Probing structure of neurotransmitter transporters by substituted-cysteine accessibility method.
Javitch
J A
JA
Department of Psychiatry, College of Physicians and Surgeons, Columbia University, New York, New York 10032, USA.
D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism*; D003545:Cysteine; D004298:Dopamine / Q000378:metabolism; D050483:Dopamine Plasma Membrane Transport Proteins; D006801:Humans; D007700:Kinetics; D008562:Membrane Glycoproteins; D026901:Membrane Transport Proteins; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D009419:Nerve Tissue Proteins; D018377:Neurotransmitter Agents / Q000737:chemistry* / Q000378:metabolism*; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013439:Sulfhydryl Reagents / Q000494:pharmacology*; D014162:Transfection / Q000379:methods
D002352:Carrier Proteins; D050483:Dopamine Plasma Membrane Transport Proteins; D008562:Membrane Glycoproteins; D026901:Membrane Transport Proteins; D009419:Nerve Tissue Proteins; D018377:Neurotransmitter Agents; D011994:Recombinant Proteins; D013439:Sulfhydryl Reagents; D003545:Cysteine; D004298:Dopamine