Results 191 to 200 of about 98,169 (229)

FKBP immunophilin patents for neurological disorders

Expert Opinion on Therapeutic Patents, 2005
Immunophilins are a family of binding proteins that are highly conserved in nature and mediate the actions of immunosuppressant drugs. The FK-506-binding protein (FKBP) subclass of immunophilin bind FK-506 and rapamycin and are of particular interest due to their potent neurotrophic activity. Here, the patent literature covering the structures of novel
Robert E Babine, J Ernest Villafranca, Bruce G Gold   +2 more
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A Nonimmunosuppressant FKBP-12 Ligand Increases Nerve Regeneration

Experimental Neurology, 1997
The immunosuppressant drugs FK506 and cyclosporin A inhibit T-cell proliferation via a common mechanism: calcineurin inhibition following binding to their respective binding proteins, the peptidyl prolyl isomerases FKBP-12 and cyclophilin A. In contrast, FK506, but not cyclosporin A, accelerates nerve regeneration.
B G, Gold, M, Zeleny-Pooley, M S, Wang, P, Chaturvedi, D M, Armistead   +4 more
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Functions of the Hsp90-Binding FKBP Immunophilins

2014
Hsp90 functionally interacts with a broad array of client proteins, but in every case examined Hsp90 is accompanied by one or more co-chaperones. One class of co-chaperone contains a tetratricopeptide repeat domain that targets the co-chaperone to the C-terminal region of Hsp90.
Guy, Naihsuan, Garcia, Yenni A., Sivils, Jeffrey C., Galigniana, Mario D., Cox, Marc B.   +4 more
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FKBPs and their role in neuronal signaling

Biochimica et Biophysica Acta (BBA) - General Subjects, 2015
Ligands for FK506-binding proteins, also referred to as neuroimmunophilin ligands, have repeatedly been described as neuritotrophic, neuroprotective or neuroregenerative agents. However, the precise molecular mechanism of action underlying the observed effects has remained elusive, which eventually led to a reduced interest in FKBP ligand development.A
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Three-dimensional structure of FKBPs

1997
Abstract 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
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FKBP family proteins as promising new biomarkers for cancer

Current Opinion in Pharmacology, 2011
FK506-binding proteins (FKBPs) belong to the immunophilin family and bind immunosuppressive drugs, such as FK506 and rapamycin. These proteins, through interactions with steroid hormone receptors, kinases, or other cellular factors, play important roles in various physiological processes and, more interestingly, in pathological processes in mammals ...
Jérôme, Solassol, Alain, Mange, Thierry, Maudelonde   +2 more
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FKBP Binding Characteristics of Cardiac Microsomes from Diverse Vertebrates

Biochemical and Biophysical Research Communications, 2001
FK506 binding protein (FKBP) is a cytosolic receptor for the immunosuppressive drug FK-506. The common isoform, FKBP12, was found to be associated with the calcium release channel (ryanodine receptor 1) of different species of vertebrate skeletal muscle, whereas 12.6, a novel FKBP isoform was found to be associated with canine cardiac ryanodine ...
L H, Jeyakumar, L, Ballester, D S, Cheng, J O, McIntyre, P, Chang, H E, Olivey, L, Rollins-Smith, J V, Barnett, K, Murray, H B, Xin, S, Fleischer   +10 more
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Pleiotropic roles in cancer biology for multifaceted proteins FKBPs

Biochimica et Biophysica Acta (BBA) - General Subjects, 2015
FK506 binding proteins (FKBP) are multifunctional proteins highly conserved across the species and abundantly expressed in the cell. In addition to a well-established role in immunosuppression, FKBPs modulate several signal transduction pathways in the cell, due to their isomerase activity and the capability to interact with other proteins, inducing ...
ROMANO, SIMONA, D'ANGELILLO, ANNA, ROMANO, MARIA FIAMMETTA   +2 more
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Atomic Structure of FKBP-FK506, an Immunophilin-Immunosuppressant Complex

Science, 1991
The structure of the human FK506 binding protein (FKBP), complexed with the immunosuppressant FK506, has been determined to 1.7 angstroms resolution by x-ray crystallography. The conformation of the protein changes little upon complexation, but the conformation of FK506 is markedly different in the bound and unbound forms.
G D, Van Duyne, R F, Standaert, P A, Karplus, S L, Schreiber, J, Clardy   +4 more
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Neurospora crassa FKBPs

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.
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