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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Citations
Cites
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Self-citationMapping Aβ Amyloid Fibril Secondary Structure Using Scanning Proline Mutagenesis
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Self-citationMutations and off-pathway aggregation of proteins
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Self-citationMutational analysis of the structural organization of polyglutamine aggregates
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Self-citationGlobal Suppression of Protein Folding Defects and Inclusion Body Formation
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Self-citationA Role for Interaction of the RNA Polymerase Flap Domain with the σ Subunit in Promoter Recognition
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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
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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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