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Lucia Formigli

Researcher at University of Florence

Publications -  121
Citations -  7855

Lucia Formigli is an academic researcher from University of Florence. The author has contributed to research in topics: Cellular differentiation & Mesenchymal stem cell. The author has an hindex of 42, co-authored 121 publications receiving 7482 citations.

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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases.

TL;DR: This finding provides added evidence that avoidance of protein aggregation is crucial for the preservation of biological function and suggests common features in the origins of this family of protein deposition diseases.
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Prefibrillar amyloid protein aggregates share common features of cytotoxicity.

TL;DR: The results suggest that misfolded proteinaceous aggregates stimulate generic cellular responses as a result of the exposure of regions of the structure that are buried in the normally folded proteins and support the idea that a higher number of degenerative pathologies than previously known might be considered as protein deposition diseases.
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Aponecrosis: morphological and biochemical exploration of a syncretic process of cell death sharing apoptosis and necrosis.

TL;DR: It is concluded that chemically induced hypoxia produces different types of cell death depending on the intensity of the insult and on the ATP availability of the cell, and that the classic apoptosis and necrosis may represent only two extremes of a continuum of intermediate forms of cell demise.
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Coenzyme q10 prevents apoptosis by inhibiting mitochondrial depolarization independently of its free radical scavenging property.

TL;DR: Evaluated the antiapoptotic effects of CoQ10 in response to apoptotic stimuli, serum starvation, antimycin A, and ceramide, which do not generate free radicals, in comparison to control, free radical-generating UVC irradiation.
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Redox Regulation of β-Actin during Integrin-mediated Cell Adhesion

TL;DR: Evidence of in vivo actin redox regulation by a physiological source of reactive oxygen species, specifically those species generated by integrin receptors during cell adhesion, is reported, suggesting that actin glutathionylation is essential for cell spreading and cytoskeleton organization and that it plays a key role in disassembly of actinomyosin complex during cellAdhesion.