The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Amyloid fibrils: Abnormal protein assembly
Open accessAbstract
Amyloid refers to the abnormal fibrous, extracellular, proteinaceous deposits found in organs and tissues. Amyloid is insoluble and is structurally dominated by beta-sheet structure. Unlike other fibrous proteins it does not commonly have a structural, supportive or motility role but is associated with the pathology seen in a range of diseases known as the amyloidoses. These diseases include Alzheimer's, the spongiform encephalopathies and type II diabetes, all of which are progressive disorders with associated high morbidity and mortality. Not surprisingly, research into the physicochemical properties of amyloid and its formation is currently intensely pursued. In this chapter we will highlight the key scientific findings and discuss how the stability of amyloid fibrils impacts on bionanotechnology.
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Citations
Cites
Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
Amyloid deposition as the central event in the aetiology of Alzheimer’s disease
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Correlation Between Elevated Levels of Amyloid β-Peptide in the Brain and Cognitive Decline
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Amyloid β-Protein Fibrillogenesis
Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., & Teplow, D. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25945 · Cited by 1,046
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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 by
Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases
Soto, C., & Pritzkow, S. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0235-9 · Cited by 1,180
Prebiotic Peptides: Molecular Hubs in the Origin of Life
Frenkel-Pinter, M., Samanta, M., Ashkenasy, G., & Leman, L. J. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00664 · Cited by 354
Disentangling the complexity of low complexity proteins
Mier, P., Paladin, L., Tamana, S., Petrosian, S., Hajdu-Soltész, B., Urbanek, A., Gruca, A., Plewczynski, D., Grynberg, M., Bernadó, P., et al. (2020) · Briefings in Bioinformatics · doi:10.1093/bib/bbz007 · Cited by 104
Newcomb, C. J., Moyer, T. J., Lee, S. S., & Stupp, S. I. (2012) · Current Opinion in Colloid & Interface Science · doi:10.1016/j.cocis.2012.09.004 · Cited by 76
Human apolipoprotein A-I-derived amyloid: its association with atherosclerosis
Ramella, N. A., Rimoldi, O. J., Prieto, E. D., Schinella, G. R., Sanchez, S. A., Jaureguiberry, M. S., Vela, M. E., Ferreira, S. T., & Tricerri, M. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022532 · Cited by 66
Metadata
- Authors
- Rambaran, R. N., & Serpell, L. C.
- Venue
- Prion
- Publisher
- Informa UK Limited
- Published
- 2008-07
- Volume
- 2
- Issue
- 3
- Pages
- 112-117
- ISSN
- 1933-6896 (ISSN-L)
- 1933-690X
- OpenAlex
- W1994321237
- Cited by
- 511
- References
- 7
- FWCI
- 3.02
- Type
- journal article
- Language
- en
- Open access
- green
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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.
