(Q28215794)

English

Transmembrane domain I of the gamma-aminobutyric acid transporter GAT-1 plays a crucial role in the transition between cation leak and transport modes

scientific article (publication date: 7 February 2003)

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scholarly article

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Transmembrane domain I of the gamma-aminobutyric acid transporter GAT-1 plays a crucial role in the transition between cation leak and transport modes (English)

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transmembrane transport

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transmembrane protein

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author name string

Baruch I Kanner

1

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language of work or name

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publication date

7 February 2003

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Journal of Biological Chemistry

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278

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6

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3705-12

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An excitatory amino-acid transporter with properties of a ligand-gated chloride channel

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Ion fluxes associated with excitatory amino acid transport.

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Yeast SMF1 mediates H(+)-coupled iron uptake with concomitant uncoupled cation currents

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Sulfhydryl modification of V449C in the glutamate transporter EAAT1 abolishes substrate transport but not the substrate-gated anion conductance

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Distinct conformational states mediate the transport and anion channel properties of the glutamate transporter EAAT-1.

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Dynamic equilibrium between coupled and uncoupled modes of a neuronal glutamate transporter

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Rapid and efficient site-specific mutagenesis without phenotypic selection

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Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid-binding proteins

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Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase

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Expression of a cloned gamma-aminobutyric acid transporter in mammalian cells

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The membrane topology of GAT-1, a (Na+ + Cl-)-coupled gamma-aminobutyric acid transporter from rat brain

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Conformational basis for the Li(+)-induced leak current in the rat gamma-aminobutyric acid (GABA) transporter-1.

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21 January 2018

Identifiers

10.1074/JBC.M210525200

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