The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation.
Open accessAbstract
Islet amyloid polypeptide (IAPP), a putative polypeptide hormone, is a product of pancreatic beta-cells and the major constituent of the amyloid deposits seen mainly in islets of type 2 diabetic humans and diabetic cats. The connection between IAPP amyloid formation and diabetes is unknown, but a limited segment of the IAPP molecule, positions 20-29, seems responsible for the aggregation to fibrils. Differences in the amino acid sequence of this region probably determine whether or not islet amyloid can develop in a particular species. Amyloid fibril formation can be mimicked in vitro with the aid of synthetic peptides. With this technique we show that peptides corresponding to IAPP positions 20-29 of human and cat, species that develop IAPP-derived islet amyloid, form amyloid-like fibrils in vitro. The corresponding IAPP segment from three rodent species that do not develop IAPP-derived amyloid did not give rise to fibrils. Substitution of the human IAPP-(20-29) decapeptide with one or two amino acid residues from species without islet amyloid generally reduced the capacity to form fibrils. We conclude that the sequence Ala-Ile-Leu-Ser-Ser, corresponding to positions 25-29 of human IAPP, is strongly amyloidogenic and that a proline-for-serine substitution in position 28, as in several rodents, almost completely inhibits formation of amyloid fibrils.
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Garnier, J., Osguthorpe, D. J., & Robson, B. (1978) · Journal of Molecular Biology · doi:10.1016/0022-2836(78)90297-8 · Cited by 4,523
Empirical Predictions of Protein Conformation
Chou, P. Y., & Fasman, G. D. (1978) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.47.070178.001343 · Cited by 3,099
Prediction of the Secondary Structure of Proteins from their Amino Acid Sequence
Chou, P. Y., & Fasman, G. D. (1979) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470122921.ch2 · Cited by 2,917
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
Westermark, P., Wernstedt, C., Wilander, E., Hayden, D. W., O'Brien, T. D., & Johnson, K. H. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.11.3881 · Cited by 976
Self-citationWestermark, P., Wernstedt, C., Wilander, E., & Sletten, K. (1986) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(86)90708-4 · Cited by 510
Self-citationLukinius, A., Wilander, E., Westermark, G. T., Engstr�m, U., & Westermark, P. (1989) · Diabetologia · doi:10.1007/bf00285291 · Cited by 371
Self-citationCooper, G. J. S., Leighton, B., Dimitriadis, G., Parry‐Billings, M., Kowalchuk, J. M., Howland, K., Rothbard, J. B., Willis, A. C., & Reid, K. B. M. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.20.7763 · Cited by 351
Prediction of chain turns in globular proteins on a hydrophobic basis
Rose, G. D. (1978) · Nature · doi:10.1038/272586a0 · Cited by 329
The influence of amyloid deposits on the islet volume in maturity onset diabetes mellitus
Westermark, P., & Wilander, E. (1978) · Diabetologia · doi:10.1007/bf01219652 · Cited by 291
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Dewi, T. U. (2026) · Universitas Pasundan institutional repositories & scientific journals (Universitas Pasundan)
Mehta, T., & Goyal, B. (2026) · Physical Chemistry Chemical Physics · doi:10.1039/d6cp01811d
Knapton, A. E., Verma, N., Kotiya, D., Sowton, A. P., Thackray, B. D., Holzner, L. M. W., Darwin, P. M., Despa, S. I., Despa, F., & Murray, A. J. (2026) · Comprehensive physiology · doi:10.1002/cph4.70252
Jana, S., Haque, S. R., Palanikumar, L., Verley, G. D., Das, R. S., Patra, S., Magzoub, M. M., & Maity, D. (2026) · Biochemistry · doi:10.1021/acs.biochem.6c00469
Shivani, S. T., Maurais, J., LeMasters, B. E., Esterly, H. J., & Zanni, M. T. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c16754
The amyloid fold: An historical account of an intrinsic property of proteins
Lima, L. M. T. R. (2026) · Elsevier eBooks · doi:10.1016/b978-0-323-99507-8.00044-5
Metadata
- Authors
- Westermark, P., Engström, U., Johnson, K. H., Westermark, G. T., & Betsholtz, C.
- Affiliations
- Linköping University Hospital (SE)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1990-07
- Volume
- 87
- Issue
- 13
- Pages
- 5036-5040
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC54256
- OpenAlex
- W2061111679
- Cited by
- 807
- References
- 30
- Citations by year
- 2026: 18 · 2025: 20 · 2024: 27 · 2023: 17 · 2022: 25 · 2021: 31 · 2020: 43 · 2019: 21 · 2018: 28 · 2017: 41 · 2016: 36 · 2015: 36 · 2014: 29 · 2013: 33 · 2012: 36
- FWCI
- 7.26
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01dk036734-06)
- Medical Research Council
- National Institute of Diabetes and Digestive and Kidney Diseases (R01 DK36734)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Pancreatic function and diabetes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- amylin, amyloid fibril formation, type 2 diabetes, pancreatic beta cells, peptide aggregation
- MeSH terms
- Amino Acid Sequence, Amyloid, Amyloidosis, Animals, Cats, Diabetes Mellitus, Type 2, Cricetinae, Humans, Islets of Langerhans, Microscopy, Electron, Molecular Sequence Data, Mutation, Protein Precursors, Sequence Homology, Nucleic Acid, Species Specificity, Rats, Islet Amyloid Polypeptide
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