| 1992 |
FKBP52 (FKBP59) possesses peptidyl-prolyl cis-trans isomerase (PPIase) activity inhibited by FK506 and rapamycin, and associates with hsp90 in untransformed mammalian steroid receptor complexes. The immunosuppressant-binding site is distinct from the hsp90-binding site, implying separate structural domains. |
Recombinant protein expression in E. coli, PPIase enzymatic assay, co-immunoprecipitation with hsp90 |
Proceedings of the National Academy of Sciences of the United States of America |
High |
1279700
|
| 1992 |
Rabbit FKBP52 (FKBP59-HBI) binds calmodulin in a Ca2+-dependent manner, retained on calmodulin-Sepharose in 2 mM Ca2+ and eluted by EGTA; it is also a substrate for calpain II, a Ca2+-activated protease. |
Calmodulin-Sepharose affinity chromatography, in vitro proteolysis assay |
Biochemical and biophysical research communications |
Medium |
1384470
|
| 1993 |
The PPIase activity of FKBP52 (p59-HBI) resides entirely in its N-terminal domain (domain I), which has the highest homology to FKBP12; a second domain (domain II) shows residual enzymatic activity. |
Overexpression of domain deletion mutants in E. coli, PPIase activity assay |
Biochemical and biophysical research communications |
High |
8216288
|
| 1993 |
The tetratricopeptide repeat (TPR) domain of FKBP52 (p59, FKBP59) is proposed to mediate protein-protein interactions including hsp90 binding; this was supported by identification of a conserved TPR domain in the estrogen receptor-binding cyclophilin (ERBC/CyP40). |
Affinity chromatography, sequence homology analysis, protein identification from estrogen receptor complex |
The Journal of biological chemistry |
Medium |
8514757
|
| 1993 |
Recombinant mouse FKBP52 can be assembled in vitro with the glucocorticoid receptor complex, confirming it is a functional component of the unactivated GR heterocomplex; it also possesses ATP/GTP binding activity stimulated by divalent cations. |
Baculovirus expression, in vitro assembly assay with glucocorticoid receptor, ATP binding assay |
Proceedings of the National Academy of Sciences of the United States of America |
Medium |
8341706
|
| 1994 |
The TPR domain located in the C-terminal part of FKBP52 (FKBP59-HBI) is necessary for hsp90 binding; this interaction is ATP-independent and not affected by FK506 or rapamycin. |
Gel-retardation assay with purified proteins, deletion mutant analysis |
Proceedings of the National Academy of Sciences of the United States of America |
High |
7526392
|
| 1996 |
FKBP52 competes with cyclophilin 40 (CyP40) for hsp90 binding, leading to mutually exclusive immunophilin-hsp90-receptor complexes; the TPR domain alone is not sufficient for stable hsp90 association—flanking acidic and basic residues are also required. |
GST-fusion deletion mutant pulldown, competition assay with myometrial cytosol |
The Journal of biological chemistry |
Medium |
8621687
|
| 1996 |
NMR structure of the N-terminal immunophilin domain of FKBP52 (FKBP59-I, residues 1–149) was determined; it adopts a twisted antiparallel beta-sheet and short alpha-helix, globally similar to FKBP12, with an unusual Trp89–Phe129 hydrogen bond important for immunosuppressant binding. |
Multidimensional NMR spectroscopy, distance geometry, molecular dynamics |
Biochemistry |
High |
8780506
|
| 1997 |
Casein kinase II (CK2) phosphorylates FKBP52 at Thr-143 in the hinge I region both in vitro and in vivo; CK2-phosphorylated FKBP52 fails to bind hsp90, revealing phosphorylation as a mechanism to regulate chaperone complex composition. |
In vitro kinase assay with purified CK2, deletion mutant mapping, [32P] in vivo labeling, hsp90 binding assay |
Proceedings of the National Academy of Sciences of the United States of America |
High |
9405642
|
| 1998 |
The TPR domain of FKBP52 requires appropriate downstream C-terminal sequences for hsp90 binding; unlike FKBP51, FKBP52's TPR domain does not require specific C-terminal sequences beyond the core TPR for hsp90 binding. FKBP52 and FKBP51 associate differentially with steroid receptors based on the TPR domain and poorly-conserved C-terminal sequences. |
