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Protein Aggregates Toxicity: New Insights into the Mechanisms 2.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Neurobiology".

Deadline for manuscript submissions: closed (20 April 2023) | Viewed by 1237

Special Issue Editors


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Guest Editor
Department of Experimental and Clinical Biomedical Sciences, Section of Biochemistry, University of Florence, 50134 Florence, Italy
Interests: Alzheimer's disease; Parkinson's disease; amyotrophic lateral sclerosis; aberrant protein oligomers (β amyloid peptide, α-synuclein, TDP-43); structure/toxicity relationship; molecular chaperones; glutathione thioesters; oxidative stress; Ca2+ dyshomeostasis; aminosterols; conformational antibodies
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E-Mail Website
Guest Editor
Department of Experimental and Clinical Biomedical Sciences, Section of Biochemistry, University of Florence, 50134 Florence, Italy
Interests: Alzheimer's disease; Parkinson's disease; amyotrophic lateral sclerosis; aberrant protein oligomers (β amyloid peptide, α-synuclein, TDP-43); structure/toxicity relationship; oxidative stress; glutathione thioesters; Ca2+ dyshomeostasis; molecular chaperones; aminosterols; membrane lipid components (cholesterol and GM1)

Special Issue Information

Dear Colleagues,

A broad range of evidence suggests that the aggregation of misfolded peptides or proteins is the predominant process underlying neurodegenerative disorders, such as Alzheimer’s disease (AD), Parkinson’s disease (PD), synucleopathies, prion diseases, amyotrophic lateral sclerosis (ALS) and other dementias. These peptides/proteins convert from their soluble states into aggregated species accumulating within organs and tissues, either as intracellular inclusions or extracellular deposits, causing an imbalance of the intracellular redox status and ion levels, membrane perturbation, mitochondria injury, and cell death. To date, the exact molecular pathogenesis of neurodegeneration remains unclear. Progress in the development of neuroprotective therapies has been hindered, because it is difficult to define the right targets for treatment and what should be considered as an efficient neuroprotective agent (or medicament). Thus, understanding the mechanisms of neuronal toxicity should provide insights into new therapeutic strategies for prevention and/or treatment of neurodegenerative diseases. In this Special Issue, we invite researchers to update the readers on the most advanced knowledge about the specific mechanisms underlying the pathogenesis and progression of protein deposition diseases. Review articles describing the current state-of-the-art and future diagnostic and therapeutic approaches and are also welcome.

Dr. Roberta Cascella
Dr. Cristina Cecchi
Guest Editors

Manuscript Submission Information

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Keywords

  • protein misfolding
  • protein aggregation
  • structure-function relationship, cellular dyshomeostasis
  • neuronal membrane
  • amyloid cytotoxicity

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Published Papers (1 paper)

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Editorial

4 pages, 641 KiB  
Editorial
The Toxicity of Protein Aggregates: New Insights into the Mechanisms
by Alessandra Bigi, Eva Lombardo, Roberta Cascella and Cristina Cecchi
Int. J. Mol. Sci. 2023, 24(9), 7974; https://doi.org/10.3390/ijms24097974 - 28 Apr 2023
Cited by 1 | Viewed by 975
Abstract
The aberrant aggregation of specific peptides and proteins is the common feature of a range of more than 50 human pathologies, collectively referred to as protein misfolding diseases [...] Full article
(This article belongs to the Special Issue Protein Aggregates Toxicity: New Insights into the Mechanisms 2.0)
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