The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Biology of Amyloid: Structure, Function, and Regulation
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1 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RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory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
RetractedThe Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
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Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
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Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
A Production of Amino Acids Under Possible Primitive Earth Conditions
Miller, S. L. (1953) · Science · doi:10.1126/science.117.3046.528 · Cited by 3,522
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
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Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils
Petkova, A. T., Leapman, R. D., Guo, Z., Yau, W.-M., Mattson, M. P., & Tycko, R. (2005) · Science · doi:10.1126/science.1105850 · Cited by 1,687
Cited by
Aggregation-Induced Emission: Together We Shine, United We Soar!
Mei, J., Leung, N. L. C., Kwok, R. T. K., Lam, J. W. Y., & Tang, B. Z. (2015) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00263 · Cited by 8,270
The Amyloid State of Proteins in Human Diseases
Eisenberg, D., & Jucker, M. (2012) · Cell · doi:10.1016/j.cell.2012.02.022 · Cited by 1,744
Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
Jucker, M., & Walker, L. C. (2013) · Nature · doi:10.1038/nature12481 · Cited by 1,663
Interactions of iron, dopamine and neuromelanin pathways in brain aging and Parkinson's disease
Zucca, F. A., Segura-Aguilar, J., Ferrari, E., Muñoz, P., Paris, I., Sulzer, D., Sarna, T., Casella, L., & Zecca, L. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.09.012 · Cited by 659
The activities of amyloids from a structural perspective
Riek, R., & Eisenberg, D. S. (2016) · Nature · doi:10.1038/nature20416 · Cited by 508
Self-citation
Metadata
- Authors
- Greenwald, J., & Riek, R.
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2010-10
- Volume
- 18
- Issue
- 10
- Pages
- 1244-1260
- ISSN
- 0969-2126 (ISSN-L)
- OpenAlex
- W2025595434
- Cited by
- 575
- References
- 17
- FWCI
- 20.93
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Biology of Amyloid: Structure, Function, and Regulation. https://app.cochat.ai/papers/10.1016/j.str.2010.08.009
- The paper
- Greenwald, J., & Riek, R. (2010). Biology of Amyloid: Structure, Function, and Regulation. Structure. https://doi.org/10.1016/j.str.2010.08.009
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.
