we attempted to test a novel hypothesis that hypoxia may induce Ca(2+) release through reactive oxygen species (ROS)-mediated dissociation of FK506-binding protein 12.6 (FKBP12.6) from ryanodine receptors (RyRs) on the sarcoplasmic reticulum (SR) in pulmonary artery smooth muscle cells (PASMCs).	Reactive Oxygen Species	117-120	FKBP prolyl isomerase 1B	Homo sapiens	175-183
20518593-1	2011	Here we attempted to test a novel hypothesis that hypoxia may induce Ca(2+) release through reactive oxygen species (ROS)-mediated dissociation of FK506-binding protein 12.6 (FKBP12.6) from ryanodine receptors (RyRs) on the sarcoplasmic reticulum (SR) in pulmonary artery smooth muscle cells (PASMCs).	pasmcs	293-299	FKBP prolyl isomerase 1B	Homo sapiens	175-183
20518593-3	2011	The colocalization of FKBP12.6 with RyRs was decreased in intact PASMCs.	pasmcs	65-71	FKBP prolyl isomerase 1B	Homo sapiens	22-30
20518593-4	2011	Pharmacological and genetic inhibition of intracellular ROS generation prevented hypoxia from decreasing FKBP12.6 on the SR and increasing FKBP12.6 in the cytosol.	Reactive Oxygen Species	56-59	FKBP prolyl isomerase 1B	Homo sapiens	105-113
20518593-4	2011	Pharmacological and genetic inhibition of intracellular ROS generation prevented hypoxia from decreasing FKBP12.6 on the SR and increasing FKBP12.6 in the cytosol.	Reactive Oxygen Species	56-59	FKBP prolyl isomerase 1B	Homo sapiens	139-147
20518593-5	2011	Exogenous ROS (H(2)O(2)) reduced FKBP12.6 on the SR and augmented FKBP12.6 in the cytosol.	Reactive Oxygen Species	10-13	FKBP prolyl isomerase 1B	Homo sapiens	33-41
20518593-5	2011	Exogenous ROS (H(2)O(2)) reduced FKBP12.6 on the SR and augmented FKBP12.6 in the cytosol.	Reactive Oxygen Species	10-13	FKBP prolyl isomerase 1B	Homo sapiens	66-74
20518593-7	2011	Hypoxia and H(2)O(2) diminished the association of FKBP12.6 from type 2 RyRs (RyR2).	Hydrogen Peroxide	12-20	FKBP prolyl isomerase 1B	Homo sapiens	51-59
20518593-10	2011	Collectively, we conclude that hypoxia may induce Ca(2+) release by causing ROS-mediated dissociation of FKBP12.6 from RyR2 in PASMCs.	Reactive Oxygen Species	76-79	FKBP prolyl isomerase 1B	Homo sapiens	105-113
20518593-10	2011	Collectively, we conclude that hypoxia may induce Ca(2+) release by causing ROS-mediated dissociation of FKBP12.6 from RyR2 in PASMCs.	pasmcs	127-133	FKBP prolyl isomerase 1B	Homo sapiens	105-113
18759859-15	2009	Rapamycin treatment downregulated the expression of p-ERK1/2, p38 MAPK and Bax in stimulated cardiomyocytes, with or without FKBP12.6 overexpression, and enhanced protein synthesis, but had no effect on DNA synthesis in cardiomyocytes.	Sirolimus	0-9	FKBP prolyl isomerase 1B	Homo sapiens	125-133
20614016-8	2010	Structural modeling, enrichment of CsA-binding proteins from parasite extracts by FPLC, and PPIase activity assays revealed direct interaction of the inhibitor with LmaCyP40, a bifunctional cyclophilin with potential co-chaperone function.	lmacyp40	165-173	FKBP prolyl isomerase 1B	Homo sapiens	92-98
20404344-3	2010	Single-cysteine substitutions were introduced at five positions distributed over the surface of FKBP12.6.	Cysteine	7-15	FKBP prolyl isomerase 1B	Homo sapiens	96-104
19258192-6	2009	The slow refolding step could be partly attributed to proline isomerization, based on an increased rate during refolding in the presence of PPIase and an increased relative amplitude of this step with increasing delay time in double-jump refolding experiments observed over delays of 5-100 s. However, double-jump refolding experiments with delay times longer than 100 s along with size exclusion chromatography and dynamic light scattering of refolding samples showed that the overall refolding yield decreased as bhx was unfolded for longer periods of time.	Proline	54-61	FKBP prolyl isomerase 1B	Homo sapiens	140-146
