The Amyloid Formation Mechanism in Human IAPP: Dimers Have β-Strand Monomer−Monomer Interfaces

Dupuis, Nicholas F., Wu, Chun, Shea, Joan-Emma, Bowers, Michael T.·2011·Journal of the American Chemical Society
DOI 10.1021/ja1081537

Cited by (216)

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  10. Stability Analysis of Human Islet Amyloid Polypeptide and Its Mutated Oligomeric Forms
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  11. Conformational Changes of the Wild-Type hIAPP and the S20P Mutant in Water Revealed by Molecular Dynamics Simulations
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  12. Développement de techniques physiques et chimiques pour l’étude et l’inhibition de l’oligomérisation et de l’agrégation de IAPP : intérêt dans le diabète de type II
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  13. Fine-Tuning hIAPP Amyloidogenesis: Probing Molecular Mechanisms via Fluorinated Core Substitutions
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  15. Decongested 2D IR Spectra Reveal N-Terminal Helices in Amyloid Oligomers Associated with Type 2 Diabetes
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  16. Native Ion Mobility–Mass Spectrometry Reports Kinetically Trapped Conformational Ensembles, Not Single Structures
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