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Danilo Milardi

Researcher at National Research Council

Publications -  134
Citations -  3028

Danilo Milardi is an academic researcher from National Research Council. The author has contributed to research in topics: Chemistry & Proteasome. The author has an hindex of 30, co-authored 119 publications receiving 2357 citations. Previous affiliations of Danilo Milardi include University of Catania.

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Cations as switches of amyloid-mediated membrane disruption mechanisms: calcium and IAPP.

TL;DR: It is demonstrated that the presence of Ca(2+) ions inhibits membrane damage occurring immediately after the interaction of freshly dissolved hIAPP with the membrane, but significantly enhances fiber-dependent membrane disruption.
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α-Helical Structures Drive Early Stages of Self-Assembly of Amyloidogenic Amyloid Polypeptide Aggregate Formation in Membranes

TL;DR: The importance of curvature-induced stress at the early stages of hIAPP assembly and the α-helical structures over β-sheets is shown, which agrees with recent fluorescence spectroscopy experiments.
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Proteostasis of Islet Amyloid Polypeptide: A Molecular Perspective of Risk Factors and Protective Strategies for Type II Diabetes

TL;DR: A review of the current knowledge of the structures and pathology associated with hIAPP self-assembly and point out the opportunities for therapy that a detailed biochemical, biophysical, and cellular understanding of its aggregation may unveil.
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Amyloid growth and membrane damage: Current themes and emerging perspectives from theory and experiments on Aβ and hIAPP.

TL;DR: Biophysical and in silico studies addressing effects of calcium, cholesterol and membrane lipid composition in driving aberrant Aβ or IAPP interaction with the membrane will be specifically considered.
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Lipid-Chaperone Hypothesis: A Common Molecular Mechanism of Membrane Disruption by Intrinsically Disordered Proteins.

TL;DR: This study demonstrates the crucial role of free lipids in the formation of lipid-protein complex, which enables an easy membrane insertion for amylin, amyloid-β, and α-synuclein and proposes a "lipid-chaperone" hypothesis as a unifying framework for protein-membrane poration.