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

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

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

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

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 510

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

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 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

S20G Mutant Amylin Exhibits Increased in Vitro Amyloidogenicity and Increased Intracellular Cytotoxicity Compared to Wild-Type Amylin

Sakagashira, S., Hiddinga, H. J., Tateishi, K., Sanke, T., Hanabusa, T., Nanjo, K., & Eberhardt, N. L. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64848-1 · Cited by 142

β-Cell Deficit Due to Increased Apoptosis in the Human Islet Amyloid Polypeptide Transgenic (HIP) Rat Recapitulates the Metabolic Defects Present in Type 2 Diabetes

Matveyenko, A. V., & Butler, P. C. (2006) · Diabetes · doi:10.2337/db05-1672 · Cited by 144

Peptide‐Based Inhibitors of Amyloid Assembly

Sciarretta, K. L., Gordon, D. J., & Meredith, S. C. (2006) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(06)13015-3 · Cited by 141

Membrane fragmentation by an amyloidogenic fragment of human Islet Amyloid Polypeptide detected by solid-state NMR spectroscopy of membrane nanotubes

Brender, J., Dürr, U., Heyl, D., Budarapu, M. B., & Ramamoorthy, A. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.07.001 · Cited by 141

Induction of Negative Curvature as a Mechanism of Cell Toxicity by Amyloidogenic Peptides: The Case of Islet Amyloid Polypeptide

Smith, P. E. S., Brender, J., & Ramamoorthy, A. (2009) · Journal of the American Chemical Society · doi:10.1021/ja809002a · Cited by 140

Gut hormones: Implications for the treatment of obesity

Neary, M. T., & Batterham, R. L. (2009) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2009.06.005 · Cited by 140

Cryo-EM structure and inhibitor design of human IAPP (amylin) fibrils

Cao, Q., Boyer, D. R., Sawaya, M. R., Ge, P., & Eisenberg, D. S. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0435-3 · Cited by 140

Hyperamylinemia Contributes to Cardiac Dysfunction in Obesity and Diabetes

Despa, S. I., Margulies, K. B., Chen, L., Knowlton, A. A., Havel, P. J., Taegtmeyer, H., Bers, D. M., & Despa, F. (2012) · Circulation Research · doi:10.1161/circresaha.111.258285 · Cited by 140

The β-cell assassin: IAPP cytotoxicity

Raleigh, D. P., Zhang, X., Hastoy, B., & Clark, A. (2017) · Journal of Molecular Endocrinology · doi:10.1530/jme-17-0105 · Cited by 138

Pancreatic beta-cell loss and preservation in type 2 diabetes

Buchanan, T. A. (2003) · Clinical Therapeutics · doi:10.1016/s0149-2918(03)80241-2 · Cited by 132

Membrane permeabilization by Islet Amyloid Polypeptide

Engel, M. F. M. (2009) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2009.03.008 · Cited by 129

Calcium elevation in mouse pancreatic beta cells evoked by extracellular human islet amyloid polypeptide involves activation of the mechanosensitive ion channel TRPV4

Casas, S., Novials, A., Reimann, F. M., Gomis, R., & Gribble, F. M. (2008) · Diabetologia · doi:10.1007/s00125-008-1111-z · Cited by 128

Full-length Rat Amylin Forms Fibrils Following Substitution of Single Residues from Human Amylin

Green, J., Goldsbury, C. S., Mini, T., Sunderji, S., Frey, P., Kistler, J., Cooper, G. J. S., & Aebi, U. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01377-3 · Cited by 127

The Effect of Glycosaminoglycans (GAGs) on Amyloid Aggregation and Toxicity

Iannuzzi, C., Irace, G., & Sirangelo, I. (2015) · Molecules · doi:10.3390/molecules20022510 · Cited by 124

Low levels of asparagine deamidation can have a dramatic effect on aggregation of amyloidogenic peptides: Implications for the study of amyloid formation

Nilsson, M. R., Driscoll, M., & Raleigh, D. P. (2002) · Protein Science · doi:10.1110/ps.48702 · Cited by 124

