Sequence and Crowding Effects in the Aggregation of a 10-Residue Fragment Derived from Islet Amyloid Polypeptide
- 3 June 2009
- journal article
- Published by Elsevier BV in Biophysical Journal
- Vol. 96 (11), 4552-4560
- https://doi.org/10.1016/j.bpj.2009.03.039
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- A Single-Point Mutation Converts the Highly Amyloidogenic Human Islet Amyloid Polypeptide into a Potent Fibrillization InhibitorJournal of the American Chemical Society, 2007
- Protein Misfolding, Functional Amyloid, and Human DiseaseAnnual Review of Biochemistry, 2006
- The Amyloid Hypothesis of Alzheimer's Disease: Progress and Problems on the Road to TherapeuticsScience, 2002
- Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in VitroJournal of Molecular Biology, 1999
- Effects of Sequential Proline Substitutions on Amyloid Formation by Human Amylin20-29Biochemistry, 1999
- Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxinsProceedings of the National Academy of Sciences, 1998
- Rotational Resonance Solid-State NMR Elucidates a Structural Model of Pancreatic AmyloidJournal of the American Chemical Society, 1995
- Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitusNature, 1994
- Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation.Proceedings of the National Academy of Sciences of the United States of America, 1990
- Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients.Proceedings of the National Academy of Sciences, 1987