17606610-3	2007	Hyperphosphorylation at a single amino acid residue, Ser-2808, has been proposed to directly disrupt the binding of a 12.6-kDa FK506-binding protein (FKBP12.6) to RyR2, causing a RyR2 malfunction that triggers cardiac arrhythmias in human heart failure.	Serine	53-56	FKBP prolyl isomerase 1B	Homo sapiens	118-148
18212100-1	2008	Debio-025 is a synthetic cyclosporine with no immunosuppressive capacity but a high inhibitory potency against cyclophilin A (CypA)-associated cis-trans prolyl isomerase (PPIase) activity.	alisporivir	0-9	FKBP prolyl isomerase 1B	Homo sapiens	171-177
18212100-3	2008	For three cyclosporines, the inhibitory potential against PPIase activity was quantitatively correlated with that against human immunodeficiency virus type 1 (HIV-1) replication.	Cyclosporins	10-23	FKBP prolyl isomerase 1B	Homo sapiens	58-64
17921453-6	2007	FK506 increased the amplitude and decreased the frequency of SOICR in HEK293 cells expressing RyR2 with or without FKBP12.6, indicating that the action of FK506 on SOICR is independent of FKBP12.6.	Tacrolimus	0-5	FKBP prolyl isomerase 1B	Homo sapiens	115-123
17869231-0	2007	Inhibition of SR Ca2+ uptake: a novel action of the RyR2-FKBP12.6 antagonist K201.	K201 compound	77-81	FKBP prolyl isomerase 1B	Homo sapiens	57-65
18652778-8	2008	The acute negative inotropic effect of rapamycin on human cardiomyocytes might be due to altered calcium homeostasis through the binding of rapamycin to FKBP12.6 and its regulatory function on the ryanodine receptor, with increased calcium leakage from the sarcoplasmic reticulum.	Calcium	97-104	FKBP prolyl isomerase 1B	Homo sapiens	153-161
18652778-8	2008	The acute negative inotropic effect of rapamycin on human cardiomyocytes might be due to altered calcium homeostasis through the binding of rapamycin to FKBP12.6 and its regulatory function on the ryanodine receptor, with increased calcium leakage from the sarcoplasmic reticulum.	Calcium	232-239	FKBP prolyl isomerase 1B	Homo sapiens	153-161
17606610-3	2007	Hyperphosphorylation at a single amino acid residue, Ser-2808, has been proposed to directly disrupt the binding of a 12.6-kDa FK506-binding protein (FKBP12.6) to RyR2, causing a RyR2 malfunction that triggers cardiac arrhythmias in human heart failure.	Serine	53-56	FKBP prolyl isomerase 1B	Homo sapiens	150-158
17606610-4	2007	To determine the structural basis of the interaction between Ser-2808 and FKBP12.6, we have employed two independent approaches to map this phosphorylation site in RyR2 by three-dimensional cryo-electron microscopy.	Serine	61-64	FKBP prolyl isomerase 1B	Homo sapiens	74-82
17606610-9	2007	Importantly, the three-dimensional location of the Ser-2808 phosphorylation site is 105-120 A distance from the FKBP12.6 binding site mapped previously, indicating that Ser-2808 is unlikely to be directly involved in the binding of FKBP12.6 to RyR2, as had been proposed previously.	Serine	51-54	FKBP prolyl isomerase 1B	Homo sapiens	232-240
16908189-4	2007	All three natively purified proteins have, within experimental error, the same peptidyl-prolyl isomerase (PPIase) activity (k(cat)/K(m) approximately 1 x 10(6)M(-1)s(-1)), and bind a natural inhibitor, rapamycin, with the same high affinity (K(d) approximately 6 nM).	Sirolimus	202-211	FKBP prolyl isomerase 1B	Homo sapiens	106-112
17313373-6	2007	Similarly, K201 was able to suppress spontaneous Ca2+ release in FK506-treated HEK-293 cells co-expressing RyR2 and FKBP12.6.	K201 compound	11-15	FKBP prolyl isomerase 1B	Homo sapiens	116-124
17313373-6	2007	Similarly, K201 was able to suppress spontaneous Ca2+ release in FK506-treated HEK-293 cells co-expressing RyR2 and FKBP12.6.	Tacrolimus	65-70	FKBP prolyl isomerase 1B	Homo sapiens	116-124
17313373-7	2007	Furthermore, K201 suppressed spontaneous Ca2+ release in HEK-293 cells expressing RyR2 alone and in cells co-expressing RyR2 and FKBP12.6 with the same potency.	K201 compound	13-17	FKBP prolyl isomerase 1B	Homo sapiens	129-137
