The DOI matches its Crossref record; 68 of the 68 references it cites were found in a registry or an index.
Aβ42 is More Rigid than Aβ40 at the C Terminus: Implications for Aβ Aggregation and Toxicity
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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RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory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
RetractedNMRPipe: A multidimensional spectral processing system based on UNIX pipes
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The 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
Alzheimer's Disease: Genes, Proteins, and Therapy
Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063
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The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
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Cited by
Nguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Dominguez, L., Shea, J.-E., Dokholyan, N. V., De Simone, A., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01122 · Cited by 678
Amyloid β Protein and Alzheimer’s Disease: When Computer Simulations Complement Experimental Studies
Nasica-Labouze, J., Nguyen, P. H., Sterpone, F., Berthoumieu, O., Buchete, N.-V., Coté, S., De Simone, A., Doig, A. J., Faller, P., Garcia, A., et al. (2015) · Chemical Reviews · doi:10.1021/cr500638n · Cited by 584
Self-citationLee, W.-H., Loo, C.-Y., Bebawy, M., Luk, F., Mason, R., & Rohanizadeh, R. (2013) · Current Neuropharmacology · doi:10.2174/1570159x11311040002 · Cited by 537
Atomic-resolution dynamics on the surface of amyloid-β protofibrils probed by solution NMR
Fawzi, N. L., Ying, J., Ghirlando, R., Torchia, D. A., & Clore, G. M. (2011) · Nature · doi:10.1038/nature10577 · Cited by 419
Jiang, T., Tan, L., Zhu, X.-C., Zhang, Q.-Q., Cao, L., Tan, M.-S., Gu, L.-Z., Wang, H.-F., Ding, Z.-Z., Zhang, Y.-D., et al. (2014) · Neuropsychopharmacology · doi:10.1038/npp.2014.164 · Cited by 320
Metadata
- Authors
- Yan, Y., & Wang, C.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2006-12
- Volume
- 364
- Issue
- 5
- Pages
- 853-862
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2035963355
- Cited by
- 273
- References
- 68
- FWCI
- 4.51
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Aβ42 is More Rigid than Aβ40 at the C Terminus: Implications for Aβ Aggregation and Toxicity. https://app.cochat.ai/papers/10.1016/j.jmb.2006.09.046
- The paper
- Yan, Y., & Wang, C. (2006). Aβ42 is More Rigid than Aβ40 at the C Terminus: Implications for Aβ Aggregation and Toxicity. Journal of Molecular Biology. https://doi.org/10.1016/j.jmb.2006.09.046
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.
