PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10601253-1 1999 FKBP52 is a high molecular mass immunophilin possessing peptidylprolyl isomerase (PPIase) activity that is inhibited by the immunosuppressant drug FK506. Tacrolimus 147-152 FKBP prolyl isomerase 4 Homo sapiens 0-6 10601253-1 1999 FKBP52 is a high molecular mass immunophilin possessing peptidylprolyl isomerase (PPIase) activity that is inhibited by the immunosuppressant drug FK506. Tacrolimus 147-152 FKBP prolyl isomerase 4 Homo sapiens 82-88 10601253-1 1999 FKBP52 is a high molecular mass immunophilin possessing peptidylprolyl isomerase (PPIase) activity that is inhibited by the immunosuppressant drug FK506. Tacrolimus 147-152 FKBP prolyl isomerase 4 Homo sapiens 56-80 10336507-3 1999 In human neuroblastoma SH-SY5Y cells, the neurotrophic action of FK506 (10 pM to 10 nM) is completely prevented by the addition of a monoclonal antibody (50-100 nM) to the immunophilin FKBP-52 (also known as FKBP-59 or heat shock protein 56), a component of mature steroid receptor complexes. Tacrolimus 65-70 FKBP prolyl isomerase 4 Homo sapiens 185-192 10461545-4 1999 Regardless of the underlying mechanism involved, the FKBP-52 antibody data reveal that it should be possible to design, based on the structure of FK506, non-FKBP-12-binding (nonimmunosuppressant) compounds selective for FKBP-52 and test these new libraries for their ability to augment nerve regeneration. Tacrolimus 146-151 FKBP prolyl isomerase 4 Homo sapiens 53-60 10461545-4 1999 Regardless of the underlying mechanism involved, the FKBP-52 antibody data reveal that it should be possible to design, based on the structure of FK506, non-FKBP-12-binding (nonimmunosuppressant) compounds selective for FKBP-52 and test these new libraries for their ability to augment nerve regeneration. Tacrolimus 146-151 FKBP prolyl isomerase 4 Homo sapiens 220-227 10336507-3 1999 In human neuroblastoma SH-SY5Y cells, the neurotrophic action of FK506 (10 pM to 10 nM) is completely prevented by the addition of a monoclonal antibody (50-100 nM) to the immunophilin FKBP-52 (also known as FKBP-59 or heat shock protein 56), a component of mature steroid receptor complexes. Tacrolimus 65-70 FKBP prolyl isomerase 4 Homo sapiens 208-215 8760046-3 1996 Of interest, FK-506 and RAP, but not CyA, are bound by the steroid receptor-associated FK-506-binding heat shock protein of 56 kDa, HSP56. Tacrolimus 13-19 FKBP prolyl isomerase 4 Homo sapiens 132-137 9195923-11 1997 Of the 9 residues in this portion of FKBP52 involved in high affinity interactions with FK506, 3 residues are retained and 4 have homologous substitutions in PP5. Tacrolimus 88-93 FKBP prolyl isomerase 4 Homo sapiens 37-43 8955134-3 1996 FKBP59 and FKBP12 belong to the large family of immunophilins that bind the macrolide immunosuppressant drugs FK506 and rapamycin. Tacrolimus 110-115 FKBP prolyl isomerase 4 Homo sapiens 0-6 8955134-10 1996 The formation of the complexes between FKBP59 or FKBP12 and FAP48 is prevented by FK506 and rapamycin in a dose-dependent manner. Tacrolimus 82-87 FKBP prolyl isomerase 4 Homo sapiens 39-45 10051602-1 1999 FKBP52 (FKBP59, FKBP4) is a "macro" immunophilin that, although sharing high structural and functional homologies in its amino-terminal domain with FKBP12 (FKBP1), does not have immunosuppressant activity when complexed with FK506, unlike FKBP12. Tacrolimus 225-230 FKBP prolyl isomerase 4 Homo sapiens 0-6 10051602-1 1999 FKBP52 (FKBP59, FKBP4) is a "macro" immunophilin that, although sharing high structural and functional homologies in its amino-terminal domain with FKBP12 (FKBP1), does not have immunosuppressant activity when complexed with FK506, unlike FKBP12. Tacrolimus 225-230 FKBP prolyl isomerase 4 Homo sapiens 8-14 10051602-1 1999 FKBP52 (FKBP59, FKBP4) is a "macro" immunophilin that, although sharing high structural and functional homologies in its