The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
Mechanisms of protein-folding diseases at a glance
Open accessAbstract
For a protein to function appropriately, it must first achieve its proper conformation and location within the crowded environment inside the cell. Multiple chaperone systems are required to fold proteins correctly. In addition, degradation pathways participate by destroying improperly folded proteins. The intricacy of this multisystem process provides many opportunities for error. Furthermore, mutations cause misfolded, nonfunctional forms of proteins to accumulate. As a result, many pathological conditions are fundamentally rooted in the protein-folding problem that all cells must solve to maintain their function and integrity. Here, to illustrate the breadth of this phenomenon, we describe five examples of protein-misfolding events that can lead to disease: improper degradation, mislocalization, dominant-negative mutations, structural alterations that establish novel toxic functions, and amyloid accumulation. In each case, we will highlight current therapeutic options for battling such diseases.
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Cites
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Cited by
Mahul-Mellier, A.-L., Burtscher, J., Maharjan, N., Weerens, L., Croisier, M., Kuttler, F., Leleu, M., Knott, G. W., & Lashuel, H. A. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1913904117 · Cited by 710
Protein Quality Control by Molecular Chaperones in Neurodegeneration
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The therapeutic effects of 4-phenylbutyric acid in maintaining proteostasis
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ER stress and UPR in Alzheimer’s disease: mechanisms, pathogenesis, treatments
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Second-Generation Pharmacological Chaperones: Beyond Inhibitors
Tran, M. L., Génisson, Y., Ballereau, S., & Dehoux, C. (2020) · Molecules · doi:10.3390/molecules25143145 · Cited by 63
Metadata
- Authors
- Valastyan, J. S., & Lindquist, S.
- Venue
- Disease Models & Mechanisms
- Publisher
- The Company of Biologists
- Published
- 2014-01-01
- Volume
- 7
- Issue
- 1
- Pages
- 9-14
- ISSN
- 1754-8403 (ISSN-L)
- 1754-8411
- OpenAlex
- W2156098042
- Cited by
- 307
- References
- 19
- FWCI
- 12.41
- Type
- journal article
- Language
- en
- Open access
- gold
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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