4.6 Article

The Accessibility in the External Part of the TM5 of the Glutamate Transporter EAAT1 Is Conformationally Sensitive during the Transport Cycle

Related references

Note: Only part of the references are listed.
Article Multidisciplinary Sciences

The 3-4 loop of an archaeal glutamate transporter homolog experiences ligand-induced structural changes and is essential for transport

Emma L. R. Compton et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2010)

Article Multidisciplinary Sciences

The equivalent of a thallium binding residue from an archeal homolog controls cation interactions in brain glutamate transporters

Shlomit Teichman et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2009)

Article Multidisciplinary Sciences

Inward-facing conformation of glutamate transporters as revealed by their inverted-topology structural repeats

Thomas J. Crisman et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2009)

Article Biochemistry & Molecular Biology

Time-resolved mechanism of extracellular gate opening and substrate binding in a glutamate transporter

Indira H. Shrivastava et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2008)

Article Biochemistry & Molecular Biology

Rigidity of the subunit interfaces of the trimeric glutamate transporter GItT during translocation

Maarten Groeneveld et al.

JOURNAL OF MOLECULAR BIOLOGY (2007)

Article Physiology

Aspartate-444 is essential for productive substrate interactions in a neuronal glutamate transporter

Shlomit Teichman et al.

JOURNAL OF GENERAL PHYSIOLOGY (2007)

Article Multidisciplinary Sciences

Structure of a glutamate transporter homologue from Pyrococcus horikoshii

D Yernool et al.

NATURE (2004)

Article Biochemistry & Molecular Biology

Coupled, but not uncoupled, fluxes in a neuronal glutamate transporter can be activated by lithium ions

L Borre et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2001)

Article Biochemistry & Molecular Biology

Arginine 447 plays a pivotal role in substrate interactions in a neuronal glutamate transporter

A Bendahan et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2000)

Article Biochemistry & Molecular Biology

The accessibility of a novel reentrant loop of the glutamate transporter GLT-1 is restricted by its substrate

M Grunewald et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2000)