The DOI matches its Crossref record; 109 of the 109 references it cites were found in a registry or an index.
Deadly Conformations—Protein Misfolding in Prion Disease
Open accessAbstract
Novel infectious particles, termed prions, composed largely and perhaps solely of a single protein, are the likely causative agents of a group of transmissible spongiform encephalopathies that produce lethal decline of cognitive and motor function. As if the notion of a transmissible pathogenic protein is not jarring enough, evidence indicates that the responsible protein arrives at a pathogenic state by misfolding from a normal form that has ubiquitous tissue distribution. The remarkable nature of these diseases and the nature of the prion protein conversion process as we currently understand it are reviewed below.
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Cites
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Cited by
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HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin.
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Metadata
- Authors
- Horwich, A. L., & Weissman, J. S.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1997-05
- Volume
- 89
- Issue
- 4
- Pages
- 499-510
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W1974288679
- Cited by
- 278
- References
- 109
- FWCI
- 7.42
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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