Biochemical and biophysical characterization of pathological aggregation of amyloid proteins.
Aggregation kinetics
Amyloid protein
Neurodegenerative diseases
Parkinson’s disease
Pathological fibrillation
Transmission electron microscopy
α-Synuclein
Journal
Biophysics reports
ISSN: 2364-3420
Titre abrégé: Biophys Rep
Pays: China
ID NLM: 101676603
Informations de publication
Date de publication:
28 Feb 2022
28 Feb 2022
Historique:
received:
30
07
2021
accepted:
17
09
2021
medline:
28
2
2022
pubmed:
28
2
2022
entrez:
8
6
2023
Statut:
ppublish
Résumé
Protein amyloid fibrillation, a process of liquid to solid phase transition, is involved in the pathogenesis of a variety of human diseases. Several amyloid proteins including α-synuclein (α-syn), Tau, amyloid β (Aβ) protein, and TAR DNA-binding protein 43 kDa (TDP-43) form pathological fibrils and deposit in patient brains of different neurodegenerative diseases (NDs) such as Parkinson's disease (PD), Alzheimer's disease (AD) and Amyotrophic lateral sclerosis (ALS). Preparation and characterization of amyloid fibrils
Identifiants
pubmed: 37287686
doi: 10.52601/bpr.2022.210032
pii: br-8-1-42
pmc: PMC10196661
doi:
Types de publication
Journal Article
Langues
eng
Pagination
42-54Informations de copyright
© The Author(s) 2022.
Déclaration de conflit d'intérêts
Houfang Long, Shuyi Zeng, Yunpeng Sun and Cong Liu declare that they have no conflict of interest.
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