Amyloid fibrillogenesis: themes and variations.
Recent progress has improved our knowledge of how proteins form amyloid fibrils. Both 'natively unfolded' and globular proteins have been shown to initiate fibrillization by adopting a partially structured conformation. Oligomeric prefibrillar intermediates have been extensively characterized with respect to their morphology and temporal evolution. Three-dimensional models obtained using biophysical and computational methods have provided information about fibril structure. All of these advances suggest common features of self-assembly pathways, with subtle variations accounting for differences among distinct amyloid fibrils.
Rochet
J C
JC
Department of Neurology, Center for Neurologic Diseases, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA. rochet@cnd.bwh.harvard.edu
Lansbury
P T
PT
D000682:Amyloid / Q000378:metabolism*; D017772:Amyloid Neuropathies / Q000378:metabolism; D000818:Animals; D001704:Biopolymers; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D010450:Endopeptidases / Q000502:physiology; D006801:Humans; D009419:Nerve Tissue Proteins / Q000378:metabolism; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D014961:X-Ray Diffraction
D000682:Amyloid; D001704:Biopolymers; D009419:Nerve Tissue Proteins; D010450:Endopeptidases