Deletion mutant and chimera co-precipitation with hsp90, steroid receptor association assays |
Molecular endocrinology |
High |
9514152
|
| 1998 |
Hsp90 C-terminal EEVD motif is critical for interaction with TPR cochaperones including FKBP52; p23 binding maps to the N-terminal ATP-binding domain of Hsp90; deletion of Hsp90 residues 661–677 abolishes dimerization and reduces all accessory protein interactions. |
Co-precipitation of Hsp90 mutants with cochaperones including FKBP52 |
Cell stress & chaperones |
Medium |
9672247
|
| 1999 |
FKBP52 has one binding site per hsp90 dimer (cross-linking). The PPIase domain of FKBP52 mediates binding to cytoplasmic dynein (competed by PPIase fragment, not TPR fragment). FKBP52 also binds directly to the hsp90-free glucocorticoid receptor via a region distinct from both the PPIase and TPR domains. |
Chemical cross-linking of purified proteins, co-immunoadsorption from reticulocyte lysate, competitive inhibition with domain fragments |
The Journal of biological chemistry |
High |
10601253
|
| 2000 |
FKBP52 interacts with interferon regulatory factor-4 (IRF-4), inhibiting IRF-4–PU.1 binding to the immunoglobulin light chain enhancer and IRF-4–PU.1 transactivation; this inhibition requires functional PPIase activity of FKBP52 and induces a detectable structural modification of IRF-4. |
Co-immunoprecipitation, transcriptional reporter assay, partial proteolysis analysis, PPIase-inactive mutant |
Immunity |
Medium |
10714679
|
| 2001 |
The PPIase domain of FKBP52 links the GR-hsp90 heterocomplex to cytoplasmic dynein and is required for hormone-induced retrograde transport of the GFP-GR along microtubules to the nucleus; FKBP12 overexpression does not affect GFP-GR movement. |
Cotransfection with PPIase domain fragment, live-cell GFP-GR imaging, colcemid microtubule disruption, co-immunoadsorption from cytosol |
The Journal of biological chemistry |
High |
11278753
|
| 2001 |
Hormone binding to the GR induces substitution of FKBP51 by FKBP52 in the GR-hsp90 heterocomplex and concomitant recruitment of dynein, while hsp90 remains; the resulting GR-hsp90-FKBP52-dynein complex translocates from cytoplasm to nucleus before complex dissociation and conversion to DNA-binding form. |
Immunofluorescence, subcellular fractionation, co-immunoprecipitation in hormone-treated cells |
The Journal of biological chemistry |
High |
11751894
|
| 2001 |
FKBP52 chaperone activity resides in the C-terminal region (amino acids 264–400, domain 3, which overlaps with the TPR domain), while PPIase activity is confined to domain 1 (amino acids 1–148); the chaperone and hsp90-binding regions within domain 3 are distinct. |
Domain fragment expression, PPIase assay, chaperone aggregation assay, competition with Hsp90 C-terminal peptide |
The Journal of biological chemistry |
High |
11473108
|
| 2001 |
In the yeast model, FKBP52 is the only immunophilin that potentiates GR hormone-dependent transactivation (up to 20-fold at limiting hormone); this requires both Hsp90-binding ability and PPIase activity of FKBP52, and works by increasing GR hormone-binding affinity. |
Saccharomyces cerevisiae reporter gene assay, FKBP52 mutant analysis (PPIase-dead and TPR-dead mutants) |
The EMBO journal |
High |
12606580
|
| 2001 |
FKBP52 (dFKBP59) interacts directly with Drosophila TRPL Ca2+-permeable channels and with the scaffold protein INAD; expression of dFKBP59 inhibits Ca2+ influx through TRPL channels; mutations of conserved proline residues in TRPL (P702Q, P709Q) abolish interaction with dFKBP59. |
Yeast two-hybrid, co-immunoprecipitation in Sf9 and fly cells, electrophysiology (inside-out patch), fura-2 Ca2+ assay, site-directed mutagenesis |
The Journal of biological chemistry |
High |
11514552
|
| 2001 |
Two PPIase monomers bind to one Hsp90 dimer; FKBP52 has the strongest affinity for Hsp90 among the three mammalian large PPIases (vs. FKBP51 and CyP40); catalytic prolyl isomerase activity of FKBP52 corresponds to that of the small immunophilin FKBP12. |
