The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Polymorphism in Alzheimer Aβ Amyloid Organization Reflects Conformational Selection in a Rugged Energy Landscape
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ADVERTISEMENT RETURN TO ISSUEPREVReviewNEXTPolymorphism in Alzheimer Aβ Amyloid Organization Reflects Conformational Selection in a Rugged Energy LandscapeYifat Miller†, Buyong Ma‡, and Ruth Nussinov*‡§View Author Information Center for Cancer Research Nanobiology Program, NCI-Frederick, Frederick, Maryland 21702, Basic Science Program, SAIC-Frederick, Inc., Center for Cancer Research Nanobiology Program, NCI-Frederick, Frederick, Maryland 21702, and Sackler Institute of Molecular Medicine, Department of Human Genetics and Molecular Medicine, Sackler School of Medicine, Tel Aviv University, Tel Aviv 69978, Israel* To whom correspondence should be addressed. Tel.: (301) 846-5579. Fax: (301) 846-5598. E-mail: [email protected]†NCI-Frederick.‡SAIC-Frederick, Inc. and NCI-Frederick.§Tel Aviv University.Cite this: Chem. Rev. 2010, 110, 8, 4820–4838Publication Date (Web):April 19, 2010Publication History Received13 November 2009Published online19 April 2010Published inissue 11 August 2010https://doi.org/10.1021/cr900377tCopyright © 2010 American Chemical SocietyRIGHTS & PERMISSIONSACS AuthorChoiceArticle Views4640Altmetric-Citations240LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (4 MB) Get e-AlertsSUBJECTS:Conformation,Molecular mechanics,Nanofibers,Oligomers,Peptides and proteins Get e-Alerts
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Cites
1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
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RetractedThe Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
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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
Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
Common 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
Pathways towards and Away from Alzheimer’s Disease
Mattson, M. P. (2004) · Nature · doi:10.1038/nature02621 · Cited by 3,052
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
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Cited by
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
Lee, S. J. C., Nam, E., Lee, H. J., Savelieff, M. G., & Lim, M. H. (2017) · Chemical Society Reviews · doi:10.1039/c6cs00731g · Cited by 576
Untangling Amyloid-β, Tau, and Metals in Alzheimer’s Disease
Savelieff, M. G., Lee, S., Liu, Y., & Lim, M. H. (2013) · ACS Chemical Biology · doi:10.1021/cb400080f · Cited by 400
Qiao, Q., Bowman, G. R., & Huang, X. (2013) · Journal of the American Chemical Society · doi:10.1021/ja403147m · Cited by 182
Conformational basis for asymmetric seeding barrier in filaments of three- and four-repeat tau
Siddiqua, A., Luo, Y., Meyer, V., Swanson, M. A., Yu, X., Wei, G., Zheng, J., Eaton, G. R., Ma, B., Nussinov, R., et al. (2012) · Journal of the American Chemical Society · doi:10.1021/ja303498q · Cited by 75
Self-citation
Metadata
- Authors
- Miller, Y., Ma, B., & Nussinov, R.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-04-19
- Volume
- 110
- Issue
- 8
- Pages
- 4820-4838
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2063679630
- Cited by
- 286
- References
- 27
- FWCI
- 2.62
- Type
- journal article
- Language
- en
- Open access
- hybrid
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