Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation.

Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins

Garnier, J., Osguthorpe, D. J., & Robson, B. (1978) · Journal of Molecular Biology · doi:10.1016/0022-2836(78)90297-8 · Cited by 4,523 · see citing works

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 3,137 · see citing works

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 · see citing works

Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients.

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 · see citing works

Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells.

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 · see citing works

A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas

Westermark, P., Wernstedt, C., Wilander, E., & Sletten, K. (1986) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(86)90708-4 · Cited by 512 · see citing works

Co-localization of islet amyloid polypeptide and insulin in the B cell secretory granules of the human pancreatic islets

Lukinius, A., Wilander, E., Westermark, G. T., Engstr�m, U., & Westermark, P. (1989) · Diabetologia · doi:10.1007/bf00285291 · Cited by 371 · see citing works

Amylin found in amyloid deposits in human type 2 diabetes mellitus may be a hormone that regulates glycogen metabolism in skeletal muscle.

Cooper, 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 348 · see citing works

Prediction of chain turns in globular proteins on a hydrophobic basis

Rose, G. D. (1978) · Nature · doi:10.1038/272586a0 · Cited by 329 · see citing works

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 · see citing works

β-PLEATED SHEET FIBRILS A COMPARISON OF NATIVE AMYLOID WITH SYNTHETIC PROTEIN FIBRILS

Glenner, G. G., Eanes, E. D., Bladen, H. A., Linke, R. P., & Termine, J. D. (1974) · Journal of Histochemistry & Cytochemistry · doi:10.1177/22.12.1141 · Cited by 290 · see citing works

Islet amyloid in type 2 human diabetes mellitus and adult diabetic cats contains a novel putative polypeptide hormone.

Westermark, P., Wernstedt, C., O’Brien, T. D., Hayden, D. W., & Johnson, K. H. (1987) · PubMed Central · Cited by 261 · see citing works

An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing.

Sanke, T., Bell, G. I., Sample, C. E., Rubenstein, A. H., & Steiner, D. F. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77825-9 · Cited by 258 · see citing works

Immunolocalization of islet amyloid polypeptide (IAPP) in pancreatic beta cells by means of peroxidase-antiperoxidase (PAP) and protein A-gold techniques.

Johnson, K. H., O’Brien, T. D., Hayden, D. W., Jordan, K., Ghobrial, H. K. G., Mahoney, W. C., & Westermark, P. (1988) · PubMed Central · Cited by 195 · see citing works

Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species

Betsholtz, C., Christmanson, L., Engström, U., Rorsman, F., Svensson, V., Johnson, K. H., & Westermark, P. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)81467-x · Cited by 176 · see citing works

Fine structure of islets of Langerhans in insular amyloidosis

Westermark, P. (1973) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/bf00549079 · Cited by 147 · see citing works

Amyloid fibrils formed from a segment of the pancreatic islet amyloid protein

Glenner, G. G., Eanes, E. D., & Wiley, C. A. (1988) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(88)80538-2 · Cited by 145 · see citing works

Islet amyloid polypeptide. A new beta cell secretory product related to islet amyloid deposits.

Nishi, M., Sanke, T., Nagamatsu, S., Bell, G. I., & Steiner, D. F. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39539-0 · Cited by 139 · see citing works

Conservation of the sequence of islet amyloid polypeptide in five mammals is consistent with its putative role as an islet hormone.

Nishi, M., Chan, S. J., Nagamatsu, S., Bell, G. I., & Steiner, D. F. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.15.5738 · Cited by 130 · see citing works

Islet amyloid polypeptide (IAPP): cDNA cloning and identification of an amyloidogenic region associated with the species-specific occurrence of age-related diabetes mellitus

Betsholtz, C., Svensson, V., Rorsman, F., Engström, U., Westermark, G. T., Wilander, E., Johnson, K. H., & Westermark, P. (1989) · Experimental Cell Research · doi:10.1016/0014-4827(89)90407-2 · Cited by 125 · see citing works

Rat amylin: cloning and tissue-specific expression in pancreatic islets.