17313373-8	2007	In addition, K201 inhibited [3H]ryanodine binding to RyR2-wt (wild-type) and an RyR2 mutant linked to ventricular tachycardia and sudden death, N4104K, in the absence of FKBP12.6.	K201 compound	13-17	FKBP prolyl isomerase 1B	Homo sapiens	170-178
17200109-4	2007	Using co-immunoprecipitation assays of solubilized native RyR2 from cardiac muscle sarcoplasmic reticulum (SR) with recombinant [(35)S]FKBP12.6, we found that the sulfydryl-oxidizing agents, H(2)O(2) and diamide, result in diminished RyR2-FKBP12.6 binding.	Sulfur-35	129-134	FKBP prolyl isomerase 1B	Homo sapiens	135-143
17200109-4	2007	Using co-immunoprecipitation assays of solubilized native RyR2 from cardiac muscle sarcoplasmic reticulum (SR) with recombinant [(35)S]FKBP12.6, we found that the sulfydryl-oxidizing agents, H(2)O(2) and diamide, result in diminished RyR2-FKBP12.6 binding.	sulfydryl	163-172	FKBP prolyl isomerase 1B	Homo sapiens	135-143
17200109-7	2007	Notably, H(2)O(2) and diamide differentially affected the RyR2-FKBP12.6 interaction, decreasing binding to approximately 75 and approximately 50% of control, respectively.	Hydrogen Peroxide	9-17	FKBP prolyl isomerase 1B	Homo sapiens	63-71
17200109-7	2007	Notably, H(2)O(2) and diamide differentially affected the RyR2-FKBP12.6 interaction, decreasing binding to approximately 75 and approximately 50% of control, respectively.	Diamide	22-29	FKBP prolyl isomerase 1B	Homo sapiens	63-71
17200109-9	2007	A cysteine-null mutant FKBP12.6 retained redox-sensitive interaction with RyR2, suggesting that the effect of the redox reagents is exclusively via sites on the ryanodine receptor.	Cysteine	2-10	FKBP prolyl isomerase 1B	Homo sapiens	23-31
16908189-5	2007	However, refolding of the protein containing the longer tag in vitro results in reduced PPIase activity (the k(cat)/K(m) was reduced from 1 x 10(6)M(-1)s(-1) to 0.81 x 10(6)M(-1)s(-1)) and a 6-fold affinity loss for rapamycin.	Sirolimus	216-225	FKBP prolyl isomerase 1B	Homo sapiens	88-94
17176100-6	2006	Only the FK506 complexes of FKBP12, FKBP12.6, and FKBP51 showed high affinity to CaN; small interfering RNA against these FKBP allowed defining the contribution of individual FKBP in an NFAT reporter gene assay.	Tacrolimus	9-14	FKBP prolyl isomerase 1B	Homo sapiens	36-44
16122887-12	2005	The promoters contain a consensus transcription factor binding sequence for Sp family in FKBP12.6 and Ets-1 in FKBP12.	TFF2 protein, human	76-78	FKBP prolyl isomerase 1B	Homo sapiens	89-97
17959506-6	2006	Simulations of mutant RyR2 suggest that the hyperactive, "leaky" receptors characteristic of reduced FKBP12.6 function may be centrally involved in triggering DADs.	diallyl disulfide	159-163	FKBP prolyl isomerase 1B	Homo sapiens	101-109
17019810-4	2006	We and others have identified a class of small molecules derived from 1,4-benzothiazepines, that enhance the binding affinity of calstabin 2 for RyR2 and reduce the diastolic SR Ca2+ leak, even when the channel is PKA hyperphosphorylated.	1,4-benzothiazepines	70-90	FKBP prolyl isomerase 1B	Homo sapiens	129-140
16157601-4	2005	The central region includes 11 mutations, and an isoleucine-proline motif (positions 2427 and 2428) in the same region is predicted to contribute to the binding of FKBP12.6 protein.	Proline	60-67	FKBP prolyl isomerase 1B	Homo sapiens	164-172
16185151-6	2005	In HEK293 cells, these RyR2 mutants showed less binding of 35S-calstabin2 than the wild type, indicating a reduced binding affinity.	Sulfur-35	59-62	FKBP prolyl isomerase 1B	Homo sapiens	63-73
15336974-9	2004	We review the importance of calstabin2 for RyR2 function and excitation-contraction coupling, and discuss new observations that implicate dysregulation of calstabin2 binding as a central mechanism for abnormal calcium cycling in heart failure and triggered arrhythmias.	Calcium	210-217	FKBP prolyl isomerase 1B	Homo sapiens	155-165
15591045-7	2005	However, expression of a large RyR2 C-terminal construct in mammalian cells encompassing the pore-forming transmembrane domains exhibits rapamycin-sensitive binding specifically to FKBP12.6 but not to FKBP12.	Sirolimus	137-146	FKBP prolyl isomerase 1B	Homo sapiens	181-189
