Results 21 to 30 of about 16,862 (246)

GCase Enhancers: A Potential Therapeutic Option for Gaucher Disease and Other Neurological Disorders

Pharmaceuticals, 2022
Pharmaceutical chaperones (PCs) are small compounds able to bind and stabilize misfolded proteins, allowing them to recover their native folding and thus their biological activity.
Macarena Martínez-Bailén, Francesca Clemente, Camilla Matassini, Francesca Cardona   +3 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, Gary J, Murray, Stefanie, Kluepfel-Stahl, Adele M, Cooney, Jane M, Quirk, Raphael, Schiffmann, Roscoe O, Brady, Christine R, Kaneski   +7 more
openaire   +2 more sources

Therapy of Fabry disease with pharmacological chaperones: from in silico predictions to in vitro tests

Orphanet Journal of Rare Diseases, 2011
Background Fabry disease is a rare disorder caused by a large variety of mutations in the gene encoding lysosomal alpha-galactosidase. Many of these mutations are unique to individual families. Fabry disease can be treated with enzyme replacement therapy,
Cammisa Marco, Orlando Pierangelo, De Crescenzo Agostina, Citro Valentina, Andreotti Giuseppina, Correra Antonella, Cubellis Maria Vittoria   +6 more
doaj   +1 more source

Image-based screen capturing misfolding status of Niemann-Pick type C1 identifies potential candidates for chaperone drugs.

PLoS ONE, 2020
Niemann-Pick disease type C is a rare, fatal neurodegenerative disorder characterized by massive intracellular accumulation of cholesterol. In most cases, loss-of-function mutations in the NPC1 gene that encodes lysosomal cholesterol transporter NPC1 are
Ryuta Shioi, Fumika Karaki, Hiromasa Yoshioka, Tomomi Noguchi-Yachide, Minoru Ishikawa, Kosuke Dodo, Yuichi Hashimoto, Mikiko Sodeoka, Kenji Ohgane   +8 more
doaj   +1 more source

Identification of an Allosteric Binding Site on Human Lysosomal Alpha-Galactosidase Opens the Way to New Pharmacological Chaperones for Fabry Disease.

PLoS ONE, 2016
Personalized therapies are required for Fabry disease due to its large phenotypic spectrum and numerous different genotypes. In principle, missense mutations that do not affect the active site could be rescued with pharmacological chaperones.
Valentina Citro, Jorge Peña-García, Helena den-Haan, Horacio Pérez-Sánchez, Rosita Del Prete, Ludovica Liguori, Chiara Cimmaruta, Jan Lukas, Maria Vittoria Cubellis, Giuseppina Andreotti   +9 more
doaj   +1 more source

Simulation of the Interactions of Arginine with Wild-Type GALT Enzyme and the Classic Galactosemia-Related Mutant p.Q188R by a Computational Approach

Molecules, 2021
Classic galactosemia is an inborn error of metabolism associated with mutations that impair the activity and the stability of galactose-1-phosphate uridylyltransferase (GALT), catalyzing the third step in galactose metabolism.
Anna Verdino, Gaetano D’Urso, Carmen Tammone, Bernardina Scafuri, Lucrezia Catapano, Anna Marabotti   +5 more
doaj   +1 more source

Assessment of FDA-Approved Drugs as a Therapeutic Approach for Niemann-Pick Disease Type C1 Using Patient-Specific iPSC-Based Model Systems

Cells, 2022
Niemann-Pick type C1 (NP-C1) is a fatal, progressive neurodegenerative disease caused by mutations in the NPC1 gene. Mutations of NPC1 can result in a misfolded protein that is subsequently marked for proteasomal degradation.
Christin Völkner, Supansa Pantoom, Maik Liedtke, Jan Lukas, Andreas Hermann, Moritz J. Frech   +5 more
doaj   +1 more source

Using pharmacological chaperones to restore proteostasis. [PDF]

Pharmacol Res, 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.
Wang YJ, Di XJ, Mu TW.
europepmc   +4 more sources

Pharmacological Chaperones for the Mucopolysaccharidoses [PDF]

, 2019
The mucopolysaccharidoses (MPS) are a group of 11 lysosomal storage diseases (LSDs) produced by mutations in the enzymes involved in the lysosomal catabolism of glycosaminoglycans. Most of the mutations affecting these enzymes may lead to changes in processing, folding, glycosylation, pH stability, protein aggregation, and defective transport to the ...
Juan Camilo Losada Diaz, Jacobo Cepeda Del Castillo, Edwin Alexander Rodríguez López, Carlos Javier Alméciga-Díaz   +3 more
openaire   +1 more source

Chemical chaperones exceed the chaperone effects of RIC-3 in promoting assembly of functional α7 AChRs. [PDF]

PLoS ONE, 2013
Functional α7 nicotinic acetylcholine receptors (AChRs) do not assemble efficiently in cells transfected with α7 subunits unless the cells are also transfected with the chaperone protein RIC-3.
Alexander Kuryatov, Jayanta Mukherjee, Jon Lindstrom   +2 more
doaj   +1 more source