Leffert, J. D., Newgard, C. B., Okamoto, H., Milburn, J. L., & Luskey, K. L. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.9.3127 · Cited by 121 · see citing works

Localisation of islet amyloid peptide in lipofuscin bodies and secretory granules of human B-cells and in islets of type-2 diabetic subjects

Clark, A., Edwards, C., Ostle, L., Sutton, R., Rothbard, J., Morris, J., & Turner, R. (1989) · Cell and Tissue Research · doi:10.1007/bf00221649 · Cited by 115 · see citing works

Islet amyloid polypeptide: Identification and chromosomal localization of the human gene

Mosselman, S., Höppener, J. W. M., Zandberg, J., van Mansfeld, A. D. M., van Kessel, A. H. M. G., Lips, C. J. M., & Jansz, H. S. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)80922-0 · Cited by 115 · see citing works

Impaired glucose tolerance is associated with increased islet amyloid polypeptide (IAPP) immunoreactivity in pancreatic beta cells.

Johnson, K. H., O’Brien, T. D., Jordan, K., & Westermark, P. (1989) · PubMed Central · Cited by 109 · see citing works

Structure of Cat Islet Amyloid Polypeptide and Identification of Amino Acid Residues of Potential Significance for Islet Amyloid Formation

Betsholtz, C., Christmanson, L., Engström, U., Rorsman, F., Jordan, K., O’Brien, T. D., Murtaugh, M. P., Johnson, K. H., & Westermark, P. (1990) · Diabetes · doi:10.2337/diacare.39.1.118 · Cited by 95 · see citing works

Feline Insular Amyloid: Association with Diabetes Mellitus

Yano, B. L., Hayden, D. W., & Johnson, K. H. (1981) · Veterinary Pathology · doi:10.1177/030098588101800507 · Cited by 83 · see citing works

Islet amyloid polypeptide (IAPP) and pro-IAPP immunoreactivity in human islets of Langerhans

Westermark, P., Engström, U., Westermark, G. T., Johnson, K. H., Permerth, J., & Betsholtz, C. (1989) · Diabetes Research and Clinical Practice · doi:10.1016/0168-8227(89)90008-9 · Cited by 80 · see citing works

Insular Amyloidosis and Diabetes Mellitus in Macaca Nigra

Howard, C. F. (1978) · Diabetes · doi:10.2337/diab.27.4.357 · Cited by 75 · see citing works

The putative hormone islet amyloid polypeptide (IAPP) induces impaired glucose tolerance in cats

Johnson, K. H., O’Brien, T. D., Jordan, K., Betsholtz, C., & Westermark, P. (1990) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(90)92053-3 · Cited by 46 · see citing works

The pancreas in the degu

Spear, G. S., Caple, M., & Sutherland, L. R. (1984) · Experimental and Molecular Pathology · doi:10.1016/0014-4800(84)90047-9 · Cited by 35 · see citing works

β-Cell Deficit and Increased β-Cell Apoptosis in Humans With Type 2 Diabetes

Butler, A. E., Janson, J., Bonner-Weir, S., Ritzel, R., Rizza, R. A., & Butler, P. C. (2003) · Diabetes · doi:10.2337/diabetes.52.1.102 · Cited by 4,011 · see citing works

The relative contributions of insulin resistance and beta-cell dysfunction to the pathophysiology of type 2 diabetes

Kahn, S. E. (2003) · Diabetologia · doi:10.1007/s00125-002-1009-0 · Cited by 2,166 · see citing works

Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state

Pike, C., Burdick, D., Walencewicz, A., Glabe, C., & Cotman, C. (1993) · The Journal of Neuroscience · doi:10.1523/jneurosci.13-04-01676.1993 · Cited by 1,417 · see citing works

A possible role for π‐stacking in the self‐assembly of amyloid fibrils

Gazit, E. (2002) · The FASEB Journal · doi:10.1096/fj.01-0442hyp · Cited by 1,128 · see citing works

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 · see citing works

Increased Risk of Type 2 Diabetes in Alzheimer Disease

Janson, J., Laedtke, T., Parisi, J. E., O’Brien, P., Petersen, R. C., & Butler, P. C. (2004) · Diabetes · doi:10.2337/diabetes.53.2.474 · Cited by 950 · see citing works

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 819 · see citing works

The Importance of -Cell Failure in the Development and Progression of Type 2 Diabetes

Kahn, S. E. (2001) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.86.9.7713 · Cited by 694 · see citing works

The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles.