15709953-5	2005	These regulatory proteins include calstabin1/calstabin2 (FKBP12/FKBP12.6), a 12/12.6 kDa subunit that stabilizes the closed state of the channel and prevents aberrant calcium leak from the SR. Kinases and phosphatases are targeted to RyR2 channels and modulate RyR2 function in response to extracellular signals.	Calcium	167-174	FKBP prolyl isomerase 1B	Homo sapiens	45-55
15709953-5	2005	These regulatory proteins include calstabin1/calstabin2 (FKBP12/FKBP12.6), a 12/12.6 kDa subunit that stabilizes the closed state of the channel and prevents aberrant calcium leak from the SR. Kinases and phosphatases are targeted to RyR2 channels and modulate RyR2 function in response to extracellular signals.	Calcium	167-174	FKBP prolyl isomerase 1B	Homo sapiens	64-72
15497458-1	2004	FKBP1B belongs to immunophilins superfamily and functions as a cytosolic receptor protein of FK506.	Tacrolimus	93-98	FKBP prolyl isomerase 1B	Homo sapiens	0-6
15197150-7	2004	Treatment with the experimental drug JTV519 enhanced binding of calstabin2 to RyR2 and normalized channel function.	K201 compound	37-43	FKBP prolyl isomerase 1B	Homo sapiens	64-74
15497458-2	2004	The role of FKBP1B in the immunosuppressive pathway of FK506 is well established.	Tacrolimus	55-60	FKBP prolyl isomerase 1B	Homo sapiens	12-18
14605212-5	2003	In contrast to FKBP12-/- cells, splenic FKBP12.6-/- T cells exhibited a decreased proliferative response to IL-2 in the presence of rapamycin without affecting p70S6K or ERK activation.	Sirolimus	132-141	FKBP prolyl isomerase 1B	Homo sapiens	40-48
15201156-8	2004	Increased RyR2 phosphorylation and pathologically increased calstabin2 dissociation during exercise results in aberrant diastolic calcium release, which may trigger ventricular arrhythmias and sudden cardiac death.	Calcium	130-137	FKBP prolyl isomerase 1B	Homo sapiens	60-70
14715536-1	2004	Dissociation of FKBP12.6 from the cardiac Ca2+-release channel (RyR2) as a consequence of protein kinase A (PKA) hyperphosphorylation of RyR2 at a single amino acid residue, serine-2808, has been proposed as an important mechanism underlying cardiac dysfunction in heart failure.	Serine	174-180	FKBP prolyl isomerase 1B	Homo sapiens	16-24
14715536-5	2004	We found that FKBP12.6 can bind to both the serine-2808 phosphorylated and nonphosphorylated forms of RyR2.	Serine	44-50	FKBP prolyl isomerase 1B	Homo sapiens	14-22
15073377-3	2004	A derivative of 1,4-benzothiazepine (JTV519) increased the affinity of calstabin2 for RyR2, which stabilized the closed state of RyR2 and prevented the Ca2+ leak that triggers arrhythmias.	1,4-Benzothiazepine	16-35	FKBP prolyl isomerase 1B	Homo sapiens	71-81
12443530-7	2003	However, in CHO(hRyR2) cells co-expressing FKBP12.6, Ca(2+) release triggered by the addition of 4-chloro- m -cresol was markedly decreased.	chlorocresol	97-116	FKBP prolyl isomerase 1B	Homo sapiens	43-51
16120349-2	2003	The protein exhibits a Mg2+-requiring PPiase activity, with an optimum at pH 9.0, which is not stimulated by monovalent cations, but inhibited by F-, Ca2+, aminomethylenediphosphate and imidodiphosphate.	magnesium ion	23-27	FKBP prolyl isomerase 1B	Homo sapiens	38-44
16120349-2	2003	The protein exhibits a Mg2+-requiring PPiase activity, with an optimum at pH 9.0, which is not stimulated by monovalent cations, but inhibited by F-, Ca2+, aminomethylenediphosphate and imidodiphosphate.	Fluorine	146-149	FKBP prolyl isomerase 1B	Homo sapiens	38-44
16120349-2	2003	The protein exhibits a Mg2+-requiring PPiase activity, with an optimum at pH 9.0, which is not stimulated by monovalent cations, but inhibited by F-, Ca2+, aminomethylenediphosphate and imidodiphosphate.	aminomethylenediphosphate	156-181	FKBP prolyl isomerase 1B	Homo sapiens	38-44
