The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Amyloids — a functional coat for microorganisms
Open accessAbstract
Amyloids are filamentous protein structures approximately 10 nm wide and 0.1-10 mum long that share a structural motif, the cross-beta structure. These fibrils are usually associated with degenerative diseases in mammals. However, recent research has shown that these proteins are also expressed on bacterial and fungal cell surfaces. Microbial amyloids are important in mediating mechanical invasion of abiotic and biotic substrates. In animal hosts, evidence indicates that these protein structures also contribute to colonization by activating host proteases that are involved in haemostasis, inflammation and remodelling of the extracellular matrix. Activation of proteases by amyloids is also implicated in modulating blood coagulation, resulting in potentially life-threatening complications.
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Cites
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064
Staphylococcus aureus Sortase, an Enzyme that Anchors Surface Proteins to the Cell Wall
Mazmanian, S. K., Liu, G., Ton-That, H., & Schneewind, O. (1999) · Science · doi:10.1126/science.285.5428.760 · Cited by 1,053
Deane, R., Wu, Z., & Zlokovic, B. V. (2004) · Stroke · doi:10.1161/01.str.0000143452.85382.d1 · Cited by 392
Sortase‐catalysed anchoring of surface proteins to the cell wall of Staphylococcus aureus
Mazmanian, S. K., Ton‐That, H., & Schneewind, O. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02411.x · Cited by 387
Claessen, D., Rink, R., de Jong, W., Siebring, J., de Vreugd, P., Boersma, F. G. H., Dijkhuizen, L., & Wösten, H. A. B. (2003) · Genes & Development · doi:10.1101/gad.264303 · Cited by 327
Self-citationA CD36-initiated Signaling Cascade Mediates Inflammatory Effects of β-Amyloid
Moore, K. J., El Khoury, J., Medeiros, L. A., Terada, K., Geula, C., Luster, A. D., & Freeman, M. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208788200 · Cited by 327
Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene
Botto, M., Hawkins, P. N., Bickerstaff, M. C. M., Herbert, J., Bygrave, A. E., Mcbride, A., Hutchinson, W. L., Tennent, G. A., Walportz, M. J., & Pepys, M. B. (1997) · Nature Medicine · doi:10.1038/nm0897-855 · Cited by 266 · cited 1×
“, thereby contributing to the pathogenesis of amyloidosi”
Elliot, M. A., Karoonuthaisiri, N., Huang, J., Bibb, M. J., Cohen, S. N., Kao, C. M., & Buttner, M. J. (2003) · Genes & Development · doi:10.1101/gad.264403 · Cited by 246
Jong, A. Y., Chen, S. H. M., Stins, M. F., Kim, K. S., Tuan, T.-L., & Huang, S.-H. (2003) · Journal of Medical Microbiology · doi:10.1099/jmm.0.05060-0 · Cited by 206
Cited by
Zhu, X., Chen, B., Zhu, L., & Xing, B. (2017) · Environmental Pollution · doi:10.1016/j.envpol.2017.04.032 · Cited by 1,021
Hobley, L., Harkins, C., MacPhee, C. E., & Stanley-Wall, N. R. (2015) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuv015 · Cited by 581
“Intact fibres conformed to traits attributed to amyloid proteins including SDS insolubility, staining with amyloid-specific markers and β-sheet structure (Gebbink et al. 2005).”
BackgroundRasul, M., Cho, J., Shin, H.-S., & Hur, J. (2022) · Science of The Total Environment · doi:10.1016/j.scitotenv.2021.150304 · Cited by 154
Biology and Neuropathology of Dementia in Syphilis and Lyme Disease
(2008) · Handbook of Clinical Neurology · doi:10.1016/s0072-9752(07)01272-9 · Cited by 52
Assembly and disassembly of Aspergillus fumigatus conidial rodlets
Valsecchi, I., Lai, J. I., Stephen-Victor, E., Pillé, A., Beaussart, A., Lo, V., Pham, C. L. L., Aimanianda, V., Kwan, A. H., Duchateau, M., et al. (2019) · The Cell Surface · doi:10.1016/j.tcsw.2019.100023 · Cited by 46
Metadata
- Authors
- Gebbink, M. F. B. G., Claessen, D., Bouma, B., Dijkhuizen, L., & Wösten, H. A. B.
- Venue
- Nature Reviews Microbiology
- Published
- 2005-04
- Volume
- 3
- Issue
- 4
- Pages
- 333-341
- ISSN
- 1740-1526 (ISSN-L)
- 1740-1534
- OpenAlex
- W2124892192
- Cited by
- 288
- References
- 9
- FWCI
- 0.83
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Gebbink, M. F. B. G., Claessen, D., Bouma, B., Dijkhuizen, L., & Wösten, H. A. B. (2005). Amyloids — a functional coat for microorganisms. Nature Reviews Microbiology. https://doi.org/10.1038/nrmicro1127
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