amino-terminal domain with FKBP12 (FKBP1), does not have immunosuppressant activity when complexed with FK506, unlike FKBP12. Tacrolimus 225-230 FKBP prolyl isomerase 4 Homo sapiens 16-21 10051602-8 1999 Whereas the binding of calcineurin to FKBP12 is potentiated by FK506, the specific association of PAHX and FKBP52 is maintained in the presence of FK506. Tacrolimus 147-152 FKBP prolyl isomerase 4 Homo sapiens 107-113 9658403-12 1998 The nuclear 9S-[3H]Org2058-PR resulting from cells exposed to Rap, contained, in addition to the heat shock proteins of 90 kDa and 70 kDa (hsp90 and hsp70), the FK506-binding immunophilin FKBP52 but not FKBP51, although the latter was part of unliganded PR heterocomplex associated with hsp90. Tacrolimus 161-166 FKBP prolyl isomerase 4 Homo sapiens 188-194 8584032-0 1995 Evidence that the FK506-binding immunophilin heat shock protein 56 is required for trafficking of the glucocorticoid receptor from the cytoplasm to the nucleus. Tacrolimus 18-23 FKBP prolyl isomerase 4 Homo sapiens 45-66 8584032-1 1995 The FK506-binding immunophilin hsp56 (FKBP52) is one of several chaperone proteins associated with untrasformed steroid receptors in a multiprotein heterocomplex. Tacrolimus 4-9 FKBP prolyl isomerase 4 Homo sapiens 31-36 8584032-1 1995 The FK506-binding immunophilin hsp56 (FKBP52) is one of several chaperone proteins associated with untrasformed steroid receptors in a multiprotein heterocomplex. Tacrolimus 4-9 FKBP prolyl isomerase 4 Homo sapiens 38-44 7504525-0 1993 An active FK506-binding domain of 17,000 daltons is isolated following limited proteolysis of chicken thymus hsp56. Tacrolimus 10-15 FKBP prolyl isomerase 4 Homo sapiens 109-114 7544285-3 1995 FKBP59 binds immunosuppressant FK506 and has peptidylprolyl cis-trans-isomerase activity, both properties being localized in the N-terminal domain (FKBP59-I). Tacrolimus 31-36 FKBP prolyl isomerase 4 Homo sapiens 0-6 7476967-5 1995 A third 59-kilodalton (kDa) protein observed previously was confirmed to be p59 (also called hsp56 or FKBP52), which has been shown to bind the immunosuppressant drug FK506. Tacrolimus 167-172 FKBP prolyl isomerase 4 Homo sapiens 93-98 7476967-5 1995 A third 59-kilodalton (kDa) protein observed previously was confirmed to be p59 (also called hsp56 or FKBP52), which has been shown to bind the immunosuppressant drug FK506. Tacrolimus 167-172 FKBP prolyl isomerase 4 Homo sapiens 102-108 7510997-9 1994 Purification of cytosol PR on immobilized FK506 yields a 9S form still containing hsp90, hsp70 and p59/HBI associated to PR units. Tacrolimus 42-47 FKBP prolyl isomerase 4 Homo sapiens 103-106 7532989-2 1995 Based on functional and sequence homology studies, it was recently discovered that hsp56 also belongs to the FKBP class of immunophilin proteins, which are thought to mediate the actions of the immunosuppressive drugs FK506 and rapamycin. Tacrolimus 218-223 FKBP prolyl isomerase 4 Homo sapiens 83-88 7532989-6 1995 It was also found that the untransformed but not the transformed GR was retained following affinity chromatography with FK506-affigel resin, reinforcing the possibility that hsp56 within the untransformed GR complex could be a target for the actions of FK506. Tacrolimus 253-258 FKBP prolyl isomerase 4 Homo sapiens 174-179 7532989-11 1995 Although we speculate that these actions of FK506 on the GR complex are mediated by the associated hsp56 component, other possible mechanisms are also discussed. Tacrolimus 44-49 FKBP prolyl isomerase 4 Homo sapiens 99-104 7530727-0 1994 A soluble binding assay for measuring 3H-FK506 binding to the hsp56 immunophilin. Tacrolimus 41-46 FKBP prolyl isomerase 4 Homo sapiens 62-67 7530727-1 1994 Heat shock protein 56 (hsp56) was previously identified as an immunophilin based on its ability to specifically bind to FK506-Affi-Gel 10. Tacrolimus 120-125 FKBP prolyl isomerase 4 Homo sapiens 0-21 