16120349-2	2003	The protein exhibits a Mg2+-requiring PPiase activity, with an optimum at pH 9.0, which is not stimulated by monovalent cations, but inhibited by F-, Ca2+, aminomethylenediphosphate and imidodiphosphate.	imidodiphosphonic acid	186-202	FKBP prolyl isomerase 1B	Homo sapiens	38-44
12919952-7	2003	RyR2:FKBP12.6 interaction remained intact after caffeine or 4-CMC activation, but was dramatically disrupted by isoproterenol or forskolin, an activator of adenylate cyclase.	Caffeine	48-56	FKBP prolyl isomerase 1B	Homo sapiens	5-13
12919952-7	2003	RyR2:FKBP12.6 interaction remained intact after caffeine or 4-CMC activation, but was dramatically disrupted by isoproterenol or forskolin, an activator of adenylate cyclase.	clephedrone	60-65	FKBP prolyl isomerase 1B	Homo sapiens	5-13
12919952-7	2003	RyR2:FKBP12.6 interaction remained intact after caffeine or 4-CMC activation, but was dramatically disrupted by isoproterenol or forskolin, an activator of adenylate cyclase.	Isoproterenol	112-125	FKBP prolyl isomerase 1B	Homo sapiens	5-13
12919952-7	2003	RyR2:FKBP12.6 interaction remained intact after caffeine or 4-CMC activation, but was dramatically disrupted by isoproterenol or forskolin, an activator of adenylate cyclase.	Colforsin	129-138	FKBP prolyl isomerase 1B	Homo sapiens	5-13
12837242-3	2003	The FK506 binding protein (FKBP12.6) stabilizes RyR2, preventing aberrant activation of the channel during the resting phase of the cardiac cycle.	Tacrolimus	4-9	FKBP prolyl isomerase 1B	Homo sapiens	27-35
12837242-4	2003	We show that during exercise, RyR2 phosphorylation by cAMP-dependent protein kinase A (PKA) partially dissociates FKBP12.6 from the channel, increasing intracellular Ca(2+) release and cardiac contractility.	Cyclic AMP	54-58	FKBP prolyl isomerase 1B	Homo sapiens	114-122
12443530-10	2003	The effects of FKBP12.6 on hRyR2-mediated intracellular Ca(2+) handling could be antagonized using rapamycin (5 microM).	Sirolimus	99-108	FKBP prolyl isomerase 1B	Homo sapiens	15-23
12446682-3	2003	To investigate the significance of the isoleucine-proline (residues 2427-2428) dipeptide epitope, which is thought to form an essential part of the FKBP12.6 binding site in RyR2, we generated single and double mutants, P2428Q, I2427E/P2428A, and P2428A/L2429E, expressed them in HEK293 cells, and assessed their ability to bind GST-FKBP12.6.	Proline	50-57	FKBP prolyl isomerase 1B	Homo sapiens	148-156
12446682-3	2003	To investigate the significance of the isoleucine-proline (residues 2427-2428) dipeptide epitope, which is thought to form an essential part of the FKBP12.6 binding site in RyR2, we generated single and double mutants, P2428Q, I2427E/P2428A, and P2428A/L2429E, expressed them in HEK293 cells, and assessed their ability to bind GST-FKBP12.6.	Dipeptides	79-88	FKBP prolyl isomerase 1B	Homo sapiens	148-156
8730126-1	1996	OBJECTIVE: Alkaline phosphatase (ALP), an enzyme with pyrophosphatase (PPiase) activity can dissolve calcium pyrophosphate dihydrate (CPPD) crystals.	Calcium Pyrophosphate	101-132	FKBP prolyl isomerase 1B	Homo sapiens	71-77
11598113-6	2001	Substitution of Val(2322) for leucine (as in IP(3)R1) or isoleucine (as in RyR2) decreased the binding efficiency and shifted the selectivity to FKBP12.6; substitution of Val(2322) for aspartate completely abolished the FKBP interaction.	Isoleucine	57-67	FKBP prolyl isomerase 1B	Homo sapiens	145-153
10830164-2	2000	The channel is a tetramer comprised of four type 2 RyR polypeptides (RyR2) and four FK506 binding proteins (FKBP12.6).	Tacrolimus	84-89	FKBP prolyl isomerase 1B	Homo sapiens	108-116
10713512-0	2000	Structure of FKBP12.6 in complex with rapamycin.	Sirolimus	38-47	FKBP prolyl isomerase 1B	Homo sapiens	13-21
10669849-12	2000	The rotamase activity of the protein, inhibited by cyclosporin A, further confirmed that Bet v 7 belongs to the group of cyclophilins.	Cyclosporine	51-64	FKBP prolyl isomerase 1B	Homo sapiens	4-12
9013543-0	1997	Cyclic ADP-ribose binds to FK506-binding protein 12.6 to release Ca2+ from islet microsomes.	Cyclic ADP-Ribose	0-17	FKBP prolyl isomerase 1B	Homo sapiens	27-53