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 · see citing works

Islet Amyloid in Type 2 Diabetes, and the Toxic Oligomer Hypothesis

Haataja, L., Gurlo, T., Huang, C. J., & Butler, P. C. (2008) · Endocrine Reviews · doi:10.1210/er.2007-0037 · Cited by 612 · see citing works

Islet Amyloid: A Critical Entity in the Pathogenesis of Type 2 Diabetes

Hull, R. L., Westermark, G. T., Westermark, P., & Kahn, S. E. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2004-0405 · Cited by 586 · see citing works

Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's disease

Hilbich, C., Kisters–Woike, B., Reed, J., Masters, C. L., & Beyreuther, K. T. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90881-6 · Cited by 580 · see citing works

Peptide Conformation and Supramolecular Organization in Amylin Fibrils: Constraints from Solid-State NMR

Luca, S., Yau, W., Leapman, R. D., & Tycko, R. (2007) · Biochemistry · doi:10.1021/bi701427q · Cited by 579 · see citing works

Islet amyloid and type 2 diabetes mellitus.

Höppener, J., Bo, A.-R., & Lips, C. J. M. (2000) · New England Journal of Medicine · doi:10.1056/nejm200008103430607 · Cited by 499 · see citing works

Neuroanatomical Localization, Pharmacological Characterization and Functions of CGRP, Related Peptides and Their Receptors

van Rossum, D., Hanisch, U., & Quirion, R. (1997) · Neuroscience & Biobehavioral Reviews · doi:10.1016/s0149-7634(96)00023-1 · Cited by 512 · see citing works

Hereditary transthyretin amyloidosis: a model of medical progress for a fatal disease

Adams, D., Koike, H., Slama, M., & Coelho, T. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-019-0210-4 · Cited by 450 · see citing works

Identification of a penta- and hexapeptide of islet amyloid polypeptide (IAPP) with amyloidogenic and cytotoxic properties

Tenidis, K., Waldner, M., Bernhagen, J., Fischle, W., Bergmann, M. M., Weber, M., Merkle, M., Voelter, W., Brunner, H., & Kapurniotu, A. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3422 · Cited by 428 · see citing works

Seeding Specificity in Amyloid Growth Induced by Heterologous Fibrils*

O'Nuallain, B., Williams, A. D., Westermark, P., & Wetzel, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311300200 · Cited by 406 · see citing works

Analysis of the Minimal Amyloid-forming Fragment of the Islet Amyloid Polypeptide

Rosenfeld, R., & Gazit, E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102883200 · Cited by 421 · see citing works

Proline and glycine control protein self-organization into elastomeric or amyloid fibrils.

Rauscher, S., Baud, S., Miao, M., Keeley, F., & Pomès, R. (2006) · Structure · doi:10.1016/j.str.2006.09.008 · Cited by 354 · see citing works

A Molecular Model of Alzheimer Amyloid β-Peptide Fibril Formation

Tjernberg, L. O., Callaway, D. J. E., Tjernberg, A., Hahne, S., Lilliehöök, C., Terenius, L. Y., Thyberg, J., & Nordstedt, C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.18.12619 · Cited by 360 · see citing works

Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in Vitro

Kayed, R., Bernhagen, J., Greenfield, N. J., Sweimeh, K., Brunner, H., Voelter, W., & Kapurniotu, A. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2646 · Cited by 351 · see citing works

Insulin resistance and amyloidogenesis as common molecular foundation for type 2 diabetes and Alzheimer's disease

Zhao, W., & Townsend, M. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.10.014 · Cited by 353 · see citing works

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 338 · see citing works

Soluble protein oligomers as emerging toxins in Alzheimer’s and other amyloid diseases

Ferreira, S. T., Vieira, M. N. N., & De Felice, F. G. (2007) · IUBMB Life · doi:10.1080/15216540701283882 · Cited by 335 · see citing works

Watching amyloid fibrils grow by time-lapse atomic force microscopy 1 1Edited by W. Baumeister

Goldsbury, C. S., Kistler, J., Aebi, U., Arvinte, T., & Cooper, G. J. S. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2299 · Cited by 324 · see citing works

Atomic structure of the cross‐β spine of islet amyloid polypeptide (amylin)

Wiltzius, J. J. W., Sievers, S. A., Sawaya, M. R., Cascio, D., Popov, D., Riekel, C., & Eisenberg, D. S. (2008) · Protein Science · doi:10.1110/ps.036509.108 · Cited by 320 · see citing works

Amyloid Fibril Formation from Full-Length and Fragments of Amylin

Goldsbury, C. S., Goldie, K. N., Pellaud, J., Seelig, J., Frey, P., Müller, S. A., Kistler, J., Cooper, G. J. S., & Aebi, U. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4268 · Cited by 316 · see citing works

