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

Cited by (216)

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  2. Stepwise oligomerization of murine amylin and assembly of amyloid fibrils.
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  3. Mechanism of Inhibition of Human Islet Amyloid Polypeptide-Induced Membrane Damage by a Small Organic Fluorogen
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  5. Molecular insights into the oligomerization dynamics and conformations of amyloidogenic and non-amyloidogenic amylin from discrete molecular dynamics simulations
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  8. Structural Properties of Human IAPP Dimer in Membrane Environment Studied by All-Atom Molecular Dynamics Simulations
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  9. 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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  10. Effects of gold complexes on the assembly behavior of human islet amyloid polypeptide
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  14. Analysis of Proline Substitutions Reveals the Plasticity and Sequence Sensitivity of Human IAPP Amyloidogenicity and Toxicity
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  18. Molecular Dynamics Simulations Indicate Aromaticity as a Key Factor in the Inhibition of IAPP(20–29) Aggregation
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  19. hIAPP-Amyloid-Core Derived d -Peptide Prevents hIAPP Aggregation and Destabilizes Its Protofibrils
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  20. Cross-Sequence Interactions between Human and Rat Islet Amyloid Polypeptides
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