9013543-4	1997	cADPR as well as FK506 bound to FK506-binding protein 12.6 (FKBP12.6), which we also found occurs naturally in islet microsomes.	Tacrolimus	17-22	FKBP prolyl isomerase 1B	Homo sapiens	32-58
9013543-4	1997	cADPR as well as FK506 bound to FK506-binding protein 12.6 (FKBP12.6), which we also found occurs naturally in islet microsomes.	Tacrolimus	17-22	FKBP prolyl isomerase 1B	Homo sapiens	60-68
8730126-5	1996	Calcium inhibited ALP PPiase activity, but not ALP Pase activity.	Calcium	0-7	FKBP prolyl isomerase 1B	Homo sapiens	22-28
8730126-6	1996	Orthovanadate and cadmium inhibited ALP PPiase activity more than ALP Pase at the same concentrations.	Vanadates	0-13	FKBP prolyl isomerase 1B	Homo sapiens	40-46
10794694-4	2000	As previously reported, the corresponding linear heptapeptide Ac-Val-His-Ala-Gly-Pro-Ile-Ala-NH(2) (2) binds to hCyp-18 with a low affinity (IC(50) = 850 +/- 220 microM) but a potentially useful selectivity for hCyp-18 relative to hFKBP-12, another abundant PPIase.	ac-val-his	62-72	FKBP prolyl isomerase 1B	Homo sapiens	258-264
10794694-4	2000	As previously reported, the corresponding linear heptapeptide Ac-Val-His-Ala-Gly-Pro-Ile-Ala-NH(2) (2) binds to hCyp-18 with a low affinity (IC(50) = 850 +/- 220 microM) but a potentially useful selectivity for hCyp-18 relative to hFKBP-12, another abundant PPIase.	ala-gly-pro-ile	73-88	FKBP prolyl isomerase 1B	Homo sapiens	258-264
10794694-4	2000	As previously reported, the corresponding linear heptapeptide Ac-Val-His-Ala-Gly-Pro-Ile-Ala-NH(2) (2) binds to hCyp-18 with a low affinity (IC(50) = 850 +/- 220 microM) but a potentially useful selectivity for hCyp-18 relative to hFKBP-12, another abundant PPIase.	Alanine	73-76	FKBP prolyl isomerase 1B	Homo sapiens	258-264
10331647-4	1999	Cyclic ADP-ribose then binds to FK506-binding protein 12.6 in the ryanodine receptor Ca2+ channel (RyR), dissociating the binding protein from RyR to induce the release of Ca2+ from the endoplasmic reticulum.	Cyclic ADP-Ribose	0-17	FKBP prolyl isomerase 1B	Homo sapiens	32-58
9176165-3	1997	Both FKBP12 and FKBP12.6 rebind to FKBP-depleted RyR1 and restore its quiescent channel behavior by altering ligand sensitivity, as studied by single-channel recordings in planar lipid bilayers, and macroscopic behavior of the channels (ryanodine binding and net energized Ca2- uptake).	Ryanodine	237-246	FKBP prolyl isomerase 1B	Homo sapiens	16-24
8730126-6	1996	Orthovanadate and cadmium inhibited ALP PPiase activity more than ALP Pase at the same concentrations.	Cadmium	18-25	FKBP prolyl isomerase 1B	Homo sapiens	40-46
8730126-1	1996	OBJECTIVE: Alkaline phosphatase (ALP), an enzyme with pyrophosphatase (PPiase) activity can dissolve calcium pyrophosphate dihydrate (CPPD) crystals.	Calcium Pyrophosphate	134-138	FKBP prolyl isomerase 1B	Homo sapiens	71-77
8730126-7	1996	The inhibition rates of ALP PPiase at the same concentrations were orthovanadate > cadmium > calcium.	Vanadates	67-80	FKBP prolyl isomerase 1B	Homo sapiens	28-34
8730126-7	1996	The inhibition rates of ALP PPiase at the same concentrations were orthovanadate > cadmium > calcium.	Cadmium	86-93	FKBP prolyl isomerase 1B	Homo sapiens	28-34
8730126-2	1996	We studied the effects of enzyme inhibitors such as bisphosphonates, orthovanadate, calcium, cadmium, and ascorbic acid on PPiase activity of ALP as well as on phosphate ester hydrolysis (Pase) activity and compared these effects to those on CPPD crystal dissolution.	Diphosphonates	52-67	FKBP prolyl isomerase 1B	Homo sapiens	123-129
8730126-7	1996	The inhibition rates of ALP PPiase at the same concentrations were orthovanadate > cadmium > calcium.	Calcium	99-106	FKBP prolyl isomerase 1B	Homo sapiens	28-34
8730126-2	1996	We studied the effects of enzyme inhibitors such as bisphosphonates, orthovanadate, calcium, cadmium, and ascorbic acid on PPiase activity of ALP as well as on phosphate ester hydrolysis (Pase) activity and compared these effects to those on CPPD crystal dissolution.	Calcium	84-91	FKBP prolyl isomerase 1B	Homo sapiens	123-129