Prolines and Aamyloidogenicity in Fragments of the Alzheimer's Peptide .beta./A4

Wood, S. J., Wetzel, R. B., Martin, J. D., & Hurle, M. R. (1995) · Biochemistry · doi:10.1021/bi00003a003 · Cited by 313 · see citing works

Conserved and Cooperative Assembly of Membrane-Bound α-Helical States of Islet Amyloid Polypeptide

Knight, J. D., Hebda, J. A., & Miranker, A. D. (2006) · Biochemistry · doi:10.1021/bi060579z · Cited by 310 · see citing works

Peptides are Building Blocks of Heat-Induced Fibrillar Protein Aggregates of β-Lactoglobulin Formed at pH 2

Akkermans, C., Venema, P., van der Goot, A. J., Gruppen, H., Bakx, E. J., Boom, R. M., & van der Linden, E. (2008) · Biomacromolecules · doi:10.1021/bm7014224 · Cited by 304 · see citing works

Islet amyloid and type 2 diabetes: from molecular misfolding to islet pathophysiology

Jaikaran, E. T. A. S., & Clark, A. (2001) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(01)00078-3 · Cited by 294 · see citing works

Structure–function relationships in peptoids: Recent advances toward deciphering the structural requirements for biological function

Fowler, S. A., & Blackwell, H. E. (2009) · Organic & Biomolecular Chemistry · doi:10.1039/b817980h · Cited by 294 · see citing works

Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution

Shim, S., Gupta, R., Ling, Y. L., Strasfeld, D. B., Raleigh, D. P., & Zanni, M. T. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805957106 · Cited by 286 · see citing works

Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet

Buchanan, L. E., Dunkelberger, E. B., Kratochvil, H. T., Cheng, P.-N., Chiu, C., Cao, P., Raleigh, D. P., Pablo, J., Nowick, J. S., & Zanni, M. T. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314481110 · Cited by 275 · see citing works

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 · see citing works

Diabetes Due to a Progressive Defect in β-Cell Mass in Rats Transgenic for Human Islet Amyloid Polypeptide (HIP Rat)

Butler, A. E., Jang, J., Gurlo, T., Carty, M. D., Soeller, W. C., & Butler, P. C. (2004) · Diabetes · doi:10.2337/diabetes.53.6.1509 · Cited by 267 · see citing works

Chiral Sum Frequency Generation Spectroscopy for Characterizing Protein Secondary Structures at Interfaces

Fu, L., Liu, J., & Yan, E. C. Y. (2011) · Journal of the American Chemical Society · doi:10.1021/ja201575e · Cited by 261 · see citing works

Islet amyloid polypeptide‐induced membrane leakage involves uptake of lipids by forming amyloid fibers

Sparr, E., Engel, M. F. M., Sakharov, D. V., Sprong, M., Jacobs, J., KRUIJFF, B. D., Höppener, J. W. M., & Killian, J. A. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.09.075 · Cited by 257 · see citing works

Thioflavine T interaction with amyloid β-sheet structures

LeVine, H. (1995) · Amyloid · doi:10.3109/13506129509031881 · Cited by 254 · see citing works

Mechanisms of amyloid fibril self‐assembly and inhibition

Gazit, E. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.05022.x · Cited by 245 · see citing works

Amylin Agonists: A Novel Approach in the Treatment of Diabetes

Schmitz, O., Brock, B., & Rungby, J. (2004) · Diabetes · doi:10.2337/diabetes.53.suppl_3.s233 · Cited by 237 · see citing works

Identification of a novel human islet amyloid polypeptide β-sheet domain and factors influencing fibrillogenesis

Jaikaran, E. T. A. S., Higham, C. E., Serpell, L. C., Zurdo, J., Gross, M., Clark, A., & Fraser, P. E. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4593 · Cited by 236 · see citing works

Recent Insights in Islet Amyloid Polypeptide‐Induced Membrane Disruption and Its Role in β‐Cell Death in Type 2 Diabetes Mellitus

Khemtémourian, L., Killian, J. A., Höppener, J. W. M., & Engel, M. F. M. (2008) · Journal of Diabetes Research · doi:10.1155/2008/421287 · Cited by 236 · see citing works

Amyloid Fiber Formation and Membrane Disruption are Separate Processes Localized in Two Distinct Regions of IAPP, the Type-2-Diabetes-Related Peptide

Brender, J., Lee, E. L., Cavitt, M. A., Gafni, A., Steel, D. G., & Ramamoorthy, A. (2008) · Journal of the American Chemical Society · doi:10.1021/ja710484d · Cited by 229 · see citing works