In vitro binding assay with purified proteins, enzymatic PPIase assay |
Journal of molecular biology |
Medium |
11350175
|
| 2002 |
Crystal structure of the N-terminal FK506-binding domain of human FKBP52 (residues 1–140) solved at 2.4 Å; reveals six-stranded antiparallel beta-sheet plus alpha-helix similar to FKBP12; Pro120 and Lys121 explain reduced FK506 affinity and inability to activate calcineurin compared with FKBP12. |
X-ray crystallography, molecular replacement |
Acta crystallographica. Section D, Biological crystallography |
High |
12499534
|
| 2003 |
C-terminal sequences outside the core TPR domain (residues ~400–420 and the final 30 amino acids) of FKBP51 and FKBP52 differentially regulate hsp90 binding; the final 30 residues of FKBP51 enhance hsp90 binding while the corresponding region of FKBP52 moderates it. |
Truncation mutant and chimera co-immunoprecipitation with Hsp90 |
The Journal of biological chemistry |
Medium |
12611898
|
| 2004 |
FKBP52 PPIase domain I directly interacts with the copper metallochaperone Atox1; the interaction is enhanced by copper supplementation and decreased by copper chelation; FKBP52 overexpression increases rapid copper efflux in cells, implicating it in the copper efflux machinery. |
Yeast two-hybrid, GST pulldown, co-immunoprecipitation, 64Cu efflux assay |
The Journal of biological chemistry |
Medium |
15133031
|
| 2005 |
FKBP52 is a critical cochaperone for progesterone receptor (PR) in the uterus; Fkbp52-knockout female mice show complete implantation failure due to reduced P4 binding to PR, attenuated PR transcriptional activity, and down-regulation of P4-regulated genes—demonstrating tissue-specific regulation of hormone action. |
Fkbp52 knockout mice, hormone binding assay, PR transcriptional reporter, gene expression analysis, uterine fractionation |
Proceedings of the National Academy of Sciences of the United States of America |
High |
16176985
|
| 2005 |
FKBP52 is required for androgen receptor (AR) signaling in specific male reproductive tissues; FKBP52 is a component of AR complexes and enhances AR-mediated transactivation in a manner requiring both PPIase activity and Hsp90-binding ability; FKBP52 can restore function of a minimally active AR point mutant. |
Fkbp52 knockout mice, yeast and mammalian cell reporter assays, FKBP52 mutant analysis, co-IP of AR complexes |
Molecular endocrinology |
High |
15831525
|
| 2005 |
FKBP52 inhibits TRPV5 channel activity via its PPIase domain; FKBP52 co-localizes with and specifically interacts with TRPV5 in the distal nephron; PPIase-inactive mutant of FKBP52 loses the inhibitory effect on TRPV5. |
Co-immunoprecipitation, 45Ca2+ uptake, patch-clamp electrophysiology, PPIase domain mutant, siRNA knockdown |
American journal of physiology. Renal physiology |
High |
16352746
|
| 2006 |
FKBP52 facilitates intracellular trafficking of AAV vectors toward the nucleus via interaction with dynein; FKBP52-knockout MEFs show impaired nuclear accumulation of AAV genomes that is restored upon FKBP52 re-expression; intact AAV particles interact with both FKBP52 and dynein. |
Knockout MEF cells, self-complementary AAV transduction, nuclear fractionation, co-immunoprecipitation, FKBP52 rescue expression |
Virology |
Medium |
16828834
|
| 2006 |
Fkbp52 knockout specifically reduces AR transcriptional activity in mouse embryonic fibroblasts; chromatin immunoprecipitation shows normal AR occupancy at gene promoters in knockout cells, indicating FKBP52 controls a downstream step in AR transactivation rather than DNA binding. |
Fkbp52 knockout mouse, mouse embryonic fibroblasts, reporter assays, chromatin immunoprecipitation, hormone binding assay |
The Journal of biological chemistry |
High |
17142810
|
| 2007 |
The FK1 domain loop residue Pro119 (vs. Leu119 in FKBP51) is the critical determinant distinguishing FKBP52's ability to potentiate steroid receptor activity from FKBP51; PPIase catalytic activity is NOT required for potentiation, as PPIase-dead mutants still potentiate; the proline-rich loop overhanging the catalytic pocket is the functionally important receptor-interaction surface. |
