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Amyloid-like peptide nanofiber templated titania nanostructures as dye sensitized solar cell anodic materials

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Drosophila Melanogaster as a Model System for Studies of Islet Amyloid Polypeptide Aggregation

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Binding of islet amyloid polypeptide to supported lipid bilayers and amyloid aggregation at the membranes.

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Physical and toxicological profiles of human IAPP amyloids and plaques

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Molecular and cytotoxic properties of hIAPP17–29 and rIAPP17–29 fragments: A comparative study with the respective full-length parent polypeptides

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Analysis of the Role of the Conserved Disulfide in Amyloid Formation by Human Islet Amyloid Polypeptide in Homogeneous and Heterogeneous Environments

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Silybins inhibit human IAPP amyloid growth and toxicity through stereospecific interactions

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Identification of an amyloid fibril forming peptide comprising residues 46–59 of apolipoprotein A‐I

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

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Islet amyloid polypeptide is expressed in the pancreatic islet parenchyma of the teleostean fish, Myoxocephalus (cottus) scorpius.

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Potential of ATP toward Prevention of hIAPP Oligomerization and Destabilization of hIAPP Protofibrils: An In Silico Perspective

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Molecular Insights into Myocilin and Its Glaucoma-Causing Misfolded Olfactomedin Domain Variants

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Is aggregated IAPP a cause of beta-cell failure in transplanted human pancreatic islets?

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The human serum protein C4b-binding protein inhibits pancreatic IAPP-induced inflammasome activation

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Diabetes Drug Discovery: hIAPP1–37 Polymorphic Amyloid Structures as Novel Therapeutic Targets

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Copper(ii) complexes of rat amylin fragments

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Analysis of Baboon IAPP Provides Insight into Amyloidogenicity and Cytotoxicity of Human IAPP

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Full length amylin oligomer aggregation: insights from molecular dynamics simulations and implications for design of aggregation inhibitors

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The Physiology of Calcitonin Gene—Related Peptide in the Islet Compared with That of Islet Amyloid Polypeptide (Amylin)

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Islet Amyloid Polypeptide Triggers Limited Complement Activation and Binds Complement Inhibitor C4b-binding Protein, Which Enhances Fibril Formation

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Monoconjugation of Human Amylin with Methylpolyethyleneglycol

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Bifunctional PEGylated Exenatide-Amylinomimetic Hybrids to Treat Metabolic Disorders: An Example of Long-Acting Dual Hormonal Therapeutics

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Amyloid in the pancreatic islets of the cougar (Felis concolor) is derived from islet amyloid polypeptide (IAPP)

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Unzipping the mysteries of amyloid fiber formation

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Amyloidogenicity of naturally occurring full‐length animal IAPP variants

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The Impact of Halogenated Phenylalanine Derivatives on NFGAIL Amyloid Formation

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High prevalence of pancreatic islet amyloid in patients with end‐stage renal failure on dialysis treatment

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The Importance of Intra-Islet Communication in the Function and Plasticity of the Islets of Langerhans during Health and Diabetes

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Exploring critical determinants of protein amyloidogenesis: a review

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Structural studies and cytotoxicity assays of “aggregation‐prone” IAPP8–16 and its non‐amyloidogenic variants suggest its important role in fibrillogenesis and cytotoxicity of human amylin

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Dynamical Stability and Assembly Cooperativity of β-Sheet Amyloid Oligomers – Effect of Polarization

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Cross-Sequence Interactions between Human and Rat Islet Amyloid Polypeptides

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New Insight in Copper‐Ion Binding to Human Islet Amyloid: The Contribution of Metal‐Complex Speciation To Reveal the Polypeptide Toxicity

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Extensive amyloid formation in transplanted microencapsulated mouse and human islets

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A Novel Pentapeptide Inhibitor Reduces Amyloid Deposit Formation by Direct Interaction with hIAPP

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Study on the inter- and intra-peptide salt-bridge mechanism of Aβ23–28 oligomer interaction with small molecules: QM/MM method

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Matrix Metalloproteinase-9 Protects Islets from Amyloid-induced Toxicity

Meier, D. T., Tu, L., Zraika, S., Hogan, M. F., Templin, A. T., Hull, R. L., Raleigh, D. P., & Kahn, S. E. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.676692 · Cited by 19

Inhibitory mechanism of pancreatic amyloid fibril formation: formation of the complex between tea catechins and the fragment of residues 22-27.