Inhibition of Islet Amyloid Polypeptide Fibril Formation: A Potential Role for Heteroaromatic Interactions

Porat, Y., Mazor, Y., Efrat, S., & Gazit, E. (2004) · Biochemistry · doi:10.1021/bi048582a · Cited by 225 · see citing works

The Interplay of Catalysis and Toxicity by Amyloid Intermediates on Lipid Bilayers: Insights from Type II Diabetes

Hebda, J. A., & Miranker, A. D. (2009) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.050708.133622 · Cited by 223 · see citing works

Advanced Luminescent Materials Based on Organoboron Polymers

Tanaka, K., & Chujo, Y. (2012) · Macromolecular Rapid Communications · doi:10.1002/marc.201200239 · Cited by 222 · see citing works

Human Islet Amyloid Polypeptide Monomers Form Ordered β-hairpins: A Possible Direct Amyloidogenic Precursor

Dupuis, N., Wu, C. F., Shea, J., & Bowers, M. T. (2009) · Journal of the American Chemical Society · doi:10.1021/ja903814q · Cited by 215 · see citing works

Oxidative stress is induced by islet amyloid formation and time-dependently mediates amyloid-induced beta cell apoptosis

Zraika, S., Hull, R. L., Udayasankar, J., Aston‐Mourney, K., Subramanian, S. L., Kisilevsky, R., Szarek, W. A., & Kahn, S. E. (2009) · Diabetologia · doi:10.1007/s00125-008-1255-x · Cited by 215 · see citing works

Direct detection of transient α‐helical states in islet amyloid polypeptide

Williamson, J. A., & Miranker, A. D. (2006) · Protein Science · doi:10.1110/ps.062486907 · Cited by 215 · see citing works

Amyloid β and Amylin Fibrils Induce Increases in Proinflammatory Cytokine and Chemokine Production by THP‐1 Cells and Murine Microglia

Yates, S. L., Burgess, L. H., Kocsis‐Angle, J., Antal, J. M., Dority, M. D., Embury, P. B., Piotrkowski, A. M., & Brunden, K. R. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0741017.x · Cited by 202 · see citing works

Mechanisms of islet amyloidosis toxicity in type 2 diabetes

Abedini, A., & Schmidt, A. M. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.017 · Cited by 201 · see citing works

Islet amyloid polypeptide and type 2 diabetes.

Marzban, L., Park, K., & Verchere, C. (2003) · Experimental Gerontology · doi:10.1016/s0531-5565(03)00004-4 · Cited by 191 · see citing works

Proteostasis of Islet Amyloid Polypeptide: A Molecular Perspective of Risk Factors and Protective Strategies for Type II Diabetes

Milardi, D., Gazit, E., Radford, S. E., Xu, Y., Gallardo, R. U., Caflisch, A., Westermark, G. T., Westermark, P., Rosa, C. L., & Ramamoorthy, A. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00981 · Cited by 199 · see citing works

Animal Models of Type 2 Diabetes: Clinical Presentation and Pathophysiological Relevance to the Human Condition

Cefalu, W. T. (2006) · ILAR Journal · doi:10.1093/ilar.47.3.186 · Cited by 195 · see citing works

Structural Insights into the Polymorphism of Amyloid-Like Fibrils Formed by Region 20−29 of Amylin Revealed by Solid-State NMR and X-ray Fiber Diffraction

Madine, J., Jack, E. R., Stockley, P. G., Radford, S. E., Serpell, L. C., & Middleton, D. A. (2008) · Journal of the American Chemical Society · doi:10.1021/ja802483d · Cited by 195 · see citing works

Insulin signaling, glucose metabolism and mitochondria: Major players in Alzheimer's disease and diabetes interrelation

Correia, S. C., Santos, R. X., Carvalho, C., Cardoso, S., Candeias, E., Santos, M. S., Oliveira, C. R., & Moreira, P. I. (2012) · Brain Research · doi:10.1016/j.brainres.2011.12.063 · Cited by 195 · see citing works

Short peptide based self-assembled nanostructures: implications in drug delivery and tissue engineering

Panda, J. J., & Chauhan, V. S. (2014) · Polymer Chemistry · doi:10.1039/c4py00173g · Cited by 195 · see citing works

The Parallel Superpleated Beta-structure as a Model for Amyloid Fibrils of Human Amylin

