title: Modeling the structural consequences of BEST1 missense mutations.
authors.affiliation: Section of Ophthalmology, Department of Clinical Studies, School of Veterinary Medicine, University of Pennsylvania, Ryan Veterinary Hospital, 3900 Delancey Street, Room 2020, Philadelphia, PA 19104, USA.
authors.forename: Karina E
authors.initials: KE
authors.lastname: Guziewicz
authors.forename: Gustavo D
authors.initials: GD
authors.lastname: Aguirre
authors.forename: Barbara
authors.initials: B
authors.lastname: Zangerl
mesh_terms: D000818:Animals; D000075002:Bestrophins; D018118:Chloride Channels / Q000737:chemistry* / Q000235:genetics*; D003198:Computer Simulation; D004195:Disease Models, Animal; D004283:Dog Diseases / Q000235:genetics* / Q000503:physiopathology; D004285:Dogs; D005136:Eye Proteins / Q000737:chemistry* / Q000235:genetics*; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics; D008956:Models, Chemical; D020125:Mutation, Missense / Q000502:physiology; D013329:Structure-Activity Relationship; D057826:Vitelliform Macular Dystrophy / Q000235:genetics* / Q000503:physiopathology; D014867:Water / Q000737:chemistry
chemical_list: C113133:BEST1 protein, human; D000075002:Bestrophins; D018118:Chloride Channels; D005136:Eye Proteins; D008565:Membrane Proteins; D014867:Water