The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology
Open accessAbstract
Self-assembling amyloid materials with various length scales and tailored functions show wide applications in the fields of biomedicine, tissue engineering, energy materials, environmental science, nanodevices, biosensors, optical materials and liquid crystals.
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Cites
Nanocarriers as an emerging platform for cancer therapy
Peer, D., Karp, J. M., Hong, S., Farokhzad, O. C., Margalit, R., & Langer, R. (2007) · Nature Nanotechnology · doi:10.1038/nnano.2007.387 · Cited by 8,710
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744
Intrinsically unstructured proteins and their functions
Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871
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
The amyloid state and its association with protein misfolding diseases.
Knowles, T. P. J., Vendruscolo, M., & Dobson, C. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3810 · Cited by 2,382
Copper, iron and zinc in Alzheimer's disease senile plaques
Lovell, M. A., Robertson, J. D., Teesdale, W. J., Campbell, J. L., & Markesbery, W. R. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00092-6 · Cited by 2,120
Rapid induction of Alzheimer A beta amyloid formation by zinc
Bush, A., Pettingell, W., Multhaup, G., d Paradis, M., Vonsattel, J., Gusella, J., Beyreuther, K., Masters, C., & Tanzi, R. (1994) · Science · doi:10.1126/science.8073293 · Cited by 1,522
[18] Quantification of β-sheet amyloid fibril structures with thioflavin T
LeVine, H. (1999) · Methods in Enzymology · doi:10.1016/s0076-6879(99)09020-5 · Cited by 1,365
Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils
Ahmed, M., Davis, J., Aucoin, D., Sato, T., Ahuja, S., Aimoto, S., Elliott, J. I., Van Nostrand, W. E., & Smith, S. O. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1799 · Cited by 1,111
Atwood, C. S., Moir, R. D., Huang, X., Scarpa, R. C., Bacarra, N. M. E., Romano, D. M., Hartshorn, M. A., Tanzi, R. E., & Bush, A. I. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.12817 · Cited by 1,009
Cited by
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
Accelerating the prediction and discovery of peptide hydrogels with human-in-the-loop
Xu, T., Wang, J., Zhao, S., Chen, D., Zhang, H., Fang, Y., Kong, N., Zhou, Z., Li, W., & Wang, H. (2023) · Nature Communications · doi:10.1038/s41467-023-39648-2 · Cited by 132
Rhaman, M. M., Islam, M. R., Akash, S., Mim, M., Noor alam, M., Nepovimova, E., Valis, M., Kuca, K., & Sharma, R. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.989471 · Cited by 63
Production and characterization of amaranth amyloid fibrils from food protein waste
Mykolenko, S., Soon, W. L., & Mezzenga, R. (2024) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2023.109604 · Cited by 60
Self-citationMashweu, A. R., & Azov, V. A. (2024) · doi:10.20944/preprints202410.2092.v1 · Cited by 10
Metadata
- Authors
- Wei, G., Su, Z., Reynolds, N. P., Arosio, P., Hamley, I. W., Gazit, E., & Mezzenga, R.
- Venue
- Chemical Society Reviews
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2017
- Volume
- 46
- Issue
- 15
- Pages
- 4661-4708
- ISSN
- 0306-0012 (ISSN-L)
- 1460-4744
- OpenAlex
- W2619203867
- Cited by
- 904
- References
- 21
- FWCI
- 5.34
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Wei, G., Su, Z., Reynolds, N. P., Arosio, P., Hamley, I. W., Gazit, E., & Mezzenga, R. (2017). Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology. Chemical Society Reviews. https://doi.org/10.1039/c6cs00542j
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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.
