The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution
Open accessAbstract
There is considerable interest in uncovering the pathway of amyloid formation because the toxic properties of amyloid likely stems from prefibril intermediates and not the fully formed fibrils. Using a recently invented method of collecting 2-dimensional infrared spectra and site-specific isotope labeling, we have measured the development of secondary structures for 6 residues during the aggregation process of the 37-residue polypeptide associated with type 2 diabetes, the human islet amyloid polypeptide (hIAPP). By monitoring the kinetics at 6 different labeled sites, we find that the peptides initially develop well-ordered structure in the region of the chain that is close to the ordered loop of the fibrils, followed by formation of the 2 parallel β-sheets with the N-terminal β-sheet likely forming before the C-terminal sheet. This experimental approach provides a detailed view of the aggregation pathway of hIAPP fibril formation as well as a general methodology for studying other amyloid forming proteins without the use of structure-perturbing labels.
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Cites
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064
Self-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
Cooper, G. J., Willis, A. C., Clark, A., Turner, R. C., Sim, R. B., & Reid, K. B. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.23.8628 · Cited by 1,299
Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation.
Westermark, P., Engström, U., Johnson, K. H., Westermark, G. T., & Betsholtz, C. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.13.5036 · Cited by 807
Islet amyloid: a long-recognized but underappreciated pathological feature of type 2 diabetes.
Kahn, S. E., Andrikopoulos, S., & Verchere, C. B. (1999) · Diabetes · doi:10.2337/diabetes.48.2.241 · Cited by 488
Cited by
Ultrafast Spectroscopy: State of the Art and Open Challenges
Maiuri, M., Garavelli, M., & Cerullo, G. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.9b10533 · Cited by 460
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-citationNanga, R. P. R., Brender, J. R., Vivekanandan, S., & Ramamoorthy, A. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.06.012 · Cited by 278
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
Self-citationHow to Get Insight into Amyloid Structure and Formation from Infrared Spectroscopy
Moran, S. D., & Zanni, M. T. (2014) · The Journal of Physical Chemistry Letters · doi:10.1021/jz500794d · Cited by 264
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Metadata
- Authors
- Shim, S.-H., Gupta, R., Ling, Y. L., Strasfeld, D. B., Raleigh, D. P., & Zanni, M. T.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2009-04-21
- Volume
- 106
- Issue
- 16
- Pages
- 6614-6619
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2053168342
- Cited by
- 286
- References
- 5
- FWCI
- 18.30
- Type
- journal article
- Language
- en
- Open access
- green
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- Shim, S.-H., Gupta, R., Ling, Y. L., Strasfeld, D. B., Raleigh, D. P., & Zanni, M. T. (2009). Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0805957106
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