The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Methionine 35 Oxidation Reduces Fibril Assembly of the Amyloid Aβ-(1–42) Peptide of Alzheimer's Disease
Open accessAbstract
The major component of amyloid plaques in Alzheimer's disease (AD) is Abeta, a small peptide that has high propensity to assemble as aggregated beta-sheet structures. Using three well established techniques for studying amyloid structure, namely circular dichroism, thioflavin-T fluorescence, and atomic force microscopy, we demonstrate that oxidation of the Met-35 side chain to a methionine sulfoxide (Met-35(ox)) significantly hinders the rate of fibril formation for the 42-residue Abeta-(1-42) at physiological pH. Met-35(ox) also alters the characteristic Abeta fibril morphology and prevents formation of the protofibril, which is a key intermediate in beta-amyloidosis and the associated neurotoxicity. The implications of these results for the biological function and role of Abeta with oxidative stress in AD are discussed.
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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
Snyder, S. W., Ladror, U. S., Wade, W. S., Wang, G. T., Barrett, L. W., Matayoshi, E. D., Huffaker, H. J., Krafft, G. A., & Holzman, T. F. (1994) · Biophysical Journal · doi:10.1016/s0006-3495(94)80591-0 · Cited by 381
Different Mechanisms of Oxidative Stress and Neurotoxicity for Alzheimer‘s Aβ(1−42) and Aβ(25−35)
Varadarajan, S., Kanski, J., Aksenova, M., Lauderback, C., & Butterfield, D. A. (2001) · Journal of the American Chemical Society · doi:10.1021/ja010452r · Cited by 346
Cited by
Gaggelli, E., Kozlowski, H., Valensin, D., & Valensin, G. (2006) · Chemical Reviews · doi:10.1021/cr040410w · Cited by 1,729
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
Amyloid β-Protein Assembly and Alzheimer Disease
Roychaudhuri, R., Yang, M., Hoshi, M. M., & Teplow, D. B. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.r800036200 · Cited by 615
The chemistry of Alzheimer’s disease
Rauk, A. (2009) · Chemical Society Reviews · doi:10.1039/b807980n · Cited by 417
Interaction between Human Prion Protein and Amyloid-β (Aβ) Oligomers
Chen, S., Yadav, S. P., & Surewicz, W. K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.145516 · Cited by 289
Metadata
- Authors
- Hou, L., Kang, I., Marchant, R. E., & Zagorski, M. G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-10
- Volume
- 277
- Issue
- 43
- Pages
- 40173-40176
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2084513527
- Cited by
- 218
- References
- 3
- FWCI
- 5.51
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Hou, L., Kang, I., Marchant, R. E., & Zagorski, M. G. (2002). Methionine 35 Oxidation Reduces Fibril Assembly of the Amyloid Aβ-(1–42) Peptide of Alzheimer's Disease. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.c200338200
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