The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
Amyloid β-Protein Assembly and Alzheimer Disease
Open accessAbstract
The biochemistry of amyloid proteins has been a fascinating and important area of research because of its contribution to our understanding of protein folding dynamics and assembly and of the pathogenetic mechanisms of human disease. One such disease is AD,2 the most common neurodegenerative disorder of aging. In AD, Aβ (Fig. 1A), which is expressed normally and ubiquitously throughout life as a 40–42-residue peptide, forms fibrils that deposit in the brain as “amyloid plaques.” This pathologic deposition process led researchers to investigate fibril formation as a target for therapeutic intervention.
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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RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory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
Amyloid 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
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
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Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
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Atomic structures of amyloid cross-β spines reveal varied steric zippers
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Hydrogen peroxide mediates amyloid β protein toxicity
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The metallobiology of Alzheimer's disease
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Amyloid β-Protein Fibrillogenesis
Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., & Teplow, D. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25945 · Cited by 1,046
Self-citation
Cited by
Zempel, H., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.2357-10.2010 · Cited by 686
Proteases and Proteolysis in Alzheimer Disease: A Multifactorial View on the Disease Process
De Strooper, B. (2010) · Physiological Reviews · doi:10.1152/physrev.00023.2009 · Cited by 455
The chemistry of Alzheimer’s disease
Rauk, A. (2009) · Chemical Society Reviews · doi:10.1039/b807980n · Cited by 417
Preparing Synthetic Aβ in Different Aggregation States
Stine, W. B., Jungbauer, L., Yu, C., & LaDu, M. J. (2010) · Methods in Molecular Biology · doi:10.1007/978-1-60761-744-0_2 · Cited by 403
Structure of an Intermediate State in Protein Folding and Aggregation
Neudecker, P., Robustelli, P., Cavalli, A., Walsh, P., Lundström, P., Zarrine-Afsar, A., Sharpe, S., Vendruscolo, M., & Kay, L. E. (2012) · Science · doi:10.1126/science.1214203 · Cited by 398
Metadata
- Authors
- Roychaudhuri, R., Yang, M., Hoshi, M. M., & Teplow, D. B.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-02
- Volume
- 284
- Issue
- 8
- Pages
- 4749-4753
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2062438517
- Cited by
- 615
- References
- 50
- FWCI
- 28.55
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Roychaudhuri, R., Yang, M., Hoshi, M. M., & Teplow, D. B. (2009). Amyloid β-Protein Assembly and Alzheimer Disease. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.r800036200
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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.
