The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Comparison of Alzheimer Aβ(1–40) and Aβ(1–42) amyloid fibrils reveals similar protofilament structures
Open accessAbstract
We performed mass-per-length (MPL) measurements and electron cryomicroscopy (cryo-EM) with 3D reconstruction on an Aβ(1–42) amyloid fibril morphology formed under physiological pH conditions. The data show that the examined Aβ(1–42) fibril morphology has only one protofilament, although two protofilaments were observed with a previously studied Aβ(1–40) fibril. The latter fibril was resolved at 8 Å resolution showing pairs of β-sheets at the cores of the two protofilaments making up a fibril. Detailed comparison of the Aβ(1–42) and Aβ(1–40) fibril structures reveals that they share an axial twofold symmetry and a similar protofilament structure. Furthermore, the MPL data indicate that the protofilaments of the examined Aβ(1–40) and Aβ(1–42) fibrils have the same number of Aβ molecules per cross-β repeat. Based on this data and the previously studied Aβ(1–40) fibril structure, we describe a model for the arrangement of peptides within the Aβ(1–42) fibril.
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Cites
Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils
Petkova, A. T., Leapman, R. D., Guo, Z., Yau, W.-M., Mattson, M. P., & Tycko, R. (2005) · Science · doi:10.1126/science.1105850 · Cited by 1,687
FTIR reveals structural differences between native β‐sheet proteins and amyloid fibrils
Zandomeneghi, G., Krebs, M. R. H., McCammon, M. G., & Fändrich, M. (2004) · Protein Science · doi:10.1110/ps.041024904 · Cited by 725
Self-citationInhibitors of Amyloid Toxicity Based on β-sheet Packing of Aβ40 and Aβ42
Sato, T., Kienlen-Campard, P., Ahmed, M., Liu, W., Li, H., Elliott, J. I., Aimoto, S., Constantinescu, S. N., Octave, J.-N., & Smith, S. O. (2006) · Biochemistry · doi:10.1021/bi052485f · Cited by 191
Cited by
The Amyloid State of Proteins in Human Diseases
Eisenberg, D., & Jucker, M. (2012) · Cell · doi:10.1016/j.cell.2012.02.022 · Cited by 1,744
EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity
Bieschke, J., Russ, J., Friedrich, R. P., Ehrnhoefer, D. E., Wobst, H., Neugebauer, K., & Wanker, E. E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910723107 · Cited by 1,011
Xiao, Y., Ma, B., McElheny, D., Parthasarathy, S., Long, F., Hoshi, M., Nussinov, R., & Ishii, Y. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2991 · Cited by 818
Cao, Y., & Mezzenga, R. (2019) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2019.05.002 · Cited by 649
Atomic structure and hierarchical assembly of a cross-β amyloid fibril
Fitzpatrick, A. W. P., Debelouchina, G. T., Bayro, M. J., Clare, D. K., Caporini, M. A., Bajaj, V. S., Jaroniec, C. P., Wang, L., Ladizhansky, V., Müller, S. A., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1219476110 · Cited by 565
Metadata
- Authors
- Schmidt, M., Sachse, C., Richter, W., Xu, C., Fändrich, M., & Grigorieff, N.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2009-11-24
- Volume
- 106
- Issue
- 47
- Pages
- 19813-19818
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1980709154
- Cited by
- 261
- References
- 3
- FWCI
- 10.63
- Type
- journal article
- Language
- en
- Open access
- green
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- Schmidt, M., Sachse, C., Richter, W., Xu, C., Fändrich, M., & Grigorieff, N. (2009). Comparison of Alzheimer Aβ(1–40) and Aβ(1–42) amyloid fibrils reveals similar protofilament structures. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0905007106
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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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