7530727-1 1994 Heat shock protein 56 (hsp56) was previously identified as an immunophilin based on its ability to specifically bind to FK506-Affi-Gel 10. Tacrolimus 120-125 FKBP prolyl isomerase 4 Homo sapiens 23-28 7530727-6 1994 These results demonstrate that hsp56 binds FK506 and rapamycin with similar affinities, and suggest that hsp56 may play a role in mediating the cellular function of both of these drugs. Tacrolimus 43-48 FKBP prolyl isomerase 4 Homo sapiens 31-36 7530727-6 1994 These results demonstrate that hsp56 binds FK506 and rapamycin with similar affinities, and suggest that hsp56 may play a role in mediating the cellular function of both of these drugs. Tacrolimus 43-48 FKBP prolyl isomerase 4 Homo sapiens 105-110 7510997-3 1994 A recombinant p59/HBI-glutathione-S-transferase fusion protein, purified by Sephadex LH-20 filtration of tritiated drug-p59/HBI complexes, binds FK506 and RAP with apparent Kd values of 75 +/- 40 and 40 +/- 15 nM, respectively. Tacrolimus 145-150 FKBP prolyl isomerase 4 Homo sapiens 124-127 7504525-5 1993 We now report that hsp56 is also found to be a major immunophilin in chicken thymus, by virtue of binding to FK506-Affi-Gel-10 as well as positive cross-reactivity with a polyclonal antiserum directed against human hsp56. Tacrolimus 109-114 FKBP prolyl isomerase 4 Homo sapiens 19-24 7504525-7 1993 Peptide mapping provided additional proof that p17 is a fragment which comprises the entire FK506 binding domain I of chicken hsp56, terminating with an Arg-Lys which might represent a processing site. Tacrolimus 92-97 FKBP prolyl isomerase 4 Homo sapiens 126-131 7504525-11 1993 This work demonstrates the excision of a domain from an hsp56 protein that is active in binding FK506 and functionally distinct from FKBP-12, a protein of similar size and structure. Tacrolimus 96-101 FKBP prolyl isomerase 4 Homo sapiens 56-61 7689858-2 1993 Recently, we showed that p59 purified from human lymphocytes is an immunophilin (FKBP59) which binds both FK506 and rapamycin. Tacrolimus 106-111 FKBP prolyl isomerase 4 Homo sapiens 81-87 7681058-2 1993 The ability of hsp56 to bind the immunosuppressive macrolide FK506 has led to the speculation that the steroid receptor and immunophilin signal transduction pathways are functionally interrelated. Tacrolimus 61-66 FKBP prolyl isomerase 4 Homo sapiens 15-20 1383222-2 1992 Heat shock protein 56 (hsp56) has been shown to be involved in two cellular pathways, as an immunophilin for FK506 and as a component of steroid receptor complexes. Tacrolimus 109-114 FKBP prolyl isomerase 4 Homo sapiens 0-21 1279700-1 1992 Using an FK506 affinity column to identify mammalian immunosuppressant-binding proteins, we identified an immunophilin with an apparent M(r) approximately 55,000, which we have named FKBP52. Tacrolimus 9-14 FKBP prolyl isomerase 4 Homo sapiens 183-189 1279700-4 1992 Recombinant hFKBP52 has peptidyl-prolyl cis-trans isomerase activity that is inhibited by FK506 and rapamycin and an FKBP12-like consensus sequence that probably defines the immunosuppressant-binding site. Tacrolimus 90-95 FKBP prolyl isomerase 4 Homo sapiens 12-19 1383222-2 1992 Heat shock protein 56 (hsp56) has been shown to be involved in two cellular pathways, as an immunophilin for FK506 and as a component of steroid receptor complexes. Tacrolimus 109-114 FKBP prolyl isomerase 4 Homo sapiens 23-28 34830130-10 2021 Differential effects of FK506-binding immunophilins, FKBP4 and FKBP5, contribute to the efficiency of glucocorticoids under stress resilience. Tacrolimus 24-29 FKBP prolyl isomerase 4 Homo sapiens 53-58 1371107-0 1992 The Hsp56 component of steroid receptor complexes binds to immobilized FK506 and shows homology to FKBP-12 and FKBP-13. Tacrolimus 71-76 FKBP prolyl isomerase 4 Homo sapiens 4-9 1371107-5 1992 It would appear, therefore, that this 60-kDa protein, or as we refer to it