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Anti-diabetic drug pioglitazone reduces Islet amyloid aggregation overload in the Drosophila neuronal cells

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Decoding the Relationship between Alzheimer’s Disease and Type-2 Diabetes via the Protein Aggregation Prism

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Effect of Copper-Catalyzed Oxidation on the Aggregation of the Islet Amyloid Polypeptide

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Synergistic Effect of Mutations in the Amyloidogenic Core of Human Amylin (hAM) Affords a New Potent Inhibitor of hAM Fibrillation: Computational Design and Experimental Validation

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Molecular Mechanisms of Islet Amyloid Polypeptide Aggregation: Towards Chemical Strategies to Prevent Amyloid Formation and to Design Non-Aggregating Peptide Therapeutics

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Amyloid Fibril Formation of a Simple Decapeptide in a Micellar Environment

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Structure, Self-Association, and Aggregation Properties of a Long-Acting Amylin Receptor Agonist

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The Role of ER Stress and the Unfolded Protein Response in Obesity Associated Type 2 Diabetes

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Determining the Aggregation Prone Structure of hIAPP

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Effect of Terminal Capping on Aggregation of Peptide Fragments

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Imaging Agent Binding to Amyloid Protofibrils

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Probing Molecular Basis for Constructing Interface Bionanostructures

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Mechanism and Development of Peptide-Based Inhibitors to Human Islet Amyloid Polypeptide (hIAPP) Self-Assembly

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Pancreatic beta cells turnover: effects of endogenous hyperinsulinemia and amyloid deposits

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Role of insulin-degrading enzyme (IDE) in diabetes mellitus and insulin resistance

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Global dynamics for a model of amyloid fibril formation in pancreatic islet beta cells subjected to a therapy

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Amylin-mediated regulation of LRP1 by miR-103/107 induces cerebral microvascular dysfunction and impairs β-amyloid effluxPreprint

Velmurugan, G. V., Ly, H., Sharma, S., Verma, N., Despa, S. I., Nelson, P. T., Goldstein, L. B., & Despa, F. (2020) · doi:10.21203/rs.3.rs-52604/v1

EXPLORATORY STUDY OF CORPORATE SOCIAL RESPONSIBILITY: BLOGS AS A COMMUNICATION TOOL TO ENHANCE COMPANY- STAKEHOLDERS RELATIONSHIPS

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Exploration of Non-Specific Peptide Inhibitors of Amylin Aggregation in Type-2 Diabetes

Figueroa, H. (2013)

Functional Characterization of the Human Islet Microvasculature Using Living Pancreas Slices v1Preprint

Gonçalves, L. M., & Almaça, J. (2021) · protocols.io · doi:10.17504/protocols.io.bwgupbww

The contribution of individual residues of an aggregative hexapeptide derived from the human γD-crystallin to its amyloidogenicity

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Insulinoma

Scoazec, J. (2015) · Springer eBooks · doi:10.1007/978-3-319-17235-4_8

Relationship between the Level of Amylinemia and Albuminuria Categories in Patients with Latent Autoimmune Diabetes in Adults

Tsaryk, I., & Pashkovska, N. V. (2022) · Open Access Macedonian Journal of Medical Sciences · doi:10.3889/oamjms.2022.9802

Molecular Insights into the Role of Water in Early-stage Human Amylin AggregationPreprint

Guo, A. Z., & Pablo, J. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.08.29.505769

Skin capillary amylin deposition resembles brain amylin vasculopathy in rats

Das, S., Verma, N., Goldstein, L. B., & Despa, F. (2023) · Journal of Stroke and Cerebrovascular Diseases · doi:10.1016/j.jstrokecerebrovasdis.2023.107300

Oral delivery of the amylin receptor agonist pramlintide

Sinézia, C., Sisnande, T., Icart, L. P., & Lima, L. M. T. R. (2024) · Peptide Science · doi:10.1002/pep2.24346

Each big journey starts with a first step: Importance of oligomerization

Agha, M. M., Aziziyan, F., & Uversky, V. N. (2024) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2024.03.011

Elucidating conformational alteration of human islet amyloid polypeptide by nonsynonymous substitutionPreprint

Bashar, M. A., Barua, L., Paul, S., Dash, N., Sadhu, T., Mitra, S., & Dash, R. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.16.623924 · Cited by 1

Activation of the 20S proteasome as a possible strategy to counteract amylin oligomerization in type 2 diabetes

Sowik, D., Giżyńska, M., Trepczyk, K., Witkowska, J., & Jankowska, E. (2025) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2025.108157

Screening of small molecules with varying inhibitory effects on islet amyloid peptide aggregation using liquid crystal-based sensors

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Role of the extracellular matrix in amylin aggregation: Opportunities for improved therapy in type 2 diabetes mellitus

Prabhakar, S., Veerabhadraswamy, P., & Gandasi, N. R. (2025) · Journal of Biosciences · doi:10.1007/s12038-025-00554-y

Coordination Chemistry of Diabetes‐Associated Islet Peptide Hormones

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Metabolic regulatory proteins play an intermediate role in diabetes and Parkinson’s disease

Roy, R., Paul, S., & Chattopadhyay, K. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-33355-2.00038-4

Single-molecule imaging of small aggregates of IAPP in type 2 diabetes serum with rationally-designed antibody-like scaffolds

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Rat Islet Amyloid Polypeptide (IAPP): Isolation and Sequence Determination, Immunohistochemical Study, and its Secretion from Pancreas

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β-Hairpin peptidomimetics as inhibitors of hIAPP amyloid protein aggregation : design, synthesis and evaluation

Lesma, J. (2020) · theses.fr (ABES) · doi:10.70675/d70e1c96z8b04z4f4az88d4ze4416ff17856

Investigation of IAPP fibrillation inhibition by co-chaperonin prefoldin

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Rôle des récepteurs purinergiques P2 dans la plasticité fonctionnelle du pancréas endocrine

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Islet Amyloid Polypeptide Analogues with Reduced Aggregation: Implications for Type 2 Diabetes

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Inhibition of the NLRP3 Inflammasome Prevents Hyperglycemia in a Humanized Rodent Model of Type 2 DiabetesPreprint

Meier, D. T., Dalmas, É., Rachid, L., Guernic, A. L., Baumann, Z., Venteclef, N., & Donath, M. Y. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.19.733338

State-selective inhibition of alpha-synuclein aggregation by de novo oligomer-binding proteinsPreprint

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Pancreatic hormones: a focus on amylin—a new narrative

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

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

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