Control of peptide conformation by the Thorpe-Ingold effect (C?-tetrasubstitution)

Toniolo, C., Crisma, M., Formaggio, F., & Peggion, C. (2001) · Biopolymers · doi:10.1002/1097-0282(2001)60:6 · Cited by 676

Neurotoxicity of Human Amylin in Rat Primary Hippocampal Cultures: Similarity to Alzheimer's Disease Amyloid‐β Neurotoxicity

May, P. C., Boggs, L. N., & Fuson, K. S. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb07480.x · Cited by 124

Molecular understanding of a potential functional link between antimicrobial and amyloid peptides

Zhang, M., Zhao, J., & Zheng, J. (2014) · Soft Matter · doi:10.1039/c4sm00907j · Cited by 123

Preparation of synthetic human islet amyloid polypeptide (IAPP) in a stable conformation to enable study of conversion to amyloid‐like fibrils

Higham, C. E., Jaikaran, E. T. A. S., Fraser, P. E., Gross, M., & Clark, A. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01287-4 · Cited by 123

Type 2 diabetes mellitus as a conformational disease.

Hayden, M. R., Tyagi, S. C., Kerklo, M. M., & Nicolls, M. R. (2005) · PubMed · Cited by 120

Short Peptide Amyloid Organization: Stabilities and Conformations of the Islet Amyloid Peptide NFGAIL

Zanuy, D., Ma, B., & Nussinov, R. (2003) · Biophysical Journal · doi:10.1016/s0006-3495(03)74996-0 · Cited by 120

Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology

Cao, P., Abedini, A., & Raleigh, D. P. (2012) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2012.11.003 · Cited by 119

Islet amyloid polypeptide: identification of long-range contacts and local order on the fibrillogenesis pathway 1 1Edited by F. Cohen

Padrick, S. B., & Miranker, A. D. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4608 · Cited by 119

Human Islets Have Fewer Blood Vessels than Mouse Islets and the Density of Islet Vascular Structures Is Increased in Type 2 Diabetes

Briššová, M., Shostak, A., Fligner, C. L., Revetta, F. L., Washington, M. K., Powers, A. C., & Hull, R. L. (2015) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155415573324 · Cited by 120

Prevalence and Clinicopathological Characteristics of Islet Amyloid in Chinese Patients With Type 2 Diabetes

Zhao, H., Lai, F. M., Tong, P. C. Y., Zhong, D., Yang, D., Tomlinson, B., & Chan, J. C. N. (2003) · Diabetes · doi:10.2337/diabetes.52.11.2759 · Cited by 117

Islet Amyloid Polypeptide: A Review of Its Biology and Potential Roles in the Pathogenesis of Diabetes Mellitus

O’Brien, T. D., Butler, P. C., Westermark, P., & Johnson, K. H. (1993) · Veterinary Pathology · doi:10.1177/030098589303000401 · Cited by 117

Cations as Switches of Amyloid-Mediated Membrane Disruption Mechanisms: Calcium and IAPP

Sciacca, M. F. M., Milardi, D., Messina, G. M. L., Marletta, G., Brender, J., Ramamoorthy, A., & Rosa, C. L. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2012.11.3811 · Cited by 115

The Molecular Basis of Distinct Aggregation Pathways of Islet Amyloid Polypeptide*

Wei, L., Jiang, P., Xu, W., Li, H., Zhang, H., Yan, L., Chan-Park, M., Liu, X.-W., Tang, K., Mu, Y., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.166678 · Cited by 105

Amylin, Food Intake, and Obesity

Reda, T. K., Geliebter, A., & Pi‐Sunyer, F. X. (2002) · Obesity Research · doi:10.1038/oby.2002.147 · Cited by 118

Role of β-Cell Prohormone Convertase (PC)1/3 in Processing of Pro-Islet Amyloid Polypeptide

Marzban, L., Trigo‐Gonzalez, G., Zhu, X., Rhodes, C. J., Halban, P. A., Steiner, D. F., & Verchere, C. B. (2004) · Diabetes · doi:10.2337/diabetes.53.1.141 · Cited by 113

Amyloid Cross-Seeding: Mechanism, Implication, and Inhibition

Subedi, S., Sasidharan, S., Nag, N., Saudagar, P., & Tripathi, T. (2022) · Molecules · doi:10.3390/molecules27061776 · Cited by 115

Apolipoprotein A1-derived amyloid in human aortic atherosclerotic plaques.

