G. Johnston

Publications436
h-index73
Citations20,291
Highly Influential Citations408
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THE ‘ABC’ OF GABA RECEPTORS: A BRIEF REVIEW
TLDR
Conformationally restricted analogues of GABA have been used to help identify three major GABA receptors, termed GABAA, GABAB and GABAC receptors.
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GABA(A) receptor channel pharmacology.
  • G. Johnston
  • Biology
    Current pharmaceutical design
  • 31 May 2005
TLDR
The emphasis of this review is on the rich chemical diversity of ligands that influence GABA(A) receptor function, which provides many avenues for the design and development of new chemical entities acting on GABA (A) receptors.
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Amino acid transmitters in the mammalian central nervous system.
TLDR
Evidence for A m i n o Acids as T ransmi t t e r s as well as evidence for Synthesis and Storage are presented.
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GABAA receptor pharmacology.
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GABAc receptors: relatively simple transmitter -gated ion channels?
  • G. Johnston
  • Biology
    Trends in pharmacological sciences
  • 1 September 1996
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Bicuculline, an antagonist of GABA and synaptic inhibition in the spinal cord of the cat.
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Effects of a naturally occurring neurosteroid on GABAA IPSCs during development in rat hippocampal or cerebellar slices
TLDR
It is suggested that the progressive relative insensitivity of the 20 day hippocampal cells may depend on increasing expression of the δ subunit of the GABAA receptor and possibly an increase in the α4 subunit in the brain.
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Central nervous system depressant action of flavonoid glycosides.
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Flavonoid modulation of GABAA receptors
There has been a resurgence of interest in synthetic and plant‐derived flavonoids as modulators of γ‐amino butyric acid‐A (GABAA) receptor function influencing inhibition mediated by the major…
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Molecular basis for differential inhibition of glutamate transporter subtypes by zinc ions.
TLDR
The molecular basis for differential inhibition of EAAT1 and EAAT2 by Zn2+ is investigated using site-directed mutagenesis and it is demonstrated that histidine residues ofEAAT1 at positions 146 and 156 form part of the Zn1+ binding site, confirming the role of this residue in conferring differential Zn 2+ sensitivity.
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