Results 21 to 30 of about 477,265 (189)
Pharmacological Targeting of the Hsp70 Chaperone [PDF]
Current Topics in Medicinal Chemistry, 2009 The molecular chaperone, heat shock protein 70 (Hsp70), acts at multiple steps in a protein's life cycle, including during the processes of folding, trafficking, remodeling and degradation. To accomplish these various tasks, the activity of Hsp70 is shaped by a host of co-chaperones, which bind to the core chaperone and influence its functions. Genetic
Srikanth, Patury +2 more
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Molecules, 2020 Glycosidase inhibitors have shown great potential as pharmacological chaperones for lysosomal storage diseases. In light of this, a series of new cyclopentanoid β-galactosidase inhibitors were prepared and their inhibitory and pharmacological chaperoning
Patrick Weber +18 more
doaj +1 more source
Screening for pharmacological chaperones in Fabry disease [PDF]
Biochemical and Biophysical Research Communications, 2007 As a prerequisite for clinical trials of pharmacological chaperone therapy (PCT) for Fabry disease, we developed a rapid screening assay for enhancement of endogenous alpha-galactosidase A (alpha-Gal A) in patient-derived cells. We used a T-cell based system to screen 11 mutations causing Fabry disease for enhanceability using 1-deoxygalactonojirimycin
Sang-Hoon, Shin +7 more
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Kinetic model of ER folding and export, with and without pharmacological chaperone (PC).
, 2021 (A) The kinetic model, including unfolded state, U, folded state F, folded state bound to chaperone FB, and protein exported from the ER E. P is the rate of production of unfolded protein, kf is the folding rate, ku is the unfolding rate, konL is the ...
Jaie Woodard (8377059) +2 more
core +1 more source
Small molecule-mediated refolding and activation of myosin motor function
eLife, 2014 The small molecule EMD 57033 has been shown to stimulate the actomyosin ATPase activity and contractility of myofilaments. Here, we show that EMD 57033 binds to an allosteric pocket in the myosin motor domain.
Michael B Radke +5 more
doaj +1 more source
Frontiers in Neurology, 2022 Gaucher Disease (GD) 2 is a rare inherited lysosomal disorder. Early-onset and rapid progression of neurovisceral symptoms lead to fatal outcome in early childhood. Treatment is symptomatic, a curative therapy is currently not available. This prospective
Charlotte Aries +8 more
doaj +1 more source
Bringing dead proteins back to life
eLife, 2014 A small molecule called EMD 57033 can repair motor proteins that have stopped working as a result of stress.
Brandon A Wustman +3 more
doaj +1 more source
Pharmacological chaperone therapy for Fabry disease. [PDF]
Proc Jpn Acad Ser B Phys Biol Sci, 2012 Fabry disease is an inherited lysosomal storage disorder caused by deficient α-galactosidase A activity. Many missense mutations in Fabry disease often cause misfolded gene products, which leads to their retention in the endoplasmic reticulum by the quality control system; they are then removed by endoplasmic reticulum-associated degradation.
Ishii S.
europepmc +4 more sources
Cells, 2022 Chaperone-mediated autophagy (CMA) is a protein degradation mechanism through lysosomes. By targeting the KFERQ motif of the substrate, CMA is responsible for the degradation of about 30% of cytosolic proteins, including a series of proteins associated ...
Yi-Ting Wang, Jia-Hong Lu
doaj +1 more source
Using pharmacological chaperones to restore proteostasis [PDF]
Pharmacological Research, 2014 Normal organismal physiology depends on the maintenance of proteostasis in each cellular compartment to achieve a delicate balance between protein synthesis, folding, trafficking, and degradation while minimizing misfolding and aggregation. Defective proteostasis leads to numerous protein misfolding diseases.
Ya-Juan Wang, Xiao-Jing Di, Ting-Wei Mu
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