Westermark, P., Mucchiano, G. I., Marthin, T., Johnson, K. H., & Sletten, K. (1995) · Europe PMC (PubMed Central) · Cited by 113

Inhibition of hIAPP Amyloid-Fibril Formation and Apoptotic Cell Death by a Designed hIAPP Amyloid- Core-Containing Hexapeptide

Tatarek‐Nossol, M., Yan, L., Schmauder, A., Tenidis, K., Westermark, G. T., & Kapurniotu, A. (2005) · Chemistry & Biology · doi:10.1016/j.chembiol.2005.05.010 · Cited by 114

Protein engineering as a strategy to avoid formation of amyloid fibrils

Villegas, S., Zurdo, J., Filimonov, V. V., Avilés, F. X., Dobson, C. M., & Serrano, L. (2000) · Protein Science · doi:10.1110/ps.9.9.1700 · Cited by 113

Small‐Molecule Inhibitors of Islet Amyloid Polypeptide Fibril Formation

Mishra, R., Bulic, B., Sellin, D., Jha, S., Waldmann, H., & Winter, R. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200705372 · Cited by 112

Coexistence of ribbon and helical fibrils originating from hIAPP 20–29 revealed by quantitative nanomechanical atomic force microscopy

Zhang, S., Andreasen, M., Nielsen, J. T., Liu, L., Nielsen, E. N., Song, J., Ji, G., Sun, F., Skrydstrup, T., Besenbacher, F., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1209955110 · Cited by 111

Fibrillogenic Amylin Evokes Islet β-Cell Apoptosis through Linked Activation of a Caspase Cascade and JNK1

Zhang, S., Liu, J., Dragunow, M., & Cooper, G. J. S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308244200 · Cited by 111

Tissue-Type Plasminogen Activator Is a Multiligand Cross-β Structure Receptor

Kranenburg, O., Bouma, B., Kroon-Batenburg, L. M. J., Reijerkerk, A., Wu, Y., Voest, E. E., & Gebbink, M. F. B. G. (2002) · Current Biology · doi:10.1016/s0960-9822(02)01224-1 · Cited by 112

Fibril structures of diabetes-related amylin variants reveal a basis for surface-templated assembly

Gallardo, R. U., Iadanza, M. G., Xu, Y., Heath, G. R., Foster, R., Radford, S. E., & Ranson, N. A. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0496-3 · Cited by 108

Increased Dietary Fat Promotes Islet Amyloid Formation and β-Cell Secretory Dysfunction in a Transgenic Mouse Model of Islet Amyloid

Hull, R. L., Andrikopoulos, S., Verchere, C. B., Vidal, J., Wang, F., Cnop, M., Prigeon, R. L., & Kahn, S. E. (2003) · Diabetes · doi:10.2337/diabetes.52.2.372 · Cited by 109

A structure‐based approach to predict predisposition to amyloidosis

Ahmed, A. B., Znassi, N., Château, M., & Kajava, A. V. (2014) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2014.06.007 · Cited by 109

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

Intra- and extracellular amyloid fibrils are formed in cultured pancreatic islets of transgenic mice expressing human islet amyloid polypeptide.

de Koning, E. J. P., Morris, E. R., Hofhuis, F. M., Posthuma, G., Höppener, J. W. M., Morris, J. F., Capel, P. J., Clark, A., & Verbeek, J. S. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8467 · Cited by 102

Amylin structure–function relationships and receptor pharmacology: implications for amylin mimetic drug development

