Missense Mutations Modify the Conformational Ensemble of the α-Synuclein Monomer Which Exhibits a Two-Phase Characteristic
α-Synuclein is an intrinsically disordered protein occurring in different conformations and prone to aggregate in β-sheet structures, which are the hallmark of the Parkinson disease. Missense mutations are associated with familial forms of this neuropathy. How these single amino-acid substitutions m...
Enregistré dans:
Auteurs principaux: | Adrien Guzzo, Patrice Delarue, Ana Rojas, Adrien Nicolaï, Gia G. Maisuradze, Patrick Senet |
---|---|
Format: | article |
Langue: | EN |
Publié: |
Frontiers Media S.A.
2021
|
Sujets: | |
Accès en ligne: | https://doaj.org/article/112f16c14a3c47bbb2e9336e93c00391 |
Tags: |
Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!
|
Documents similaires
-
α-synuclein interaction with zero-valent iron nanoparticles accelerates structural rearrangement into amyloid-susceptible structure with increased cytotoxic tendency
par: Tahaei Gilan SS, et autres
Publié: (2019) -
50 years of amino acid hydrophobicity scales: revisiting the capacity for peptide classification
par: Simm,Stefan, et autres
Publié: (2016) -
Effect of superparamagnetic nanoparticles coated with various electric charges on α-synuclein and β-amyloid proteins fibrillation process
par: Javdani N, et autres
Publié: (2019) -
Polymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein Concentration
par: Mantas Ziaunys, et autres
Publié: (2021) -
CK1BP Reduces α-Synuclein Oligomerization and Aggregation Independent of Serine 129 Phosphorylation
par: Lea Elsholz, et autres
Publié: (2021)