Results 11 to 20 of about 92,716 (181)
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
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Bright Molecular Strain Probe Templates for Reporting Protein–Protein Interactions
Sensors, 2023 Imaging protein–protein interactions (PPIs) is a hot topic in molecular medicine in the postgenomic sequencing era. In the present study, we report bright and highly sensitive single-chain molecular strain probe templates which embed full-length Renilla ...
Sung-Bae Kim +5 more
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Molecular Therapy: Nucleic Acids, 2022 Genetic lineage tracing is indispensable to unraveling the origin, fate, and plasticity of cells. However, the intrinsic leakiness in the CreER-loxP system raises concerns on data interpretation. Here, we reported the generation of a novel dual inducible
Mianqiao Chen +7 more
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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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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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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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Solution structure of FK506 bound to FKBP‐12 [PDF]
FEBS Letters, 1992 The complex of the immunosuppressant FK506 bound to FKBP‐12 has been studied in solution using 1H and inverse‐detected 13C NMR methods. The resonances of bound, 13C‐labelled FK506 were assigned and a set of 66 intraligand NOE distance restraints were used to calculate the structure of the bound ligand by distance geometry and restrained molecular ...
Lepre, Christopher A. +2 more
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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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FKBP51 and FKBP12.6-Novel and tight interactors of Glomulin.
PLoS ONE, 2019 The protein factor Glomulin (Glmn) is a regulator of the SCF (Skp1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex. Mutations of Glmn lead to glomuvenous malformations.
Andreas Hähle +6 more
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