NeuralCipher Open access
Alpha-synuclein aggregates are phosphatase resistant.
DOI: 10.1186/s40478-024-01785-0PMID: 38822421
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15.468 articles found
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Cathepsin-mediated regulation of alpha-synuclein in Parkinson's disease: a Mendelian randomization study.
DOI: 10.3389/fnagi.2024.1394807PMID: 38872630
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Open access
High-Yield α-Synuclein Purification and Ionic Strength Modification Pivotal to Seed Amplification Assay Performance and Reproducibility.
DOI: 10.3390/ijms25115988PMID: 38892177
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Advancing Parkinson's Disease Diagnostics: The Potential of Arylpyrazolethiazole Derivatives for Imaging α-Synuclein Aggregates.
DOI: 10.1021/acsomega.4c01301PMID: 38882134
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p.L1795F LRRK2 variant is a common cause of Parkinson’s disease in Central Europe
DOI: 10.21203/rs.3.rs-4378197/v1
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Dysregulated Wnt and NFAT signaling in a Parkinson's disease LRRK2 G2019S knock-in model.
DOI: 10.1038/s41598-024-63130-8PMID: 38811759
A bibliographic record traceable to Europe PMC. Türkçe başlık: makine çevirisi, editoryal kontrol bekliyor.
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Unraveling the Epigenetic Landscape: Insights into Parkinson's Disease, Amyotrophic Lateral Sclerosis, and Multiple Sclerosis.
DOI: 10.3390/brainsci14060553PMID: 38928553
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α-Synuclein and Mitochondria: Probing the Dynamics of Disordered Membrane-protein Regions Using Solid-State Nuclear Magnetic Resonance.
DOI: 10.1021/jacsau.4c00323PMID: 38938811
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Effect of host and strain factors on α-synuclein prion pathogenesis.
DOI: 10.1016/j.tins.2024.05.004PMID: 38806297
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Catechol-induced covalent modifications modulate the aggregation tendency of α-synuclein: An in-solution and in-silico study.
DOI: 10.1002/biof.2086PMID: 38801346
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Primary Nucleation of Polymorphic α-Synuclein Dimers Depends on Copper Concentrations and Definite Copper-Binding Site.
DOI: 10.3390/biom14060627PMID: 38927031
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Lysophosphatidylcholine binds α-synuclein and prevents its pathological aggregation.
DOI: 10.1093/nsr/nwae182PMID: 38962715
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