provisionally, "Hsp56," could have the capacity to bind FK506 directly. Tacrolimus 131-136 FKBP prolyl isomerase 4 Homo sapiens 91-96 26858893-1 2015 The steroid receptor (SR) complex contains FKBP51 and FKBP52, which bind to tacrolimus (TAC) and cyclophilin 40, which, in turn, bind to cyclosporine (CYA); these influence the intranuclear mobility of steroid-SR complexes. Tacrolimus 76-86 FKBP prolyl isomerase 4 Homo sapiens 54-60 29023988-3 2018 However, the structural conservation of the FK1 domains between FKBP51 and FKBP52 make it difficult to obtain satisfactory selectivity in FK506-based drug design. Tacrolimus 138-143 FKBP prolyl isomerase 4 Homo sapiens 75-81 32664235-9 2020 Interestingly, IRF4 encodes the FK506-binding protein 52 (FKBP52), a protein associated with tacrolimus. Tacrolimus 93-103 FKBP prolyl isomerase 4 Homo sapiens 32-56 32664235-9 2020 Interestingly, IRF4 encodes the FK506-binding protein 52 (FKBP52), a protein associated with tacrolimus. Tacrolimus 93-103 FKBP prolyl isomerase 4 Homo sapiens 58-64 32580389-3 2020 This complex glucocorticoid regulation is mediated through the glucocorticoid receptor, also known as nuclear receptor subfamily 3 group C member 1 (NR3C1/GR) and related genes, like 11beta-hydroxysteroid dehydrogenases (HSD11Bs) and the FK506-binding immunophilins, FKBP5 and FKBP4. Tacrolimus 238-243 FKBP prolyl isomerase 4 Homo sapiens 277-282 31661769-1 2019 Previous studies demonstrated that the 52-kDa FK506-binding protein (FKBP52) proline-rich loop is functionally relevant in the regulation of steroid hormone receptor activity. Tacrolimus 46-51 FKBP prolyl isomerase 4 Homo sapiens 69-75 26903089-2 2016 The FK506 binding protein FKBP52 is able to induce oligomers in the pathogenic Tau P301L mutant and in a truncated form of the wild-type human Tau protein. Tacrolimus 4-9 FKBP prolyl isomerase 4 Homo sapiens 26-32 26903089-4 2016 We find that FKBP52 indeed can isomerize selected prolyl bonds in the different Tau proteins, and that this activity is carried solely by its first FK506 binding domain. Tacrolimus 148-153 FKBP prolyl isomerase 4 Homo sapiens 13-19 26903089-6 2016 In addition, we identified a novel molecular interaction implying the PHF6 peptide of Tau and the FK1/FK2 domains of FKBP52 independent of FK506 binding; these data point toward a non-catalytic molecular interaction that might govern the effect of FKBP52 on Tau. Tacrolimus 139-144 FKBP prolyl isomerase 4 Homo sapiens 117-123 25888602-0 2015 The FK506-binding protein FKBP52 in vitro induces aggregation of truncated Tau forms with prion-like behavior. Tacrolimus 4-9 FKBP prolyl isomerase 4 Homo sapiens 26-32 25888602-3 2015 We showed previously that the immunophilin FK506-binding protein of MW ~52 kDa (FKBP52) interferes with this function of full-length Tau and provokes aggregation of a disease-related mutant of Tau. Tacrolimus 43-48 FKBP prolyl isomerase 4 Homo sapiens 80-86 25953903-1 2015 Interchanging Leu-119 for Pro-119 at the tip of the beta4-beta5 loop in the first FK506 binding domain (FK1) of the FKBP51 and FKBP52 proteins, respectively, has been reported to largely reverse the inhibitory (FKBP51) or stimulatory (FKBP52) effects of these co-chaperones on the transcriptional activity of glucocorticoid and androgen receptor-protein complexes. Tacrolimus 82-87 FKBP prolyl isomerase 4 Homo sapiens 127-133 25953903-1 2015 Interchanging Leu-119 for Pro-119 at the tip of the beta4-beta5 loop in the first FK506 binding domain (FK1) of the FKBP51 and FKBP52 proteins, respectively, has been reported to largely reverse the inhibitory (FKBP51) or stimulatory (FKBP52) effects of these co-chaperones on the transcriptional activity of glucocorticoid and androgen receptor-protein complexes. Tacrolimus 82-87 FKBP prolyl isomerase 4 Homo sapiens 235-241 22455398-3 2012 Rapamycin and FK506 are two macrocyclic natural products, which tightly bind to most