Kajava, A. V., Aebi, U., & Steven, A. C. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.02.029 · Cited by 191 · see citing works

Ion Mobility Spectrometry–Mass Spectrometry Defines the Oligomeric Intermediates in Amylin Amyloid Formation and the Mode of Action of Inhibitors

Young, L. M., Cao, P., Raleigh, D. P., Ashcroft, A. E., & Radford, S. E. (2013) · Journal of the American Chemical Society · doi:10.1021/ja406831n · Cited by 190 · see citing works

Identification and Characterization of a Novel Molecular-recognition and Self-assembly Domain within the Islet Amyloid Polypeptide

Mazor, Y., Gilead, S., Benhar, I., & Gazit, E. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00887-2 · Cited by 186 · see citing works

Helix Stabilization Precedes Aqueous and Bilayer-Catalyzed Fiber Formation in Islet Amyloid Polypeptide

Williamson, J. A., Loria, J. P., & Miranker, A. D. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.07.077 · Cited by 186 · see citing works

Islet amyloid: a complication of islet dysfunction or an aetiological factor in Type 2 diabetes?

Clark, A., & Nilsson, M. R. (2004) · Diabetologia · doi:10.1007/s00125-003-1304-4 · Cited by 189 · see citing works

Cryo-EM structure of islet amyloid polypeptide fibrils reveals similarities with amyloid-β fibrils

Röder, C., Kupreichyk, T., Gremer, L., Schäfer, L. U., Pothula, K. R., Ravelli, R. B. G., Willbold, D., Hoyer, W., & Schröder, G. F. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0442-4 · Cited by 180 · see citing works

Structure of α-Helical Membrane-bound Human Islet Amyloid Polypeptide and Its Implications for Membrane-mediated Misfolding

Apostolidou, M., Jayasinghe, S. A., & Langen, R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801383200 · Cited by 184 · see citing works

Toxic Human Islet Amyloid Polypeptide (h-IAPP) Oligomers Are Intracellular, and Vaccination to Induce Anti-Toxic Oligomer Antibodies Does Not Prevent h-IAPP–Induced β-Cell Apoptosis in h-IAPP Transgenic Mice

Lin, C., Gurlo, T., Kayed, R., Butler, A. E., Haataja, L., Glabe, C. G., & Butler, P. C. (2007) · Diabetes · doi:10.2337/db06-1579 · Cited by 182 · see citing works

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 179 · see citing works

In Situ Misfolding of Human Islet Amyloid Polypeptide at Interfaces Probed by Vibrational Sum Frequency Generation

Fu, L., Ma, G., & Yan, E. C. Y. (2010) · Journal of the American Chemical Society · doi:10.1021/ja909546b · Cited by 181 · see citing works

Toxic oligomers and islet beta cell death: guilty by association or convicted by circumstantial evidence?

Zraika, S., Hull, R. L., Verchere, C. B., Clark, A., Potter, K. J., Fraser, P. E., Raleigh, D. P., & Kahn, S. E. (2010) · Diabetologia · doi:10.1007/s00125-010-1671-6 · Cited by 181 · see citing works

Islet amyloid: From fundamental biophysics to mechanisms of cytotoxicity

Cao, P., Marek, P., Noor, H., Patsalo, V., Tu, L., Wang, H., Abedini, A., & Raleigh, D. P. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.046 · Cited by 179 · see citing works

Human IAPP–induced pancreatic β cell toxicity and its regulation by autophagy

Shigihara, N., Fukunaka, A., Hara, A., Komiya, K., Honda, A., Uchida, T., Abe, H., Toyofuku, Y., Tamaki, M., Ogihara, T., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci69866 · Cited by 177 · see citing works

Membrane interaction of islet amyloid polypeptide.

Jayasinghe, S. A., & Langen, R. (2007) · Biochimica et Biophysica Acta · doi:10.1016/j.bbamem.2007.01.022 · Cited by 170 · see citing works

Structure-based design and study of non-amyloidogenic, double N-methylated IAPP amyloid core sequences as inhibitors of IAPP amyloid formation and cytotoxicity

Kapurniotu, A., Schmauder, A., & Tenidis, K. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5244 · Cited by 173 · see citing works

Islet Amyloid Polypeptide Inserts into Phospholipid Monolayers as Monomer

Engel, M. F. M., Yigittop, H., Elgersma, R. C., Rijkers, D. T. S., Liskamp, R. M. J., KRUIJFF, B. D., Höppener, J. W. M., & Killian, J. A. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.12.020 · Cited by 174 · see citing works

Structures of Rat and Human Islet Amyloid Polypeptide IAPP1−19 in Micelles by NMR Spectroscopy

Nanga, R. P. R., Brender, J., Xu, J., Veglia, G., & Ramamoorthy, A. (2008) · Biochemistry · doi:10.1021/bi8014357 · Cited by 172 · see citing works

The structure and mechanism of formation of human calcitonin fibrils.

