title: Protein aggregation and misfolding: good or evil?
abstract: Protein aggregation and misfolding have important implications in an increasing number of fields ranging from medicine to biology to nanotechnology  and material science. The interest in understanding this field has accordingly increased steadily over the last two decades. During this time the number of publications that have been dedicated to protein aggregation has increased exponentially, tackling the problem from several different and sometime contradictory perspectives. This review is meant to summarize some of the highlights that come from these studies and introduce this topical issue on the subject. The factors that make a protein aggregate and the cellular strategies that defend from aggregation are discussed together with the perspectives that the accumulated knowledge may open.
authors.affiliation: MRC NIMR, The Ridgeway, London, UK. apastor@nimr.mrc.ac.uk
authors.forename: Annalisa
authors.initials: A
authors.lastname: Pastore
authors.forename: Pierandrea
authors.initials: P
authors.lastname: Temussi
mesh_terms: D000682:Amyloid / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D006801:Humans; D017510:Protein Folding; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D012995:Solubility
chemical_list: D000682:Amyloid; D011506:Proteins