SIRT3 Protects Rotenone-induced Injury in SH-SY5Y Cells by Promoting Autophagy through the LKB1-AMPK-mTOR Pathway. [PDF]
, 2018 SIRT3 is a class III histone deacetylase that modulates energy metabolism, genomic stability and stress resistance. It has been implicated as a potential therapeutic target in a variety of neurodegenerative diseases, including Parkinson's disease (PD ...
Deng, Yong-Ning +6 more
core +1 more source
Five‐Year Disease Progression in Synuclein Seeding Positive Sporadic Parkinson's Disease
Annals of Clinical and Translational Neurology, EarlyView.ABSTRACT Objective To provide a comprehensive description of disease progression in synuclein seeding assay (SAA) positive sporadic Parkinson Disease participants, using Neuronal Synuclein Disease integrated biological and functional impairment staging framework.
Paulina Gonzalez‐Latapi +19 more
wiley +1 more source
Differential expression of alpha-synuclein in hippocampal neurons.
PLoS ONE, 2014 α-Synuclein is the major pathological component of synucleinopathies including Parkinson's disease and dementia with Lewy bodies. Recent studies have demonstrated that α-synuclein also plays important roles in the release of synaptic vesicles and ...
Katsutoshi Taguchi +7 more
doaj +1 more source
DEAD-box RNA helicase Dbp4/DDX10 is an enhancer of α-synuclein toxicity and oligomerization.
PLoS Genetics, 2021 Parkinson's disease is a neurodegenerative disorder associated with misfolding and aggregation of α-synuclein as a hallmark protein. Two yeast strain collections comprising conditional alleles of essential genes were screened for the ability of each ...
Blagovesta Popova +11 more
doaj +1 more source
Monomeric Alpha-Synuclein Exerts a Physiological Role on Brain ATP Synthase [PDF]
, 2016 Misfolded α-synuclein is a key factor in the pathogenesis of Parkinson's disease (PD). However, knowledge about a physiological role for the native, unfolded α-synuclein is limited.
Abramov, A +5 more
core
Deletion of the alpha-synuclein locus in a subpopulation of C57BL/6J inbred mice [PDF]
, 2001 Background The presynaptic protein α-synuclein is involved in a range of neurodegenerative diseases. Here we analyze potential compensatory mechanisms in α-synuclein null mutant mice.
Schoepfer Ralf, Specht Christian G
core +1 more source
SPG4 and Dementia: Expanding the Clinical Spectrum
Annals of Clinical and Translational Neurology, EarlyView.ABSTRACT Objective Hereditary spastic paraplegia (HSP) is a group of disorders characterized by progressive spasticity and lower limb weakness, with mutations in SPG4/SPAST being the most common cause. Detailed studies and clinical and molecular comparisons across different populations are missing.
Emanuele Panza +19 more
wiley +1 more source
npj Parkinson's Disease, 2022 The pathological hallmark of Parkinson’s disease (PD) is the presence of Lewy bodies (LBs) with aggregated α-synuclein being the major component. The abnormal α-synuclein aggregates transfer between cells, recruit endogenous α-synuclein into toxic LBs ...
Mingmin Yan +7 more
doaj +1 more source
Neurodegenerative phenotypes in an A53T α-synuclein transgenic mouse model are independent of LRRK2 [PDF]
, 2017 Mutations in the genes encoding LRRK2 and α-synuclein cause autosomal dominant forms of familial Parkinson's disease (PD). Fibrillar forms of α-synuclein are a major component of Lewy bodies, the intracytoplasmic proteinaceous inclusions that are a ...
Biskup, Saskia +10 more
core
Accumulation of oligomer-prone α-synuclein exacerbates synaptic and neuronal degeneration in vivo [PDF]
, 2016 The toxicity of α-synuclein invivo is not well understood. Rockenstein etal. describe an α-synuclein transgenic model expressing the E57K mutant that forms stable oligomers. They show that oligomers accumulate at synapses and that the mutation interferes
Adame, Anthony +16 more
core +2 more sources