Results 131 to 140 of about 92,716 (181)

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, Bruce G Gold
exaly   +2 more sources

FKBPs: at the crossroads of folding and transduction

Trends in Plant Science, 2001
FK506-binding proteins (FKBPs) belong to the large family of peptidyl-prolyl cis-trans isomerases, which are known to be involved in many cellular processes, such as cell signalling, protein trafficking and transcription. FKBPs associate into protein complexes, although the involvement and precise role of their foldase activity remain to be elucidated.
Harrar, Y., Bellini, Catherine, Faure, Jean Denis   +2 more
openaire   +3 more sources

Functions of the Hsp90-Binding FKBP Immunophilins

2022
The Hsp90 chaperone is known to interact with a diverse array of client proteins. However, in every case examined, Hsp90 is also accompanied by a single or several co-chaperone proteins. One class of co-chaperone contains a tetratricopeptide repeat (TPR) domain that targets the co-chaperone to the C-terminal region of Hsp90. Within this class are Hsp90-
Nina R, Ortiz, Naihsuan, Guy, Yenni A, Garcia, Jeffrey C, Sivils, Mario D, Galigniana, Marc B, Cox   +5 more
openaire   +2 more sources

FKBPs in chromatin modification and cancer

Current Opinion in Pharmacology, 2011
FK506-binding proteins (FKBPs) are intracellular receptors for FK506 and rapamycin, immunosuppressants that have recently been utilized as anticancer drugs. In the cytoplasm, FKBPs and these drugs modulate signal transduction pathways. However, recent reports reveal novel functions of FKBPs in the nucleus, which include regulation of transcription ...
Ya-Li, Yao, Ya-Chen, Liang, Huai-Huei, Huang, Wen-Ming, Yang   +3 more
openaire   +2 more sources

Design and synthesis of novel FKBP inhibitors

Journal of Medicinal Chemistry, 1992
Small molecule FKBP inhibitors were prepared with inhibitory activity ranging from micromolar to nanomolar. The design of these inhibitors derives from a structural analysis of the substrates for FKBP and cyclophilin. As a consequence of this analysis two key observations were made, namely: (1) amino ketone moieties are suitable as FKBP recognition ...
J R, Hauske, P, Dorff, S, Julin, J, DiBrino, R, Spencer, R, Williams   +5 more
openaire   +2 more sources

Recent Progress in FKBP Ligand Development

Current Molecular Pharmacology, 2015
FK506-binding proteins have been implicated in numerous human diseases suggesting novel therapeutic opportunities. In particular, the large FKBP51 has emerged as an important regulator of the stress-coping system and as an established risk factor for stress-related disorders.
Xixi, Feng, Sebastian, Pomplun, Felix, Hausch   +2 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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FKBP Ligands as Novel Therapeutics for Neurological Disorders

Mini-Reviews in Medicinal Chemistry, 2001
Given their clinical importance for the treatment of acute and chronic neurodegenerative diseases in humans including nerve injuries (e.g. Alzheimer's disease, Parkinson's disease, diabetic neuropathy) a number of different approaches were pursued to obtain selectively acting FK506-binding protein (FKBP) ligands: computational methods and target ...
C, Christner, T, Herdegen, G, Fischer
openaire   +2 more sources

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
openaire   +3 more sources

Targeting FKBP isoforms with small-molecule ligands

Current Opinion in Pharmacology, 2011
The FK506 binding protein (FKBP) family of proteins provide an interesting series of drug targets since different isoforms modulate diverse cellular pathways. There are therapeutic opportunities in the fields of cancer therapy, neurodegenerative conditions and psychiatric disorders. X-ray crystallographic or NMR data are available for eight of fourteen
Elizabeth A, Blackburn, Malcolm D, Walkinshaw   +1 more
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