Associated Papers
Defining essential charged residues in fibril formation of a lysosomal derived N-terminal α-synuclein truncation.
McGlinchey RP et al.
Nature Communications, 2025
Role of the mitochondrial regulatory factor CHCHD2 in neurodegenerative diseases.
Guo X et al.
Frontiers in Neuroscience, 2025
Structurally targeted mutagenesis identifies key residues supporting α-synuclein misfolding in multiple system atrophy.
Reis PM et al.
Journal of Parkinson's Disease, 2024
Structurally targeted mutagenesis identifies key residues supporting α -synuclein misfolding in multiple system atrophy.
Reis PM et al.
Biorxiv : the Preprint Server for Biology, 2024
In silico analysis of alpha-synuclein protein variants and posttranslational modifications related to Parkinson's disease.
da Silva ANR et al.
Journal of Cellular Biochemistry, 2024
In Silico Evaluation of the Potential Association of the Pathogenic Mutations of Alpha Synuclein Protein with Induction of Synucleinopathies.
Elnageeb ME et al.
Diseases (basel, Switzerland), 2023
Protein kinase R dependent phosphorylation of α-synuclein regulates its membrane binding and aggregation.
Reimer L et al.
Pnas Nexus, 2022
β-Turn exchanges in the α-synuclein segment 44-TKEG-47 reveal high sequence fidelity requirements of amyloid fibril elongation.
Agerschou ED et al.
Biophysical Chemistry, 2021
Identification of CHCHD2 mutations in patients with Alzheimer's disease, amyotrophic lateral sclerosis and frontotemporal dementia in China.
Liu X et al.
Molecular Medicine Reports, 2018
Structural basis of synaptic vesicle assembly promoted by α-synuclein.
Fusco G et al.
Nature Communications, 2016
Ankylosing spondylitis: from cells to genes.
Zambrano-Zaragoza JF et al.
International Journal of Inflammation, 2013
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