Wild-type opsin does not aggregate with a misfolded opsin mutant.
Department of Ophthalmology and Visual Sciences, Case Western Reserve University, Cleveland, OH 44106, USA.
Megan
M
Gragg
Department of Ophthalmology and Visual Sciences, Case Western Reserve University, Cleveland, OH 44106, USA.
Tae Gyun
TG
Kim
Department of Ophthalmology and Visual Sciences, Case Western Reserve University, Cleveland, OH 44106, USA.
Scott
S
Howell
Department of Ophthalmology and Visual Sciences, Case Western Reserve University, Cleveland, OH 44106, USA. Electronic address: paul.park@case.edu.
P S-H
PS
Park
D019943:Amino Acid Substitution; D002462:Cell Membrane / Q000378:metabolism; D031541:Fluorescence Resonance Energy Transfer; D005799:Genes, Dominant; D057809:HEK293 Cells; D006801:Humans; D008164:Luminescent Proteins; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics; D020125:Mutation, Missense; D017354:Point Mutation; D066329:Protein Aggregates; D017510:Protein Folding; D025941:Protein Interaction Mapping; D055503:Protein Multimerization; D021381:Protein Transport; D057165:Proteostasis Deficiencies / Q000235:genetics / Q000378:metabolism*; D012174:Retinitis Pigmentosa / Q000235:genetics / Q000378:metabolism*; D012243:Rhodopsin / Q000737:chemistry* / Q000172:deficiency* / Q000235:genetics / Q000378:metabolism; D012374:Rod Cell Outer Segment / Q000378:metabolism
D008164:Luminescent Proteins; D008565:Membrane Proteins; D066329:Protein Aggregates; D012243:Rhodopsin
Conformational disease; G protein-coupled receptor; Protein aggregation; Protein misfolding; Retinal degeneration