S
Saskia Milton
Researcher at University of California, Irvine
Publications - 27
Citations - 8283
Saskia Milton is an academic researcher from University of California, Irvine. The author has contributed to research in topics: Amyloid & P3 peptide. The author has an hindex of 19, co-authored 27 publications receiving 7873 citations. Previous affiliations of Saskia Milton include University of California & University of Southern California.
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Journal ArticleDOI
Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis
Rakez Kayed,Elizabeth Head,Jennifer L. Thompson,Theresa M. McIntire,Saskia Milton,Carl W. Cotman,Charles G. Glabe +6 more
TL;DR: It is shown that all of the soluble oligomers tested display a common conformation-dependent structure that is unique to soluble oligomer regardless of sequence, suggesting they share a common mechanism of toxicity.
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Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers.
TL;DR: Observations that Aβ42 and other oligomers caused rapid cellular leakage of anionic fluorescent dyes point to a generalized increase in membrane permeability, which may provide a common mechanism for oligomer-mediated toxicity in many amyloidogenic diseases.
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Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
Rakez Kayed,Yuri Sokolov,Brian W Edmonds,Theresa M. McIntire,Saskia Milton,James E. Hall,Charles G. Glabe +6 more
TL;DR: It is reported that soluble oligomers from several types of amyloidogenic proteins and peptides specifically increase lipid bilayer conductance regardless of the sequence, while fibrils and soluble low molecular weight species have no effect.
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Small Molecule Inhibitors of Aggregation Indicate That Amyloid β Oligomerization and Fibrillization Pathways Are Independent and Distinct
TL;DR: The results indicate that oligomers are not an obligate intermediate in the fibril formation pathway and suggest that small molecule inhibitors are useful for clarifying the mechanisms underlying protein aggregation and may represent potential therapeutic agents that target fundamental disease mechanisms.
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Structural and Dynamic Features of Alzheimer's Aβ Peptide in Amyloid Fibrils Studied by Site-directed Spin Labeling
Marianna Török,Saskia Milton,Rakez Kayed,Peng Wu,Theresa McIntire,Charles G. Glabe,Ralf Langen +6 more
TL;DR: Despite their different aggregation properties and roles in disease, the two peptides, Aβ40 and Aβ42, homogeneously co-mix in amyloid fibrils suggesting that they possess the same structural architecture.