8730126-8	1996	Although ALP Pase activity was not inhibited, at high concentrations, ascorbic acid slightly inhibited ALP PPiase activity.	Ascorbic Acid	70-83	FKBP prolyl isomerase 1B	Homo sapiens	107-113
8730126-10	1996	The strong inhibitory effects of bisphosphonates on ALP CPPD crystal dissolution compared to those on ALP PPiase activity suggest that bisphosphonates inhibit crystal dissolution by their affinity for the CPPD crystal surface.	Diphosphonates	135-150	FKBP prolyl isomerase 1B	Homo sapiens	106-112
8730126-2	1996	We studied the effects of enzyme inhibitors such as bisphosphonates, orthovanadate, calcium, cadmium, and ascorbic acid on PPiase activity of ALP as well as on phosphate ester hydrolysis (Pase) activity and compared these effects to those on CPPD crystal dissolution.	Cadmium	93-100	FKBP prolyl isomerase 1B	Homo sapiens	123-129
8730126-2	1996	We studied the effects of enzyme inhibitors such as bisphosphonates, orthovanadate, calcium, cadmium, and ascorbic acid on PPiase activity of ALP as well as on phosphate ester hydrolysis (Pase) activity and compared these effects to those on CPPD crystal dissolution.	Ascorbic Acid	106-119	FKBP prolyl isomerase 1B	Homo sapiens	123-129
7592869-5	1995	Recently, a novel protein, FKBP12.6, was found to inhibit calcineurin at clinically relevant FK506 concentrations.	Tacrolimus	93-98	FKBP prolyl isomerase 1B	Homo sapiens	27-35
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 1B	Homo sapiens	29-37
7592869-10	1995	Our results suggest that FKBP12.6 has both a unique physiological role in excitation-contraction coupling in cardiac muscle and the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin.	Tacrolimus	202-207	FKBP prolyl isomerase 1B	Homo sapiens	25-33
7592869-10	1995	Our results suggest that FKBP12.6 has both a unique physiological role in excitation-contraction coupling in cardiac muscle and the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin.	Sirolimus	212-221	FKBP prolyl isomerase 1B	Homo sapiens	25-33
7520438-8	1994	When complexed with FK-506, FKBP12.6 binds to and inhibits calcineurin, making it only the second FKBP discovered thus far to do so.	Tacrolimus	20-26	FKBP prolyl isomerase 1B	Homo sapiens	28-36
7520438-9	1994	The ability to inhibit calcineurin establishes the potential relevance of FKBP12.6 to the immunosuppressive or toxic side effects of FK-506.	Tacrolimus	133-139	FKBP prolyl isomerase 1B	Homo sapiens	74-82
34454589-7	2021	Re-establishment of FKBP1B expression in the resistant OVCAR3 phenotype in which this gene is hypermethylated and inhibited allowed it to achieve a degree of platinum sensitivity similar to the sensitive phenotype.	Platinum	158-166	FKBP prolyl isomerase 1B	Homo sapiens	20-26
34454589-10	2021	CONCLUSIONS: Epigenetic regulation of PAX9 and FKBP1B genes shows that methylation in non-promoter areas has the potential to control gene expression and thus biological consequences, such as the loss of platinum sensitivity.	Platinum	204-212	FKBP prolyl isomerase 1B	Homo sapiens	47-53
34690808-9	2021	Diminished expression of the FK506 binding protein, FKBP12.6, may also contribute.	Tacrolimus	29-34	FKBP prolyl isomerase 1B	Homo sapiens	52-60
6127784-6	1982	Instead, Zn2+ and Co2+ reactivated the PPiase, indicating they might act as cofactors for the enzyme.	Zinc	9-13	FKBP prolyl isomerase 1B	Homo sapiens	39-45
6127784-6	1982	Instead, Zn2+ and Co2+ reactivated the PPiase, indicating they might act as cofactors for the enzyme.	Cobalt(2+)	18-22	FKBP prolyl isomerase 1B	Homo sapiens	39-45
6127784-7	1982	Mg2+ increased the PPiase activity, probably because Mg PP2-i was the true substrate for the enzyme.	magnesium ion	0-4	FKBP prolyl isomerase 1B	Homo sapiens	19-25
