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Title
Aβ43 is neurotoxic and primes aggregation of Aβ40 in vivo
Authors
Keywords
Alzheimer’s disease, Amyloid-β, <em class=EmphasisTypeItalic >Drosophila</em> models, Neurodegeneration, Neurotoxicity
Journal
ACTA NEUROPATHOLOGICA
Volume 130, Issue 1, Pages 35-47
Publisher
Springer Nature
Online
2015-04-10
DOI
10.1007/s00401-015-1419-y
References
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Note: Only part of the references are listed.- The C-Terminal Threonine of Aβ43 Nucleates Toxic Aggregation via Structural and Dynamical Changes in Monomers and Protofibrils
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- PINK1 Loss-of-Function Mutations Affect Mitochondrial Complex I Activity via NdufA10 Ubiquinone Uncoupling
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- C9orf72 repeat expansions cause neurodegeneration in Drosophila through arginine-rich proteins
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- DJ-1 is critical for mitochondrial function and rescues PINK1 loss of function
- (2010) L.-Y. Hao et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Inhibition of GSK-3 Ameliorates Aβ Pathology in an Adult-Onset Drosophila Model of Alzheimer's Disease
- (2010) Oyinkan Sofola et al. PLoS Genetics
- Aβ43 is more frequent than Aβ40 in amyloid plaque cores from Alzheimer disease brains
- (2009) Hedvig Welander et al. JOURNAL OF NEUROCHEMISTRY
- Exploiting position effects and the gypsy retrovirus insulator to engineer precisely expressed transgenes
- (2008) Michele Markstein et al. NATURE GENETICS
- Aβ42 Mutants with Different Aggregation Profiles Induce Distinct Pathologies in Drosophila
- (2008) Koichi Iijima et al. PLoS One
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