The DOI matches its Crossref record; 94 of the 94 references it cites were found in a registry or an index.
Peptide Conformation and Supramolecular Organization in Amylin Fibrils: Constraints from Solid-State NMR
Open accessAbstract
The 37-residue amylin peptide, also known as islet amyloid polypeptide, forms fibrils that are the main peptide or protein component of amyloid that develops in the pancreas of type 2 diabetes patients. Amylin also readily forms amyloid fibrils in vitro that are highly polymorphic under typical experimental conditions. We describe a protocol for the preparation of synthetic amylin fibrils that exhibit a single predominant morphology, which we call a striated ribbon, in electron microscopy and atomic force microscopy images. Solid-state nuclear magnetic resonance (NMR) measurements on a series of isotopically labeled samples indicate a single molecular structure within the striated ribbons. We use scanning transmission electron microscopy and several types of one- and two-dimensional solid-state NMR techniques to obtain constraints on the peptide conformation and supramolecular structure in these amylin fibrils and to derive molecular structural models that are consistent with the experimental data. The basic structural unit in amylin striated ribbons, which we call the protofilament, contains four layers of parallel beta-sheets, formed by two symmetric layers of amylin molecules. The molecular structure of amylin protofilaments in striated ribbons closely resembles the protofilament in amyloid fibrils with a similar morphology formed by the 40-residue beta-amyloid peptide that is associated with Alzheimer's disease.
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Cited by
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
Chiti, F., & Dobson, C. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045115 · Cited by 2,629
Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils
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Self-citationIslet 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
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Amyloid Polymorphism: Structural Basis and Neurobiological Relevance
Tycko, R. (2015) · Neuron · doi:10.1016/j.neuron.2015.03.017 · Cited by 440
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Metadata
- Authors
- Luca, S., Yau, W.-M., Leapman, R., & Tycko, R.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2007-11-01
- Volume
- 46
- Issue
- 47
- Pages
- 13505-13522
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1964727310
- Cited by
- 578
- References
- 94
- FWCI
- 19.58
- Type
- journal article
- Language
- en
- Open access
- green
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