Protein Misfolding Diseases.
Annu Rev Biochem
; 86: 21-26, 2017 06 20.
Article
en En
| MEDLINE
| ID: mdl-28441058
ABSTRACT
The majority of protein molecules must fold into defined three-dimensional structures to acquire functional activity. However, protein chains can adopt a multitude of conformational states, and their biologically active conformation is often only marginally stable. Metastable proteins tend to populate misfolded species that are prone to forming toxic aggregates, including soluble oligomers and fibrillar amyloid deposits, which are linked with neurodegeneration in Alzheimer and Parkinson disease, and many other pathologies. To prevent or regulate protein aggregation, all cells contain an extensive protein homeostasis (or proteostasis) network comprising molecular chaperones and other factors. These defense systems tend to decline during aging, facilitating the manifestation of aggregate deposition diseases. This volume of the Annual Review of Biochemistry contains a set of three articles addressing our current understanding of the structures of pathological protein aggregates and their associated disease mechanisms. These articles also discuss recent insights into the strategies cells have evolved to neutralize toxic aggregates by sequestering them in specific cellular locations.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Enfermedad de Parkinson
/
Envejecimiento
/
Deficiencias en la Proteostasis
/
Enfermedad de Alzheimer
/
Agregación Patológica de Proteínas
Límite:
Humans
Idioma:
En
Revista:
Annu Rev Biochem
Año:
2017
Tipo del documento:
Article