Structured Review

Boston Therapeutics kchip2
Effects of NS5806 on cloned <t>Kv4.3/KChIP2/DPP6‐L</t> channels in HEK293 cells. A, Representative current traces elicited by the depolarizing voltage steps from −40 to +40 mV for 2 seconds from a holding potential of −80 mV at different transfection ratios of Kv4.3: KChIP2: DPP6‐L (Left). The superimposed current traces at +40 mV in the absence and presence of NS5806 are shown on the right. B, Effect of 10 μM NS5806 on the peak current of the Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios, measured at +40 mV. C, The time constant of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios (n = 22). D, I–V relationships of Kv4.3/KChIP2/DPP6‐L peak current density at plasmid ratio 1:1:1 before and after 10 μM NS5806 (n = 18, * P
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Images

1) Product Images from "Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex, et al. Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex"

Article Title: Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex, et al. Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex

Journal: The FASEB Journal

doi: 10.1096/fj.201902010RR

Effects of NS5806 on cloned Kv4.3/KChIP2/DPP6‐L channels in HEK293 cells. A, Representative current traces elicited by the depolarizing voltage steps from −40 to +40 mV for 2 seconds from a holding potential of −80 mV at different transfection ratios of Kv4.3: KChIP2: DPP6‐L (Left). The superimposed current traces at +40 mV in the absence and presence of NS5806 are shown on the right. B, Effect of 10 μM NS5806 on the peak current of the Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios, measured at +40 mV. C, The time constant of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios (n = 22). D, I–V relationships of Kv4.3/KChIP2/DPP6‐L peak current density at plasmid ratio 1:1:1 before and after 10 μM NS5806 (n = 18, * P
Figure Legend Snippet: Effects of NS5806 on cloned Kv4.3/KChIP2/DPP6‐L channels in HEK293 cells. A, Representative current traces elicited by the depolarizing voltage steps from −40 to +40 mV for 2 seconds from a holding potential of −80 mV at different transfection ratios of Kv4.3: KChIP2: DPP6‐L (Left). The superimposed current traces at +40 mV in the absence and presence of NS5806 are shown on the right. B, Effect of 10 μM NS5806 on the peak current of the Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios, measured at +40 mV. C, The time constant of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios (n = 22). D, I–V relationships of Kv4.3/KChIP2/DPP6‐L peak current density at plasmid ratio 1:1:1 before and after 10 μM NS5806 (n = 18, * P

Techniques Used: Clone Assay, Transfection, Produced, Plasmid Preparation

DPP6 and KChIP2 subunits confer the modality of I to channel response to NS5806
Figure Legend Snippet: DPP6 and KChIP2 subunits confer the modality of I to channel response to NS5806

Techniques Used:

Analysis on the putative interactions between KChIP2 and DPP6‐L. A 1 , Modeling and docking simulation of putative interactions between DPP6‐Lin and KChIP2 . Homology model of KChIP2. A 2 , The top‐ranked model of the intracellular domain of DPP6‐L (DPP6‐Lin). A 3 , Top‐ranked models of both proteins. A 4 , Best scored model of docking KChIP2 with DPP6‐Lin; putative‐interacting residues are indicated. B 1 , Schematic depiction of DPP6‐L and the location of mutated residues within the putative KChIP2 interaction site. B 2 , Representative recordings of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut currents from HEK293 cells using 500 ms square voltage pulses (from −40 to +40 mV; holding potential is −80 mV). B 3 , The time constants of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut current traces plotted against voltage (** P
Figure Legend Snippet: Analysis on the putative interactions between KChIP2 and DPP6‐L. A 1 , Modeling and docking simulation of putative interactions between DPP6‐Lin and KChIP2 . Homology model of KChIP2. A 2 , The top‐ranked model of the intracellular domain of DPP6‐L (DPP6‐Lin). A 3 , Top‐ranked models of both proteins. A 4 , Best scored model of docking KChIP2 with DPP6‐Lin; putative‐interacting residues are indicated. B 1 , Schematic depiction of DPP6‐L and the location of mutated residues within the putative KChIP2 interaction site. B 2 , Representative recordings of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut currents from HEK293 cells using 500 ms square voltage pulses (from −40 to +40 mV; holding potential is −80 mV). B 3 , The time constants of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut current traces plotted against voltage (** P

Techniques Used:

2) Product Images from "Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex, et al. Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex"

