Islet amyloid polypeptide: structure, function, and pathophysiology

Type 2 diabetes as an inflammatory disease

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Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes

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

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

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Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus

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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.

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CD36 coordinates NLRP3 inflammasome activation by facilitating intracellular nucleation of soluble ligands into particulate ligands in sterile inflammation

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Diabetes Mellitus and the β Cell: The Last Ten Years

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

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Minireview: Secondary β-Cell Failure in Type 2 Diabetes—A Convergence of Glucotoxicity and Lipotoxicity

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

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Saturated Fatty Acids Synergize with Elevated Glucose to Cause Pancreatic β-Cell Death

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

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

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Multiple Amylin Receptors Arise from Receptor Activity-Modifying Protein Interaction with the Calcitonin Receptor Gene Product

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Recent advances in understanding leptin signaling and leptin resistance

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Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane

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Evidence of Cosecretion of Islet Amyloid Polypeptide and Insulin by β-Cells

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Pore Formation by the Cytotoxic Islet Amyloid Peptide Amylin

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Leptin responsiveness restored by amylin agonism in diet-induced obesity: Evidence from nonclinical and clinical studies

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

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Increased β-Cell Apoptosis Prevents Adaptive Increase in β-Cell Mass in Mouse Model of Type 2 Diabetes

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

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Membrane Disruption and Early Events in the Aggregation of the Diabetes Related Peptide IAPP from a Molecular Perspective

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The effect of macromolecular crowding on protein aggregation and amyloid fibril formation

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

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Macromolecular Crowding and Protein Stability

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

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

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Amylin replacement with pramlintide as an adjunct to insulin therapy improves long‐term glycaemic and weight control in Type 1 diabetes mellitus: a 1‐year, randomized controlled trial

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THE RELATION OE DIABETES MELLITUS TO LESIONS OF THE PANCREAS. HYALINE DEGENERATION OF THE ISLANDS OE LANGERHANS

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

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Protofibrillar Islet Amyloid Polypeptide Permeabilizes Synthetic Vesicles by a Pore-like Mechanism that May Be Relevant to Type II Diabetes

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Polymorphic Fibrillar Assembly of Human Amylin

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Protein Stabilization by Macromolecular Crowding through Enthalpy Rather Than Entropy

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Molecular Crowding Accelerates Fibrillization of α-Synuclein: Could an Increase in the Cytoplasmic Protein Concentration Induce Parkinson's Disease?

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Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment

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

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An Amylin Receptor Is Revealed Following Co-Transfection of a Calcitonin Receptor with Receptor Activity Modifying Proteins-1 or -3

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Lipid Membranes Modulate the Structure of Islet Amyloid Polypeptide

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

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

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Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide (IAPP) as nanomolar affinity inhibitor of IAPP cytotoxic fibrillogenesis

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Physical and structural basis for polymorphism in amyloid fibrils

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

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Evidence for Proteotoxicity in β Cells in Type 2 Diabetes

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β-Cell Failure in Type 2 Diabetes: Postulated Mechanisms and Prospects for Prevention and Treatment

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

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The aggregation potential of human amylin determines its cytotoxicity towards islet β‐cells

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

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

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Molecular membrane biology

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Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process

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Identification of Hot Regions of the Aβ–IAPP Interaction Interface as High‐Affinity Binding Sites in both Cross‐ and Self‐Association

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Mechanisms of islet amyloidosis toxicity in type 2 diabetes

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Effects of beta cell granule components on human islet amyloid polypeptide fibril formation

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IL-1 Blockade Attenuates Islet Amyloid Polypeptide-Induced Proinflammatory Cytokine Release and Pancreatic Islet Graft Dysfunction

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Impact of reconstituted cytosol on protein stability

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

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

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

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Islet amyloid: From fundamental biophysics to mechanisms of cytotoxicity

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A Single-Point Mutation Converts the Highly Amyloidogenic Human Islet Amyloid Polypeptide into a Potent Fibrillization Inhibitor

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The role of amylin in the control of energy homeostasis

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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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Widespread amyloid deposition in transplanted human pancreatic islets.

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The Human Islet Amyloid Polypeptide Forms Transient Membrane-Active Prefibrillar Assemblies

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

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The internal pH and membrane potential of the insulin-secretory granule

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

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Antiobesity Effects of the β-Cell Hormone Amylin in Diet-Induced Obese Rats: Effects on Food Intake, Body Weight, Composition, Energy Expenditure, and Gene Expression

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Ionic Strength Effects on Amyloid Formation by Amylin Are a Complicated Interplay among Debye Screening, Ion Selectivity, and Hofmeister Effects

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

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The Role of His-18 in Amyloid Formation by Human Islet Amyloid Polypeptide

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A Single Mutation in the Nonamyloidogenic Region of Islet Amyloid Polypeptide Greatly Reduces Toxicity

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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

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

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Islet amyloid polypeptide toxicity and membrane interactions

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

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

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Aromatic Interactions Are Not Required for Amyloid Fibril Formation by Islet Amyloid Polypeptide but Do Influence the Rate of Fibril Formation and Fibril Morphology

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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 142 · see citing works

Hyperamylinemia Contributes to Cardiac Dysfunction in Obesity and Diabetes

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Human-IAPP disrupts the autophagy/lysosomal pathway in pancreatic β-cells: protective role of p62-positive cytoplasmic inclusions