Yeast genetic screen of randomly mutated FKBP51, site-directed mutagenesis, mammalian cell reporter assay |
Molecular and cellular biology |
High |
17938211
|
| 2007 |
FKBP52 directly and specifically binds tubulin; the TPR-containing region (aa 267–400) is required for tubulin binding; a C-terminal sequence (aa 375–458) is necessary and sufficient for microtubule depolymerization activity; FKBP52 prevents tubulin polymerization in vitro. |
Direct binding assay with purified proteins, domain deletion analysis, tubulin polymerization assay, co-localization in PC12 cells, siRNA knockdown |
FASEB journal |
High |
17435176
|
| 2009 |
FKBP52 links the mineralocorticoid receptor (MR)-hsp90 complex to dynein/dynactin motors for cytoplasmic-to-nuclear transport; replacement of FKBP52 by FKBP51 or TPR peptide favors cytoplasmic MR retention; the intact MR-hsp90 heterocomplex transits the nuclear pore undissociated. |
Immunofluorescence, fractionation, cross-linking of MR-hsp90 complexes, microtubule stabilization/reassembly assay on stripped MR immune pellets |
Molecular and cellular biology |
High |
20038533
|
| 2009 |
FKBP52 mediates stimulus-dependent gating of TRPC1 channels via cis/trans isomerization of proline residues in TRPC1; this is required for chemotropic turning of neuronal growth cones to netrin-1 and for netrin-1/DCC-dependent midline axon guidance in the spinal cord. FKBP12 mediates spontaneous (not stimulus-dependent) TRPC1 opening. |
Biochemical PPIase assay on TRPC1 peptides, dominant-negative FKBP52 expression, axon guidance assays in vitro and in vivo (mouse spinal cord) |
Neuron |
High |
19945390
|
| 2010 |
FKBP52 binds directly and specifically to Tau (preferentially its hyperphosphorylated form); FKBP52 antagonizes Tau-mediated microtubule assembly; FKBP52 overexpression in differentiated PC12 cells reduces neurite length and decreases Tau accumulation. |
Direct binding assay with purified proteins, microtubule assembly assay, co-localization in cortical neurons, PC12 overexpression, quantitative neurite length measurement |
Proceedings of the National Academy of Sciences of the United States of America |
High |
20133804
|
| 2011 |
FKBP52 favors nuclear retention of RelA/NF-κB, enhances its association with DNA consensus sequences, and increases NF-κB transcriptional activity; these effects require FKBP52 PPIase activity and TPR domain but not Hsp90 interaction. Upon stimulation, NF-κB complex exchanges FKBP51 for FKBP52 (analogous to steroid receptor switching). FKBP52 is functionally recruited to promoters of NF-κB target genes. |
Reporter gene assay, Co-IP with purified proteins, EMSA, ChIP, siRNA knockdown |
The Journal of biological chemistry |
High |
25104352
|
| 2011 |
Hsp90 can simultaneously accommodate FKBP52 and HOP, forming stable Hsp90(2)-FKBP52(1)-HOP(2) and Hsp90(2)-FKBP52(1)-p23(2)-HOP(2) complexes. |
Co-immunoprecipitation, dynamic light scattering, electron microscopy |
Oncotarget |
Medium |
21378414
|
| 2011 |
MJC13, a small molecule inhibitor, blocks FKBP52-enhanced AR function by preventing hormone-dependent dissociation of the Hsp90-FKBP52-AR complex, leading to less hormone-bound receptor in the nucleus and inhibiting AR-dependent gene expression and prostate cancer cell proliferation. |
Yeast reporter assay screen, co-immunoprecipitation, nuclear fractionation, qPCR of AR target genes, cell proliferation assay |
Proceedings of the National Academy of Sciences of the United States of America |
High |
21730179
|
| 2013 |
FKBP52 (FKBP52/Fkbp4) physically associates with Argonaute2 (hAgo2); FK506 treatment or siRNA depletion of Fkbp4/5 decreases Ago2 protein levels and impairs miRNA-mediated silencing; FKBP4 overexpression promotes miRNA-mediated Ago2 stabilization; unloaded Ago2 accumulates in FK506-treated cells. |
