title: Protein misfolding and aggregation in ageing and disease: molecular processes and therapeutic perspectives.
abstract: Although intensively researched, the fundamental mechanism of protein misfolding that leads to protein aggregation and associated diseases remains somewhat enigmatic. The failure of a protein to correctly fold de novo or to remain correctly folded can have profound consequences on a living system especially when the cellular quality control processes fail to eliminate the rogue proteins. Over 20 different human diseases have now been designated as 'conformational diseases' and include neurodegenerative diseases such as Alzheimer's disease (AD), Huntington's disease (HD) and Creutzfeldt Jakob disease (CJD) that are becoming increasingly prevalent in an ageing human population. Such diseases are usually characterised by the deposition of specific misfolded proteins as amyloid fibrils and hence are often referred to as the amyloidoses.
authors.affiliation: Department of Biosciences, University of Kent, Canterbury, Kent, UK. m.f.tuite@kent.ac.uk
authors.forename: Mick F
authors.initials: MF
authors.lastname: Tuite
authors.forename: Ronald
authors.initials: R
authors.lastname: Melki
mesh_terms: D000375:Aging; D000686:Amyloidosis; D000818:Animals; D003226:Congresses as Topic; D006801:Humans; D017096:Prion Diseases; D011328:Prions; D017510:Protein Folding
chemical_list: D011328:Prions