Tuning protein folding in lysosomal storage diseases: the chemistry behind pharmacological chaperones

被引：69
作者：
Pereira, David M. [1 ]
Valentao, Patricia [1 ]
Andrade, Paula B. [1 ]
机构：
[1] Univ Porto, REQUIMTE LAQV, Lab Farmacognosia, Dept Quim,Fac Farm, Rua Jorge Viterbo Ferreira 228, P-4050313 Oporto, Portugal
来源：
CHEMICAL SCIENCE | 2018年 / 9卷 / 07期
关键词：
TYPE-1; GAUCHER-DISEASE; GLOBOID-CELL LEUKODYSTROPHY; ENZYME REPLACEMENT THERAPY; ACID-BETA-GLUCOSIDASE; KRABBE-DISEASE; CHEMICAL CHAPERONES; ALPHA-GALACTOSIDASE; MOLECULAR-BASIS; FABRY DISEASE; ENDOPLASMIC-RETICULUM;
D O I：
10.1039/c7sc04712f
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Misfolding of proteins is the basis of several proteinopathies. Chemical and pharmacological chaperones are small molecules capable of inducing the correct conformation of proteins, thus being of interest for human therapeutics. The most recent developments in medicinal chemistry and in the drug development of pharmacological chaperones are discussed, with focus on lysosomal storage diseases.
引用
收藏
页码：1740 / 1752
页数：13
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