title: Conformational disease.
abstract: A large and diverse number of diseases are now recognized as 'conformational diseases', caused by adoption of non-native protein conformations that lead to aggregation. The recent conference, 'Alpha1-antitrypsin deficiency and other conformational diseases', held in Airlie, Virginia, USA (27-30 June, 2000) focused on some of the common pathways by which cells protect themselves from toxicity associated with protein misfolding and aggregation.
authors.affiliation: Department of Biological Sciences, Stanford University, Stanford, California 94305-5020, USA. kopito@leland.stanford.edu
authors.forename: R R
authors.initials: RR
authors.lastname: Kopito
authors.forename: D
authors.initials: D
authors.lastname: Ron
mesh_terms: D002135:Calcium-Binding Proteins / Q000378:metabolism; D037281:Calnexin; D037282:Calreticulin; D019005:Cystic Fibrosis Transmembrane Conductance Regulator / Q000378:metabolism; D015852:Eukaryotic Initiation Factor-2 / Q000378:metabolism; D006006:Glycogen Synthase / Q000378:metabolism; D006801:Humans; D008358:Mannose / Q000378:metabolism; D008361:Mannosidases / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012261:Ribonucleoproteins / Q000378:metabolism; D000515:alpha 1-Antitrypsin / Q000737:chemistry*; D019896:alpha 1-Antitrypsin Deficiency / Q000378:metabolism*
chemical_list: C505032:CFTR protein, human; D002135:Calcium-Binding Proteins; D037282:Calreticulin; D015852:Eukaryotic Initiation Factor-2; D012261:Ribonucleoproteins; D000515:alpha 1-Antitrypsin; D019005:Cystic Fibrosis Transmembrane Conductance Regulator; D037281:Calnexin; D006006:Glycogen Synthase; D008361:Mannosidases; C046090:mannosyl-oligosaccharide 1,2-alpha-mannosidase; D008358:Mannose