Protein Misfolding and Aggregation in Proteinopathies: Causes, Mechanism and Cellular Response

被引:26
作者
Ajmal, Mohammad Rehan [1 ]
机构
[1] Univ Tabuk, Fac Sci, Biochem Dept, Phys Biochem Res Lab, Tabuk 71491, Saudi Arabia
关键词
protein aggregation; amyloid diseases; aggregation inhibition; inflammation; neurodegeneration; AMYLOID-BETA; QUALITY-CONTROL; ENDOPLASMIC-RETICULUM; MOLECULAR CHAPERONES; BASIC MECHANISMS; COMMON MECHANISM; GALLIC ACID; ALZHEIMERS; DISEASES; YEAST;
D O I
10.3390/diseases11010030
中图分类号
R-3 [医学研究方法]; R3 [基础医学];
学科分类号
1001 ;
摘要
Proteins are central to life functions. Alterations in the structure of proteins are reflected in their function. Misfolded proteins and their aggregates present a significant risk to the cell. Cells have a diverse but integrated network of protection mechanisms. Streams of misfolded proteins that cells are continuously exposed to must be continually monitored by an elaborated network of molecular chaperones and protein degradation factors to control and contain protein misfolding problems. Aggregation inhibition properties of small molecules such as polyphenols are important as they possess other beneficial properties such as antioxidative, anti-inflammatory, and pro-autophagic properties and help neuroprotection. A candidate with such desired features is important for any possible treatment development for protein aggregation diseases. There is a need to study the protein misfolding phenomenon so that we can treat some of the worst kinds of human ailments related to protein misfolding and aggregation.
引用
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页数:18
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