The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Amyloids, prions and the inherent infectious nature of misfolded protein aggregates
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Citations
Cites
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434
Unfolding the role of protein misfolding in neurodegenerative diseases
Soto, C. (2003) · Nature Reviews Neuroscience · doi:10.1038/nrn1007 · Cited by 1,506
Self-citationExogenous induction of cerebral β-amyloidosis in βAPP-transgenic mice
Walker, L. C., Callahan, M. J., Bian, F., Durham, R. A., Roher, A. E., & Lipinski, W. J. (2002) · Peptides · doi:10.1016/s0196-9781(02)00059-1 · Cited by 96
Cited by
Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases
Soto, C., & Pritzkow, S. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0235-9 · Cited by 1,180
Self-citationPathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders
Jucker, M., & Walker, L. C. (2011) · Annals of Neurology · doi:10.1002/ana.22615 · Cited by 622
The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease
Ferreira, S. T., & Klein, W. L. (2011) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2011.08.003 · Cited by 442
Models of β-amyloid induced Tau-pathology: The long and “folded” road to understand the mechanism
Stancu, I.-C., Vasconcelos, B., Terwel, D., & Dewachter, I. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-51 · Cited by 256
Misfolded protein aggregates: Mechanisms, structures and potential for disease transmission
Moreno-Gonzalez, I., & Soto, C. (2011) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2011.04.002 · Cited by 252
Self-citation
Metadata
- Authors
- Soto, C., Estrada, L., & Castilla, J.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2006-03
- Volume
- 31
- Issue
- 3
- Pages
- 150-155
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2016351953
- Cited by
- 266
- References
- 3
- FWCI
- 1.01
- Type
- journal article
- Language
- en
- Open access
- closed
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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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How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
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- CoChat. (2026). Citation check: Amyloids, prions and the inherent infectious nature of misfolded protein aggregates. https://app.cochat.ai/papers/10.1016/j.tibs.2006.01.002
- The paper
- Soto, C., Estrada, L., & Castilla, J. (2006). Amyloids, prions and the inherent infectious nature of misfolded protein aggregates. Trends in Biochemical Sciences. https://doi.org/10.1016/j.tibs.2006.01.002
Data sources
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).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