Bower, R. L., & Hay, D. L. (2016) · British Journal of Pharmacology · doi:10.1111/bph.13496 · Cited by 104

Islet amyloid polypeptide ? a novel controversy in diabetes research

Westermark, P., Johnson, K. H., O’Brien, T. D., & Betsholtz, C. (1992) · Diabetologia · doi:10.1007/bf00401195 · Cited by 99

Impaired NH2-Terminal Processing of Human Proislet Amyloid Polypeptide by the Prohormone Convertase PC2 Leads to Amyloid Formation and Cell Death

Marzban, L., Rhodes, C. J., Steiner, D. F., Haataja, L., Halban, P. A., & Verchere, C. B. (2006) · Diabetes · doi:10.2337/db05-1566 · Cited by 101

An Account of Amyloid Oligomers: Facts and Figures Obtained from Experiments and Simulations

Nagel‐Steger, L., Owen, M. C., & Strodel, B. (2016) · ChemBioChem · doi:10.1002/cbic.201500623 · Cited by 103

Amyloid and polypeptide hormones: What is their interrelationship?

Westermark, P. (1994) · Amyloid · doi:10.3109/13506129409148624 · Cited by 98

Atomic structures of fibrillar segments of hIAPP suggest tightly mated β-sheets are important for cytotoxicity

Krotee, P., Rodríguez, J. A., Sawaya, M. R., Cascio, D., Reyes, F. E., Shi, D., Hattne, J., Nannenga, B. L., Oskarsson, M. E., Philipp, S., et al. (2017) · eLife · doi:10.7554/elife.19273 · Cited by 100

Islet amyloid with macrophage migration correlates with augmented β-cell deficits in type 2 diabetic patients

Kamata, K., Mizukami, H., Inaba, W., Tsuboi, K., Tateishi, Y., Yoshida, T., & Yagihashi, S. (2014) · Amyloid · doi:10.3109/13506129.2014.937857 · Cited by 100

IAPP in type II diabetes: Basic research on structure, molecular interactions, and disease mechanisms suggests potential intervention strategies

Asthana, S., Mallick, B., Alexandrescu, A. T., & Jha, S. (2018) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2018.02.020 · Cited by 96

Self-assembled one-dimensional soft nanostructures

Ataca, S. T., Acar, H., & Guler, M. O. (2010) · Soft Matter · doi:10.1039/c0sm00121j · Cited by 93

Amylin Uncovered: A Review on the Polypeptide Responsible for Type II Diabetes

Pillay, K., & Govender, P. (2013) · BioMed Research International · doi:10.1155/2013/826706 · Cited by 101

Advances in ion mobility spectrometry–mass spectrometry reveal key insights into amyloid assembly

Woods, L. A., Radford, S. E., & Ashcroft, A. E. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.10.002 · Cited by 97

Scalable molecular dynamics with NAMD on the IBM Blue Gene/L system

Kumar, S., Huang, C., Zheng, G., Bohm, E. J., Bhatele, A. S., Phillips, J. C., Yu, H., & Kalé, L. V. (2008) · IBM Journal of Research and Development · doi:10.1147/rd.521.0177 · Cited by 93

Long-Term Treatment With Rosiglitazone and Metformin Reduces the Extent of, but Does Not Prevent, Islet Amyloid Deposition in Mice Expressing the Gene for Human Islet Amyloid Polypeptide

Hull, R. L., Shen, Z.-P., Watts, M. R., Kodama, K., Carr, D. B., Utzschneider, K. M., Zraika, S., Wang, F., & Kahn, S. E. (2005) · Diabetes · doi:10.2337/diabetes.54.7.2235 · Cited by 93

AßT Amyloidogenesis: Unique, or Variation on a Systemic Theme

Kisilevsky, R., Fraser, P. E., & Benson, M. D. (1997) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409239709082674 · Cited by 92

The effect of curcumin on human islet amyloid polypeptide misfolding and toxicity

