Structural biology: It's not all in the family.

The Human Sodium-Glucose Cotransporter (hSGLT1) Is a Disulfide-Bridged Homodimer with a Re-Entrant C-Terminal Loop. PLoS One (2016) 0.75

Mechanism of chloride interaction with neurotransmitter:sodium symporters. Nature (2007) 2.25

Inward-facing conformation of glutamate transporters as revealed by their inverted-topology structural repeats. Proc Natl Acad Sci U S A (2009) 1.64

Dynamic equilibrium between coupled and uncoupled modes of a neuronal glutamate transporter. J Biol Chem (2002) 1.30

Proximity of two oppositely oriented reentrant loops in the glutamate transporter GLT-1 identified by paired cysteine mutagenesis. J Biol Chem (2001) 1.29

Mechanism of cation binding to the glutamate transporter EAAC1 probed with mutation of the conserved amino acid residue Thr101. J Biol Chem (2010) 1.25

Identification of a lithium interaction site in the gamma-aminobutyric acid (GABA) transporter GAT-1. J Biol Chem (2006) 1.22

The substrates of the gamma-aminobutyric acid transporter GAT-1 induce structural rearrangements around the interface of transmembrane domains 1 and 6. J Biol Chem (2008) 1.19

Arginine 445 controls the coupling between glutamate and cations in the neuronal transporter EAAC-1. J Biol Chem (2003) 1.18

Cysteine-scanning mutagenesis reveals a conformationally sensitive reentrant pore-loop in the glutamate transporter GLT-1. J Biol Chem (2002) 1.17

Aspartate-444 is essential for productive substrate interactions in a neuronal glutamate transporter. J Gen Physiol (2007) 1.13

Multiple consequences of mutating two conserved beta-bridge forming residues in the translocation cycle of a neuronal glutamate transporter. J Biol Chem (2006) 1.12

The aqueous accessibility in the external half of transmembrane domain I of the GABA transporter GAT-1 Is modulated by its ligands. J Biol Chem (2004) 1.11

The substrate specificity of a neuronal glutamate transporter is determined by the nature of the coupling ion. J Neurochem (2006) 1.09

The equivalent of a thallium binding residue from an archeal homolog controls cation interactions in brain glutamate transporters. Proc Natl Acad Sci U S A (2009) 1.06

Proximity of transmembrane domains 1 and 3 of the gamma-aminobutyric acid transporter GAT-1 inferred from paired cysteine mutagenesis. J Biol Chem (2005) 1.04

Sulfhydryl modification of cysteine mutants of a neuronal glutamate transporter reveals an inverse relationship between sodium dependent conformational changes and the glutamate-gated anion conductance. Neuropharmacology (2005) 1.02

Substrates and non-transportable analogues induce structural rearrangements at the extracellular entrance of the glial glutamate transporter GLT-1/EAAT2. J Biol Chem (2008) 0.99

The interaction of the gamma-aminobutyric acid transporter GAT-1 with the neurotransmitter is selectively impaired by sulfhydryl modification of a conformationally sensitive cysteine residue engineered into extracellular loop IV. J Biol Chem (2003) 0.97

A conserved methionine residue controls the substrate selectivity of a neuronal glutamate transporter. J Biol Chem (2010) 0.96

Conformationally sensitive reactivity to permeant sulfhydryl reagents of cysteine residues engineered into helical hairpin 1 of the glutamate transporter GLT-1. Mol Pharmacol (2007) 0.95

Disulfide cross-linking of transport and trimerization domains of a neuronal glutamate transporter restricts the role of the substrate to the gating of the anion conductance. J Biol Chem (2014) 0.94

Conserved asparagine residue located in binding pocket controls cation selectivity and substrate interactions in neuronal glutamate transporter. J Biol Chem (2012) 0.93

Transmembrane domain 8 of the {gamma}-aminobutyric acid transporter GAT-1 lines a cytoplasmic accessibility pathway into its binding pocket. J Biol Chem (2009) 0.92

A glutamine residue conserved in the neurotransmitter:sodium:symporters is essential for the interaction of chloride with the GABA transporter GAT-1. J Biol Chem (2010) 0.91

Transporter-associated currents in the gamma-aminobutyric acid transporter GAT-1 are conditionally impaired by mutations of a conserved glycine residue. J Biol Chem (2005) 0.90

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. J Biol Chem (2012) 0.86

A conserved aspartate residue located at the extracellular end of the binding pocket controls cation interactions in brain glutamate transporters. J Biol Chem (2011) 0.84

Transmembrane domains I and II of the gamma-aminobutyric acid transporter GAT-4 contain molecular determinants of substrate specificity. Mol Pharmacol (2004) 0.82

Expression of neurotransmitter transporters for structural and biochemical studies. Protein Expr Purif (2010) 0.81

Functional defects in the external and internal thin gates of the γ-aminobutyric acid (GABA) transporter GAT-1 can compensate each other. J Biol Chem (2013) 0.80

Molecular physiology: intimate contact enables transport. Nature (2005) 0.78

Cysteine scanning mutagenesis of transmembrane helix 3 of a brain glutamate transporter reveals two conformationally sensitive positions. J Biol Chem (2012) 0.77