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Year Number of Results
2004 1
2005 20
2006 43
2007 42
2008 56
2009 58
2010 60
2011 74
2012 92
2013 94
2014 87
2015 89
2016 107
2017 79
2018 90
2019 60
2020 1
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Alpha-Synuclein Proximity Ligation Assay (AS-PLA) in Brain Sections to Probe for Alpha-Synuclein Oligomers.
Roberts RF, et al. Methods Mol Biol 2019. PMID 30771171
Here we describe a method, the alpha-synuclein proximity ligation assay (AS-PLA), to detect alpha-synuclein oligomers in paraffin-embedded brain sections. Using AS-PLA previously unobserved alpha-synuclein oligomeric pathology is revealed....
Here we describe a method, the alpha-synuclein proximity ligation assay (AS-PLA), to detect alpha-synuclein olig …
Alpha-synuclein activates BV2 microglia dependent on its aggregation state.
Hoffmann A, et al. Biochem Biophys Res Commun 2016. PMID 27666480
The distinct alpha-synuclein species, which mediates the activation of microglia, is not well defined. We hypothesized that microglial activation depends on a specific aggregation state of alpha-synuclein. ...BV2 cells also preferentially phagocytosed fibrillar alpha-synuclein compared to alpha-synuclein monomers and oligomers. Microglial uptake of alpha-synuclein fibrils and the consequent activation were time- and concentration-dependent. ...
The distinct alpha-synuclein species, which mediates the activation of microglia, is not well defined. We hypothesized that mi …
Cell Biology and Pathophysiology of α-Synuclein.
Burré J, et al. Cold Spring Harb Perspect Med 2018 - Review. PMID 28108534 Free PMC article.
α-Synuclein is an abundant neuronal protein that is highly enriched in presynaptic nerve terminals. Genetics and neuropathology studies link α-synuclein to Parkinson's disease (PD) and other neurodegenerative disorders. Accumulation of misfolded oligomers and larger aggregates of α-synuclein defines multiple neurodegenerative diseases called synucleinopathies, but the mechanisms by which α-synuclein acts in neurodegeneration are unknown. ...
α-Synuclein is an abundant neuronal protein that is highly enriched in presynaptic nerve terminals. Genetics and neuropathology studi …
Alpha-synuclein: relating metals to structure, function and inhibition.
McDowall JS and Brown DR. Metallomics 2016 - Review. PMID 26864076
Many factors can influence changes in the structure of alpha-synuclein such as disease mutations and interaction with metals and neurotransmitters. ...The recent proposal that alpha-synuclein is a ferrireductase is important as it can possibly catalyse the formation of such reactive species and as a result exacerbate neurodegeneration....
Many factors can influence changes in the structure of alpha-synuclein such as disease mutations and interaction with metals a …
Modification by glyceraldehyde-3-phosphate prevents amyloid transformation of alpha-synuclein.
Barinova K, et al. Biochim Biophys Acta Proteins Proteom 2019. PMID 30639428
Alpha-synuclein is a protein involved in the development of synucleinopathies including Parkinson's disease. In the present work, alpha-synuclein was for the first time modified by the intermediate product of glycolysis, glyceraldehyde-3-phosphate (GA-3-P). ...Investigation of the aggregates by the fluorescence assay with Thioflavin T and CD spectroscopy showed that, in contrast to native alpha-synuclein, alpha-synuclein treated with GA-3-P does not produce real amyloid structures. ...
Alpha-synuclein is a protein involved in the development of synucleinopathies including Parkinson's disease. In the present wo
Structural and functional characterization of two alpha-synuclein strains.
Bousset L, et al. Nat Commun 2013. PMID 24108358 Free PMC article.
α-Synuclein aggregation is implicated in a variety of diseases including Parkinson's disease, dementia with Lewy bodies, pure autonomic failure and multiple system atrophy. ...Here we structurally and functionally characterize two polymorphs of α-synuclein. We present evidence that the two forms indeed fulfil the molecular criteria to be identified as two strains of α-synuclein. ...
α-Synuclein aggregation is implicated in a variety of diseases including Parkinson's disease, dementia with Lewy bodies, pure autonom …
α-synuclein aggregation and its modulation.
Ghosh D, et al. Int J Biol Macromol 2017 - Review. PMID 27737778
The LBs and LNs in PD are mainly composed of aggregated form of a presynaptic protein, α-synuclein (α-Syn). However, the mechanisms of α-Syn aggregation and actual aggregated species responsible for the degeneration of dopaminergic neurons have not yet been resolved. ...
The LBs and LNs in PD are mainly composed of aggregated form of a presynaptic protein, α-synuclein (α-Syn). However, the mechanisms o …
Alpha-synuclein adopts an alpha-helical conformation in the presence of polyunsaturated fatty acids to hinder micelle formation.
Broersen K, et al. Biochemistry 2006. PMID 17176082
We show that alpha-synuclein allows DHA to be present in a soluble rather than micellar form. Upon interaction with DHA, the normally unstructured alpha-synuclein rapidly adopts an alpha-helical conformation. Prolonged exposure to DHA, however, gradually converts alpha-synuclein into amyloid-like fibrils. These results identify a potential biological function for alpha-synuclein and define an omega-3-linked pathway leading to alpha-synuclein aggregation....
We show that alpha-synuclein allows DHA to be present in a soluble rather than micellar form. Upon interaction with DHA, the n …
Structure and dynamics of the extended-helix state of alpha-synuclein: Intrinsic lability of the linker region.
Sung YH and Eliezer D. Protein Sci 2018. PMID 29663556 Free PMC article.
The Parkinson's protein alpha-synuclein binds to synaptic vesicles in vivo and adopts a highly extended helical conformation when binding to lipid vesicles in vitro. ...This suggests that conversion of alpha-synuclein from the extended-helix to the broken-helix state represents a functionally relevant structural transition....
The Parkinson's protein alpha-synuclein binds to synaptic vesicles in vivo and adopts a highly extended helical conformation w …
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