Article Title: Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex, et al. Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex

Journal: The FASEB Journal

doi: 10.1096/fj.201902010RR

Effects of NS5806 on cloned Kv4.3/KChIP2/DPP6‐L channels in HEK293 cells. A, Representative current traces elicited by the depolarizing voltage steps from −40 to +40 mV for 2 seconds from a holding potential of −80 mV at different transfection ratios of Kv4.3: KChIP2: DPP6‐L (Left). The superimposed current traces at +40 mV in the absence and presence of NS5806 are shown on the right. B, Effect of 10 μM NS5806 on the peak current of the Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios, measured at +40 mV. C, The time constant of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios (n = 22). D, I–V relationships of Kv4.3/KChIP2/DPP6‐L peak current density at plasmid ratio 1:1:1 before and after 10 μM NS5806 (n = 18, * P
Figure Legend Snippet: Effects of NS5806 on cloned Kv4.3/KChIP2/DPP6‐L channels in HEK293 cells. A, Representative current traces elicited by the depolarizing voltage steps from −40 to +40 mV for 2 seconds from a holding potential of −80 mV at different transfection ratios of Kv4.3: KChIP2: DPP6‐L (Left). The superimposed current traces at +40 mV in the absence and presence of NS5806 are shown on the right. B, Effect of 10 μM NS5806 on the peak current of the Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios, measured at +40 mV. C, The time constant of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios (n = 22). D, I–V relationships of Kv4.3/KChIP2/DPP6‐L peak current density at plasmid ratio 1:1:1 before and after 10 μM NS5806 (n = 18, * P

Techniques Used: Clone Assay, Transfection, Produced, Plasmid Preparation

DPP6 and KChIP2 subunits confer the modality of I to channel response to NS5806
Figure Legend Snippet: DPP6 and KChIP2 subunits confer the modality of I to channel response to NS5806

Techniques Used:

Analysis on the putative interactions between KChIP2 and DPP6‐L. A 1 , Modeling and docking simulation of putative interactions between DPP6‐Lin and KChIP2 . Homology model of KChIP2. A 2 , The top‐ranked model of the intracellular domain of DPP6‐L (DPP6‐Lin). A 3 , Top‐ranked models of both proteins. A 4 , Best scored model of docking KChIP2 with DPP6‐Lin; putative‐interacting residues are indicated. B 1 , Schematic depiction of DPP6‐L and the location of mutated residues within the putative KChIP2 interaction site. B 2 , Representative recordings of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut currents from HEK293 cells using 500 ms square voltage pulses (from −40 to +40 mV; holding potential is −80 mV). B 3 , The time constants of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut current traces plotted against voltage (** P
Figure Legend Snippet: Analysis on the putative interactions between KChIP2 and DPP6‐L. A 1 , Modeling and docking simulation of putative interactions between DPP6‐Lin and KChIP2 . Homology model of KChIP2. A 2 , The top‐ranked model of the intracellular domain of DPP6‐L (DPP6‐Lin). A 3 , Top‐ranked models of both proteins. A 4 , Best scored model of docking KChIP2 with DPP6‐Lin; putative‐interacting residues are indicated. B 1 , Schematic depiction of DPP6‐L and the location of mutated residues within the putative KChIP2 interaction site. B 2 , Representative recordings of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut currents from HEK293 cells using 500 ms square voltage pulses (from −40 to +40 mV; holding potential is −80 mV). B 3 , The time constants of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut current traces plotted against voltage (** P

Techniques Used:

3) Product Images from "Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex, et al. Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex"

Article Title: Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex, et al. Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex

Journal: The FASEB Journal

doi: 10.1096/fj.201902010RR

Effects of NS5806 on cloned Kv4.3/KChIP2/DPP6‐L channels in HEK293 cells. A, Representative current traces elicited by the depolarizing voltage steps from −40 to +40 mV for 2 seconds from a holding potential of −80 mV at different transfection ratios of Kv4.3: KChIP2: DPP6‐L (Left). The superimposed current traces at +40 mV in the absence and presence of NS5806 are shown on the right. B, Effect of 10 μM NS5806 on the peak current of the Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios, measured at +40 mV. C, The time constant of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios (n = 22). D, I–V relationships of Kv4.3/KChIP2/DPP6‐L peak current density at plasmid ratio 1:1:1 before and after 10 μM NS5806 (n = 18, * P
Figure Legend Snippet: Effects of NS5806 on cloned Kv4.3/KChIP2/DPP6‐L channels in HEK293 cells. A, Representative current traces elicited by the depolarizing voltage steps from −40 to +40 mV for 2 seconds from a holding potential of −80 mV at different transfection ratios of Kv4.3: KChIP2: DPP6‐L (Left). The superimposed current traces at +40 mV in the absence and presence of NS5806 are shown on the right. B, Effect of 10 μM NS5806 on the peak current of the Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios, measured at +40 mV. C, The time constant of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios (n = 22). D, I–V relationships of Kv4.3/KChIP2/DPP6‐L peak current density at plasmid ratio 1:1:1 before and after 10 μM NS5806 (n = 18, * P