Daval, M., Bedrood, S., Gurlo, T., Huang, C., Costes, S., Butler, P. C., & Langen, R. (2010) · Amyloid · doi:10.3109/13506129.2010.530008 · Cited by 94

The Sequence Dependence of Fiber Organization. A Comparative Molecular Dynamics Study of the Islet Amyloid Polypeptide Segments 22–27 and 22–29

Zanuy, D., & Nussinov, R. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00491-1 · Cited by 91

Of rodents and men: Species-specific glucose regulation and type 2 diabetes research

Chandrasekera, P. C. (2014) · ALTEX · doi:10.14573/1309231 · Cited by 88

Self-organization of Short Peptide Fragments: From Amyloid Fibrils to Nanoscale Supramolecular Assemblies

Gilead, S., & Gazit, E. (2004) · Supramolecular chemistry · doi:10.1080/10610270412331328943 · Cited by 89

Apoptosis induced by islet amyloid polypeptide soluble oligomers is neutralized by diabetes-associated specific antibodies

Bram, Y., Frydman‐Marom, A., Yanai, I., Gilead, S., Shaltiel‐Karyo, R., Amdursky, N., & Gazit, E. (2014) · Scientific Reports · doi:10.1038/srep04267 · Cited by 89

Human islet amyloid polypeptide transgenic mice as a model of non‐insulin‐dependent diabetes mellitus (NIDDM)

Fox, N. W., Schrementi, J. P., Nishi, M., Ohagi, S., Chan, S. J., Heisserman, J. A., Westermark, G. T., Leckström, A., Westermark, P., & Steiner, D. F. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81444-5 · Cited by 86

Role and Cytotoxicity of Amylin and Protection of Pancreatic Islet β-Cells from Amylin Cytotoxicity

Kiriyama, Y., & Nochi, H. (2018) · Cells · doi:10.3390/cells7080095 · Cited by 88

Identification of minimal peptide sequences in the (8–20) domain of human islet amyloid polypeptide involved in fibrillogenesis

Scrocchi, L. A., Ha, K., Chen, Y., Wu, L., Wang, F., & Fraser, P. E. (2003) · Journal of Structural Biology · doi:10.1016/s1047-8477(02)00630-5 · Cited by 87

Identification of cis- and trans-Active Factors Regulating Human Islet Amyloid Polypeptide Gene Expression in Pancreatic β-Cells

Carty, M. D., Lillquist, J. S., Peshavaria, M., Stein, R. W., & Soeller, W. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.18.11986 · Cited by 87

Induction of IAPP amyloid deposition and associated diabetic abnormalities by a prion-like mechanism

Mukherjee, A., Morales‐Scheihing, D., Salvadores, N., Moreno‐González, I., González, C., Taylor-Presse, K., Méndez, N., Shahnawaz, M., Gaber, A. O., Sabek, O. M., et al. (2017) · The Journal of Experimental Medicine · doi:10.1084/jem.20161134 · Cited by 86

Role of Amylin in Type 1 and Type 2 Diabetes

Hieronymus, L. B., & Griffin, S. (2015) · The Science of Diabetes Self-Management and Care · doi:10.1177/0145721715607642 · Cited by 87

Stabilization and structural analysis of a membrane-associated hIAPP aggregation intermediate

Camargo, D. C. R., Korshavn, K. J., Jussupow, A., Raltchev, K., Goričanec, D., Fleisch, M., Sarkar, R., Xue, K., Aichler, M., Mettenleiter, G., et al. (2017) · eLife · doi:10.7554/elife.31226 · Cited by 86

Beta cell dysfunction in diabetes: the islet microenvironment as an unusual suspect

Almaça, J., Caicedo, A., & Landsman, L. (2020) · Diabetologia · doi:10.1007/s00125-020-05186-5 · Cited by 86

β cell aging and age-related diabetes

Zhu, M., Liu, X., Liu, W., Lu, Y., Cheng, J., & Chen, Y. (2021) · Aging · doi:10.18632/aging.202593 · Cited by 96

