Results 11 to 20 of about 91,213 (314)
Structural Basis for Dityrosine-Mediated Inhibition of α-Synuclein Fibrillization [PDF]
Journal of the American Chemical Society, 2022 α-Synuclein (α-Syn) is an intrinsically disordered protein which self-assembles into highly organized β-sheet structures that accumulate in plaques in brains of Parkinson's disease patients. Oxidative stress influences α-Syn structure and self-assembly; however, the basis for this remains unclear.
Cagla Sahin +19 more
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On the ubiquity of helical α-synuclein tetramers [PDF]
Physical Chemistry Chemical Physics, 2019 The stability of oligomers linearly increases from dimers to octamers, but assembly of oligomers larger than tetramers requires high activation energies.
Liang Xu +2 more
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α-Synuclein, oxidative stress and apoptosis from the perspective of a yeast model of Parkinson's disease [PDF]
FEMS Yeast Research, 2006 The neuronal protein alpha-synuclein (alpha-syn) has been suggested to be one of the factors linked to Parkinson's disease (PD). Several organisms, including the rat, mouse, worm, and fruit fly, are being used to study alpha-syn pathobiology. A new model organism was recently added to this armamentarium: the budding yeast Saccharomyces cerevisiae.
Stephan N, Witt, Todd R, Flower
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Frontiers in Neuroscience, 2021 Reducing α-synuclein pathology constitutes a plausible strategy against Parkinson’s disease. As we recently demonstrated, the β-wrapin protein AS69 binds an N-terminal region in monomeric α-synuclein, interferes with fibril nucleation, and reduces α ...
Éva M. Szegő +16 more
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Novel subcellular localization for α-synuclein: possible functional consequences [PDF]
Frontiers in Neuroanatomy, 2015 α-synuclein (α-syn) is one of the genes that when mutated or overexpressed causes Parkinson's Disease (PD). Initially, it was described as a synaptic terminal protein and later was found to be localized at mitochondria. Mitochondria-associated membranes (MAM) have emerged as a central endoplasmic reticulum (ER) subcellular compartments where key ...
Cristina eGuardia-Laguarta +4 more
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Detection of disease-associated α-synuclein in the cerebrospinal fluid: a feasibility study [PDF]
Clinical Neuropathology, 2014 With the aim to evaluate the significance and reliability of detecting disease-specific α-synuclein in the cerebrospinal fluid (CSF) we developed an ELISA and bead-assay. We used a commercial antibody (5G4) that does not bind to the physiological monomeric form of α-synuclein, but is highly specific for the disease-associated forms, including high ...
Unterberger, Ursula +9 more
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p62/SQSTM1-dependent autophagy of Lewy body-like α-synuclein inclusions. [PDF]
PLoS ONE, 2012 α-Synuclein is the main component of Lewy bodies, the intraneuronal inclusion bodies characteristic of Parkinson's disease. Although α-synuclein accumulation is caused by inhibition of proteasome and autophagy-lysosome, the degradation of α-synuclein ...
Yoshihisa Watanabe +7 more
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Lysosomes and α-synuclein form a dangerous duet leading to neuronal cell death [PDF]
Frontiers in Neuroanatomy, 2014 Neurodegenerative diseases are (i) characterized by a selective neuronal vulnerability to degeneration in specific brain regions; and (ii) likely to be caused by disease-specific protein misfolding. Parkinson's disease (PD) is characterized by the presence of intraneuronal proteinacious cytoplasmic inclusions, called Lewy Bodies (LB).
Mathieu eBourdenx +5 more
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Temperature-dependent structural changes of Parkinson's alpha-synuclein reveal the role of pre-existing oligomers in alpha-synuclein fibrillization. [PDF]
PLoS ONE, 2013 Amyloid fibrils of α-synuclein are the main constituent of Lewy bodies deposited in substantial nigra of Parkinson's disease brains. α-Synuclein is an intrinsically disordered protein lacking compact secondary and tertiary structures.
Winny Ariesandi +3 more
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O-GlcNAc modification blocks the aggregation and toxicity of the protein α-synuclein associated with Parkinson's disease. [PDF]
, 2015 Several aggregation-prone proteins associated with neurodegenerative diseases can be modified by O-linked N-acetyl-glucosamine (O-GlcNAc) in vivo. One of these proteins, α-synuclein, is a toxic aggregating protein associated with synucleinopathies ...
Ambroso, Mark R +8 more
core +2 more sources