The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Identifying the Minimal Copper- and Zinc-binding Site Sequence in Amyloid-β Peptides
Open accessAbstract
With a combination of complementary experimental techniques, namely sedimentation assay, Fourier transform infrared spectroscopy, and x-ray absorption spectroscopy, we are able to determine the atomic structure around the metal-binding site in samples where amyloid-beta (Abeta) peptides are complexed with either Cu(II) or Zn(II). Exploiting information obtained on a selected set of fragments of the Abeta peptide, we identify along the sequence the histidine residues coordinated to the metal in the various peptides we have studied (Abeta(1-40), Abeta(1-16), Abeta(1-28), Abeta(5-23), and Abeta(17-40)). Our data can be consistently interpreted assuming that all of the peptides encompassing the minimal 1-16 amino acidic sequence display a copper coordination mode that involves three histidines (His(6), His(13), and His(14)). In zinc-Abeta complexes, despite the fact that the metal coordination appears to be more sensitive to solution condition and shows a less rigid geometry around the binding site, a four-histidine coordination mode is seen to be preferred. Lacking a fourth histidine along the Abeta peptide sequence, this geometrical arrangement hints at a Zn(II)-promoted interpeptide aggregation mode.
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Cites
Neurodegenerative diseases and oxidative stress
Barnham, K. J., Masters, C. L., & Bush, A. I. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1330 · Cited by 3,683
Copper, iron and zinc in Alzheimer's disease senile plaques
Lovell, M. A., Robertson, J. D., Teesdale, W. J., Campbell, J. L., & Markesbery, W. R. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00092-6 · Cited by 2,120
Cherny, R. A., Atwood, C. S., Xilinas, M. E., Gray, D. N., Jones, W. D., McLean, C. A., Barnham, K. J., Volitakis, I., Fraser, F. W., Kim, Y.-S., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00317-8 · Cited by 1,447
High‐resolution NMR studies of the zinc‐binding site of the Alzheimer's amyloid β‐peptide
Danielsson, J., Pierattelli, R., Banci, L., & Gräslund, A. (2007) · The FEBS Journal · doi:10.1111/j.1742-4658.2006.05563.x · Cited by 253
New Insights on How Metals Disrupt Amyloid β-Aggregation and Their Effects on Amyloid-β Cytotoxicity
Yoshiike, Y., Tanemura, K., Murayama, O., Akagi, T., Murayama, M., Sato, S., Sun, X., Tanaka, N., & Takashima, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010706200 · Cited by 244
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
Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-β peptide
Faller, P., & Hureau, C. (2009) · Dalton Trans. · doi:10.1039/b813398k · Cited by 530
The chemistry of Alzheimer’s disease
Rauk, A. (2009) · Chemical Society Reviews · doi:10.1039/b807980n · Cited by 417
The role of metallobiology and amyloid-β peptides in Alzheimer's disease
Roberts, B. R., Ryan, T. M., Bush, A. I., Masters, C. L., & Duce, J. A. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07500.x · Cited by 266
Sarell, C. J., Wilkinson, S. R., & Viles, J. H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.171355 · Cited by 199
Metadata
- Authors
- Minicozzi, V., Stellato, F., Comai, M., Serra, M. D., Potrich, C., Meyer-Klaucke, W., & Morante, S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2008-04
- Volume
- 283
- Issue
- 16
- Pages
- 10784-10792
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2021989110
- Cited by
- 208
- References
- 5
- FWCI
- 8.65
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Minicozzi, V., Stellato, F., Comai, M., Serra, M. D., Potrich, C., Meyer-Klaucke, W., & Morante, S. (2008). Identifying the Minimal Copper- and Zinc-binding Site Sequence in Amyloid-β Peptides. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m707109200
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