The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet
Open accessAbstract
Significance: There is an enormous interest in the mechanism by which proteins misfold and aggregate into amyloid fibrils. Amyloid has been implicated in many human diseases, but the mechanism of aggregation is not understood. Intermediates have been postulated to play an important role in the process, but there have been very few direct measurements that provide specific structural details. The use of isotope labeling and 2D IR methods has allowed the characterization of a critical intermediate generated during amyloid formation by islet amyloid polypeptide, the peptide responsible for amyloid formation in type 2 diabetes. Identification of this intermediate provides a structural explanation for the lag phase and may explain why some species develop amyloid deposits of hIAPP while others do not.
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Cites
Protein Misfolding, Functional Amyloid, and Human Disease
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Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
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Atomic structures of amyloid cross-β spines reveal varied steric zippers
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Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism
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An Analytical Solution to the Kinetics of Breakable Filament Assembly
Knowles, T. P. J., Waudby, C. A., Devlin, G. L., Cohen, S. I. A., Aguzzi, A., Vendruscolo, M., Terentjev, E. M., Welland, M. E., & Dobson, C. M. (2009) · Science · doi:10.1126/science.1178250 · Cited by 1,139
Identifying the amylome, proteins capable of forming amyloid-like fibrils
Goldschmidt, L., Teng, P. K., Riek, R., & Eisenberg, D. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0915166107 · Cited by 809
Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation.
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A Bias-Exchange Approach to Protein Folding
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Cited by
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
Vibrational Spectroscopic Map, Vibrational Spectroscopy, and Intermolecular Interaction
Baiz, C. R., Błasiak, B., Bredenbeck, J., Cho, M., Choi, J.-H., Corcelli, S. A., Dijkstra, A. G., Feng, C.-J., Garrett-Roe, S., Ge, N.-H., et al. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00813 · Cited by 412
Self-citationIslet inflammation in type 2 diabetes and physiology
Eguchi, K., & Nagai, R. (2017) · Journal of Clinical Investigation · doi:10.1172/jci88877 · Cited by 361
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
Protein aggregation – Mechanisms, detection, and control
Wang, W., & Roberts, C. J. (2018) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2018.08.043 · Cited by 299
Metadata
- Authors
- 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.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2013-11-11
- Volume
- 110
- Issue
- 48
- Pages
- 19285-19290
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1981793913
- Cited by
- 274
- References
- 46
- FWCI
- 12.85
- Type
- journal article
- Language
- en
- Open access
- green
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- 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). Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1314481110
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