Results 141 to 150 of about 92,716 (181)
Some of the next articles are maybe not open access.
FKBP-12 is not an Inhibitor of Protein Kinase C
Immunological Investigations, 1992It was recently noted that the amino acid sequence of FK506 binding protein (FKBP-12) is nearly identical to that of an endogenous inhibitor of protein kinase C, PKCI-2. To follow up on this observation, we have tested the hypothesis that FKBP-12 is an inhibitor of PKC.
V A, Ruff +4 more
openaire +2 more sources
2016
In the 70s, after a decade from the purification of cyclosporine, a selective immunosuppressant agent and potent tool in transplantation medicine, a novel molecule was purified from bacteria Streptomyces tsukubaensis. This molecule, called FK506, showed the same selective immunosuppressant action as cyclosporine but was 10 to 100 fold more potent.
D'ARRIGO, PAOLO +4 more
openaire +2 more sources
In the 70s, after a decade from the purification of cyclosporine, a selective immunosuppressant agent and potent tool in transplantation medicine, a novel molecule was purified from bacteria Streptomyces tsukubaensis. This molecule, called FK506, showed the same selective immunosuppressant action as cyclosporine but was 10 to 100 fold more potent.
D'ARRIGO, PAOLO +4 more
openaire +2 more sources
Three-dimensional structure of FKBPs
1997Abstract The mammalian cytosolic FKBP12 protein was discovered through its ability to bind the immunosuppressive agents FK506 (tacrolimus) and rapamycin (sirolimus) (Harding et al., 1989; Siekierka et al., 1989). The FKBP family, for FK506 binding proteins, is growing rapidly, and the best characterized members are the mammalian proteins
J Liang, J Clardy
openaire +1 more source
Direct calculation of the binding free energies of FKBP ligands
The Journal of Chemical Physics, 2005Direct calculations of the absolute free energies of binding for eight ligands to FKBP protein were performed using the Fujitsu BioServer massively parallel computer. Using the latest version of the general assisted model building with energy refinement (AMBER) force field for ligand model parameters and the Bennett acceptance ratio for computing free ...
Hideaki, Fujitani +7 more
openaire +2 more sources
1997
Abstract FK506-binding proteins; rapamycin-binding proteins; peptidyl-prolyl cis-trans isomerases (PPIase, EC no. 5.2.1.8.); rotamases, immunophilins (Schreiber, 1992). Neurospora crassa is sensitive against the immunosuppressants FK506 and rapamycin, which originally were isolated as antifungal agents.
openaire +1 more source
Abstract FK506-binding proteins; rapamycin-binding proteins; peptidyl-prolyl cis-trans isomerases (PPIase, EC no. 5.2.1.8.); rotamases, immunophilins (Schreiber, 1992). Neurospora crassa is sensitive against the immunosuppressants FK506 and rapamycin, which originally were isolated as antifungal agents.
openaire +1 more source
Genome-Wide Identification and Analysis of FKBP Gene Family in Wheat (Triticum asetivum)
International Journal of Molecular Sciences, 2022Yuan Cao, Yu Long, Mingyue Cheng
exaly
Penetrating Exploration of Prognostic Correlations of the FKBP Gene Family with Lung Adenocarcinoma
Journal of Personalized Medicine, 2023Gangga Anuraga +2 more
exaly