Phenotypic diversity in ALS and the role of poly-conformational protein misfolding.
Acta Neuropathol
; 142(1): 41-55, 2021 07.
Article
en En
| MEDLINE
| ID: mdl-32930869
ABSTRACT
In many types of familial amyotrophic lateral sclerosis (fALS), mutations cause proteins to gain toxic properties that mediate neurodegenerative processes. It is becoming increasingly clear that the proteins involved in ALS, and those responsible for a host of other neurodegenerative diseases, share many characteristics with a growing number of prion diseases. ALS is a heterogenous disease in which the majority of cases are sporadic in their etiology. Studies investigating the inherited forms of the disease are now beginning to provide evidence that some of this heterogeneity may be due to the existence of distinct conformations that ALS-linked proteins can adopt to produce the equivalent of prion strains. In this review, we discuss the in vitro and in vivo evidence that has been generated to better understand the characteristics of these proteins and how their tertiary structure may impact the disease phenotype.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Deficiencias en la Proteostasis
/
Esclerosis Amiotrófica Lateral
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Acta Neuropathol
Año:
2021
Tipo del documento:
Article
País de afiliación:
Estados Unidos