Co-immunoprecipitation (FKBP4-hAgo2), siRNA depletion, FK506 pharmacological inhibition, lysosome inhibitor rescue, miRNA reporter assay |
RNA (New York, N.Y.) |
Medium |
24049110
|
| 2013 |
FKBP4 (FKBP52) and p23 form a stable complex with hAgo2 and are required for efficient RNAi/RISC loading; the interaction occurs before small RNA loading and in the cytoplasm; depletion of FKBP4 or pharmacological disruption with FK506 reduces Ago2 levels and impairs RNAi. |
Co-immunoprecipitation, siRNA depletion, FK506 treatment, luciferase reporter silencing assay |
Molecular biology of the cell |
Medium |
23741051
|
| 2014 |
FKBP52 directly interacts with Tau-P301L (pathological mutant) and induces formation of Tau-P301L oligomers and filaments in vitro; FKBP52 knockdown in Tau-P301L transgenic zebrafish rescues defective axonal outgrowth and branching, and reduces pT181 phospho-Tau. |
Direct binding assay, EM analysis of oligomers/filaments, zebrafish Tau-P301L transgenic model with FKBP52 knockdown |
Proceedings of the National Academy of Sciences of the United States of America |
High |
24623856
|
| 2014 |
The FK1 domain of FKBP52 physically interacts with the glucocorticoid receptor (GR) as demonstrated by bimolecular fluorescence complementation and proximity ligation assays; this interaction is part of the FKBP52-dependent suppression of TDO expression in glioblastoma cells. |
Bimolecular fluorescence complementation, in situ proximity ligation assay, siRNA knockdown of FKBP52, TDO activity assay |
Glia |
Medium |
25132599
|
| 2015 |
FKBP52 induces aggregation of Tau-F4 fragment (Ser208–Ser324) into oligomers and filaments with prion-like seeding capacity; FKBP52-induced Tau-F4 oligomers can transfer conformational changes to full-length Tau in cells and seed aggregation of endogenous Tau in neuroblastoma cells. |
Light-scattering assay, blue native PAGE, electron microscopy, microtubule assembly assay, seeding in SH-SY5Y cells |
FASEB journal |
High |
25888602
|
| 2016 |
FKBP52 links the hTERT-Hsp90 complex to the dynein-dynactin motor via binding of the TPR domain to Hsp90 and the PPIase domain to dynamitin (Dyt); FKBP52 depletion inhibits hTERT nuclear transport and causes cytoplasmic accumulation and ubiquitin-dependent degradation of hTERT, abrogating telomerase activity. |
Co-immunoprecipitation, siRNA knockdown, nuclear/cytoplasmic fractionation, telomerase activity assay, dynamitin overexpression |
The Biochemical journal |
Medium |
27503910
|
| 2016 |
FKBP52's capacity to oligomerize Tau is independent of its PPIase catalytic activity (PPIase-dead mutant still oligomerizes Tau); the PHF6 peptide of Tau interacts with FK1/FK2 domains of FKBP52 independently of FK506 binding, identifying a non-catalytic interaction governing Tau oligomerization. |
In vitro oligomerization assay with PPIase-dead mutant, NMR interaction mapping, PPIase activity assay on Tau peptides |
Journal of molecular biology |
High |
26903089
|
| 2019 |
FKBP4 is a proximal interacting protein of PI3K, Akt, and mTOR components; FKBP4 depletion specifically reduces cell growth and proliferation of triple-negative breast cancer cells; FKBP4 can enhance Akt activation through PDK1 and mTORC2. |
BirA proximity-dependent biotin identification (BioID) proteomics, siRNA knockdown, xenograft tumor model, cell proliferation assay |
Theranostics |
Medium |
31660083
|
| 2021 |
FKBP4 promotes IKK complex assembly by interacting with both Hsp90 and IKK subunits (TPR domain required for Hsp90/IKK interaction, PPIase domain for IKKγ interaction), potentiating IKK kinase activity; FKBP4 also forms a complex with Hsp70/RelA to promote RelA nuclear translocation, activating NF-κB signaling in lung adenocarcinoma. |
Co-immunoprecipitation, domain deletion mutants, IKK kinase activity assay, nuclear fractionation, siRNA knockdown, xenograft |
Cell death & disease |
Medium |
34112753
|
| 2021 |
FKBP52 overexpression in wild-type mouse hippocampus promotes phosphorylation of AD-relevant tau species, activates gliosis, and causes neuronal loss; FKBP52 overexpression (not Aha1) impairs spatial reversal learning in aged mice. |