Resveratrol Inhibits the Formation of Multiple-Layered β-Sheet Oligomers of the Human Islet Amyloid Polypeptide Segment 22–27

Jiang, P., Li, W., Shea, J., & Mu, Y. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.02.010 · Cited by 85

Chronic overproduction of islet amyloid polypeptide/amylin in transgenic mice: lysosomal localization of human islet amyloid polypeptide and lack of marked hyperglycaemia or hyperinsulinaemia

Höppener, J. W. M., Verbeek, J. S., de Koning, E. J. P., Oosterwijk, C., van Hulst, K. L., Visser-Vernooy, H. J., Hofhuis, F. M., van Gaalen, S., Berends, M. J. H., Hackeng, W. H. L., et al. (1993) · Diabetologia · doi:10.1007/bf00400803 · Cited by 81

Multisite aggregation of p53 and implications for drug rescue

Wang, G., & Fersht, A. R. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1700308114 · Cited by 82

Amyloidogenic hexapeptide fragment of medin: homology to functional islet amyloid polypeptide fragments

Reches, M., & Gazit, E. (2004) · Amyloid · doi:10.1080/13506120412331272287 · Cited by 82

Concentration‐dependent transitions govern the subcellular localization of islet amyloid polypeptide

Magzoub, M. M., & Miranker, A. D. (2011) · The FASEB Journal · doi:10.1096/fj.11-194613 · Cited by 82

Amyloid β protein inhibits cellular MTT reduction not by suppression of mitochondrial succinate dehydrogenase but by acceleration of MTT formazan exocytosis in cultured rat cortical astrocytes

Abe, K., & Saitō, H. (1998) · Neuroscience Research · doi:10.1016/s0168-0102(98)00055-8 · Cited by 81

RAGE binds preamyloid IAPP intermediates and mediates pancreatic β cell proteotoxicity

Abedini, A., Cao, P., Plesner, A., Zhang, J., He, M., Derk, J., Patil, S. A., Rosario, R., Lonier, J., Song, F., et al. (2018) · Journal of Clinical Investigation · doi:10.1172/jci85210 · Cited by 83

The N‐terminal region of non‐Aβ component of Alzheimer's Disease amyloid is responsible for its tendency to assume β‐sheet and aggregate to form fibrils

El‐Agnaf, O. M. A., Bodles, A. M., Guthrie, D. J. S., Harriott, P., & Irvine, G. B. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2580157.x · Cited by 80

Peptide Sequence and Amyloid Formation

Zanuy, D., Porat, Y., Gazit, E., & Nussinov, R. (2004) · Structure · doi:10.1016/j.str.2004.02.002 · Cited by 81

Brain microvascular injury and white matter disease provoked by diabetes‐associated hyperamylinemia

Ly, H., Verma, N., Wu, F., Liu, M., Saatman, K. E., Nelson, P. T., Slevin, J. T., Goldstein, L. B., Biessels, G. J., & Despa, F. (2017) · Annals of Neurology · doi:10.1002/ana.24992 · Cited by 79

A Free Energy Barrier Caused by the Refolding of an Oligomeric Intermediate Controls the Lag Time of Amyloid Formation by hIAPP

Serrano, A. L., Lomont, J. P., Tu, L., Raleigh, D. P., & Zanni, M. T. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b08830 · Cited by 77

Role of amino acid hydrophobicity, aromaticity, and molecular volume on IAPP(20–29) amyloid self‐assembly

Doran, T. M., Kamens, A. J., Byrnes, N. K., & Nilsson, B. L. (2011) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24007 · Cited by 80

Islet amyloid polypeptide: Another key molecule in Alzheimer’s pathogenesis?

