A Synuclein
Mostrando 1-12 de 61 artigos, teses e dissertações.
-
1. Protective effect of luteolin on the transgenic Drosophila model of Parkinson’s disease
In the present study we have studied the effect of 25, 50, 75 and 100 µM of luteolin on the transgenic Drosophila expressing human alpha synuclein. The doses of luteolin were established in diet and the PD flies were allowed to feed on it for 24 days. After 24 days of exposure the flies were assayed for climbing assay, oxidative stress markers, caspase-3 &
Braz. J. Pharm. Sci.. Publicado em: 29/11/2018
-
2. Fármacos multifuncionais: monoamina oxidase e α-sinucleína como alvos terapêuticos na doença de Parkinson
Parkinson's disease (PD) is a neurodegenerative disorder associated to selective degeneration of dopaminergic neurons caused by an intricate relationship among dopamine metabolism, oxidative stress and α-synuclein fibrillation. Most therapies for PD have focused on dopamine replacement through the use of both monoamine oxidase inhibitors (MAOIs) and dopamin
Quím. Nova. Publicado em: 2013
-
3. Protection against neurotoxicity by an autophagic mechanism
The objective of the present study was to investigate the effects of 3-n-butylphthalide (NBP) on a 1-methyl-4-phenylpyridinium (MPP+)-induced cellular model of Parkinson’s disease (PD) and to illustrate the potential mechanism of autophagy in this process. For this purpose, rat PC12 pheochromocytoma cells were treated with MPP+ (1 mM) for 24 h following pr
Brazilian Journal of Medical and Biological Research. Publicado em: 2012-05
-
4. Efeitos da alfa-sinucleína na modulação da atividade do fator de transcrição nuclear kB em células SH-SY5Y. / Activation of trasnscription fator kB induced by alpha-synuclein in SH-SY5Y cells.
Parkinsons Disease (PD) is a neurodegenerative disease. The characteristics and symptoms are well defined; nevertheless its etiology remains unknown. The sporadic PD is characterized by the presence of Lewy Body (aggregate of proteins) inside the neurons. Alpha-synuclein is a soluble protein present in the pre synaptic terminal of neurons. Evidences suggest
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 31/08/2011
-
5. Estudo dos grânulos de lipofucsina e das sinapses do córtex temporal durante o envelhecimento / Study of lipofuscin granules and synapses in the temporal cortex during aging.
Alterações morfológicas e funcionais ocorrem durante o envelhecimento, período da vida com maior incidência de doenças neurodegenerativas. No presente trabalho acompanhou-se a evolução dos grânulos de lipofucsina durante o envelhecimento para investigar alterações sinápticas, assim como proteínas associadas com doenças neurodegenerativas (alfa-
Publicado em: 2011
-
6. Estudos das interações da septina 4 humana / Study of Human Septin 4 interactions
Septinas são proteínas ligantes a GTP encontradas desde fungos até metazoários. A primeira função identificada para septinas foi o seu papel central na organização e dinâmica do septo de divisão de leveduras. Uma das características marcantes é que septinas se organizam em heterofilamentos de 7 a 9 nm de espessura que foram purificados de diverso
Publicado em: 2009
-
7. Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformation
Filamentous inclusions made of α-synuclein constitute the defining neuropathological characteristic of Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy. Rare familial cases of Parkinson's disease are associated with mutations A53T and A30P in α-synuclein. We report here the assembly properties and secondary structure characterist
The National Academy of Sciences.
-
8. The Molecular Chaperone Hsp90 Modulates Intermediate Steps of Amyloid Assembly of the Parkinson-related Protein α-Synuclein*
α-Synuclein is an intrinsically unstructured protein that binds to membranes, forms fibrils, and is involved in neurodegeneration. We used a reconstituted in vitro system to show that the molecular chaperone Hsp90 influenced α-synuclein vesicle binding and amyloid fibril formation, two processes that are tightly coupled to α-synuclein folding. Binding of
American Society for Biochemistry and Molecular Biology.
-
9. β-Amyloid peptides enhance α-synuclein accumulation and neuronal deficits in a transgenic mouse model linking Alzheimer's disease and Parkinson's disease
Alzheimer's disease and Parkinson's disease are associated with the cerebral accumulation of β-amyloid and α-synuclein, respectively. Some patients have clinical and pathological features of both diseases, raising the possibility of overlapping pathogenetic pathways. We generated transgenic (tg) mice with neuronal expression of human β-amyloid peptides, �
The National Academy of Sciences.
-
10. α-Synuclein produces a long-lasting increase in neurotransmitter release
Wild-type α-synuclein, a protein of unknown function, has received much attention because of its involvement in a series of diseases that are known as synucleinopathies. We find that long-lasting potentiation of synaptic transmission between cultured hippocampal neurons is accompanied by an increase in the number of α-synuclein clusters. Conversely, suppre
Nature Publishing Group.
-
11. Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
The Parkinson's disease (PD) substantia nigra is characterized by the presence of Lewy bodies containing fibrillar α-synuclein. Early-onset PD has been linked to two point mutations in the gene that encodes α-synuclein, suggesting that disease may arise from accelerated fibrillization. However, the identity of the pathogenic species and its relationsh
The National Academy of Sciences.
-
12. Tissue transglutaminase-induced aggregation of α-synuclein: Implications for Lewy body formation in Parkinson's disease and dementia with Lewy bodies
Proteinaceous aggregates containing α-synuclein represent a feature of neurodegenerative disorders such as Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy. Despite extensive research, the mechanisms underlying α-synuclein aggregation remain elusive. Previously, tissue transglutaminase (tTGase) was found to contribute to the gene
The National Academy of Sciences.