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Unveiling the Effects of Copper Ions in the Aggregation of Amyloidogenic Proteins
Amyloid diseases have become a global concern due to their increasing prevalence. Transition metals, including copper, can affect the aggregation of the pathological proteins involved in these diseases. Copper ions play vital roles in organisms, but the disruption of their homeostasis can negatively...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10537474/ https://www.ncbi.nlm.nih.gov/pubmed/37764220 http://dx.doi.org/10.3390/molecules28186446 |
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author | Oliveri, Valentina |
author_facet | Oliveri, Valentina |
author_sort | Oliveri, Valentina |
collection | PubMed |
description | Amyloid diseases have become a global concern due to their increasing prevalence. Transition metals, including copper, can affect the aggregation of the pathological proteins involved in these diseases. Copper ions play vital roles in organisms, but the disruption of their homeostasis can negatively impact neuronal function and contribute to amyloid diseases with toxic protein aggregates, oxidative stress, mitochondrial dysfunction, impaired cellular signaling, inflammation, and cell death. Gaining insight into the imbalance of copper ions and its impact on protein folding and aggregation is crucial for developing focused therapies. This review examines the influence of copper ions on significant amyloid proteins/peptides, offering a comprehensive overview of the current understanding in this field. |
format | Online Article Text |
id | pubmed-10537474 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-105374742023-09-29 Unveiling the Effects of Copper Ions in the Aggregation of Amyloidogenic Proteins Oliveri, Valentina Molecules Review Amyloid diseases have become a global concern due to their increasing prevalence. Transition metals, including copper, can affect the aggregation of the pathological proteins involved in these diseases. Copper ions play vital roles in organisms, but the disruption of their homeostasis can negatively impact neuronal function and contribute to amyloid diseases with toxic protein aggregates, oxidative stress, mitochondrial dysfunction, impaired cellular signaling, inflammation, and cell death. Gaining insight into the imbalance of copper ions and its impact on protein folding and aggregation is crucial for developing focused therapies. This review examines the influence of copper ions on significant amyloid proteins/peptides, offering a comprehensive overview of the current understanding in this field. MDPI 2023-09-05 /pmc/articles/PMC10537474/ /pubmed/37764220 http://dx.doi.org/10.3390/molecules28186446 Text en © 2023 by the author. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Oliveri, Valentina Unveiling the Effects of Copper Ions in the Aggregation of Amyloidogenic Proteins |
title | Unveiling the Effects of Copper Ions in the Aggregation of Amyloidogenic Proteins |
title_full | Unveiling the Effects of Copper Ions in the Aggregation of Amyloidogenic Proteins |
title_fullStr | Unveiling the Effects of Copper Ions in the Aggregation of Amyloidogenic Proteins |
title_full_unstemmed | Unveiling the Effects of Copper Ions in the Aggregation of Amyloidogenic Proteins |
title_short | Unveiling the Effects of Copper Ions in the Aggregation of Amyloidogenic Proteins |
title_sort | unveiling the effects of copper ions in the aggregation of amyloidogenic proteins |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10537474/ https://www.ncbi.nlm.nih.gov/pubmed/37764220 http://dx.doi.org/10.3390/molecules28186446 |
work_keys_str_mv | AT oliverivalentina unveilingtheeffectsofcopperionsintheaggregationofamyloidogenicproteins |