The DOI matches its Crossref record; 161 of the 161 references it cites were found in a registry or an index.
Functional Amyloids
Open accessAbstract
When protein/peptides aggregate, they usually form the amyloid state consisting of cross β-sheet structure built by repetitively stacked β-strands forming long fibrils.Amyloids are usually associated with disease including Alzheimer's.However, amyloid has many useful features.It efficiently transforms protein from the soluble to the insoluble state in an essentially two-state process, while its repetitive structure provides high stability and a robust prion-like replication mechanism.Accordingly, amyloid is used by nature in multifaceted and ingenious ways of life, ranging from bacteria and fungi to mammals.These include (1) Structure: Templating for small chemical molecules (Pmel17), biofilm formation in bacteria (curli), assisting aerial hyphae formation in streptomycetes (chaplins) or monolayer formation at a surface (hydrophobins).(2) Reservoirs: A storage state for peptide/proteins to protect them from their surroundings or vice versa (storage of peptide hormones in mammalian secretory granules or major basic protein in eosinophils).(3) Information carriers: The fungal immune system (HET-s prion in Podospora anserina, yeast prions) or long-term memory (e.g., mnemons in yeast, cytoplasmic polyadenylation element-binding protein in aplysia).Aggregation is also used to ( 4) "suppress" the function of the soluble protein (e.g., Cdc19 in yeast stress granules), or (5) "signaling" through formation of oligomers (e.g., HET-s prion, necroptosis-related proteins RIP1/RIP3).This review summarizes current knowledge on functional amyloids with a focus on the amyloid systems curli in bacteria, HET-s prion in P. anserina, and peptide hormone storage in mammals together with an attempt to highlight differences between functional and disease-associated amyloids.
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Cites
SignalP 4.0: discriminating signal peptides from transmembrane regions
Petersen, T. N., Brunak, S., von Heijne, G., & Nielsen, H. (2011) · Nature Methods · doi:10.1038/nmeth.1701 · Cited by 8,847
Protein Misfolding, Functional Amyloid, and Human Disease
Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,423
Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
Atomic structures of amyloid cross-β spines reveal varied steric zippers
Sawaya, M. R., Sambashivan, S., Nelson, R., Ivanova, M. I., Sievers, S. A., Apostol, M. I., Thompson, M. J., Balbirnie, M., Wiltzius, J. J. W., McFarlane, H. T., et al. (2007) · Nature · doi:10.1038/nature05695 · Cited by 2,271
Structure of the cross-β spine of amyloid-like fibrils
Nelson, R., Sawaya, M. R., Balbirnie, M., Madsen, A. Ø., Riekel, C., Grothe, R., & Eisenberg, D. (2005) · Nature · doi:10.1038/nature03680 · Cited by 2,202
Cryo-EM structures of tau filaments from Alzheimer’s disease
Fitzpatrick, A. W. P., Falcon, B., He, S., Murzin, A. G., Murshudov, G., Garringer, H. J., Crowther, R. A., Ghetti, B., Goedert, M., & Scheres, S. H. W. (2017) · Nature · doi:10.1038/nature23002 · Cited by 2,061 · cited 2×
“Recent structures of amyloid composed of full-length proteins reveal a much greater structural complexity, involving a combination of multiple cross-β-sheet motifs (Wasmer et al. 2008; Colvin et al. 2016; Riek and Eisenberg 2016; Wälti et al. 2016; Fitzpatrick et al. 2017).”
BackgroundSelf-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
Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
Fernandez-Escamilla, A.-M., Rousseau, F., Schymkowitz, J., & Serrano, L. (2004) · Nature Biotechnology · doi:10.1038/nbt1012 · Cited by 1,658
Role of Escherichia coli Curli Operons in Directing Amyloid Fiber Formation
Chapman, M. R., Robinson, L. S., Pinkner, J. S., Roth, R., Heuser, J., Hammar, M., Normark, S., & Hultgren, S. J. (2002) · Science · doi:10.1126/science.1067484 · Cited by 1,298
Li, J., McQuade, T., Siemer, A. B., Napetschnig, J., Moriwaki, K., Hsiao, Y.-S., Damko, E., Moquin, D., Walz, T., McDermott, A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.06.019 · Cited by 1,222
Cited by
Biomimetic peptide self-assembly for functional materials
Levin, A., Hakala, T. A., Schnaider, L., Bernardes, G. J. L., Gazit, E., & Knowles, T. P. J. (2020) · Nature Reviews Chemistry · doi:10.1038/s41570-020-0215-y · Cited by 853
The expanding amyloid family: Structure, stability, function, and pathogenesis
Sawaya, M. R., Hughes, M. P., Rodriguez, J. A., Riek, R., & Eisenberg, D. S. (2021) · Cell · doi:10.1016/j.cell.2021.08.013 · Cited by 475
Self-citationChow, W. Y., De Paëpe, G., & Hediger, S. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c01043 · Cited by 87
Liu, J., Song, J., Zeng, L., & Hu, B. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25147994 · Cited by 28
Metadata
- Authors
- Otzen, D., & Riek, R.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2019-05-14
- Volume
- 11
- Issue
- 12
- Pages
- a033860
- ISSN
- 1943-0264 (ISSN-L)
- OpenAlex
- W4205867548
- Cited by
- 331
- References
- 161
- Type
- posted content
- Language
- en
- Open access
- hybrid
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