Techniques Used: Clone Assay, Transfection, Produced, Plasmid Preparation

DPP6 and KChIP2 subunits confer the modality of I to channel response to NS5806
Figure Legend Snippet: DPP6 and KChIP2 subunits confer the modality of I to channel response to NS5806

Techniques Used:

Analysis on the putative interactions between KChIP2 and DPP6‐L. A 1 , Modeling and docking simulation of putative interactions between DPP6‐Lin and KChIP2 . Homology model of KChIP2. A 2 , The top‐ranked model of the intracellular domain of DPP6‐L (DPP6‐Lin). A 3 , Top‐ranked models of both proteins. A 4 , Best scored model of docking KChIP2 with DPP6‐Lin; putative‐interacting residues are indicated. B 1 , Schematic depiction of DPP6‐L and the location of mutated residues within the putative KChIP2 interaction site. B 2 , Representative recordings of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut currents from HEK293 cells using 500 ms square voltage pulses (from −40 to +40 mV; holding potential is −80 mV). B 3 , The time constants of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut current traces plotted against voltage (** P
Figure Legend Snippet: Analysis on the putative interactions between KChIP2 and DPP6‐L. A 1 , Modeling and docking simulation of putative interactions between DPP6‐Lin and KChIP2 . Homology model of KChIP2. A 2 , The top‐ranked model of the intracellular domain of DPP6‐L (DPP6‐Lin). A 3 , Top‐ranked models of both proteins. A 4 , Best scored model of docking KChIP2 with DPP6‐Lin; putative‐interacting residues are indicated. B 1 , Schematic depiction of DPP6‐L and the location of mutated residues within the putative KChIP2 interaction site. B 2 , Representative recordings of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut currents from HEK293 cells using 500 ms square voltage pulses (from −40 to +40 mV; holding potential is −80 mV). B 3 , The time constants of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut current traces plotted against voltage (** P

Techniques Used:

4) Product Images from "Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex, et al. Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex"

Article Title: Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex, et al. Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex

Journal: The FASEB Journal

doi: 10.1096/fj.201902010RR

Effects of NS5806 on cloned Kv4.3/KChIP2/DPP6‐L channels in HEK293 cells. A, Representative current traces elicited by the depolarizing voltage steps from −40 to +40 mV for 2 seconds from a holding potential of −80 mV at different transfection ratios of Kv4.3: KChIP2: DPP6‐L (Left). The superimposed current traces at +40 mV in the absence and presence of NS5806 are shown on the right. B, Effect of 10 μM NS5806 on the peak current of the Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios, measured at +40 mV. C, The time constant of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios (n = 22). D, I–V relationships of Kv4.3/KChIP2/DPP6‐L peak current density at plasmid ratio 1:1:1 before and after 10 μM NS5806 (n = 18, * P
Figure Legend Snippet: Effects of NS5806 on cloned Kv4.3/KChIP2/DPP6‐L channels in HEK293 cells. A, Representative current traces elicited by the depolarizing voltage steps from −40 to +40 mV for 2 seconds from a holding potential of −80 mV at different transfection ratios of Kv4.3: KChIP2: DPP6‐L (Left). The superimposed current traces at +40 mV in the absence and presence of NS5806 are shown on the right. B, Effect of 10 μM NS5806 on the peak current of the Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios, measured at +40 mV. C, The time constant of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios (n = 22). D, I–V relationships of Kv4.3/KChIP2/DPP6‐L peak current density at plasmid ratio 1:1:1 before and after 10 μM NS5806 (n = 18, * P