FKBP family members, including FKBP51 and FKBP52. Tacrolimus 14-19 FKBP prolyl isomerase 4 Homo sapiens 127-133 24749623-0 2014 Differential conformational dynamics in the closely homologous FK506-binding domains of FKBP51 and FKBP52. Tacrolimus 63-68 FKBP prolyl isomerase 4 Homo sapiens 99-105 23933011-5 2013 The immunophilin FKBP52 is composed of three domains, an FK506-binding domain with peptidyl-prolyl isomerase activity, an FKBP-like domain of unknown function and a TPR-clamp domain, which recognizes the C-terminal peptide of Hsp90 with high affinity. Tacrolimus 57-62 FKBP prolyl isomerase 4 Homo sapiens 17-23 23933011-6 2013 The herein reported crystal structures of FKBP52 reveal that the short linker connecting the FK506-binding domain and the FKBP-like domain acts as a flexible hinge. Tacrolimus 93-98 FKBP prolyl isomerase 4 Homo sapiens 42-48 23933011-8 2013 We further present two co-crystal structures of FKBP52 in complex with the prototypic ligand FK506 and a synthetic analog thereof. Tacrolimus 93-98 FKBP prolyl isomerase 4 Homo sapiens 48-54 23228564-7 2013 FK506 and rapamycin reduced the association between TRPC1 and Orai1 with FK506 binding protein (52) (FKBP52) in human platelets, and between TRPC1 and the type II IP(3)R, which association is known to be crucial for the maintenance of SOCE in human platelets. Tacrolimus 0-5 FKBP prolyl isomerase 4 Homo sapiens 101-107 23228564-10 2013 Finally, in MEG 01 incubated with FK506 we observed a reduction in TRPC1/FKBP52 coupling, and similarly, FKBP52 silencing reduced the association between IP3R type II and TRPC1 during SOCE. Tacrolimus 34-39 FKBP prolyl isomerase 4 Homo sapiens 73-79 23228564-10 2013 Finally, in MEG 01 incubated with FK506 we observed a reduction in TRPC1/FKBP52 coupling, and similarly, FKBP52 silencing reduced the association between IP3R type II and TRPC1 during SOCE. Tacrolimus 34-39 FKBP prolyl isomerase 4 Homo sapiens 105-111 24623856-3 2014 Here, we assess the impact of FK506-binding protein with a molecular mass of ~52 kDa (FKBP52), an immunophilin protein that interacts with physiological Tau, on Tau-P301L activity. Tacrolimus 30-35 FKBP prolyl isomerase 4 Homo sapiens 86-92 24899909-10 2014 In addition, the purple anthocyanins, such as cyanidin-3-glucoside and malvidin-3-glucoside, might be better than FK506 in regulating FKBP52 and treating Alzheimer"s disease. Tacrolimus 114-119 FKBP prolyl isomerase 4 Homo sapiens 134-140 19201607-5 2009 Utilization of the optimized spacer enable the monolithic material bearing FK506 to identify not only FKBP12 but FKBP52, calcineurin A and calcineurin B at silver stained level, while that without spacer had failed. Tacrolimus 75-80 FKBP prolyl isomerase 4 Homo sapiens 113-119 21799260-4 2011 Binding of the immunosuppressant molecule FK506 to this domain inhibits their PPIase activity while mediating immune suppression through inhibition of calcineurin. Tacrolimus 42-47 FKBP prolyl isomerase 4 Homo sapiens 78-84 20133804-6 2010 FKBP52 is a member of the FKBP (FK506-binding protein) family that comprises intracellular protein effectors of immunosuppressive drugs (such as FK506 and rapamycin). Tacrolimus 32-37 FKBP prolyl isomerase 4 Homo sapiens 0-6 20084280-10 2010 Finally, we also found that FKBP52 formed stable complexes with APP through its FK506 interacting domain. Tacrolimus 80-85 FKBP prolyl isomerase 4 Homo sapiens 28-34 16996313-2 2006 The drugs form complexes with diverse FKBPs but apparently the FKBP52/FK506 complex was shown to be involved in the protection and regeneration of neurons. Tacrolimus 70-75 FKBP prolyl isomerase 4 Homo sapiens 63-69 16996313-8 2006 It is proposed that binding of the FKBP52/FK506 complex to the membranes via the TPR motifs and its interaction with some membrane proteins could be in part responsible for some neuro-regeneration and neuro-protection of the brain during some