Zhang, Y., & Song, W. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2017.03.001 · Cited by 79

Proteins at Interfaces Probed by Chiral Vibrational Sum Frequency Generation Spectroscopy

Yan, E. C. Y., Wang, Z., & Fu, L. (2015) · The Journal of Physical Chemistry B · doi:10.1021/jp508926e · Cited by 76

Chiral Vibrational Structures of Proteins at Interfaces Probed by Sum Frequency Generation Spectroscopy

Fu, L., Wang, Z., & Yan, E. C. Y. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12129404 · Cited by 79

The Ability of Rodent Islet Amyloid Polypeptide To Inhibit Amyloid Formation by Human Islet Amyloid Polypeptide Has Important Implications for the Mechanism of Amyloid Formation and the Design of Inhibitors

Cao, P., Meng, F., Abedini, A., & Raleigh, D. P. (2009) · Biochemistry · doi:10.1021/bi901751b · Cited by 78

Luminescent Organoboron Conjugated Polymers

Nagai, A., & Chujo, Y. (2010) · Chemistry Letters · doi:10.1246/cl.2010.430 · Cited by 76

Defining the Molecular Basis of Amyloid Inhibitors: Human Islet Amyloid Polypeptide–Insulin Interactions

Susa, A. C., Wu, C. F., Bernstein, S. L., Dupuis, N., Wang, H., Raleigh, D. P., Shea, J., & Bowers, M. T. (2014) · Journal of the American Chemical Society · doi:10.1021/ja504031d · Cited by 76

B Cell Granule Peptides Affect Human Islet Amyloid Polypeptide (IAPP) Fibril Formationin Vitro

Janciauskiene, S. M., Eriksson, S., Carlemalm, E., & Åhrén, B. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7014 · Cited by 73

cJUN N-terminal kinase (JNK) activation mediates islet amyloid-induced beta cell apoptosis in cultured human islet amyloid polypeptide transgenic mouse islets

Subramanian, S. L., Hull, R. L., Zraika, S., Aston‐Mourney, K., Udayasankar, J., & Kahn, S. E. (2011) · Diabetologia · doi:10.1007/s00125-011-2338-7 · Cited by 75

Neuroendocrine hormone amylin in diabetes

Zhang, X., Pan, Y.-H., Huang, Y., & Zhao, H. (2016) · World Journal of Diabetes · doi:10.4239/wjd.v7.i9.189 · Cited by 75

A mechanistic approach for islet amyloid polypeptide aggregation to develop anti-amyloidogenic agents for type-2 diabetes

Ahmad, E., Ahmad, A., Singh, S. P., Arshad, M., Khan, A. H., & Khan, R. H. (2011) · Biochimie · doi:10.1016/j.biochi.2010.12.012 · Cited by 74

Molecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes Mellitus

Caillon, L., Hoffmann, A. R. F., Botz, A., & Khemtémourian, L. (2015) · Journal of Diabetes Research · doi:10.1155/2016/5639875 · Cited by 74

Diseases of protein conformation: what do in vitro experiments tell us about in vivo diseases?

Buxbaum, J. N. (2003) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.09.009 · Cited by 73

Islet Amyloid Development in a Mouse Strain Lacking Endogenous Islet Amyloid Polypeptide (IAPP) but Expressing Human IAPP

Westermark, G., Gebre-Medhin, S., Steiner, D., & Westermark, P. (2000) · Molecular Medicine · doi:10.1007/bf03402051 · Cited by 74

Pathogenesis of feline diabetes mellitus

O’Brien, T. D. (2002) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(02)00265-4 · Cited by 72

Amyloid formation results in recurrence of hyperglycaemia following transplantation of human IAPP transgenic mouse islets

Udayasankar, J., Kodama, K., Hull, R. L., Zraika, S., Aston‐Mourney, K., Subramanian, S. L., Tong, J., Faulenbach, M. V., Vidal, J., & Kahn, S. E. (2008) · Diabetologia · doi:10.1007/s00125-008-1185-7 · Cited by 71

The effect of environmental cues on the differentiation of myofibroblasts in peritoneal granulation tissue

(2000) · doi:10.1002/1096-9896(2000)9999:9999 · Cited by 70

Mechanisms Underlying the Antidiabetic Activities of Polyphenolic Compounds: A Review

Nie, T., & Cooper, G. J. S. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.798329 · Cited by 75

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 94

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 180

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

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

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