Results 1 to 10 of about 93,555 (212)

FKBP Ligands—Where We Are and Where to Go? [PDF]

open access: yesFrontiers in Pharmacology, 2018
In recent years, many members of the FK506-binding protein (FKBP) family were increasingly linked to various diseases. The binding domain of FKBPs differs only in a few amino acid residues, but their biological roles are versatile.
Jürgen M Kolos   +2 more
exaly   +7 more sources

InterAKTions with FKBPs--mutational and pharmacological exploration. [PDF]

open access: yesPLoS ONE, 2013
The FK506-binding protein 51 (FKBP51) is an Hsp90-associated co-chaperone which regulates steroid receptors and kinases. In pancreatic cancer cell lines, FKBP51 was shown to recruit the phosphatase PHLPP to facilitate dephosphorylation of the kinase Akt,
Anne-Katrin Fabian   +5 more
doaj   +8 more sources

Effect of FKBP12-Derived Intracellular Peptides on Rapamycin-Induced FKBP–FRB Interaction and Autophagy [PDF]

open access: yesCells, 2022
Intracellular peptides (InPeps) generated by proteasomes were previously suggested as putative natural regulators of protein–protein interactions (PPI).
Carolina A. Parada   +12 more
doaj   +3 more sources

Steric confinement-induced emission probe for monitoring protein conformations in live cells [PDF]

open access: yesCommunications Chemistry
Protein conformational changes drive signal transduction to regulate cellular activities, yet monitoring of these changes in living cells remains challenging.
Huixia Jia   +8 more
doaj   +2 more sources

Functional identification of a Streptomyces lividans FKBP-like protein involved in the folding of overproduced secreted proteins [PDF]

open access: yesOpen Biology, 2019
Some bacterial peptidyl-prolyl cis/trans isomerases (PPIases) are involved in secretory protein folding after the translocation step. Streptomyces lividans has been used as a host for engineering extracellular overproduction of homologous and ...
R. L. Vicente   +5 more
doaj   +1 more source

The free energy landscape of small molecule unbinding. [PDF]

open access: yesPLoS Computational Biology, 2011
The spontaneous dissociation of six small ligands from the active site of FKBP (the FK506 binding protein) is investigated by explicit water molecular dynamics simulations and network analysis.
Danzhi Huang, Amedeo Caflisch
doaj   +1 more source

Detection and characterization of protein interactions in vivo by a simple live-cell imaging method. [PDF]

open access: yesPLoS ONE, 2013
Over the last decades there has been an explosion of new methodologies to study protein complexes. However, most of the approaches currently used are based on in vitro assays (e.g.
Oriol Gallego   +5 more
doaj   +1 more source

Identification, characterization and spatiotemporal expression analysis of the FKBP family genes in Locusta migratoria

open access: yesScientific Reports, 2023
FK506 binding proteins (FKBPs) are a highly-conserved group of proteins known to bind to FK506, an immunosuppressive drug. They play different physiological roles, including transcription regulation, protein folding, signal transduction and ...
Neng Zhang   +10 more
doaj   +1 more source

Bright Molecular Strain Probe Templates for Reporting Protein–Protein Interactions

open access: yesSensors, 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
doaj   +1 more source

Membrane tethering of CreER decreases uninduced cell labeling and cytotoxicity while maintaining recombination efficiency

open access: yesMolecular 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
doaj   +1 more source

Home - About - Disclaimer - Privacy