title: Protein aggregation as a cause for disease.
abstract: The ability of proteins to fold into a defined and functional conformation is one of the most fundamental processes in biology. Certain conditions, however, initiate misfolding or unfolding of proteins. This leads to the loss of functional protein or it can result in a wide range of diseases. One group of diseases, which includes Alzheimer's, Parkinson's, Huntington's disease, and the transmissible spongiform encephalopathies (prion diseases), involves deposition of aggregated proteins. Normally, such protein aggregates are not found in properly functioning biological systems, because a variety of mechanisms inhibit their formation. Understanding the nature of these protective mechanisms together with the understanding of factors reducing or deactivating the natural protection machinery will be crucial for developing strategies to prevent and treat these disastrous diseases.
authors.affiliation: Department Chemie, Lehrstuhl für Biotechnologie, Technische Universität München, Garching, Germany.
authors.forename: T
authors.initials: T
authors.lastname: Scheibel
authors.forename: J
authors.initials: J
authors.lastname: Buchner
mesh_terms: D000544:Alzheimer Disease / Q000209:etiology; D016229:Amyloid beta-Peptides / Q000633:toxicity; D000686:Amyloidosis / Q000209:etiology; D000818:Animals; D006360:Heat-Shock Proteins / Q000502:physiology; D006801:Humans; D006816:Huntington Disease / Q000209:etiology; D002479:Inclusion Bodies; D018832:Molecular Chaperones / Q000502:physiology; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
chemical_list: D016229:Amyloid beta-Peptides; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D011506:Proteins