Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 1 de 1
Filtrar
Mais filtros










Base de dados
Intervalo de ano de publicação
1.
Front Biosci (Landmark Ed) ; 26(12): 1627-1642, 2021 12 30.
Artigo em Inglês | MEDLINE | ID: mdl-34994177

RESUMO

Cells have evolved sophisticated molecular control systems to maximize the efficiency of the folding process. However, any subtle alteration of the environment or the protein can lead to misfolding or affect the conformational plasticity of the native states. It has been widely demonstrated that misfolding and/or conformational instability are the underlying mechanisms of several rare disorders caused by enzymatic deficits. In fact, disease-causing mutations often lead to the substitution of amino acids that are crucial for the achievement of a folded conformation, or play a role on the equilibrium between native-state conformers. One of the promising approaches to treat conformational disorders is the use of pharmacological chaperones (PCs), small molecules that specifically bind a target protein and stabilize a functional fold, thus increasing the amount of functionally active enzyme. Molecules acting as PCs are usually coenzymes, substrate analogues behaving as competitive inhibitors, or allosteric modulators. In this review, the general features of PCs are described, along with three examples of diseases (Gaucher disease, Phenylketonuria, and Primary Hyperoxaluria) in which this approach is currently under study at preclinical and/or clinical level.


Assuntos
Doença de Gaucher , Deficiências na Proteostase , Aminoácidos , Humanos , Chaperonas Moleculares/metabolismo , Dobramento de Proteína , Deficiências na Proteostase/tratamento farmacológico , Deficiências na Proteostase/genética
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA
...