The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
Atomic structure of the cross‐β spine of islet amyloid polypeptide (amylin)
Open accessAbstract
Human islet amyloid polypeptide (IAPP or amylin) is a 37‐residue hormone found as fibrillar deposits in pancreatic extracts of nearly all type II diabetics. Although the cellular toxicity of IAPP has been established, the structure of the fibrillar form found in these deposits is unknown. Here we have crystallized two segments from IAPP, which themselves form amyloid‐like fibrils. The atomic structures of these two segments, NNFGAIL and SSTNVG, were determined, and form the basis of a model for the most commonly observed, full‐length IAPP polymorph.
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Cites
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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
Self-citationStructure 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
Self-citationObesity and Diabetes in the Developing World — A Growing Challenge
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“Pancreatic extracts from individuals with type II diabetes have been found to contain extracellular deposits of the 37-residue peptide hormone IAPP that is expressed, stored, and secreted from the b-islet cells of the pancreas (Cooper et al. 1987; Westermark et al. 1987; Cooper 1994).”
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A possible role for π‐stacking in the self‐assembly of amyloid fibrils
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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
Nguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Dominguez, L., Shea, J.-E., Dokholyan, N. V., De Simone, A., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01122 · Cited by 678
Amyloid Structure: Conformational Diversity and Consequences
Toyama, B. H., & Weissman, J. S. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-090908-120656 · Cited by 304
Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet
Buchanan, L. E., Dunkelberger, E. B., Tran, H. Q., Cheng, P.-N., Chiu, C.-C., Cao, P., Raleigh, D. P., de Pablo, J. J., Nowick, J. S., & Zanni, M. T. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314481110 · Cited by 274
Islet amyloid polypeptide: structure, function, and pathophysiology
Akter, R., Cao, P., Noor, H., Ridgway, Z., Tu, L.-H., Wang, H., Wong, A. G., Zhang, X., Abedini, A., Schmidt, A. M., et al. (2016) · Journal of Diabetes Research · doi:10.1155/2016/2798269 · Cited by 273
Metadata
- Authors
- Wiltzius, J. J. W., Sievers, S. A., Sawaya, M. R., Cascio, D., Popov, D., Riekel, C., & Eisenberg, D.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2008-09
- Volume
- 17
- Issue
- 9
- Pages
- 1467-1474
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- OpenAlex
- W2144481414
- Cited by
- 320
- References
- 45
- FWCI
- 12.67
- Type
- journal article
- Language
- en
- Open access
- green
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- Wiltzius, J. J. W., Sievers, S. A., Sawaya, M. R., Cascio, D., Popov, D., Riekel, C., & Eisenberg, D. (2008). Atomic structure of the cross‐β spine of islet amyloid polypeptide (amylin). Protein Science. https://doi.org/10.1110/ps.036509.108
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