| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1195382 | Journal of the American Society for Mass Spectrometry | 2010 | 10 Pages |
A number of proteins are capable of converting from their soluble, monomeric form into highly-ordered, insoluble aggregates known as amyloid fibrils. In vivo, these fibrils, which accumulate in organs and tissues, are associated with a wide range of amyloid diseases for which there are currently no therapeutic solutions. The molecular details of the pathway from native monomer through oligomeric intermediates to the final amyloid fibril remain a challenging enigma. Over the past few years, mass spectrometry has been applied to investigate the various stages of amyloid fibril formation, and this report summarizes the key steps achieved to date.
Graphical AbstractFrom monomer to fibril: investigating amyloid assembly pathways and intermediates by electrospray ionization mass spectrometry.Figure optionsDownload full-size imageDownload high-quality image (98 K)Download as PowerPoint slide
