Cited by 252Prion Diseases and Protein MisfoldingAlzheimer's disease research and treatmentsHeat shock proteins research

Misfolded protein aggregates: Mechanisms, structures and potential for disease transmission

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Moreno-Gonzalez, Ines, Soto, Claudio·2011·Seminars in Cell & Developmental Biology

Abstract

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.”

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Authors
Moreno-Gonzalez, I., & Soto, C.
Corresponding author
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)
OpenAlex
W2052156860
Cited by
252
References
87
Citations by year
2026: 16 · 2025: 24 · 2024: 24 · 2023: 17 · 2022: 16 · 2021: 17 · 2020: 14 · 2019: 19 · 2018: 11 · 2017: 15 · 2016: 13 · 2015: 17 · 2014: 19 · 2013: 15 · 2012: 14
FWCI
1.42
Type
journal article
Language
en
Open access
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

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