Arvinte, T., Cudd, A., & Drake, A. F. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53268-3 · Cited by 172 · see citing works

Islet amyloid deposition limits the viability of human islet grafts but not porcine islet grafts

Potter, K. J., Abedini, A., Marek, P., Klimek-Abercrombie, A. M., Butterworth, S. A., Driscoll, M., Baker, R. L., Nilsson, M. R., Warnock, G. L., Oberholzer, J., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909024107 · Cited by 171 · see citing works

Degradation of Amylin by Insulin-degrading Enzyme

Bennett, R. G., Duckworth, W. C., & Hamel, F. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006170200 · Cited by 170 · see citing works

Cu and Zn coordination to amyloid peptides: From fascinating chemistry to debated pathological relevance

Atrián‐Blasco, E., Gonzalez, P., Santoro, A., Aliès, B., Faller, P., & Hureau, C. (2018) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2018.04.007 · Cited by 168 · see citing works

Missense Mutation of Amylin Gene (S20G) in Japanese NIDDM Patients

Sakagashira, S., Sanke, T., Hanabusa, T., Shimomura, H., Ohagi, S., Kumagaye, K. Y., Nakajima, K., & Nanjo, K. (1996) · Diabetes · doi:10.2337/diab.45.9.1279 · Cited by 167 · see citing works

Proinsulin maturation, misfolding, and proteotoxicity

Liu, M. R., Hodish, I., Rhodes, C. J., & Arvan, P. R. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702697104 · Cited by 161 · see citing works

Atomic Force Microscopy Reveals Defects Within Mica Supported Lipid Bilayers Induced by the Amyloidogenic Human Amylin Peptide

Green, J. D., Kreplak, L., Goldsbury, C. S., Li‐Blatter, X., Stolz, M., Cooper, G. J. S., Seelig, A., Kistler, J., & Aebi, U. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.07.052 · Cited by 161 · see citing works

Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics

Abedini, A., Plesner, A., Cao, P., Ridgway, Z. M., Zhang, J., Tu, L., Middleton, C. T., Chao, B., Sartori, D. J., Meng, F., et al. (2016) · eLife · doi:10.7554/elife.12977 · Cited by 160 · see citing works

Extensive islet amyloid formation is induced by development of Type II diabetes mellitus and contributes to its progression: pathogenesis of diabetes in a mouse model

Höppener, J. W. M., Oosterwijk, C., Nieuwenhuis, M. G., Posthuma, G., Thijssen, J. H. H., Vroom, T. M., Ahrén, B., & Lips, C. J. M. (1999) · Diabetologia · doi:10.1007/s001250051175 · Cited by 153 · see citing works

Amyloidogenic peptide oligomer accumulation in autophagy-deficient β cells induces diabetes

Kim, J., Cheon, H., Jeong, Y. T., Quan, W., Kim, K. H., Cho, J. M., Lim, Y.-M., Oh, S. H., Jin, S., Kim, J. H., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci69625 · Cited by 157 · see citing works

Amyloidogenesis: historical and modern observations point to heparan sulfate proteoglycans as a major culprit

Ancsin, J. B. (2003) · Amyloid · doi:10.3109/13506120309041728 · Cited by 156 · see citing works

Identifying Structural Features of Fibrillar Islet Amyloid Polypeptide Using Site-directed Spin Labeling

Jayasinghe, S. A., & Langen, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406853200 · Cited by 153 · see citing works

β-Amyloid-induced changes in cultured astrocytes parallel reactive astrocytosis associated with senile plaques in Alzheimer's disease

Pike, C. J., Cummings, B. J., Monzavi, R., & Cotman, C. W. (1994) · Neuroscience · doi:10.1016/0306-4522(94)90547-9 · Cited by 153 · see citing works

Neuroinflammation and neurologic deficits in diabetes linked to brain accumulation of amylin

