Probing CFTR channel structure and function using the substituted-cysteine-accessibility method.
Akabas
Myles H
MH
Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY, USA.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism; D003545:Cysteine / Q000737:chemistry*; D019005:Cystic Fibrosis Transmembrane Conductance Regulator / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*; D018076:DNA, Complementary / Q000378:metabolism; D004594:Electrophysiology / Q000379:methods*; D007700:Kinetics; D008024:Ligands; D016297:Mutagenesis, Site-Directed; D010766:Phosphorylation; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012333:RNA, Messenger / Q000378:metabolism; D013439:Sulfhydryl Reagents / Q000494:pharmacology; D013997:Time Factors; D014158:Transcription, Genetic; D014981:Xenopus
D018076:DNA, Complementary; D008024:Ligands; D012333:RNA, Messenger; D013439:Sulfhydryl Reagents; D019005:Cystic Fibrosis Transmembrane Conductance Regulator; D000255:Adenosine Triphosphate; D003545:Cysteine