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Amyloidogenicity of recombinant human pro-islet amyloid polypeptide (ProIAPP).
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Structural characterisation of islet amyloid polypeptide fibrils.
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Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation.
Proc Natl Acad Sci U S A. 1990 Jul;87(13):5036-40. doi: 10.1073/pnas.87.13.5036.
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Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.
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Anti-diabetic drug pioglitazone reduces Islet amyloid aggregation overload in the Drosophila neuronal cells.
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Human Amylin in the Presence of SARS-COV-2 Protein Fragments.
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A new polymorphism of human amylin fibrils with similar protofilaments and a conserved core.
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Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR.
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Atomic structures of amyloid cross-beta spines reveal varied steric zippers.
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Membrane interaction of islet amyloid polypeptide.
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Polymorphism in the intermediates and products of amyloid assembly.
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Obesity and diabetes in the developing world--a growing challenge.
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The aggregation potential of human amylin determines its cytotoxicity towards islet beta-cells.
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The 3D profile method for identifying fibril-forming segments of proteins.
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Structure of the cross-beta spine of amyloid-like fibrils.
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