AAV-mediated overexpression in mouse hippocampus, histological analysis, behavioral testing, immunohistochemistry for phospho-tau |
Acta neuropathologica communications |
Medium |
33832539
|
| 2021 |
Both FKBP51 and FKBP52 are required for AR dimer formation and chromatin binding; depletion of either reduces AR phosphorylation; PPIase activity of FKBP51 is specifically required for AR dimerization; MJC13 (FKBP52-AR inhibitor) also inhibits AR dimer formation. |
siRNA depletion, AR dimerization assay, chromatin immunoprecipitation, phosphorylation analysis, FK506/MJC13 pharmacological inhibition |
Molecular oncology |
Medium |
34057812
|
| 2022 |
FKBP52 interacts with BRCA1 and stabilizes estrogen receptor α (ERα) protein; FKBP52 depletion decreases ERα expression and breast cancer cell proliferation; FKBP51 reduces ERα stability in an opposing manner. |
Co-immunoprecipitation (FKBP52-BRCA1), siRNA knockdown, ERα protein stability assay, cell proliferation assay |
Proceedings of the National Academy of Sciences of the United States of America |
Medium |
35394865
|
| 1995 |
FKBP52 (FKBP59-HBI) localizes to cytoplasm, nucleus, and partially co-localizes with microtubules in interphase non-lymphoid cells; during mitosis it segregates from chromosomes and associates with the mitotic apparatus (centrosome, spindle, interzone, cleavage furrow, midbodies). |
Indirect immunofluorescence confocal microscopy, Western blot of subcellular fractions, cytoskeletal drug treatment (taxol, nocodazole) |
Journal of cell science |
Medium |
7544801
|
| 1996 |
FAP48 is a novel 48-kDa protein that specifically interacts with the immunosuppressant-binding domain (domain I) of FKBP52 (FKBP59) and also with FKBP12 but not CyP40; this interaction is prevented by FK506 and rapamycin in a dose-dependent manner, suggesting FAP48 shares the macrolide-binding site on FKBP52. |
Yeast two-hybrid, in vitro direct interaction assay, in vivo co-immunoprecipitation, FK506/rapamycin competition |
The Journal of biological chemistry |
Medium |
8955134
|
| 2010 |
FKBP52 forms stable complexes with amyloid precursor protein (APP) through its FK506-interacting domain; FKBP52 overexpression reduces Abeta toxicity and increases lifespan in Abeta transgenic Drosophila; FKBP52 loss-of-function exacerbates Abeta phenotypes; FKBP52 interacts with Atox1 (copper transporter) and modulates intracellular copper levels, which influence Abeta pathology. |
Co-immunoprecipitation (FKBP52-APP), Drosophila transgenic gain/loss-of-function, copper chelator diet, intracellular copper measurement, cell reconstitution |
PloS one |
Medium |
20084280
|
| 2010 |
FKBP52 interaction with RET51 tyrosine kinase receptor is triggered by GDNF and NGF activation of RET51; phosphorylation of RET51 tyrosine 905 is required for complex formation; disruption of this phosphorylation site abolishes the RET51/FKBP52 complex. |
Co-immunoprecipitation, RET51 mutagenesis (Y905 mutation), growth factor stimulation assay |
Human molecular genetics |
Medium |
20442138
|
| 2012 |
FKBP52 localizes to the endolysosomal system in neurons and co-localizes with TRPC1 and Orai1 channels in human platelets; FKBP52 interaction with TRPC1 and IP3RII is required for maintenance of store-operated Ca2+ entry (SOCE); FK506/rapamycin reduce TRPC1-FKBP52 and TRPC1-IP3RII association, impairing SOCE. |
Immunoprecipitation, siRNA knockdown, Mn2+ entry assay, single-cell Ca2+ imaging, fura-2 Ca2+ measurement |
Biochimica et biophysica acta |
Medium |
23228564
|
| 2020 |
The neuroregenerative effects of FK506 in vivo are mediated specifically by FKBP52; Fkbp52-knockout mice fail to show FK506-induced locomotor recovery after spinal cord injury, while Fkbp51-knockout mice respond normally; FKBP51 binding of FK506 antagonizes FKBP52-mediated neurotrophic action. |
Fkbp52 and Fkbp51 knockout mice, spinal cord injury model, FK506 treatment, behavioral assessment of locomotion |
Biochemical pharmacology |
High |
32828804
|