Kamihira-Ishijima, M., Nakazawa, H., Kira, A., Naito, A., & Nakayama, T. (2012) · Biochemistry · doi:10.1021/bi3012274 · Cited by 20

A Rationally Designed Hsp70 Variant Rescues the Aggregation-Associated Toxicity of Human IAPP in Cultured Pancreatic Islet β-Cells

Bongiovanni, M. N., Aprile, F. A., Sormanni, P., & Vendruscolo, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051443 · Cited by 19

Physico-chemical properties of co-formulated fast-acting insulin with pramlintide

da Silva, D. C., & Lima, L. M. T. R. (2018) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2018.06.039 · Cited by 19

Are fibrilgrowth and membrane damage linked processes? An experimental and computational study of IAPP 12–18 and IAPP 21–27 peptides

Sciacca, M. F. M., Pappalardo, M., Attanasio, F., Milardi, D., Rosa, C. L., & Grasso, D. (2009) · New Journal of Chemistry · doi:10.1039/b9nj00253g · Cited by 19

Human Amylin Stimulates Inflammatory Cytokine Secretion from Human Glioma Cells

Gitter, B. D., Cox, L. M., Carlson, C. D., & May, P. C. (2000) · NeuroImmunoModulation · doi:10.1159/000026432 · Cited by 19

The Rationale for Insulin Therapy in Alzheimer’s Disease

Ribarič, S. (2016) · Molecules · doi:10.3390/molecules21060689 · Cited by 20

Small‐Molecule Inhibitors of Islet Amyloid Polypeptide Fibril Formation

Mishra, R., Bulic, B., Sellin, D., Jha, S., Waldmann, H., & Winter, R. (2008) · Angewandte Chemie · doi:10.1002/ange.200705372 · Cited by 19

Role of Cholesterol and Phospholipids in Amylin Misfolding, Aggregation and Etiology of Islet Amyloidosis

Singh, S., Trikha, S., Bhowmick, D. C., Sarkar, A. A., & Jeremic, A. M. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-17344-3_4 · Cited by 18

Fluorescent Dopamine–Tryptophan Nanocomposites as Dual-Imaging and Antiaggregation Agents: New Generation of Amyloid Theranostics with Trimeric Effects

Sharma, M., Tiwari, V., Shukla, S., & Panda, J. J. (2020) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.0c13223 · Cited by 18

The Physiological and Pathological Implications of the Formation of Hydrogels, with a Specific Focus on Amyloid Polypeptides

Jean, L., Foley, A. C., & Vaux, D. J. (2017) · Biomolecules · doi:10.3390/biom7040070 · Cited by 18

Interaction of Proteins Involved in Neuronal Proteinopathies

Kulichikhin, K. Y., Malikova, O. A., Zobnina, A. E., Zalutskaya, N. M., & Rubel, A. A. (2023) · Life · doi:10.3390/life13101954 · Cited by 17

Fibrillar dimer formation of islet amyloid polypeptides

Chiu, C. C., & de Pablo, J. J. (2015) · AIP Advances · doi:10.1063/1.4921073 · Cited by 17

Modulation of fibrillation of hIAPP core fragments by chemical modification of the peptide backbone

Andreasen, M., Nielsen, S. B., Mittag, T., Bjerring, M., Nielsen, J. T., Zhang, S., Nielsen, E. N., Jeppesen, M. D., Christiansen, G., Besenbacher, F., et al. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.10.014 · Cited by 18

Determination of Optimal Sample Size for Quantification of β-Cell Area, Amyloid Area and β-Cell Apoptosis in Isolated Islets

Meier, D. T., Entrup, L., Templin, A. T., Hogan, M. F., Samarasekera, T., Zraika, S., Boyko, E. J., & Kahn, S. E. (2015) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155415585995 · Cited by 17

Analysis of Amylin Consensus Sequences Suggests that Human Amylin is Not Optimized to Minimize Amyloid Formation and Provides Clues to Factors that Modulate Amyloidogenicity

Noh, D., Bower, R. L., Hay, D. L., Zhyvoloup, A., & Raleigh, D. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.9b01050 · Cited by 16

The critical role of the central hydrophobic core (residues 71–77) of amyloid-forming αA66-80 peptide in α-crystallin aggregation: a systematic proline replacement study

Kannan, R., Raju, M., & Sharma, K. K. (2014) · Amyloid · doi:10.3109/13506129.2014.888994 · Cited by 17

Monitoring oligomer formation from self-aggregating amylin peptides using ESI-IMS-MS

Young, L. M., Ndlovu, H., Knapman, T. W., Harris, S. A., Radford, S. E., & Ashcroft, A. E. (2013) · International Journal for Ion Mobility Spectrometry · doi:10.1007/s12127-012-0115-z · Cited by 18

Pramlintide: Clinical Strategies for Success

Alrefai, H. A., Latif, K. A., Hieronymus, L. B., Weakley, C. R., & Moss, R. J. (2010) · Diabetes Spectrum · doi:10.2337/diaspect.23.2.124 · Cited by 16

Fibril elongation by human islet amyloid polypeptide is the main event linking aggregation to membrane damage

Elenbaas, B. O. W., Kremsreiter, S. M., Khemtémourian, L., Killian, J. A., & Sinnige, T. (2023) · BBA Advances · doi:10.1016/j.bbadva.2023.100083 · Cited by 17

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

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