6127784-7	1982	Mg2+ increased the PPiase activity, probably because Mg PP2-i was the true substrate for the enzyme.	mg pp2-i	53-61	FKBP prolyl isomerase 1B	Homo sapiens	19-25
6127784-8	1982	The diphosphonates ethane-1-hydroxy 1,1 diphosphonate (EHDP), methane diphosphonate (MDP) and dichloromethane diphosphonate (Cl2MDP) inhibited the PPiase activity.	Diphosphonates	4-18	FKBP prolyl isomerase 1B	Homo sapiens	147-153
6127784-8	1982	The diphosphonates ethane-1-hydroxy 1,1 diphosphonate (EHDP), methane diphosphonate (MDP) and dichloromethane diphosphonate (Cl2MDP) inhibited the PPiase activity.	Etidronic Acid	19-53	FKBP prolyl isomerase 1B	Homo sapiens	147-153
6127784-8	1982	The diphosphonates ethane-1-hydroxy 1,1 diphosphonate (EHDP), methane diphosphonate (MDP) and dichloromethane diphosphonate (Cl2MDP) inhibited the PPiase activity.	Etidronic Acid	55-59	FKBP prolyl isomerase 1B	Homo sapiens	147-153
6127784-8	1982	The diphosphonates ethane-1-hydroxy 1,1 diphosphonate (EHDP), methane diphosphonate (MDP) and dichloromethane diphosphonate (Cl2MDP) inhibited the PPiase activity.	methylene diphosphonate	62-83	FKBP prolyl isomerase 1B	Homo sapiens	147-153
6127784-8	1982	The diphosphonates ethane-1-hydroxy 1,1 diphosphonate (EHDP), methane diphosphonate (MDP) and dichloromethane diphosphonate (Cl2MDP) inhibited the PPiase activity.	methylene diphosphonate	85-88	FKBP prolyl isomerase 1B	Homo sapiens	147-153
6127784-8	1982	The diphosphonates ethane-1-hydroxy 1,1 diphosphonate (EHDP), methane diphosphonate (MDP) and dichloromethane diphosphonate (Cl2MDP) inhibited the PPiase activity.	Clodronic Acid	94-123	FKBP prolyl isomerase 1B	Homo sapiens	147-153
6127784-8	1982	The diphosphonates ethane-1-hydroxy 1,1 diphosphonate (EHDP), methane diphosphonate (MDP) and dichloromethane diphosphonate (Cl2MDP) inhibited the PPiase activity.	Clodronic Acid	125-131	FKBP prolyl isomerase 1B	Homo sapiens	147-153
33572801-7	2021	The 2.17 A structure of this ALK2-FKBP12.6 complex bound to the inhibitor dorsomorphin showed FKBP12.6 binding to the GS domain of ALK2 in a manner equivalent to the FKBP12 complex, with ALK2 residues Phe198 and Leu199 extending into the FK506-binding pocket of FKBP12.6.	dorsomorphin	74-86	FKBP prolyl isomerase 1B	Homo sapiens	34-42
33572801-7	2021	The 2.17 A structure of this ALK2-FKBP12.6 complex bound to the inhibitor dorsomorphin showed FKBP12.6 binding to the GS domain of ALK2 in a manner equivalent to the FKBP12 complex, with ALK2 residues Phe198 and Leu199 extending into the FK506-binding pocket of FKBP12.6.	dorsomorphin	74-86	FKBP prolyl isomerase 1B	Homo sapiens	94-102
33572801-7	2021	The 2.17 A structure of this ALK2-FKBP12.6 complex bound to the inhibitor dorsomorphin showed FKBP12.6 binding to the GS domain of ALK2 in a manner equivalent to the FKBP12 complex, with ALK2 residues Phe198 and Leu199 extending into the FK506-binding pocket of FKBP12.6.	dorsomorphin	74-86	FKBP prolyl isomerase 1B	Homo sapiens	94-102
33572801-7	2021	The 2.17 A structure of this ALK2-FKBP12.6 complex bound to the inhibitor dorsomorphin showed FKBP12.6 binding to the GS domain of ALK2 in a manner equivalent to the FKBP12 complex, with ALK2 residues Phe198 and Leu199 extending into the FK506-binding pocket of FKBP12.6.	Tacrolimus	238-243	FKBP prolyl isomerase 1B	Homo sapiens	34-42
33572801-7	2021	The 2.17 A structure of this ALK2-FKBP12.6 complex bound to the inhibitor dorsomorphin showed FKBP12.6 binding to the GS domain of ALK2 in a manner equivalent to the FKBP12 complex, with ALK2 residues Phe198 and Leu199 extending into the FK506-binding pocket of FKBP12.6.	Tacrolimus	238-243	FKBP prolyl isomerase 1B	Homo sapiens	94-102
33572801-7	2021	The 2.17 A structure of this ALK2-FKBP12.6 complex bound to the inhibitor dorsomorphin showed FKBP12.6 binding to the GS domain of ALK2 in a manner equivalent to the FKBP12 complex, with ALK2 residues Phe198 and Leu199 extending into the FK506-binding pocket of FKBP12.6.	Tacrolimus	238-243	FKBP prolyl isomerase 1B	Homo sapiens	94-102