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

Residual Structure in Islet Amyloid Polypeptide Mediates Its Interactions with Soluble Insulin†

(2009) Lei Wei et al.   BIOCHEMISTRY

Dynamic α-Helix Structure of Micelle-bound Human Amylin

(2009) Sharadrao M. Patil et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Two-dimensional Infrared Spectroscopy Provides Evidence of an Intermediate in the Membrane-catalyzed Assembly of Diabetic Amyloid

(2009) Yun L. Ling et al.   JOURNAL OF PHYSICAL CHEMISTRY B

Amylin Proprotein Processing Generates Progressively More Amyloidogenic Peptides that Initially Sample the Helical State†

(2008) Isaac T. Yonemoto et al.   BIOCHEMISTRY

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

(2008) Ravi Prakash Reddy Nanga et al.   BIOCHEMISTRY

Structure of α-Helical Membrane-bound Human Islet Amyloid Polypeptide and Its Implications for Membrane-mediated Misfolding

(2008) Melania Apostolidou et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

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

(2008) Jed J.W. Wiltzius et al.   PROTEIN SCIENCE

Contribution of the intrinsic disulfide to the assembly mechanism of islet amyloid

(2004) Bon W. Koo et al.   PROTEIN SCIENCE