Self-assembly of short aromatic peptides: From amyloid disease to nanotechnology
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Biomedical Engineering,Bioengineering
Link
http://link.springer.com/content/pdf/10.1007/s12030-005-0043-7.pdf
Reference27 articles.
1. Gilead, S. & Gazit, E. (2005) Self-Organization of Short Peptide Fragments: From Amyloid Fibrils to Nanoscale Supramolecular Assemblies. Supramol. Chem. 17, 87–92.
2. Gazit, E. (2002) Mechanistic studies of the process of amyloid fibrils formation by the use of peptide fragments and analogues: Implications for the design of fibrillization inhibitors. Curr. Med. Chem. 9, 1725–1735.
3. Gazit, E. (2002) The “correctly-folded” state of proteins: Is it a metastable state? Angew. Chem. Int. Ed. Engl. 41, 257–259.
4. Azriel, R. & Gazit, E. (2001) Analysis of the Structural and Functional Elements of the Minimal Active Fragment of Islet Amyloid Polypeptide (IAPP): An Experimental Support for the Key Role for the Phenylanaline Residue in Amyloid Formation J. Biol. Chem. 276, 34156–34161.
5. Gazit, E. (2002) A possible role for pi-stacking in the self-assembly of amyloid fibrils. FASEB J. 16, 77–83.
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