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Fibril Structure of Human Islet Amyloid Polypeptide*♦

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β-Hairpin Peptide Mimics Decrease Human Islet Amyloid Polypeptide (hIAPP) Aggregation

Lesma, J., Bizet, F., Berardet, C., Tonali, N., Pellegrino, S., Taverna, M., Khemtemourian, L., Soulier, J., van Heijenoort, C., Halgand, F., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.729001 · Cited by 14 · see citing works

Destabilization of Human Islet Amyloid Polypeptide Fibrils by Charged Graphene Quantum Dots: A Molecular Dynamics Investigation with Implications for Nanomedicine

Zhu, L., Wang, G., Zhu, X., Zhang, Q., & Qian, Z. (2023) · ACS Applied Nano Materials · doi:10.1021/acsanm.3c01332 · Cited by 21 · see citing works

Quantum-enhanced photoprotection in neuroprotein architectures emerges from collective light-matter interactions

Patwa, H., Babcock, N. S., & Kurian, P. (2024) · Frontiers in Physics · doi:10.3389/fphy.2024.1387271 · Cited by 20 · see citing works

A single mutation on the human amyloid polypeptide modulates fibril growth and affects the mechanism of amyloid-induced membrane damage

Hoffmann, A. R. F., Sadasivam, S. M., Lequin, O., Killian, J. A., & Khemtémourian, L. (2018) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2018.02.018 · Cited by 19 · see citing works

Charge effects at nano-bio interfaces: a model of charged gold nanoclusters on amylin fibrillation

Tang, X., Gao, G., Zhang, T., Li, J., Yu, M. S., He, M., & Sun, T. (2020) · Nanoscale · doi:10.1039/d0nr03877f · Cited by 19 · see citing works

Interplay between Antimicrobial Peptides and Amyloid Proteins in Host Defense and Disease Modulation

Wani, N. A., Gazit, E., & Ramamoorthy, A. (2024) · Langmuir · doi:10.1021/acs.langmuir.4c03123 · Cited by 19 · see citing works

PAM haploinsufficiency does not accelerate the development of diet- and human IAPP-induced diabetes in mice

Chen, Y., Mains, R. E., Eipper, B. A., Hoffman, B. G., Czyzyk, T. A., Pintar, J. E., & Verchere, C. B. (2020) · Diabetologia · doi:10.1007/s00125-019-05060-z · Cited by 18 · see citing works

Inhibition of Amyloid Protein Aggregation Using Selected Peptidomimetics

Maity, D. (2022) · ChemMedChem · doi:10.1002/cmdc.202200499 · Cited by 17 · see citing works

Peptide Conjugates of Benzene Carboxylic Acids as Agonists and Antagonists of Amylin Aggregation

Profit, A. A., Vedad, J., & Desamero, R. Z. B. (2017) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.6b00732 · Cited by 17 · see citing works

Amyloids of multiple species: are they helpful in survival?

Upadhyay, A., & Mishra, A. (2018) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12399 · Cited by 17 · see citing works

Unpacking the aggregation-oligomerization-fibrillization process of naturally-occurring hIAPP amyloid oligomers isolated directly from sera of children with obesity or diabetes mellitus

Altamirano‐Bustamante, M. M., Altamirano-Bustamante, N. F., Larralde-Laborde, M., Lara‐Martínez, R., Leyva-García, E., Garrido-Magaña, E. P., Rojas, G., Jiménez‐García, L. F., Revilla, M., Altamirano, P., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-54570-8 · Cited by 17 · see citing works

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 · see citing works

Linking Alzheimer’s Disease and Type 2 Diabetes: Characterization and Inhibition of Cytotoxic Aβ and IAPP Hetero-Aggregates

Adem, K. A., Shanti, A., Srivastava, A., Homouz, D., Thomas, S. A., Khair, M., Stefanini, C., Chan, V., Kim, T., & Lee, S. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.842582 · Cited by 17 · see citing works

Ameliorating amyloid aggregation through osmolytes as a probable therapeutic molecule against Alzheimer's disease and type 2 diabetes

Kumari, A., Somvanshi, P., & Grover, A. (2020) · RSC Advances · doi:10.1039/d0ra00429d · Cited by 16 · see citing works

Factors That Contribute to hIAPP Amyloidosis in Type 2 Diabetes Mellitus

Sevcuka, A., White, K., & Terry, C. (2022) · Life · doi:10.3390/life12040583 · Cited by 16 · see citing works

The role of α-sheet structure in amyloidogenesis: characterization and implications

Prosswimmer, T., & Daggett, V. (2022) · Open Biology · doi:10.1098/rsob.220261 · Cited by 16 · 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

Islet amyloid toxicity: From genesis to counteracting mechanisms

Marmentini, C., Branco, R. C. S., Boschero, A. C., & Kurauti, M. A. (2021) · Journal of Cellular Physiology · doi:10.1002/jcp.30600 · Cited by 19 · see citing works

Recent progress of islet amyloid polypeptide

Huang, K. (2010) · Shengming kexue · Cited by 1 · see citing works

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 · see citing works

George Scatchard, John G. Kirkwood, and the electrical interactions of amino acids and proteins

Edsall, J. T. (1982) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(82)90189-x · Cited by 4 · see citing works