Misfolded protein aggregates: Mechanisms, structures and potential for disease transmission
Open accessAbstract
Some of the most prevalent human degenerative diseases appear as a result of the misfolding and aggregation of proteins. Compelling evidence suggest that misfolded protein aggregates play an important role in cell dysfunction and tissue damage, leading to the disease. Prion protein (Prion diseases), amyloid-beta (Alzheimer's disease), alpha-synuclein (Parkinson's disease), Huntingtin (Huntington's disease), serum amyloid A (AA amyloidosis) and islet amyloid polypeptide (type 2 diabetes) are some of the proteins that trigger disease when they get misfolded. The recent understanding of the crucial role of misfolded proteins as well as the structural requirements and mechanism of protein misfolding have raised the possibility that these diseases may be transmissible by self-propagation of the protein misfolding process in a similar way as the infamous prions transmit prion diseases. Future research in this field should aim to clarify this possibility and translate the knowledge of the basic disease mechanisms into development of novel strategies for early diagnosis and efficient treatment.
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Age is one of the main risk factors for most diseases associated with protein misfolding, including neurodegenerative diseases such as Alzheimer's, Parkinson's, Huntington's, and amyotrophic lateral sclerosis.
“age is one of the main risk factors for most diseases associated with protein misfolding, including neurodegenerative diseases such as Alzheimer’s disease, Parkinson’s disease, Huntington’s disease and amyotrophic lateral sclerosis72.”
From Stem cell aging: mechanisms, regulators and therapeutic opportunities (2014) · cites this paper as [72]
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- Authors
- Moreno-Gonzalez, I., & Soto, C.
- Corresponding author
- Soto, Claudio
- ORCID
- Soto, Claudio
- Venue
- Seminars in Cell & Developmental Biology
- Publisher
- Elsevier BV
- Published
- 2011-07
- Volume
- 22
- Issue
- 5
- Pages
- 482-487
- ISSN
- 1084-9521 (ISSN-L)
- PMC
- PMC3175247
- OpenAlex
- W2052156860
- Cited by
- 252
- References
- 87
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- FWCI
- 1.42
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Seminars in Cell and Developmental Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (P01AI077774)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- protein misfolding, protein aggregates, prion disease, amyloid-beta, alpha-synuclein, Huntington's disease, amylin, type 2 diabetes, neurodegenerative diseases, infectious diseases, prion-like propagation, protein aggregation mechanism, early diagnosis
- MeSH terms
- Alzheimer Disease, Amyloid, Amyloidosis, Diabetes Mellitus, Type 2, Humans, Huntington Disease, Parkinson Disease, Prions, Protein Conformation, Prion Diseases, Protein Folding, Proteostasis Deficiencies
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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