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Baruch I Kanner

Showing results (1-10 of 47) with videos related to

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The Journal of Biological Chemistry|November 26, 2002
Transmembrane domain I of the gamma-aminobutyric acid transporter GAT-1 plays a crucial role in the transition between cation leak and transport modesBaruch I Kanner
Nature|September 9, 2005
Molecular physiology: intimate contact enables transportBaruch I Kanner
Nature Structural & Molecular Biology|October 8, 2013
Substrate-induced rearrangements in glutamate-transporter homologsBaruch I Kanner
Nature|August 1, 2008
Structural biology: It's not all in the familyBaruch I Kanner
ACS Chemical Biology|March 22, 2007
Gate movements in glutamate transportersBaruch I Kanner
The Journal of Membrane Biology|April 10, 2007
Structure and function of sodium-coupled GABA and glutamate transportersBaruch I Kanner
The Journal of General Physiology|May 31, 2007
Aspartate-444 is essential for productive substrate interactions in a neuronal glutamate transporterShlomit Teichman, Baruch I Kanner
The Journal of Biological Chemistry|August 20, 2003
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 IVElia Zomot, Baruch I Kanner
The Journal of Biological Chemistry|April 3, 2008
The substrates of the gamma-aminobutyric acid transporter GAT-1 induce structural rearrangements around the interface of transmembrane domains 1 and 6Alex Rosenberg, Baruch I Kanner
Molecular Pharmacology|May 25, 2004
Transmembrane domains I and II of the gamma-aminobutyric acid transporter GAT-4 contain molecular determinants of substrate specificityNir Melamed, Baruch I Kanner
Pageof 5

Showing results (1-10 of 47) with videos related to

Sort By:
Pageof 5
The Journal of Biological Chemistry|November 26, 2002
Transmembrane domain I of the gamma-aminobutyric acid transporter GAT-1 plays a crucial role in the transition between cation leak and transport modesBaruch I Kanner
Nature|September 9, 2005
Molecular physiology: intimate contact enables transportBaruch I Kanner
Nature Structural & Molecular Biology|October 8, 2013
Substrate-induced rearrangements in glutamate-transporter homologsBaruch I Kanner
Nature|August 1, 2008
Structural biology: It's not all in the familyBaruch I Kanner
ACS Chemical Biology|March 22, 2007
Gate movements in glutamate transportersBaruch I Kanner
The Journal of Membrane Biology|April 10, 2007
Structure and function of sodium-coupled GABA and glutamate transportersBaruch I Kanner
The Journal of General Physiology|May 31, 2007
Aspartate-444 is essential for productive substrate interactions in a neuronal glutamate transporterShlomit Teichman, Baruch I Kanner
The Journal of Biological Chemistry|August 20, 2003
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 IVElia Zomot, Baruch I Kanner
The Journal of Biological Chemistry|April 3, 2008
The substrates of the gamma-aminobutyric acid transporter GAT-1 induce structural rearrangements around the interface of transmembrane domains 1 and 6Alex Rosenberg, Baruch I Kanner
Molecular Pharmacology|May 25, 2004
Transmembrane domains I and II of the gamma-aminobutyric acid transporter GAT-4 contain molecular determinants of substrate specificityNir Melamed, Baruch I Kanner
Pageof 5