Results 21 to 30 of about 93,555 (212)
Biochimica et Biophysica Acta (BBA) - General Subjects, 2015 FK506-binding proteins (FKBPs) contain a domain with peptidyl-prolyl-cis/trans-isomerase (PPIase) activity and bind the immunosuppressive drugs FK506 and rapamycin. FKBPs belong to the immunophilin family and are found in eukaryotes and bacteria.In this review we describe two major groups of bacterial virulence-associated FKBPs, the trigger factor and ...
Unal, Can M., Steinert, Michael
openaire +4 more sources
Computational and Structural Biotechnology Journal, 2018 The two classical immunophilin families, found essentially in all living cells, are: cyclophilin (CYN) and FK506-binding protein (FKBP). We previously reported a novel class of immunophilins that are natural chimera of these two, which we named dual ...
Sailen Barik
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FK506 regulates IP3 evoked Ca2+ release independently of FKBP in endothelial cells [PDF]
, 2020 Background and Purpose FK506 and rapamycin are modulators of FK-binding proteins (FKBP) that are used to suppress immune function after organ and hematopoietic stem cell transplantations.
Charlotte Buckley +5 more
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Dual-Family Peptidylprolyl Isomerases (Immunophilins) of Select Monocellular Organisms
Biomolecules, 2018 The dual-family peptidylprolyl cis-trans isomerases (immunophilins) represent a naturally occurring chimera of the classical FK506-binding protein (FKBP) and cyclophilin (CYN), connected by a flexible linker.
Sailen Barik
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Caffeine‐Operated Synthetic Modules for Chemogenetic Control of Protein Activities by Life Style
Advanced Science, 2021 A genetically encoded caffeine‐operated synthetic module (COSMO) is introduced herein as a robust chemically induced dimerization (CID) system. COSMO enables chemogenetic manipulation of biological processes by caffeine and its metabolites, as well as ...
Tianlu Wang +8 more
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Distribution of Peptidyl-Prolyl Isomerase (PPIase) in the Archaea
Frontiers in Microbiology, 2021 Cis-trans isomerization of the peptide bond prior to proline is an intrinsically slow process but plays an essential role in protein folding. In vivo cis-trans isomerization reaction is catalyzed by Peptidyl-prolyl isomerase (PPIases), a category of ...
Anchal, Vineeta Kaushik, Manisha Goel
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, 2023 Legionella pneumophila is the causative agent of Legionnaires’ disease, a serious form of pneumonia. Its macrophage infectiv-ity potentiator (Mip), a member of a highly conserved family of FK506-binding proteins, plays a major role in the prolifera-tion ...
Robin, Deutscher +12 more
core +1 more source
Basic surface features of nuclear FKBPs facilitate chromatin binding
Scientific Reports, 2017 The nucleoplasmin family of histone chaperones is identified by a pentamer-forming domain and multiple acidic tracts that mediate histone binding and chaperone activity.
Andrew Leung +10 more
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Recent progress with FKBP-derived destabilizing domains [PDF]
Bioorganic & Medicinal Chemistry Letters, 2008 The FKBP-derived destabilizing domains are increasingly being used to confer small molecule-dependent stability to many different proteins. The L106P domain confers instability to yellow fluorescent protein when it is fused to the N-terminus, the C-terminus, or spliced into the middle of yellow fluorescent protein, however multiple copies of L106P do ...
Bernard W, Chu +3 more
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JCI Insight, 2023 We examine whether calcineurin or protein phosphatase 2B (PP2B) regulates the basolateral inwardly rectifying potassium channel Kir4.1/Kir5.1 in the distal convoluted tubule (DCT). Application of tacrolimus (FK506) or cyclosporine A (CsA) increased whole-
Dan-Dan Zhang +7 more
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