Defining the Molecular Basis of Amyloid Inhibitors: Human Islet Amyloid Polypeptide–Insulin Interactions

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• Human Islet Amyloid Polypeptide Monomers Form Ordered β-hairpins: A Possible Direct Amyloidogenic Precursor
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• Analysis of the Amyloidogenic Potential of Pufferfish (Takifugu rubripes) Islet Amyloid Polypeptide Highlights the Limitations of Thioflavin-T Assays and the Difficulties in Defining Amyloidogenicity
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• The Ability of Rodent Islet Amyloid Polypeptide to Inhibit Amyloid Formation by Human Islet Amyloid Polypeptide Has Important Implications For the Mechanism of Amyloid Formation and the Design of Inhibitors.
  Bằng: Cao, Ping, et al.
  Được phát hành: (2010)
• Structural Similarities and Differences between Amyloidogenic and Non-Amyloidogenic Islet Amyloid Polypeptide (IAPP) Sequences and Implications for the Dual Physiological and Pathological Activities of These Peptides
  Bằng: Wu, Chun, et al.
  Được phát hành: (2013)
• The role of aromatic interactions in amyloid formation by islet amyloid polypeptide
  Bằng: Tu, Ling-Hsien, et al.
  Được phát hành: (2013)