Ken Eum - Revision history

Kenneth S. Eum at 01:13, 8 January 2013

Kenneth S. Eum — Tue, 08 Jan 2013 01:13:27 GMT

←Older revision		Revision as of 01:13, 8 January 2013
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	{{Template: Sack Lab}}		{{Template: Sack Lab}}
-		+	==Kenneth Eum==
	'''Research Interests:'''<br>		'''Research Interests:'''<br>
	Regulation of voltage gated ion channels.<br>		Regulation of voltage gated ion channels.<br>

Kenneth S. Eum at 22:39, 21 December 2012

Kenneth S. Eum — Fri, 21 Dec 2012 22:39:06 GMT

←Older revision		Revision as of 22:39, 21 December 2012
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	Regulation of voltage gated ion channels.<br>		Regulation of voltage gated ion channels.<br>
	Using enhanced tarantula toxins to modulate voltage gated potassium channels.		Using enhanced tarantula toxins to modulate voltage gated potassium channels.
		+


	'''Research Summary:'''<br>		'''Research Summary:'''<br>
	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.
		+
		+

	'''Education:'''<br>		'''Education:'''<br>

Kenneth S. Eum at 22:22, 21 December 2012

Kenneth S. Eum — Fri, 21 Dec 2012 22:22:08 GMT

←Older revision		Revision as of 22:22, 21 December 2012
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	{{Template: Sack Lab}}		{{Template: Sack Lab}}

-	Research Interests:<br>	+	'''Research Interests:'''<br>
	Regulation of voltage gated ion channels.<br>		Regulation of voltage gated ion channels.<br>
	Using enhanced tarantula toxins to modulate voltage gated potassium channels.		Using enhanced tarantula toxins to modulate voltage gated potassium channels.

-	Research Summary:<br>	+
		+	'''Research Summary:'''<br>
	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.
		+
		+	'''Education:'''<br>
		+	*2005-2009<br>
		+	:UC San Diego<br>
		+	:B.S. Physiology and Neuroscience<br>
		+
		+	*2010-Present<br>
		+	:UC Davis<br>
		+	:PhD Molecular, Cellular, and Integrative Physiology (MCIP)<br>
		+	:Designated Emphasis in Biotechnology (DEB)<br>

Kenneth S. Eum at 22:11, 21 December 2012

Kenneth S. Eum — Fri, 21 Dec 2012 22:11:42 GMT

←Older revision		Revision as of 22:11, 21 December 2012
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	{{Template: Sack Lab}}		{{Template: Sack Lab}}

-	Research Interests:	+	Research Interests:<br>
-	Regulation of voltage gated ion channels.	+	Regulation of voltage gated ion channels.<br>
	Using enhanced tarantula toxins to modulate voltage gated potassium channels.		Using enhanced tarantula toxins to modulate voltage gated potassium channels.

		+	Research Summary:<br>
	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.

Kenneth S. Eum at 22:10, 21 December 2012

Kenneth S. Eum — Fri, 21 Dec 2012 22:10:21 GMT

←Older revision		Revision as of 22:10, 21 December 2012
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	{{Template: Sack Lab}}		{{Template: Sack Lab}}
		+
		+	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.		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.

Kenneth S. Eum at 21:56, 21 December 2012

Kenneth S. Eum — Fri, 21 Dec 2012 21:56:55 GMT

←Older revision		Revision as of 21:56, 21 December 2012
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	{{Template: Sack Lab}}		{{Template: Sack Lab}}
-	~~K-dawg!~~	+	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.

Daniel Clay Austin at 03:36, 13 December 2012

Daniel Clay Austin — Thu, 13 Dec 2012 03:36:55 GMT

←Older revision		Revision as of 03:36, 13 December 2012
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	{{Template: Sack Lab}}		{{Template: Sack Lab}}
	K-dawg!		K-dawg!
-	*Return to [[Sack]] Homepage

Daniel Clay Austin at 03:33, 13 December 2012

Daniel Clay Austin — Thu, 13 Dec 2012 03:33:19 GMT

←Older revision		Revision as of 03:33, 13 December 2012
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		+	{{Template: Sack Lab}}
	K-dawg!		K-dawg!
	*Return to [[Sack]] Homepage		*Return to [[Sack]] Homepage

Jon Sack at 04:09, 26 October 2012

Jon Sack — Fri, 26 Oct 2012 04:09:34 GMT

←Older revision		Revision as of 04:09, 26 October 2012
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		+	K-dawg!
	*Return to [[Sack]] Homepage		*Return to [[Sack]] Homepage

Jon Sack: New page: *Return to Sack Homepage

Jon Sack — Wed, 03 Oct 2012 22:32:30 GMT

New page: *Return to Sack Homepage

New page

*Return to [[Sack]] Homepage