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Published in 2021 at "European Biophysics Journal"
DOI: 10.1007/s00249-020-01486-1
Abstract: Intracellular macromolecular crowding can lead to increased aggregation of proteins, especially those that lack a natively folded conformation. Crowding may also be mimicked by the addition of polymers like polyethylene glycol (PEG) in vitro. α-Synuclein…
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Keywords:
aggregation;
synuclein;
aggregation synuclein;
molecular crowding ... See more keywords
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Published in 2018 at "Scientific Reports"
DOI: 10.1038/s41598-018-30808-9
Abstract: Aggregation of α-synuclein, the hallmark of α-synucleinopathies such as Parkinson’s disease, occurs in various glycosphingolipidoses. Although α-synuclein aggregation correlates with deficiencies in the lysosomal degradation of glycosphingolipids (GSL), the mechanism(s) involved in this aggregation remains…
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Keywords:
synuclein aggregation;
aggregation;
synuclein interacts;
interacts directly ... See more keywords
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Published in 2019 at "Human molecular genetics"
DOI: 10.1093/hmg/ddz005
Abstract: Gaucher disease (GD) patients and carriers of GD mutations have a higher propensity to develop Parkinson's disease (PD) in comparison to the non-GD population. This implies that mutant GBA1 allele is a predisposing factor for…
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Keywords:
accumulation aggregation;
synuclein;
mutant gcase;
aggregation synuclein ... See more keywords
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Published in 2022 at "Frontiers in Cellular Neuroscience"
DOI: 10.3389/fncel.2022.927682
Abstract: Parkinson’s disease (PD) is the second most common neurodegenerative disease. PARK9 (also known as ATP13A2) is recognized as one of the key genes that cause PD, and a mutation in this gene was first discovered…
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Keywords:
atp13a2 gene;
abnormal aggregation;
disease;
aggregation synuclein ... See more keywords