Techniques Used: Clone Assay, Transfection, Produced, Plasmid Preparation

DPP6 and KChIP2 subunits confer the modality of I to channel response to NS5806
Figure Legend Snippet: DPP6 and KChIP2 subunits confer the modality of I to channel response to NS5806

Techniques Used:

Analysis on the putative interactions between KChIP2 and DPP6‐L. A 1 , Modeling and docking simulation of putative interactions between DPP6‐Lin and KChIP2 . Homology model of KChIP2. A 2 , The top‐ranked model of the intracellular domain of DPP6‐L (DPP6‐Lin). A 3 , Top‐ranked models of both proteins. A 4 , Best scored model of docking KChIP2 with DPP6‐Lin; putative‐interacting residues are indicated. B 1 , Schematic depiction of DPP6‐L and the location of mutated residues within the putative KChIP2 interaction site. B 2 , Representative recordings of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut currents from HEK293 cells using 500 ms square voltage pulses (from −40 to +40 mV; holding potential is −80 mV). B 3 , The time constants of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut current traces plotted against voltage (** P
Figure Legend Snippet: Analysis on the putative interactions between KChIP2 and DPP6‐L. A 1 , Modeling and docking simulation of putative interactions between DPP6‐Lin and KChIP2 . Homology model of KChIP2. A 2 , The top‐ranked model of the intracellular domain of DPP6‐L (DPP6‐Lin). A 3 , Top‐ranked models of both proteins. A 4 , Best scored model of docking KChIP2 with DPP6‐Lin; putative‐interacting residues are indicated. B 1 , Schematic depiction of DPP6‐L and the location of mutated residues within the putative KChIP2 interaction site. B 2 , Representative recordings of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut currents from HEK293 cells using 500 ms square voltage pulses (from −40 to +40 mV; holding potential is −80 mV). B 3 , The time constants of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut current traces plotted against voltage (** P

Techniques Used:

5) Product Images from "Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex, et al. Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex"

Article Title: Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex, et al. Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex

Journal: The FASEB Journal

doi: 10.1096/fj.201902010RR

Effects of NS5806 on cloned Kv4.3/KChIP2/DPP6‐L channels in HEK293 cells. A, Representative current traces elicited by the depolarizing voltage steps from −40 to +40 mV for 2 seconds from a holding potential of −80 mV at different transfection ratios of Kv4.3: KChIP2: DPP6‐L (Left). The superimposed current traces at +40 mV in the absence and presence of NS5806 are shown on the right. B, Effect of 10 μM NS5806 on the peak current of the Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios, measured at +40 mV. C, The time constant of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios (n = 22). D, I–V relationships of Kv4.3/KChIP2/DPP6‐L peak current density at plasmid ratio 1:1:1 before and after 10 μM NS5806 (n = 18, * P
Figure Legend Snippet: Effects of NS5806 on cloned Kv4.3/KChIP2/DPP6‐L channels in HEK293 cells. A, Representative current traces elicited by the depolarizing voltage steps from −40 to +40 mV for 2 seconds from a holding potential of −80 mV at different transfection ratios of Kv4.3: KChIP2: DPP6‐L (Left). The superimposed current traces at +40 mV in the absence and presence of NS5806 are shown on the right. B, Effect of 10 μM NS5806 on the peak current of the Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios, measured at +40 mV. C, The time constant of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios (n = 22). D, I–V relationships of Kv4.3/KChIP2/DPP6‐L peak current density at plasmid ratio 1:1:1 before and after 10 μM NS5806 (n = 18, * P

Techniques Used: Clone Assay, Transfection, Produced, Plasmid Preparation

DPP6 and KChIP2 subunits confer the modality of I to channel response to NS5806
Figure Legend Snippet: DPP6 and KChIP2 subunits confer the modality of I to channel response to NS5806

Techniques Used:

