The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Kinetics and Thermodynamics of Amyloid Fibril Assembly
Abstract
With some exceptions, amyloids appear to be accidental aggregated structures whose formation was not selected for in molecular evolution. Despite this, amyloid fibrils are in many respects surprisingly well-behaved molecules. For example, Huntington's disease-related polyglutamine sequences aggregate via a relatively simple nucleated growth polymerization mechanism. In addition, the Alzheimer's plaque protein Abeta has been shown to undergo reversible amyloid fibril formation to a position of dynamic equilibrium such that reaction thermodynamics can be quantified. Studies of these well-behaved amyloid systems are allowing us to peer more deeply into the process and products of off-pathway misfolding and aggregation.
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Cites
Molecular Mechanisms of Amyloidosis
Merlini, G., & Bellotti, V. (2003) · New England Journal of Medicine · doi:10.1056/nejmra023144 · Cited by 1,920
Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils
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[18] Quantification of β-sheet amyloid fibril structures with thioflavin T
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Role of Escherichia coli Curli Operons in Directing Amyloid Fiber Formation
Chapman, M. R., Robinson, L. S., Pinkner, J. S., Roth, R., Heuser, J., Hammar, M., Normark, S., & Hultgren, S. J. (2002) · Science · doi:10.1126/science.1067484 · Cited by 1,298
Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid Fibrils
Petkova, A. T., Yau, W.-M., & Tycko, R. (2006) · Biochemistry · doi:10.1021/bi051952q · Cited by 1,044
ARGONAUTE4 Control of Locus-Specific siRNA Accumulation and DNA and Histone Methylation
Zilberman, D., Cao, X., & Jacobsen, S. E. (2003) · Science · doi:10.1126/science.1079695 · Cited by 885
Scherzinger, E., Sittler, A., Schweiger, K., Heiser, V., Lurz, R., Hasenbank, R., Bates, G. P., Lehrach, H., & Wanker, E. E. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.8.4604 · Cited by 705
Semaphorin 3E and Plexin-D1 Control Vascular Pattern Independently of Neuropilins
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Prevention of Transthyretin Amyloid Disease by Changing Protein Misfolding Energetics
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Seeding Specificity in Amyloid Growth Induced by Heterologous Fibrils
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Self-citation
Cited by
Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)
Theillet, F.-X., Binolfi, A., Frembgen-Kesner, T., Hingorani, K., Sarkar, M., Kyne, C., Li, C., Crowley, P. B., Gierasch, L., Pielak, G. J., et al. (2014) · Chemical Reviews · doi:10.1021/cr400695p · Cited by 503
Amyloid Polymorphism: Structural Basis and Neurobiological Relevance
Tycko, R. (2015) · Neuron · doi:10.1016/j.neuron.2015.03.017 · Cited by 440
Folding versus aggregation: Polypeptide conformations on competing pathways
Jahn, T. R., & Radford, S. E. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.05.015 · Cited by 428
Goure, W. F., Krafft, G. A., Jerecic, J., & Hefti, F. (2014) · Alzheimer's Research & Therapy · doi:10.1186/alzrt272 · Cited by 190
Treadmill exercise prevents learning and memory impairment in Alzheimer's disease-like pathology
Dao, A. T., Zagaar, M. A., Levine, A. T., Salim, S., Eriksen, J. L., & Alkadhi, K. A. (2013) · Current Alzheimer Research · doi:10.2174/1567205011310050006 · Cited by 99
Metadata
- Authors
- Wetzel, R.
- Venue
- Accounts of Chemical Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2006-07-22
- Volume
- 39
- Issue
- 9
- Pages
- 671-679
- ISSN
- 0001-4842 (ISSN-L)
- 1520-4898
- OpenAlex
- W2171413096
- Cited by
- 284
- References
- 29
- FWCI
- 8.82
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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