title: Protein misfolding and disease; protein refolding and therapy.
abstract: Diverse human disorders, including several neurodegenerative diseases and systemic amyloidosis, are thought to arise from the misfolding and aggregation of an underlying protein. Recent findings strongly support this hypothesis and have increased our understanding of the molecular mechanism of protein conformational disorders. Many questions are still pending, but the data overall suggest that correction of protein misfolding constitutes a viable therapeutic strategy for conformational diseases.
authors: Serono Pharmaceutical Research Institute, 14 Chemin des Aulx, 1228 Plan les Ouates, Geneva, Switzerland. claudio.soto@serono.com
authors: C
authors: C
authors: Soto
mesh_terms: D000818:Animals; D002493:Central Nervous System Diseases / Q000235:genetics / Q000378:metabolism* / Q000628:therapy; D006801:Humans; D010455:Peptides / Q000627:therapeutic use; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D010455:Peptides; D011506:Proteins