Structural and functional basis for GABA A receptor heterogeneity

When gamma-aminobutyric acid (GABA), the major inhibitory neurotransmitter in vertebrate brain, binds to its receptor it activates a chloride channel. A study which isolates cDNAs encoding two additional GABAA receptor alpha-subunits and confirms the heterogeneous nature of the receptor/chloride cha...

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Published in:Nature (London) 1988-09, Vol.335 (6185), p.76-79
Main Authors: Levitan, Edwin S, Schofield, Peter R, Burt, David R, Rhee, Lucy M, Wisden, William, Köhler, Martin, Fujita, Norihisa, Rodriguez, Henry F, Stephenson, Anne, Darlison, Mark G, Barnard, Eric A, Seeburg, Peter H
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Language:English
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Brain
Cellular biology
Genetics
Heterogeneity
Medical research
Nervous system
Vertebrates
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container_end_page 79
container_issue 6185
container_start_page 76
container_title Nature (London)
container_volume 335
creator Levitan, Edwin S
Schofield, Peter R
Burt, David R
Rhee, Lucy M
Wisden, William
Köhler, Martin
Fujita, Norihisa
Rodriguez, Henry F
Stephenson, Anne
Darlison, Mark G
Barnard, Eric A
Seeburg, Peter H
description When gamma-aminobutyric acid (GABA), the major inhibitory neurotransmitter in vertebrate brain, binds to its receptor it activates a chloride channel. A study which isolates cDNAs encoding two additional GABAA receptor alpha-subunits and confirms the heterogeneous nature of the receptor/chloride channel complex is discussed.
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subjects Brain
Cellular biology
Genetics
Heterogeneity
Medical research
Nervous system
Vertebrates
title Structural and functional basis for GABA A receptor heterogeneity
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