title: "Native-like aggregation" of the acylphosphatase from Sulfolobus solfataricus and its biological implications.
abstract: Studies in vitro show that globular proteins can experience the formation of native-like conformational states able to self-assemble with no need of transitions across the energy barrier for unfolding, and that such processes can lead eventually to the formation of amyloid-like species. Circumstantial evidence collected in vivo suggests that aggregation of native-like states can be a concrete possibility for living organisms and thus more relevant than previously thought. In this review we summarize the key observations collected on the "native-like aggregation" of the acylphosphatase from Sulfolobus solfataricus, a protein that has allowed the direct monitoring and analysis of native-like aggregates for its propensity to form rapidly native-like aggregates and their slow conversion into amyloid-like aggregates.
authors: Department of Chemistry, University of Cambridge, Cambridge, United Kingdom. fb330@cam.ac.uk
authors: Francesco
authors: F
authors: Bemporad
authors: Fabrizio
authors: F
authors: Chiti
mesh_terms: D017766:Acid Anhydride Hydrolases / Q000737:chemistry* / Q000187:drug effects; D000682:Amyloid / Q000737:chemistry* / Q000187:drug effects; D004795:Enzyme Stability / Q000187:drug effects; D006801:Humans; D008024:Ligands; D008956:Models, Chemical; D019636:Neurodegenerative Diseases / Q000188:drug therapy / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D048229:Sulfolobus solfataricus / Q000201:enzymology*; D000097024:Acylphosphatase
chemical_list: D017766:Acid Anhydride Hydrolases; D000682:Amyloid; D008024:Ligands; D000097024:Acylphosphatase