Porcine islet amyloid polypeptide fragments are refractory to amyloid formation

Islet amyloid deposition limits the viability of human islet grafts but not porcine islet grafts

(2010) K. J. Potter et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Unique Identification of Supramolecular Structures in Amyloid Fibrils by Solid-State NMR Spectroscopy

(2009) Jakob T. Nielsen et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

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

(2009) Ping Cao et al.   BIOCHEMISTRY

Sequence and Crowding Effects in the Aggregation of a 10-Residue Fragment Derived from Islet Amyloid Polypeptide

(2009) Eva Rivera et al.   BIOPHYSICAL JOURNAL

Structural diversity of the soluble trimers of the human amylin(20–29) peptide revealed by molecular dynamics simulations

(2009) Yuxiang Mo et al.   JOURNAL OF CHEMICAL PHYSICS

Human Islet Amyloid Polypeptide Monomers Form Ordered β-hairpins: A Possible Direct Amyloidogenic Precursor

(2009) Nicholas F. Dupuis et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Inhibition of IAPP and IAPP(20−29)Fibrillation by Polymeric Nanoparticles

(2009) C. Cabaleiro-Lago et al.   LANGMUIR

Structural Insights into the Polymorphism of Amyloid-Like Fibrils Formed by Region 20−29 of Amylin Revealed by Solid-State NMR and X-ray Fiber Diffraction

(2008) Jillian Madine et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

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

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