Analysis on the putative interactions between KChIP2 and DPP6‐L. A 1 , Modeling and docking simulation of putative interactions between DPP6‐Lin and KChIP2 . Homology model of KChIP2. A 2 , The top‐ranked model of the intracellular domain of DPP6‐L (DPP6‐Lin). A 3 , Top‐ranked models of both proteins. A 4 , Best scored model of docking KChIP2 with DPP6‐Lin; putative‐interacting residues are indicated. B 1 , Schematic depiction of DPP6‐L and the location of mutated residues within the putative KChIP2 interaction site. B 2 , Representative recordings of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut currents from HEK293 cells using 500 ms square voltage pulses (from −40 to +40 mV; holding potential is −80 mV). B 3 , The time constants of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut current traces plotted against voltage (** P
Figure Legend Snippet: Analysis on the putative interactions between KChIP2 and DPP6‐L. A 1 , Modeling and docking simulation of putative interactions between DPP6‐Lin and KChIP2 . Homology model of KChIP2. A 2 , The top‐ranked model of the intracellular domain of DPP6‐L (DPP6‐Lin). A 3 , Top‐ranked models of both proteins. A 4 , Best scored model of docking KChIP2 with DPP6‐Lin; putative‐interacting residues are indicated. B 1 , Schematic depiction of DPP6‐L and the location of mutated residues within the putative KChIP2 interaction site. B 2 , Representative recordings of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut currents from HEK293 cells using 500 ms square voltage pulses (from −40 to +40 mV; holding potential is −80 mV). B 3 , The time constants of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut current traces plotted against voltage (** P

Techniques Used:

6) Product Images from "Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex, et al. Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex"

Article Title: Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex, et al. Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex

Journal: The FASEB Journal

doi: 10.1096/fj.201902010RR

Effects of NS5806 on cloned Kv4.3/KChIP2/DPP6‐L channels in HEK293 cells. A, Representative current traces elicited by the depolarizing voltage steps from −40 to +40 mV for 2 seconds from a holding potential of −80 mV at different transfection ratios of Kv4.3: KChIP2: DPP6‐L (Left). The superimposed current traces at +40 mV in the absence and presence of NS5806 are shown on the right. B, Effect of 10 μM NS5806 on the peak current of the Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios, measured at +40 mV. C, The time constant of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios (n = 22). D, I–V relationships of Kv4.3/KChIP2/DPP6‐L peak current density at plasmid ratio 1:1:1 before and after 10 μM NS5806 (n = 18, * P
Figure Legend Snippet: Effects of NS5806 on cloned Kv4.3/KChIP2/DPP6‐L channels in HEK293 cells. A, Representative current traces elicited by the depolarizing voltage steps from −40 to +40 mV for 2 seconds from a holding potential of −80 mV at different transfection ratios of Kv4.3: KChIP2: DPP6‐L (Left). The superimposed current traces at +40 mV in the absence and presence of NS5806 are shown on the right. B, Effect of 10 μM NS5806 on the peak current of the Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios, measured at +40 mV. C, The time constant of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios (n = 22). D, I–V relationships of Kv4.3/KChIP2/DPP6‐L peak current density at plasmid ratio 1:1:1 before and after 10 μM NS5806 (n = 18, * P

Techniques Used: Clone Assay, Transfection, Produced, Plasmid Preparation

DPP6 and KChIP2 subunits confer the modality of I to channel response to NS5806
Figure Legend Snippet: DPP6 and KChIP2 subunits confer the modality of I to channel response to NS5806

Techniques Used:

Analysis on the putative interactions between KChIP2 and DPP6‐L. A 1 , Modeling and docking simulation of putative interactions between DPP6‐Lin and KChIP2 . Homology model of KChIP2. A 2 , The top‐ranked model of the intracellular domain of DPP6‐L (DPP6‐Lin). A 3 , Top‐ranked models of both proteins. A 4 , Best scored model of docking KChIP2 with DPP6‐Lin; putative‐interacting residues are indicated. B 1 , Schematic depiction of DPP6‐L and the location of mutated residues within the putative KChIP2 interaction site. B 2 , Representative recordings of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut currents from HEK293 cells using 500 ms square voltage pulses (from −40 to +40 mV; holding potential is −80 mV). B 3 , The time constants of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut current traces plotted against voltage (** P
Figure Legend Snippet: Analysis on the putative interactions between KChIP2 and DPP6‐L. A 1 , Modeling and docking simulation of putative interactions between DPP6‐Lin and KChIP2 . Homology model of KChIP2. A 2 , The top‐ranked model of the intracellular domain of DPP6‐L (DPP6‐Lin). A 3 , Top‐ranked models of both proteins. A 4 , Best scored model of docking KChIP2 with DPP6‐Lin; putative‐interacting residues are indicated. B 1 , Schematic depiction of DPP6‐L and the location of mutated residues within the putative KChIP2 interaction site. B 2 , Representative recordings of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut currents from HEK293 cells using 500 ms square voltage pulses (from −40 to +40 mV; holding potential is −80 mV). B 3 , The time constants of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut current traces plotted against voltage (** P

