The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Aspects on human amyloid forms and their fibril polypeptides
Open accessAbstract
Amyloid is an in vivo fibrillar substance containing a fibril protein and several additional molecules. Presently, 25 proteins have been reported as main fibril components. Why just a few proteins form amyloid in vivo is still insufficiently understood. Many fibril proteins appear as fragments of larger precursors and for some types it is not clear whether fragmentation comes before or after fibrillation. The self‐assembly by amyloid proteins can be speeded up by seeding with preformed fibrils. In mice, systemic amyloidoses are transmissible by a seeding mechanism. Whether this prion‐like mechanism occurs in humans is not known, but can definitely not be ruled out.
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Cites
Caughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650
Molecular pathways to neurodegeneration
Bossy-Wetzel, E., Schwarzenbacher, R., & Lipton, S. A. (2004) · Nature Medicine · doi:10.1038/nm1067 · Cited by 740
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
Neurotoxic protein oligomers — what you see is not always what you get
Bitan, G., Fradinger, E. A., Spring, S. M., & Teplow, D. B. (2005) · Amyloid · doi:10.1080/13506120500106958 · Cited by 221
Cited by
Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus
Westermark, P., Andersson, A., & Westermark, G. T. (2011) · Physiological Reviews · doi:10.1152/physrev.00042.2009 · Cited by 1,044
Self-citationSack, G. H. (2018) · Molecular Medicine · doi:10.1186/s10020-018-0047-0 · Cited by 499
AA Amyloidosis: Pathogenesis and Targeted Therapy
Westermark, G. T., Fändrich, M., & Westermark, P. (2015) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-020712-163913 · Cited by 264
Self-citationZecca, L., Bellei, C., Costi, P., Albertini, A., Monzani, E., Casella, L., Gallorini, M., Bergamaschi, L., Moscatelli, A., Turro, N. J., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808768105 · Cited by 240
Potential aggregation prone regions in biotherapeutics: A survey of commercial monoclonal antibodies
Wang, X., Das, T. K., Singh, S. K., & Kumar, S. (2009) · mAbs · doi:10.4161/mabs.1.3.8035 · Cited by 198
Metadata
- Authors
- Westermark, P.
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2005-11-16
- Volume
- 272
- Issue
- 23
- Pages
- 5942-5949
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W2140559080
- Cited by
- 251
- References
- 4
- FWCI
- 8.64
- Type
- journal article
- Language
- en
- Open access
- bronze
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