Results 81 to 90 of about 91,213 (314)

β-synuclein regulates the phase transitions and amyloid conversion of α-synuclein

open access: yesNature Communications
Parkinson’s disease (PD) and Dementia with Lewy Bodies (DLB) are neurodegenerative disorders characterized by the accumulation of α-synuclein aggregates. α-synuclein forms droplets via liquid-liquid phase separation (LLPS), followed by liquid-solid phase
Xi Li   +18 more
doaj   +1 more source

DEAD-box RNA helicase Dbp4/DDX10 is an enhancer of α-synuclein toxicity and oligomerization.

open access: yesPLoS 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

Neurodegenerative phenotypes in an A53T α-synuclein transgenic mouse model are independent of LRRK2 [PDF]

open access: yes, 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  

Metabolic Investigations of the Molecular Mechanisms Associated with Parkinson's Disease. [PDF]

open access: yes, 2017
Parkinson's disease (PD) is a neurodegenerative disorder characterized by fibrillar cytoplasmic aggregates of α-synuclein (i.e., Lewy bodies) and the associated loss of dopaminergic cells in the substantia nigra.
Anandhan, Annadurai   +10 more
core   +2 more sources

Region‐to‐Region Unidirectional Connection In Vitro Brain Model for Studying Directional Propagation of Neuropathologies

open access: yesAdvanced Functional Materials, EarlyView.
A unidirectional cerebral organoid–organoid neural circuit is established using a microfluidic platform, enabling controlled directional propagation of electrical signals, neuroinflammatory cues, and neurodegenerative disease–related proteins between spatially separated organoids.
Kyeong Seob Hwang   +9 more
wiley   +1 more source

Cofilin 1 promotes the pathogenicity and transmission of pathological α-synuclein in mouse models of Parkinson’s disease

open access: yesnpj 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

Monomeric Alpha-Synuclein Exerts a Physiological Role on Brain ATP Synthase [PDF]

open access: yes, 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  

Allosteric Modulation of Pathological Ataxin‐3 Aggregation: A Path to Spinocerebellar Ataxia Type‐3 Therapies

open access: yesAdvanced Science, EarlyView.
This study uncovers a new allosteric site in the Josephin domain of ataxin‐3 targeted by the molecular tweezer CLR01, which modulates protein aggregation, improves synaptic function in neuronal cells, and delays motor dysfunction in animal models.
Alexandra Silva   +28 more
wiley   +1 more source

Differential expression of alpha-synuclein in hippocampal neurons.

open access: yesPLoS 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

Ambroxol effects in glucocerebrosidase and -synuclein transgenic mice [PDF]

open access: yes, 2016
Objective. Gaucher disease is caused by mutations in the glucocerebrosidase 1 gene that result in deficiency of the lysosomal enzyme glucocerebrosidase.
Bezard, E   +3 more
core  

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