Techniques Used:

7) Product Images from "Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex, et al. Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex"

Article Title: Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex, et al. Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex

Journal: The FASEB Journal

doi: 10.1096/fj.201902010RR

Effects of NS5806 on cloned Kv4.3/KChIP2/DPP6‐L channels in HEK293 cells. A, Representative current traces elicited by the depolarizing voltage steps from −40 to +40 mV for 2 seconds from a holding potential of −80 mV at different transfection ratios of Kv4.3: KChIP2: DPP6‐L (Left). The superimposed current traces at +40 mV in the absence and presence of NS5806 are shown on the right. B, Effect of 10 μM NS5806 on the peak current of the Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios, measured at +40 mV. C, The time constant of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios (n = 22). D, I–V relationships of Kv4.3/KChIP2/DPP6‐L peak current density at plasmid ratio 1:1:1 before and after 10 μM NS5806 (n = 18, * P
Figure Legend Snippet: Effects of NS5806 on cloned Kv4.3/KChIP2/DPP6‐L channels in HEK293 cells. A, Representative current traces elicited by the depolarizing voltage steps from −40 to +40 mV for 2 seconds from a holding potential of −80 mV at different transfection ratios of Kv4.3: KChIP2: DPP6‐L (Left). The superimposed current traces at +40 mV in the absence and presence of NS5806 are shown on the right. B, Effect of 10 μM NS5806 on the peak current of the Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios, measured at +40 mV. C, The time constant of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios (n = 22). D, I–V relationships of Kv4.3/KChIP2/DPP6‐L peak current density at plasmid ratio 1:1:1 before and after 10 μM NS5806 (n = 18, * P

Techniques Used: Clone Assay, Transfection, Produced, Plasmid Preparation

DPP6 and KChIP2 subunits confer the modality of I to channel response to NS5806
Figure Legend Snippet: DPP6 and KChIP2 subunits confer the modality of I to channel response to NS5806

Techniques Used:

Analysis on the putative interactions between KChIP2 and DPP6‐L. A 1 , Modeling and docking simulation of putative interactions between DPP6‐Lin and KChIP2 . Homology model of KChIP2. A 2 , The top‐ranked model of the intracellular domain of DPP6‐L (DPP6‐Lin). A 3 , Top‐ranked models of both proteins. A 4 , Best scored model of docking KChIP2 with DPP6‐Lin; putative‐interacting residues are indicated. B 1 , Schematic depiction of DPP6‐L and the location of mutated residues within the putative KChIP2 interaction site. B 2 , Representative recordings of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut currents from HEK293 cells using 500 ms square voltage pulses (from −40 to +40 mV; holding potential is −80 mV). B 3 , The time constants of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut current traces plotted against voltage (** P
Figure Legend Snippet: Analysis on the putative interactions between KChIP2 and DPP6‐L. A 1 , Modeling and docking simulation of putative interactions between DPP6‐Lin and KChIP2 . Homology model of KChIP2. A 2 , The top‐ranked model of the intracellular domain of DPP6‐L (DPP6‐Lin). A 3 , Top‐ranked models of both proteins. A 4 , Best scored model of docking KChIP2 with DPP6‐Lin; putative‐interacting residues are indicated. B 1 , Schematic depiction of DPP6‐L and the location of mutated residues within the putative KChIP2 interaction site. B 2 , Representative recordings of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut currents from HEK293 cells using 500 ms square voltage pulses (from −40 to +40 mV; holding potential is −80 mV). B 3 , The time constants of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut current traces plotted against voltage (** P

Techniques Used:

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    Boston Therapeutics kchip2
    Effects of NS5806 on cloned <t>Kv4.3/KChIP2/DPP6‐L</t> channels in HEK293 cells. A, Representative current traces elicited by the depolarizing voltage steps from −40 to +40 mV for 2 seconds from a holding potential of −80 mV at different transfection ratios of Kv4.3: KChIP2: DPP6‐L (Left). The superimposed current traces at +40 mV in the absence and presence of NS5806 are shown on the right. B, Effect of 10 μM NS5806 on the peak current of the Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios, measured at +40 mV. C, The time constant of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios (n = 22). D, I–V relationships of Kv4.3/KChIP2/DPP6‐L peak current density at plasmid ratio 1:1:1 before and after 10 μM NS5806 (n = 18, * P
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    Effects of NS5806 on cloned Kv4.3/KChIP2/DPP6‐L channels in HEK293 cells. A, Representative current traces elicited by the depolarizing voltage steps from −40 to +40 mV for 2 seconds from a holding potential of −80 mV at different transfection ratios of Kv4.3: KChIP2: DPP6‐L (Left). The superimposed current traces at +40 mV in the absence and presence of NS5806 are shown on the right. B, Effect of 10 μM NS5806 on the peak current of the Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios, measured at +40 mV. C, The time constant of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios (n = 22). D, I–V relationships of Kv4.3/KChIP2/DPP6‐L peak current density at plasmid ratio 1:1:1 before and after 10 μM NS5806 (n = 18, * P

