The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Islet amyloid polypeptide toxicity and membrane interactions
Open accessAbstract
Significance: Amyloid formation is a hallmark of a range of human diseases. The polypeptide hormone amylin forms amyloid deposits in type 2 diabetes, and amyloid formation is thought to be a contributor to the decline in β-cell mass in the disease, however the basis of amylin-induced cytotoxicity is not fully understood. Amylin-induced membrane disruption has attracted considerable interest, and the interactions of amylin with model membranes have been characterized, but the relationship between studies with model membranes and toxicity is not understood. In this article the relationship between cell toxicity and the ability to disrupt model membranes is examined. There is no direct correlation between the two processes.
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“Recent results from transplantation of human and transgenic animal islets suggest that oligomers of amylin play a key role in the progressive failure of  cells (25,216).”
From The Activity of Peptides of the Calcitonin Family in Bone (2019) · cites this paper as [25]
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Citations
Cites
Protein Misfolding, Functional Amyloid, and Human Disease
Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,497
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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
Diabetes Mellitus and the β Cell: The Last Ten Years
Ashcroft, F. M., & Rorsman, P. (2012) · Cell · doi:10.1016/j.cell.2012.02.010 · Cited by 902
Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases
Selkoe, D. J. (2004) · Nature Cell Biology · doi:10.1038/ncb1104-1054 · Cited by 863
Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus
Lorenzo, A., Razzaboni, B. L., Weir, G. C., & Yankner, B. A. (1994) · Nature · doi:10.1038/368756a0 · Cited by 820
Janson, J., Ashley, R. H., Harrison, D. J., McIntyre, S., & Butler, P. C. (1999) · Diabetes · doi:10.2337/diabetes.48.3.491 · Cited by 614
Clark, A., Wells, C. A., BULEY, I. D., Cruickshank, J. K., Vanhegan, R. I., Matthews, D. R., Cooper, G. J. S., Holman, R. R., & Turner, R. C. (1988) · PubMed · Cited by 518
Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane
Engel, M. F., Khemtemourian, L., Kleijer, C. C., Meeldijk, H. J. D., Jacobs, J., Verkleij, A., de Kruijff, B., Killian, J., & Höppener, J. (2008) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0708354105 · Cited by 465
Evidence of Cosecretion of Islet Amyloid Polypeptide and Insulin by β-Cells
Kahn, S. E., D'Alessio, D. A., Schwartz, M. W., Fujimoto, W. Y., Ensinck, J. W., Taborsky, G. J., & Porte, D. (1990) · Diabetes · doi:10.2337/diab.39.5.634 · Cited by 454
Cited by
Sorted by citations
Type 2 diabetes as a protein misfolding disease
Mukherjee, A., Morales‐Scheihing, D., Butler, P. C., & Soto, C. A. (2015) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2015.04.005 · Cited by 349
Implications of peptide assemblies in amyloid diseases
Ke, P. C., Sani, M., Ding, F., Käkinen, A., Javed, I., Separovic, F., Davis, T. P., & Mezzenga, R. (2017) · Chemical Society Reviews · doi:10.1039/c7cs00372b · Cited by 340
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
Self-citationAmyloid assembly and disassembly
Chuang, E., Hori, A. M., Hesketh, C. D., & Shorter, J. (2018) · Journal of Cell Science · doi:10.1242/jcs.189928 · Cited by 188
Effects of in vivo conditions on amyloid aggregation
Owen, M. C., Gnutt, D., Gao, M., Wärmländer, S. K. T. S., Jarvet, J., Gräslund, A., Winter, R., Ebbinghaus, S., & Strodel, B. (2019) · Chemical Society Reviews · doi:10.1039/c8cs00034d · Cited by 181
Metadata
- Authors
- Cao, P., Abedini, A., Wang, H., Tu, L.-H., Zhang, X., Schmidt, A. M., & Raleigh, D. P.
- Affiliations
- Stony Brook University (US)
- NYU Langone Health (US)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2013-11-11
- Volume
- 110
- Issue
- 48
- Pages
- 19279-19284
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC3845181
- OpenAlex
- W1980138515
- Cited by
- 146
- References
- 48
- Citations by year
- 2026: 5 · 2025: 6 · 2024: 6 · 2023: 10 · 2022: 7 · 2021: 5 · 2020: 15 · 2019: 13 · 2018: 26 · 2017: 16 · 2016: 6 · 2015: 21 · 2014: 9 · 2013: 1
- FWCI
- 8.56
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (GM078114, R01GM078114)
- National Institute of Diabetes and Digestive and Kidney Diseases (F32DK089734)
- 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 › Lipid Membrane Structure and Behavior
- Keywords
- amylin, membrane leakage, amyloid fibril formation, type 2 diabetes, islet transplantation, fibril growth, lipid rafts, cholesterol, pramlintide, cytotoxicity
- MeSH terms
- Amino Acid Sequence, Amyloid, Animals, Biophysics, Diabetes Mellitus, Type 2, Humans, Membranes, Artificial, Molecular Sequence Data, Oxazines, Species Specificity, Thiazoles, Xanthenes, Microscopy, Electron, Transmission, Rats, Benzothiazoles, Islet Amyloid Polypeptide
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