PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16278292-7 2005 However, FK506, which with FKBP12 inhibits calcineurin (but not mTOR), potentiated the IP3-evoked [Ca2+]c increase. Tacrolimus 9-14 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 27-33 11896462-4 2002 In this approach, the Akt PH domain has been replaced with the rapamycin (and FK506)-binding domain, FKBP12, to make F3-DeltaPH.Akt. Tacrolimus 78-83 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 101-107 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 1A pseudogene 3 Homo sapiens 85-92 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 1A pseudogene 3 Homo sapiens 15-21 9742506-1 1998 BACKGROUND: The 12 kD FK506 binding protein FKBP12 is a cytosolic receptor for the immunosuppressant drugs FK506 and rapamycin. Tacrolimus 22-27 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 44-50 10361256-2 1999 The mechanism of this inhibition is investigated using FK506, which competes with rapamycin for binding to their common target FK506-binding protein (FKBP)12. Tacrolimus 55-60 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 150-157 9742506-3 1998 We investigated a role for FKBP12 in male reproductive physiology on the basis of our identification of extremely high levels of [3H]FK506 binding in male reproductive tissues. Tacrolimus 133-138 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 27-33 9742506-12 1998 FKBP12 was purified from epididymal plasma by FK506 affinity chromatography. Tacrolimus 46-51 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 0-6 21673995-2 2011 The FK506-FKBP12 complex associates with calcineurin and inhibits its phosphatase activity, resulting in inhibition of nuclear translocation of nuclear factor of activated T-cells (NFAT). Tacrolimus 4-9 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 10-16 9096348-3 1997 FK1012 is used as a pharmacological mediator of dimerization to bring together FK506 binding domains, taken from the endogenous protein FKBP12. Tacrolimus 79-84 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 136-142 9061187-0 1997 Modeling the interaction between FK506 and FKBP12: a mechanism for formation of the calcineurin inhibitory complex. Tacrolimus 33-38 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 43-49 9061187-1 1997 FK506 is a naturally occurring immunosuppressant whose mode of action involves formation of an initial complex with the cytosolic protein FKBP12. Tacrolimus 0-5 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 138-144 9061187-7 1997 Comparison of the structure of Z-Arg32-ascomycin in water with structures of FK506 bound to FKBP12 indicate that the conformation of the pipecolate region is conserved during the binding process. Tacrolimus 77-82 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 92-98 9061187-10 1997 From computer models and molecular dynamics simulations of interactions between FK506 and FKBP12 we suggest that the conformational changes observed in bound FK506 are induced by the interaction between the 80"s loop of FKBP12 and the pyranose ring of FKBP12. Tacrolimus 80-85 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 90-96 9061187-10 1997 From computer models and molecular dynamics simulations of interactions between FK506 and FKBP12 we suggest that the conformational changes observed in bound FK506 are induced by the interaction between the 80"s loop of FKBP12 and the pyranose ring of FKBP12. Tacrolimus 80-85 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 220-226 9061187-10 1997 From computer models and molecular dynamics simulations of interactions between FK506 and FKBP12 we suggest that the conformational changes observed in bound FK506 are induced by the interaction between the 80"s loop of FKBP12 and the pyranose ring of FKBP12. Tacrolimus 80-85 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 220-226 9061187-10 1997 From computer models and molecular dynamics simulations of interactions between FK506 and FKBP12 we suggest that the conformational changes observed in bound FK506 are induced by the interaction between the 80"s loop of FKBP12 and the pyranose ring of FKBP12. Tacrolimus 158-163 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 90-96 9061187-10 1997 From computer models and molecular dynamics simulations of interactions between FK506 and FKBP12 we suggest that the conformational changes observed in bound FK506 are induced by the interaction between the 80"s loop of FKBP12 and the pyranose ring of FKBP12. Tacrolimus 158-163 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 220-226 9061187-10 1997 From computer models and molecular dynamics simulations of interactions between FK506 and FKBP12 we suggest that the conformational changes observed in bound FK506 are induced by the interaction between the 80"s loop of FKBP12 and the pyranose ring of FKBP12. Tacrolimus 158-163 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 220-226 8774885-3 1996 To examine whether induced oligomerization can alter Raf kinase activity, sequences encoding the FK506-binding protein FKBP12 were fused to the amino terminus of c-Raf-1, introducing a binding site for FK506. Tacrolimus 97-102 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 119-125 29664738-4 2018 We further report that ARNT expression itself is controlled by the FKBP12/YY1 transcriptional repressor complex and that disruption of such FKBP12/YY1 complexes by picomolar FK506 at subimmunosuppressive doses increases ARNT expression, subsequently leading to homodimeric ARNT-induced ALK3 transcription. Tacrolimus 174-179 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 140-146 23305836-4 2013 Although FKBP12 was first identified as the principal intracellular target for the immunosuppressive drugs, FK506 and rapamycin, new insights into the role of FKBPs have since emerged. Tacrolimus 108-113 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 9-15 22100703-5 2012 Using NMR chemical shift mapping, we show that the important binding residues in FKBP12 are located in its hydrophobic FK506 binding region. Tacrolimus 119-124 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 81-87 22100703-6 2012 Consistently, we demonstrate that FK506 can competitively inhibit the interaction between FKBP12 and the dipeptide motifs of the calcium channels. Tacrolimus 34-39 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 90-96 25118278-3 2014 Through insertion of a modified FK506 binding protein (insertable FKBP12, iFKBP) into the protein kinase isoforms Fyn, Src, Lyn, and Yes, we engineered kinase analogs that can be activated within minutes in living cells (RapR analogs). Tacrolimus 32-37 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 66-72 25316243-8 2014 First, FK506 binds FK506 binding protein 12 and its related isoform 12.6 (FKBP12/12.6) and removes them from intracellular ryanodine receptors that induce a calcium ion leakage from the endoplasmic/sarcoplasmic reticulum. Tacrolimus 7-12 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 74-80 25316243-8 2014 First, FK506 binds FK506 binding protein 12 and its related isoform 12.6 (FKBP12/12.6) and removes them from intracellular ryanodine receptors that induce a calcium ion leakage from the endoplasmic/sarcoplasmic reticulum. Tacrolimus 19-24 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 74-80 26589173-0 2013 Absolute Free Energy of Binding and Entropy of the FKBP12-FK506 Complex: Effects of the Force Field. Tacrolimus 58-63 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 51-57 26589173-5 2013 In this paper, we check the performance of HSMD-TI by applying it to the relatively large ligand FK506 (126 atoms) complexed with the protein FKBP12, where DeltaA(0) = -12.8 kcal/mol is known experimentally as well as the crystal structure of the complex. Tacrolimus 97-102 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 142-148 17950843-7 2008 Under these conditions FK506, which displaces FKBP12 (to inhibit calcineurin) and rapamycin, which displaces FKBP12 (to inhibit mTOR), each increased the [Ca(2+)](c) rise evoked by caffeine. Tacrolimus 23-28 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 46-52