Srodulski, S. J., Sharma, S., Bachstetter, A. D., Brelsfoard, J., Pascual, C., Xie, X., Saatman, K. E., Eldik, L. J. V., & Despa, F. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-30 · Cited by 152 · see citing works

Islet Amyloid Polypeptide (IAPP) Transgenic Rodents as Models for Type 2 Diabetes

Matveyenko, A. V., & Butler, P. C. (2006) · ILAR Journal · doi:10.1093/ilar.47.3.225 · Cited by 150 · see citing works

Inhibition of Amyloid Fibril Formation by Peptide Analogues Modified with α‐Aminoisobutyric Acid

Gilead, S., & Gazit, E. (2004) · Angewandte Chemie International Edition · doi:10.1002/anie.200353565 · Cited by 147 · see citing works

Impairment of the Ubiquitin-Proteasome Pathway Is a Downstream Endoplasmic Reticulum Stress Response Induced by Extracellular Human Islet Amyloid Polypeptide and Contributes to Pancreatic β-Cell Apoptosis

Casas, S., Gomis, R., Gribble, F. M., Altirriba, J., Knuutila, S., & Novials, A. (2007) · Diabetes · doi:10.2337/db07-0178 · Cited by 148 · see citing works

Three-Dimensional Structure and Orientation of Rat Islet Amyloid Polypeptide Protein in a Membrane Environment by Solution NMR Spectroscopy

Nanga, R. P. R., Brender, J., Xu, J., Hartman, K. L., Vivekanandan, S., & Ramamoorthy, A. (2009) · Journal of the American Chemical Society · doi:10.1021/ja9010095 · Cited by 147 · see citing works

Structural Characterisation of Islet Amyloid Polypeptide Fibrils

Makin, O. S., & Serpell, L. C. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.11.048 · Cited by 147 · see citing works

Acceleration of amyloid protein A amyloidosis by amyloid-like synthetic fibrils

Johan, K., Westermark, G. T., Engström, U., Gustavsson, Å., Hultman, P. A., & Westermark, P. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2558 · Cited by 147 · see citing works

Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin

Nilsson, M. R., & Raleigh, D. P. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3286 · Cited by 146 · see citing works

Role of islet amyloid in type 2 diabetes mellitus

Höppener, J. W. M., & Lips, C. J. M. (2006) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.12.009 · Cited by 143 · see citing works

Design of Peptide-based Inhibitors of Human Islet Amyloid Polypeptide Fibrillogenesis

Scrocchi, L. A., Chen, Y., Waschuk, S., Wang, F., Cheung, S., Darabie, A. A., McLaurin, J., & Fraser, P. E. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00164-x · Cited by 143 · see citing works

Inhibition of IAPP and IAPP(20−29) Fibrillation by Polymeric Nanoparticles

Cabaleiro-Lago, C., Lynch, I., Dawson, K. A., & Linse, S. S. (2009) · Langmuir · doi:10.1021/la902980d · Cited by 142 · see citing works

Structure of Cat Islet Amyloid Polypeptide and Identification of Amino Acid Residues of Potential Significance for Islet Amyloid Formation

Betsholtz, C., Christmanson, L., Engström, U., Rorsman, F., Jordan, K., O’Brien, T. D., Murtaugh, M. P., Johnson, K. H., & Westermark, P. (1990) · Diabetes · doi:10.2337/diacare.39.1.118 · Cited by 95 · see citing works

Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species

Betsholtz, C., Christmanson, L., Engström, U., Rorsman, F., Svensson, V., Johnson, K. H., & Westermark, P. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)81467-x · Cited by 176 · see citing works

Wildlife sequences of islet amyloid polypeptide (IAPP) identify critical species variants for fibrillization

Fortin, J. S., & Benoit‐Biancamano, M. (2015) · Amyloid · doi:10.3109/13506129.2015.1070824 · Cited by 20 · see citing works

Destabilization of Human IAPP Amyloid Fibrils by Proline Mutations Outside of the Putative Amyloidogenic Domain: Is There a Critical Amyloidogenic Domain in Human IAPP?

Abedini, A., & Raleigh, D. P. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.10.052 · Cited by 106 · see citing works

Islet Amyloid Polypeptide: Synthetic Peptides for Study of the Pathogenesis of Islet Amyloid

Westermark, P., Johnson, K. H., Engström, U., Westermark, G. T., Dominguez, H. L., Christmanson, L., & Betsholtz, C. (1991) · Springer eBooks · doi:10.1007/978-94-011-3284-8_112 · Cited by 4 · see citing works