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Neurochemical Research
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December 21, 2019
The Amino Terminus of LeuT Changes Conformation in an Environment Sensitive Manner
Jawad A Khan, Azmat Sohail, Kumaresan Jayaraman, et al.
The Journal of Biological Chemistry
|
September 14, 2011
Ouabain binding site in a functioning Na+/K+ ATPase
Walter Sandtner, Bernhard Egwolf, Fatemeh Khalili-Araghi, et al.
The Journal of Biological Chemistry
|
December 3, 2013
The two Na+ sites in the human serotonin transporter play distinct roles in the ion coupling and electrogenicity of transport
Bruce Felts, Akula Bala Pramod, Walter Sandtner, et al.
Molecular Pharmacology
|
September 12, 2015
Mechanism of Modification, by Lidocaine, of Fast and Slow Recovery from Inactivation of Voltage-Gated Na⁺ Channels
Vaibhavkumar S Gawali, Peter Lukacs, Rene Cervenka, et al.
Plos Computational Biology
|
October 21, 2015
Refinement of the Central Steps of Substrate Transport by the Aspartate Transporter GltPh: Elucidating the Role of the Na2 Sodium Binding Site
SanthoshKannan Venkatesan, Kusumika Saha, Azmat Sohail, et al.
Frontiers in Molecular Biosciences
|
July 14, 2020
Allosterically Linked Binding Sites in Serotonin Transporter Revealed by Single Molecule Force Spectroscopy
Rong Zhu, Walter Sandtner, Joan E A Ahiable, et al.
Biophysical Journal
|
August 28, 2007
Speeding the recovery from ultraslow inactivation of voltage-gated Na+ channels by metal ion binding to the selectivity filter: a foot-on-the-door?
Julia Szendroedi, Walter Sandtner, Touran Zarrabi, et al.
Neuropharmacology
|
September 28, 2005
Serotonin-transporter mediated efflux: a pharmacological analysis of amphetamines and non-amphetamines
Birgit Hilber, Petra Scholze, Mario M Dorostkar, et al.
The Journal of Biological Chemistry
|
April 30, 2017
Occupancy of the zinc-binding site by transition metals decreases the substrate affinity of the human dopamine transporter by an allosteric mechanism
Yang Li, Felix P Mayer, Peter S Hasenhuetl, et al.
The Journal of Biological Chemistry
|
January 19, 2017
Occupancy of the Zinc-binding Site by Transition Metals Decreases the Substrate Affinity of the Human Dopamine Transporter by an Allosteric Mechanism
Yang Li, Felix P Mayer, Peter S Hasenhuetl, et al.
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of 8
Search research articles
Search
Showing results (31-40 of 73) with videos related to
Sort By:
Page
of 8
Neurochemical Research
|
December 21, 2019
The Amino Terminus of LeuT Changes Conformation in an Environment Sensitive Manner
Jawad A Khan, Azmat Sohail, Kumaresan Jayaraman, et al.
The Journal of Biological Chemistry
|
September 14, 2011
Ouabain binding site in a functioning Na+/K+ ATPase
Walter Sandtner, Bernhard Egwolf, Fatemeh Khalili-Araghi, et al.
The Journal of Biological Chemistry
|
December 3, 2013
The two Na+ sites in the human serotonin transporter play distinct roles in the ion coupling and electrogenicity of transport
Bruce Felts, Akula Bala Pramod, Walter Sandtner, et al.
Molecular Pharmacology
|
September 12, 2015
Mechanism of Modification, by Lidocaine, of Fast and Slow Recovery from Inactivation of Voltage-Gated Na⁺ Channels
Vaibhavkumar S Gawali, Peter Lukacs, Rene Cervenka, et al.
Plos Computational Biology
|
October 21, 2015
Refinement of the Central Steps of Substrate Transport by the Aspartate Transporter GltPh: Elucidating the Role of the Na2 Sodium Binding Site
SanthoshKannan Venkatesan, Kusumika Saha, Azmat Sohail, et al.
Frontiers in Molecular Biosciences
|
July 14, 2020
Allosterically Linked Binding Sites in Serotonin Transporter Revealed by Single Molecule Force Spectroscopy
Rong Zhu, Walter Sandtner, Joan E A Ahiable, et al.
Biophysical Journal
|
August 28, 2007
Speeding the recovery from ultraslow inactivation of voltage-gated Na+ channels by metal ion binding to the selectivity filter: a foot-on-the-door?
Julia Szendroedi, Walter Sandtner, Touran Zarrabi, et al.
Neuropharmacology
|
September 28, 2005
Serotonin-transporter mediated efflux: a pharmacological analysis of amphetamines and non-amphetamines
Birgit Hilber, Petra Scholze, Mario M Dorostkar, et al.
The Journal of Biological Chemistry
|
April 30, 2017
Occupancy of the zinc-binding site by transition metals decreases the substrate affinity of the human dopamine transporter by an allosteric mechanism
Yang Li, Felix P Mayer, Peter S Hasenhuetl, et al.
The Journal of Biological Chemistry
|
January 19, 2017
Occupancy of the Zinc-binding Site by Transition Metals Decreases the Substrate Affinity of the Human Dopamine Transporter by an Allosteric Mechanism
Yang Li, Felix P Mayer, Peter S Hasenhuetl, et al.
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of 8