    Journal: The FASEB Journal

    Article Title: Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex, et al. Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex

    doi: 10.1096/fj.201902010RR

    Figure Lengend Snippet: Effects of NS5806 on cloned Kv4.3/KChIP2/DPP6‐L channels in HEK293 cells. A, Representative current traces elicited by the depolarizing voltage steps from −40 to +40 mV for 2 seconds from a holding potential of −80 mV at different transfection ratios of Kv4.3: KChIP2: DPP6‐L (Left). The superimposed current traces at +40 mV in the absence and presence of NS5806 are shown on the right. B, Effect of 10 μM NS5806 on the peak current of the Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios, measured at +40 mV. C, The time constant of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L currents produced by different subunit transfection ratios (n = 22). D, I–V relationships of Kv4.3/KChIP2/DPP6‐L peak current density at plasmid ratio 1:1:1 before and after 10 μM NS5806 (n = 18, * P

    Article Snippet: This may be the reason why the association between two subunits could hamper binding of NS5806 to KChIP2 and promote binding to DPP6‐L instead.

    Techniques: Clone Assay, Transfection, Produced, Plasmid Preparation

    DPP6 and KChIP2 subunits confer the modality of I to channel response to NS5806

    Journal: The FASEB Journal

    Article Title: Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex, et al. Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex

    doi: 10.1096/fj.201902010RR

    Figure Lengend Snippet: DPP6 and KChIP2 subunits confer the modality of I to channel response to NS5806

    Article Snippet: This may be the reason why the association between two subunits could hamper binding of NS5806 to KChIP2 and promote binding to DPP6‐L instead.

    Techniques:

    Analysis on the putative interactions between KChIP2 and DPP6‐L. A 1 , Modeling and docking simulation of putative interactions between DPP6‐Lin and KChIP2 . Homology model of KChIP2. A 2 , The top‐ranked model of the intracellular domain of DPP6‐L (DPP6‐Lin). A 3 , Top‐ranked models of both proteins. A 4 , Best scored model of docking KChIP2 with DPP6‐Lin; putative‐interacting residues are indicated. B 1 , Schematic depiction of DPP6‐L and the location of mutated residues within the putative KChIP2 interaction site. B 2 , Representative recordings of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut currents from HEK293 cells using 500 ms square voltage pulses (from −40 to +40 mV; holding potential is −80 mV). B 3 , The time constants of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut current traces plotted against voltage (** P

    Journal: The FASEB Journal

    Article Title: Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex, et al. Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex

    doi: 10.1096/fj.201902010RR

    Figure Lengend Snippet: Analysis on the putative interactions between KChIP2 and DPP6‐L. A 1 , Modeling and docking simulation of putative interactions between DPP6‐Lin and KChIP2 . Homology model of KChIP2. A 2 , The top‐ranked model of the intracellular domain of DPP6‐L (DPP6‐Lin). A 3 , Top‐ranked models of both proteins. A 4 , Best scored model of docking KChIP2 with DPP6‐Lin; putative‐interacting residues are indicated. B 1 , Schematic depiction of DPP6‐L and the location of mutated residues within the putative KChIP2 interaction site. B 2 , Representative recordings of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut currents from HEK293 cells using 500 ms square voltage pulses (from −40 to +40 mV; holding potential is −80 mV). B 3 , The time constants of inactivation ( τ ) of Kv4.3/KChIP2/DPP6‐L‐WT and Kv4.3/KChIP2/DPP6‐L‐Mut current traces plotted against voltage (** P

    Article Snippet: This may be the reason why the association between two subunits could hamper binding of NS5806 to KChIP2 and promote binding to DPP6‐L instead.

    Techniques: