Associated Papers
Internal gate mutants of the GABA transporter GAT1 are capable of substrate exchange.
Dayan-Alon O et al.
Neuropharmacology, 2019
An Extra Amino Acid Residue in Transmembrane Domain 10 of the γ-Aminobutyric Acid (GABA) Transporter GAT-1 Is Required for Efficient Ion-coupled Transport.
Dayan O et al.
The Journal of Biological Chemistry, 2017
The aromatic and charge pairs of the thin extracellular gate of the γ-aminobutyric acid transporter GAT-1 are differently impacted by mutation.
Dayan O et al.
The Journal of Biological Chemistry, 2014
Functional defects in the external and internal thin gates of the γ-aminobutyric acid (GABA) transporter GAT-1 can compensate each other.
Ben-Yona A et al.
The Journal of Biological Chemistry, 2013
An acidic amino acid transmembrane helix 10 residue conserved in the neurotransmitter:sodium:symporters is essential for the formation of the extracellular gate of the γ-aminobutyric acid (GABA) transporter GAT-1.
Ben-Yona A et al.
The Journal of Biological Chemistry, 2012
A glutamine residue conserved in the neurotransmitter:sodium:symporters is essential for the interaction of chloride with the GABA transporter GAT-1.
Ben-Yona A et al.
The Journal of Biological Chemistry, 2011
Transmembrane domain I of the gamma-aminobutyric acid transporter GAT-1 plays a crucial role in the transition between cation leak and transport modes.
Kanner BI
The Journal of Biological Chemistry, 2003
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