The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Nanomechanics of functional and pathological amyloid materials
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Citations
Cites
Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382
Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744
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
Rapid appearance and local toxicity of amyloid-β plaques in a mouse model of Alzheimer’s disease
Meyer-Luehmann, M., Spires-Jones, T. L., Prada, C., Garcia-Alloza, M., de Calignon, A., Rozkalne, A., Koenigsknecht-Talboo, J., Holtzman, D. M., Bacskai, B. J., & Hyman, B. T. (2008) · Nature · doi:10.1038/nature06616 · Cited by 987
Prions as adaptive conduits of memory and inheritance
Shorter, J., & Lindquist, S. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1616 · Cited by 555
Cited by
The amyloid state and its association with protein misfolding diseases.
Knowles, T. P. J., Vendruscolo, M., & Dobson, C. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3810 · Cited by 2,382
Self-citationSelf-propagation of pathogenic protein aggregates in neurodegenerative diseases
Jucker, M., & Walker, L. C. (2013) · Nature · doi:10.1038/nature12481 · Cited by 1,663
Polydopamine and Eumelanin: From Structure–Property Relationships to a Unified Tailoring Strategy
d’Ischia, M., Napolitano, A., Ball, V., Chen, C.-T., & Buehler, M. J. (2014) · Accounts of Chemical Research · doi:10.1021/ar500273y · Cited by 668
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
“This ‘cross-seeding’ is generally less potent than is homologous seeding, but the potential corruption of proteins by exogenous nanoscale materials, some of which may feature amyloid-like structural properties 103, 104 , should be factored into safety evaluations of such materials 41 .”
BackgroundDesign and applications of man-made biomimetic fibrillar hydrogels
Prince, E., & Kumacheva, E. (2019) · Nature Reviews Materials · doi:10.1038/s41578-018-0077-9 · Cited by 379
Metadata
- Authors
- Knowles, T. P. J., & Buehler, M. J.
- Venue
- Nature Nanotechnology
- Published
- 2011-07-31
- Volume
- 6
- Issue
- 8
- Pages
- 469-479
- ISSN
- 1748-3387 (ISSN-L)
- 1748-3395
- OpenAlex
- W2128879174
- Cited by
- 784
- References
- 6
- FWCI
- 21.61
- Type
- journal article
- Language
- en
- Open access
- closed
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- Knowles, T. P. J., & Buehler, M. J. (2011). Nanomechanics of functional and pathological amyloid materials. Nature Nanotechnology. https://doi.org/10.1038/nnano.2011.102
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.
