The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
Implications of peptide assemblies in amyloid diseases
Open accessAbstract
We highlight the role of molecular self-assembly in eliciting the mesoscopic and pathological properties of amyloid proteins. This knowledge is pivotal for the development of theranostics against amyloid diseases.
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Cites
2 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769
RetractedRETRACTED ARTICLE: APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
Nikolaev, A., McLaughlin, T., O’Leary, D. D. M., & Tessier-Lavigne, M. (2009) · Nature · doi:10.1038/nature07767 · Cited by 992
RetractedAmyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
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Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
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Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
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The antibody aducanumab reduces Aβ plaques in Alzheimer’s disease
Sevigny, J., Chiao, P., Bussière, T., Weinreb, P. H., Williams, L., Maier, M., Dunstan, R., Salloway, S., Chen, T., Ling, Y., et al. (2016) · Nature · doi:10.1038/nature19323 · Cited by 3,059
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Cited by
A Decade of the Protein Corona
Ke, P. C., Lin, S., Parak, W. J., Davis, T. P., & Caruso, F. (2017) · ACS Nano · doi:10.1021/acsnano.7b08008 · Cited by 672
Self-citationMulticomponent peptide assemblies
Raymond, D. M., & Nilsson, B. L. (2018) · Chemical Society Reviews · doi:10.1039/c8cs00115d · Cited by 346
Detection of amyloid fibrils in Parkinson’s disease using plasmonic chirality
Kumar, J., Eraña, H., López-Martínez, E., Claes, N., Martín, V. F., Solís, D. M., Bals, S., Cortajarena, A. L., Castilla, J., & Liz-Marzán, L. M. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1721690115 · Cited by 312
Metadata
- Authors
- Ke, P. C., Sani, M.-A., Ding, F., Kakinen, A., Javed, I., Separovic, F., Davis, T. P., & Mezzenga, R.
- Venue
- Chemical Society Reviews
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2017
- Volume
- 46
- Issue
- 21
- Pages
- 6492-6531
- ISSN
- 0306-0012 (ISSN-L)
- 1460-4744
- OpenAlex
- W2735416135
- Cited by
- 338
- References
- 50
- FWCI
- 6.09
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Implications of peptide assemblies in amyloid diseases. https://app.cochat.ai/papers/10.1039/c7cs00372b
- The paper
- Ke, P. C., Sani, M.-A., Ding, F., Kakinen, A., Javed, I., Separovic, F., Davis, T. P., & Mezzenga, R. (2017). Implications of peptide assemblies in amyloid diseases. Chemical Society Reviews. https://doi.org/10.1039/c7cs00372b
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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).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
