The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
Small-molecule aggregates inhibit amyloid polymerization
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Yang, F., Lim, G. P., Begum, A. N., Ubeda, O. J., Simmons, M. R., Ambegaokar, S. S., Chen, P. P., Kayed, R., Glabe, C. G., Frautschy, S. A., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m404751200 · Cited by 2,336
Structure of the cross-β spine of amyloid-like fibrils
Nelson, R., Sawaya, M. R., Balbirnie, M., Madsen, A. Ø., Riekel, C., Grothe, R., & Eisenberg, D. (2005) · Nature · doi:10.1038/nature03680 · Cited by 2,202
Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red.
Lorenzo, A., & Yankner, B. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.12243 · Cited by 1,324
A Common Mechanism Underlying Promiscuous Inhibitors from Virtual and High-Throughput Screening
McGovern, S. L., Caselli, E., Grigorieff, N., & Shoichet, B. K. (2002) · Journal of Medicinal Chemistry · doi:10.1021/jm010533y · Cited by 1,042
Self-citationRitchie, C. W., Bush, A. I., Mackinnon, A., Macfarlane, S., Mastwyk, M., MacGregor, L., Kiers, L., Cherny, R., Li, Q.-X., Tammer, A., et al. (2003) · Archives of Neurology · doi:10.1001/archneur.60.12.1685 · Cited by 988
Conformational variations in an infectious protein determine prion strain differences
Tanaka, M., Chien, P., Naber, N., Cooke, R., & Weissman, J. S. (2004) · Nature · doi:10.1038/nature02392 · Cited by 770
Self-citationA yeast prion provides a mechanism for genetic variation and phenotypic diversity
True, H. L., & Lindquist, S. L. (2000) · Nature · doi:10.1038/35035005 · Cited by 680
A Specific Mechanism of Nonspecific Inhibition
McGovern, S. L., Helfand, B. T., Feng, B., & Shoichet, B. K. (2003) · Journal of Medicinal Chemistry · doi:10.1021/jm030266r · Cited by 598
Self-citationGlover, J. R., Kowal, A. S., Schirmer, E. C., Patino, M. M., Liu, J.-J., & Lindquist, S. (1997) · Cell · doi:10.1016/s0092-8674(00)80264-0 · Cited by 597
The Flavonoid Baicalein Inhibits Fibrillation of α-Synuclein and Disaggregates Existing Fibrils
Zhu, M., Rajamani, S., Kaylor, J., Han, S., Zhou, F., & Fink, A. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403129200 · Cited by 473
Cited by
Advances in tau-focused drug discovery for Alzheimer's disease and related tauopathies
Brunden, K. R., Trojanowski, J. Q., & Lee, V. M.-Y. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2959 · Cited by 440
Pathological Unfoldomics of Uncontrolled Chaos: Intrinsically Disordered Proteins and Human Diseases
Uversky, V. N., Davé, V., Iakoucheva, L. M., Malaney, P., Metallo, S. J., Pathak, R. R., & Joerger, A. C. (2014) · Chemical Reviews · doi:10.1021/cr400713r · Cited by 288
Development of tau aggregation inhibitors for alzheimer's disease
Bulic, B., Pickhardt, M., Schmidt, B., Mandelkow, E., Waldmann, H., & Mandelkow, E. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200802621 · Cited by 286
Meng, F., Abedini, A., Plesner, A., Verchere, C. B., & Raleigh, D. P. (2010) · Biochemistry · doi:10.1021/bi100939a · Cited by 282
Inhibition of Amyloid Formation
Härd, T., & Lendel, C. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.12.062 · Cited by 269
Metadata
- Authors
- Feng, B. Y., Toyama, B. H., Wille, H., Colby, D. W., Collins, S. R., May, B. C. H., Prusiner, S. B., Weissman, J., & Shoichet, B. K.
- Venue
- Nature Chemical Biology
- Published
- 2008-01-27
- Volume
- 4
- Issue
- 3
- Pages
- 197-199
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- OpenAlex
- W2020970511
- Cited by
- 260
- References
- 20
- FWCI
- 10.30
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Small-molecule aggregates inhibit amyloid polymerization. https://app.cochat.ai/papers/10.1038/nchembio.65
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- Feng, B. Y., Toyama, B. H., Wille, H., Colby, D. W., Collins, S. R., May, B. C. H., Prusiner, S. B., Weissman, J., & Shoichet, B. K. (2008). Small-molecule aggregates inhibit amyloid polymerization. Nature Chemical Biology. https://doi.org/10.1038/nchembio.65
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.
