Results 11 to 20 of about 477,265 (189)

Molecular and pharmacological chaperones for SOD1 [PDF]

Biochemical Society Transactions, 2020
The efficacy of superoxide dismutase-1 (SOD1) folding impacts neuronal loss in motor system neurodegenerative diseases. Mutations can prevent SOD1 post-translational processing leading to misfolding and cytoplasmic aggregation in familial amyotrophic ...
Wright, Gareth SA
core   +4 more sources

Tamoxifen enhances the Hsp90 molecular chaperone ATPase activity. [PDF]

PLoS ONE, 2010
Hsp90 is an essential molecular chaperone that is also a novel anti-cancer drug target. There is growing interest in developing new drugs that modulate Hsp90 activity.Using a virtual screening approach, 4-hydroxytamoxifen, the active metabolite of the ...
Rongmin Zhao, Elisa Leung, Stefan Grüner, Matthieu Schapira, Walid A Houry   +4 more
doaj   +2 more sources

Carnitine is a pharmacological allosteric chaperone of the human lysosomal α-glucosidase [PDF]

Journal of Enzyme Inhibition and Medicinal Chemistry, 2021
Pompe disease is an inherited metabolic disorder due to the deficiency of the lysosomal acid α-glucosidase (GAA). The only approved treatment is enzyme replacement therapy with the recombinant enzyme (rhGAA).
Roberta Iacono, Nadia Minopoli, Maria Carmina Ferrara, Antonietta Tarallo, Carla Damiano, Caterina Porto, Sandra Strollo, Véronique Roig-Zamboni, Gianfranco Peluso, Gerlind Sulzenbacher, Beatrice Cobucci-Ponzano, Giancarlo Parenti, Marco Moracci   +12 more
doaj   +3 more sources

Pharmacological chaperone therapy for lysosomal storage diseases

Future Medicinal Chemistry, 2014
Pharmacological chaperone therapy is an emerging approach to treat lysosomal storage diseases. Small-molecule chaperones interact with mutant enzymes, favor their correct conformation and enhance their stability.
FECAROTTA, SIMONA, MORACCI, Marco, PARENTI, GIANCARLO, ANDRIA, GENEROSO, Moracci M, Andria Generoso, Parenti Giancarlo, Fecarotta Simona, Moracci Marco, Andria G, Parenti G, Fecarotta S   +11 more
core   +7 more sources

Chaperone-Dependent Mechanisms as a Pharmacological Target for Neuroprotection

International Journal of Molecular Sciences, 2023
Modern pharmacotherapy of neurodegenerative diseases is predominantly symptomatic and does not allow vicious circles causing disease development to break.
Elena V. Abramova, Ekaterina R. Verbovaya, Yulia V. Vakhitova, Sergei B. Seredenin, Mikhail V. Voronin   +4 more
core   +3 more sources

Galactosemia: Towards Pharmacological Chaperones [PDF]

Journal of Personalized Medicine, 2021
Galactosemia is a rare inherited metabolic disease resulting from mutations in the four genes which encode enzymes involved in the metabolism of galactose. The current therapy, the removal of galactose from the diet, is inadequate. Consequently, many patients suffer lifelong physical and cognitive disability.
Samantha Banford, Thomas J. McCorvie, Angel L. Pey, David J. Timson   +3 more
openaire   +3 more sources

Pharmacological therapies for monogenic obesity caused by MC4R dysfunction [PDF]

, 2010
PhDMutations in the melanocortin-4 receptor (MC4R) are the most common cause of monogenic obesity. The majority of MC4R mutations are predicted to cause the receptor to aberrantly fold.
Gooljar, Sakina B
core   +4 more sources

Bromocriptine as a Novel Pharmacological Chaperone for Mucopolysaccharidosis IV A. [PDF]

ACS Med Chem Lett, 2020
Mucopolysaccharidosis IVA (MPS IVA) is a lysosomal storage disease caused by mutations in the gene encoding for the enzyme N-acetylgalactosamine-6-sulfate sulfatase (GALNS), leading to lysosomal accumulation of keratan sulfate (KS) and chondroitin-6-sulfate. In this study, we identified and characterized bromocriptine (BC) as a novel PC for MPS IVA. BC
Olarte-Avellaneda S, Cepeda Del Castillo J, Rojas-Rodriguez AF, Sánchez O, Rodríguez-López A, Suárez García DA, Pulido LMS, Alméciga-Díaz CJ.   +7 more
europepmc   +4 more sources

Pharmacological Chaperones for the Mucopolysaccharidoses [PDF]

International Journal of Molecular Sciences, 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   +3 more sources

Pharmacological chaperoning: A primer on mechanism and pharmacology [PDF]

Pharmacological Research, 2014
Approximately forty percent of diseases are attributable to protein misfolding, including those for which genetic mutation produces misfolding mutants. Intriguingly, many of these mutants are not terminally misfolded since native-like folding, and subsequent trafficking to functional locations, can be induced by target-specific, small molecules ...
Nancy J, Leidenheimer, Katelyn G, Ryder
openaire   +2 more sources