ischaemia-induced stresses. Tacrolimus 42-47 FKBP prolyl isomerase 4 Homo sapiens 35-41 15713424-3 2005 FK1706, a derivative of FK506, showed similarly high affinity for two FKBP subtypes, FKBP-12 and FKBP-52, but inhibited T-cell proliferation and interleukin-2 cytokine production with much lower potency and efficacy than FK506. Tacrolimus 24-29 FKBP prolyl isomerase 4 Homo sapiens 97-104 16352746-6 2006 On the other hand, gene silencing of FKBP52 or administration of the FKBP52 blocker FK-506 enhances Ca(2+) influx through TRPV5. Tacrolimus 84-90 FKBP prolyl isomerase 4 Homo sapiens 69-75 12552015-3 2003 We have documented that a cellular protein that binds the immunosuppressant drug FK506, termed the FK506-binding protein (FKBP52), interacts with the single-stranded D sequence within the AAV inverted terminal repeats, inhibits viral second-strand DNA synthesis, and consequently limits high-efficiency transgene expression (K. Qing, J. Hansen, K. A. Weigel-Kelley, M. Tan, S. Zhou, and A. Srivastava, J. Tacrolimus 81-86 FKBP prolyl isomerase 4 Homo sapiens 122-128 15199065-8 2004 The binding of FKBP12 and FKBP52 was specific and could be displaced by the immunosuppressant drug FK506, at concentrations of 0.5 and 10 microm, respectively. Tacrolimus 99-104 FKBP prolyl isomerase 4 Homo sapiens 26-32 15133031-6 2004 The interaction between FKBP52 and Atox1 was observed in both glutathione S-transferase pull-down experiments and when proteins were ectopically expressed in human embryonic kidney (HEK) 293T cells and was sensitive to FK506. Tacrolimus 219-224 FKBP prolyl isomerase 4 Homo sapiens 24-30 15159550-1 2004 FK506-binding protein 52 (FKBP52), which binds FK506 and possesses peptidylprolyl isomerase activity, is an important immunophilin involved in the heterocomplex of steroid receptors with heat-shock protein 90. Tacrolimus 0-5 FKBP prolyl isomerase 4 Homo sapiens 26-32 12746298-1 2003 FKBP51 and FKBP52 are large molecular weight FK506-binding immunophilins that have diverse biochemical functions. Tacrolimus 45-50 FKBP prolyl isomerase 4 Homo sapiens 11-17 12782134-1 2003 FKBP52 is a widely expressed FK506-binding immunophilin that possesses peptidylprolyl isomerase activity and a tetratricopeptide repeat involved in protein-protein interaction. Tacrolimus 29-34 FKBP prolyl isomerase 4 Homo sapiens 0-6 15381148-1 2005 The large molecular-weight immunophilin, FKBP52, is a known target of the immunosuppressive drug FK506. Tacrolimus 97-102 FKBP prolyl isomerase 4 Homo sapiens 41-47 15381148-2 2005 FKBP52 exhibits peptidyl-prolyl cis-trans isomerase (PPIase) activity, which is inhibited by the binding of FK506--properties that it shares with the smaller but better-studied immunophilin, FKBP12. Tacrolimus 108-113 FKBP prolyl isomerase 4 Homo sapiens 0-6 15381148-2 2005 FKBP52 exhibits peptidyl-prolyl cis-trans isomerase (PPIase) activity, which is inhibited by the binding of FK506--properties that it shares with the smaller but better-studied immunophilin, FKBP12. Tacrolimus 108-113 FKBP prolyl isomerase 4 Homo sapiens 16-51 15381148-2 2005 FKBP52 exhibits peptidyl-prolyl cis-trans isomerase (PPIase) activity, which is inhibited by the binding of FK506--properties that it shares with the smaller but better-studied immunophilin, FKBP12. Tacrolimus 108-113 FKBP prolyl isomerase 4 Homo sapiens 53-59 12499534-2 2003 The N-terminal domain of FKBP52 (FKBP52-N; residues 1-140) is responsible for peptidyl-prolyl isomerase activity and binding of FK506. Tacrolimus 128-133 FKBP prolyl isomerase 4 Homo sapiens 25-31 12499534-2 2003 The N-terminal domain of FKBP52 (FKBP52-N; residues 1-140) is responsible for peptidyl-prolyl isomerase activity and binding of FK506. Tacrolimus 128-133 FKBP prolyl isomerase 4 Homo sapiens 33-39 12499534-5 2003 FKBP52-N is able to bind FK506 in a similar way to FKBP12. Tacrolimus 25-30 FKBP prolyl isomerase 4 Homo sapiens 0-6