AmyP53 Prevents the Formation of Neurotoxic β-Amyloid Oligomers through an Unprecedent Mechanism of...
AmyP53 Prevents the Formation of Neurotoxic β-Amyloid Oligomers through an Unprecedent Mechanism of Interaction with Gangliosides: Insights for Alzheimer's Disease Therapy
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Switzerland: MDPI AG
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English
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Switzerland: MDPI AG
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A broad range of data identify Ca
-permeable amyloid pores as the most neurotoxic species of Alzheimer's β-amyloid peptide (Aβ
). Following the failures of clinical trials targeting amyloid plaques by immunotherapy, a consensus is gradually emerging to change the paradigm, the strategy, and the target to cure Alzheimer's disease. In this cont...
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Full title
AmyP53 Prevents the Formation of Neurotoxic β-Amyloid Oligomers through an Unprecedent Mechanism of Interaction with Gangliosides: Insights for Alzheimer's Disease Therapy
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TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9864847
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9864847
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ISSN
1422-0067,1661-6596
E-ISSN
1422-0067
DOI
10.3390/ijms24021760
