Results 181 to 190 of about 98,169 (229)
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FKBPs in chromatin modification and cancer
Current Opinion in Pharmacology, 2011FK506-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 +3 more
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Functions of the Hsp90-Binding FKBP Immunophilins
2022The 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 +5 more
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Recent Progress in FKBP Ligand Development
Current Molecular Pharmacology, 2015FK506-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 +2 more
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Targeting FKBP isoforms with small-molecule ligands
Current Opinion in Pharmacology, 2011The 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 +1 more
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Mammalian FKBP-25 and Its Associated Proteins
Archives of Biochemistry and Biophysics, 2000Soluble proteins from porcine brain were divided into two packs: (1) proteins which pass freely through CM52-cellulose, and (2) proteins retained on CM52. Each of these two packs of proteins was fractionated on preparative flat-bed isoelectrofocusing gel in the range of pH 2-12.
M, Leclercq, F, Vinci, A, Galat
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Design and synthesis of novel FKBP inhibitors
Journal of Medicinal Chemistry, 1992Small 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 +5 more
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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
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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
FKBP Ligands as Novel Therapeutics for Neurological Disorders
Mini-Reviews in Medicinal Chemistry, 2001Given 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
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FKBPs: at the crossroads of folding and transduction
Trends in Plant Science, 2001FK506-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. +2 more
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