The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Small-molecule conversion of toxic oligomers to nontoxic β-sheet–rich amyloid fibrils
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Cites
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
Self-citationCommon structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064
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
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
Aβ Oligomers – a decade of discovery
Walsh, D. M., & Selkoe, D. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04426.x · Cited by 1,938
Self-citationCellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., & Strittmatter, S. M. (2009) · Nature · doi:10.1038/nature07761 · Cited by 1,560
[18] Quantification of β-sheet amyloid fibril structures with thioflavin T
LeVine, H. (1999) · Methods in Enzymology · doi:10.1016/s0076-6879(99)09020-5 · Cited by 1,365
Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils
Ahmed, M., Davis, J., Aucoin, D., Sato, T., Ahuja, S., Aimoto, S., Elliott, J. I., Van Nostrand, W. E., & Smith, S. O. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1799 · Cited by 1,111
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-citationNecula, M., Kayed, R., Milton, S., & Glabe, C. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608207200 · Cited by 680
Cited by
Danysz, W., & Parsons, C. G. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2012.02057.x · Cited by 500
Contributions of central and systemic inflammation to the pathophysiology of Parkinson's disease
Collins, L. M., Toulouse, A., Connor, T. J., & Nolan, Y. M. (2012) · Neuropharmacology · doi:10.1016/j.neuropharm.2012.01.028 · Cited by 306
Zempel, H., Luedtke, J., Kumar, Y., Biernat, J., Dawson, H., Mandelkow, E., & Mandelkow, E. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.207 · Cited by 283
Phytochemicals as inhibitors of NF-κB for treatment of Alzheimer’s disease
Seo, E.-J., Fischer, N., & Efferth, T. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2017.11.030 · Cited by 265
Insulin-Degrading Enzyme in the Fight against Alzheimer's Disease
Kurochkin, I. V., Guarnera, E., & Berezovsky, I. N. (2018) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.10.008 · Cited by 185
Metadata
- Authors
- Bieschke, J., Herbst, M., Wiglenda, T., Friedrich, R. P., Boeddrich, A., Schiele, F., Kleckers, D., Lopez del Amo, J. M., Grüning, B. A., Wang, Q., Schmidt, M. R., Lurz, R., Anwyl, R., Schnoegl, S., Fändrich, M., Frank, R. F., Reif, B., Günther, S., Walsh, D. M., & Wanker, E. E.
- Venue
- Nature Chemical Biology
- Published
- 2011-11-20
- Volume
- 8
- Issue
- 1
- Pages
- 93-101
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- OpenAlex
- W2139051378
- Cited by
- 445
- References
- 10
- FWCI
- 14.83
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Small-molecule conversion of toxic oligomers to nontoxic β-sheet–rich amyloid fibrils. https://app.cochat.ai/papers/10.1038/nchembio.719
- The paper
- Bieschke, J., Herbst, M., Wiglenda, T., Friedrich, R. P., Boeddrich, A., Schiele, F., Kleckers, D., Lopez del Amo, J. M., Grüning, B. A., Wang, Q., Schmidt, M. R., Lurz, R., Anwyl, R., Schnoegl, S., Fändrich, M., Frank, R. F., Reif, B., Günther, S., Walsh, D. M., & Wanker, E. E. (2012). Small-molecule conversion of toxic oligomers to nontoxic β-sheet–rich amyloid fibrils. Nature Chemical Biology. https://doi.org/10.1038/nchembio.719
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.
