Ken Eum

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{{Template: Sack Lab}}
{{Template: Sack Lab}}
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Research Interests:
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Regulation of voltage gated ion channels.
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Using enhanced tarantula toxins to modulate voltage gated potassium channels.
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The physiological functions of voltage gated potassium (Kv) channels are not well understood.  To better understand the roles of Kv channels, one must first determine pharmacological drugs that intrinsically have a high affinity for certain Kv channels (there are 40 different subtypes).  By modifying these high affinity allosteric inhibitors of Kv channels, I will be able to minimize the promiscuity these drugs and make them highly specific for one certain Kv subtype.  Doing so will allow me to unravel the conundrums of Kv channel physiology.  I am currently studying a mutant form of a tarantula toxin called Guangxitoxin (GxTX) to determine the physiological function of Kv2.1 channels.
The physiological functions of voltage gated potassium (Kv) channels are not well understood.  To better understand the roles of Kv channels, one must first determine pharmacological drugs that intrinsically have a high affinity for certain Kv channels (there are 40 different subtypes).  By modifying these high affinity allosteric inhibitors of Kv channels, I will be able to minimize the promiscuity these drugs and make them highly specific for one certain Kv subtype.  Doing so will allow me to unravel the conundrums of Kv channel physiology.  I am currently studying a mutant form of a tarantula toxin called Guangxitoxin (GxTX) to determine the physiological function of Kv2.1 channels.

Revision as of 18:10, 21 December 2012


Sack and Yarov-Yarovoy Labs

Department of Physiology and Membrane Biology
University of California, Davis

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Research Interests: Regulation of voltage gated ion channels. Using enhanced tarantula toxins to modulate voltage gated potassium channels.

The physiological functions of voltage gated potassium (Kv) channels are not well understood. To better understand the roles of Kv channels, one must first determine pharmacological drugs that intrinsically have a high affinity for certain Kv channels (there are 40 different subtypes). By modifying these high affinity allosteric inhibitors of Kv channels, I will be able to minimize the promiscuity these drugs and make them highly specific for one certain Kv subtype. Doing so will allow me to unravel the conundrums of Kv channel physiology. I am currently studying a mutant form of a tarantula toxin called Guangxitoxin (GxTX) to determine the physiological function of Kv2.1 channels.

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