The DOI matches its Crossref record; 258 of the 258 references it cites were found in a registry or an index.
Protein transmission in neurodegenerative disease
Open accessAbstract
Most neurodegenerative diseases are characterized by the intracellular or extracellular aggregation of misfolded proteins such as amyloid-β and tau in Alzheimer disease, α-synuclein in Parkinson disease, and TAR DNA-binding protein 43 in amyotrophic lateral sclerosis. Accumulating evidence from both human studies and disease models indicates that intercellular transmission and the subsequent templated amplification of these misfolded proteins are involved in the onset and progression of various neurodegenerative diseases. The misfolded proteins that are transferred between cells are referred to as 'pathological seeds'. Recent studies have made exciting progress in identifying the characteristics of different pathological seeds, particularly those isolated from diseased brains. Advances have also been made in our understanding of the molecular mechanisms that regulate the transmission process, and the influence of the host cell on the conformation and properties of pathological seeds. The aim of this Review is to summarize our current knowledge of the cell-to-cell transmission of pathological proteins and to identify key questions for future investigation.
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“The misfolded tau is then propagated through the cortex in a prion‐like fashion, leading to cellular failure and the development of cognitive deficits 140 .”
From Mental health care for older adults: recent advances and new directions in clinical practice and research (2022) · cites this paper as [140]
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Metadata
- Authors
- Peng, C., Trojanowski, J. Q., & Lee, V. M.-Y.
- Affiliations
- University of California, Los Angeles (US)
- University of Pennsylvania (US)
- Corresponding author
- Lee, Virginia M.-Y.
- Venue
- Nature Reviews Neurology
- Published
- 2020-03-23
- Volume
- 16
- Issue
- 4
- Pages
- 199-212
- ISSN
- 1759-4758 (ISSN-L)
- 1759-4766
- PMC
- PMC9242841
- OpenAlex
- W3012646333
- Cited by
- 625
- References
- 257
- Citations by year
- 2026: 73 · 2025: 106 · 2024: 116 · 2023: 99 · 2022: 92 · 2021: 100 · 2020: 39
- FWCI
- 10.56
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature Reviews Neurology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (U19AG062418)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Keywords
- protein transmission, neurodegenerative diseases, protein aggregation, amyloid-beta, tau protein, alpha-synuclein, Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, intercellular protein transfer
- MeSH terms
- Huntingtin Protein, Alzheimer Disease, Amyotrophic Lateral Sclerosis, Axonal Transport, Brain, Cell Communication, DNA-Binding Proteins, Endocytosis, Humans, Huntington Disease, Membrane Fusion, Neuroglia, Neurons, Parkinson Disease, Amyloid beta-Peptides, tau Proteins, Neurodegenerative Diseases, Genetic Predisposition to Disease, Protein Transport, Nanotubes, alpha-Synuclein, Exosomes, Protein Aggregation, Pathological
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