Ian H. Kimball
YOU?
Author Swipe
View article: Molecular determinants of μ-conotoxin KIIIA interaction with the human voltage-gated sodium channel NaV1.7
Molecular determinants of μ-conotoxin KIIIA interaction with the human voltage-gated sodium channel NaV1.7 Open
The voltage-gated sodium (Na V ) channel subtype Na V 1.7 plays a critical role in pain signaling, making it an important drug target. Here we studied the molecular interactions between μ-Conotoxin KIIIA (KIIIA) and the human Na V 1.7 chan…
View article: Molecular Determinants of μ-Conotoxin KIIIA Interaction with the Human Voltage-Gated Sodium Channel NaV1.7
Molecular Determinants of μ-Conotoxin KIIIA Interaction with the Human Voltage-Gated Sodium Channel NaV1.7 Open
The voltage-gated sodium (Na V ) channel subtype Na V 1.7 plays a critical role in pain signaling, making it an important drug target. Here we studied the molecular interactions between μ-conotoxin KIIIA (KIIIA) and the human Na V 1.7 chan…
View article: Synthetic Analogues of the Snail Toxin 6-Bromo-2-mercaptotryptamine Dimer (BrMT) Reveal That Lipid Bilayer Perturbation Does Not Underlie Its Modulation of Voltage-Gated Potassium Channels
Synthetic Analogues of the Snail Toxin 6-Bromo-2-mercaptotryptamine Dimer (BrMT) Reveal That Lipid Bilayer Perturbation Does Not Underlie Its Modulation of Voltage-Gated Potassium Channels Open
Drugs do not act solely by canonical ligand-receptor binding interactions. Amphiphilic drugs partition into membranes, thereby perturbing bulk lipid bilayer properties and possibly altering the function of membrane proteins. Distinguishing…
View article: Synthetic Analogs of the Snail Toxin 6-Bromo-2-Mercaptotryptamine Dimer (BrMT) Reveal That Lipid Bilayer Perturbation Does Not Underlie Its Modulation of Voltage-Gated Potassium Channels
Synthetic Analogs of the Snail Toxin 6-Bromo-2-Mercaptotryptamine Dimer (BrMT) Reveal That Lipid Bilayer Perturbation Does Not Underlie Its Modulation of Voltage-Gated Potassium Channels Open
Distinguishing membrane perturbation from more direct protein-ligand interactions is an ongoing challenge in chemical biology. Herein, we present one strategy for doing so, using dimeric 6-bromo-2-mercaptotryptamine (BrMT) and synthetic an…
View article: Synthetic Analogs of the Snail Toxin 6-Bromo-2-Mercaptotryptamine Dimer (BrMT) Reveal That Lipid Bilayer Perturbation Does Not Underlie Its Modulation of Voltage-Gated Potassium Channels
Synthetic Analogs of the Snail Toxin 6-Bromo-2-Mercaptotryptamine Dimer (BrMT) Reveal That Lipid Bilayer Perturbation Does Not Underlie Its Modulation of Voltage-Gated Potassium Channels Open
Distinguishing membrane perturbation from more direct protein-ligand interactions is an ongoing challenge in chemical biology. Herein, we present one strategy for doing so, using dimeric 6-bromo-2-mercaptotryptamine (BrMT) and synthetic an…
View article: Assessing the Structural Basis of μ-Conotoxin KIIIA Inhibition of the Voltage-Gated Sodium Channel Nav1.7
Assessing the Structural Basis of μ-Conotoxin KIIIA Inhibition of the Voltage-Gated Sodium Channel Nav1.7 Open
View article: Tarantula Toxin SGTx-1 alters Gating Kinetics of Human Voltage-Gated Sodium Channel Nav1.7
Tarantula Toxin SGTx-1 alters Gating Kinetics of Human Voltage-Gated Sodium Channel Nav1.7 Open
View article: Lipid Bilayer Perturbation by the Snail Toxin 6-Bromo-2-Mercaptotryptamine Dimer does not Account for its Modulation of Voltage-Gated Potassium Channels
Lipid Bilayer Perturbation by the Snail Toxin 6-Bromo-2-Mercaptotryptamine Dimer does not Account for its Modulation of Voltage-Gated Potassium Channels Open
View article: Mapping the Nav1.7 Channel Interaction with the Conotoxin KIIIA
Mapping the Nav1.7 Channel Interaction with the Conotoxin KIIIA Open
View article: Understanding the State Dependence of Voltage Sensor Toxin Action on Voltage Gated Sodium Channels
Understanding the State Dependence of Voltage Sensor Toxin Action on Voltage Gated Sodium Channels Open