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Kurt W Runge

Showing results (21-30 of 36) with videos related to

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Biochemistry|April 26, 2006
r-VKORC1 expression in factor IX BHK cells increases the extent of factor IX carboxylation but is limited by saturation of another carboxylation component or by a shift in the rate-limiting stepKevin W Hallgren, Wen Qian, Anna V Yakubenko, et al.
Nature Cell Biology|July 15, 2009
A two-step model for senescence triggered by a single critically short telomerePauline Abdallah, Pierre Luciano, Kurt W Runge, et al.
Nature Genetics|March 18, 2003
Sir3p phosphorylation by the Slt2p pathway effects redistribution of silencing function and shortened lifespanAlo Ray, Ronald E Hector, Nilanjan Roy, et al.
Blood|March 30, 2018
Warfarin alters vitamin K metabolism: a surprising mechanism of VKORC1 uncoupling necessitates an additional reductaseMark A Rishavy, Kevin W Hallgren, Lee Wilson, et al.
Chromosoma|February 1, 2012
Mec1p associates with functionally compromised telomeresRonald E Hector, Alo Ray, Bo-Ruei Chen, et al.
Molecular and Cellular Biology|May 23, 2018
A Heterochromatin Domain Forms Gradually at a New Telomere and Is Dynamic at Stable TelomeresJinyu Wang, Jessica R Eisenstatt, Julien Audry, et al.
The Journal of Biological Chemistry|August 7, 2013
The vitamin K oxidoreductase is a multimer that efficiently reduces vitamin K epoxide to hydroquinone to allow vitamin K-dependent protein carboxylationMark A Rishavy, Kevin W Hallgren, Lee A Wilson, et al.
Biochemistry|November 1, 2006
Brønsted analysis reveals Lys218 as the carboxylase active site base that deprotonates vitamin K hydroquinone to initiate vitamin K-dependent protein carboxylationMark A Rishavy, Kevin W Hallgren, Anna V Yakubenko, et al.
Blood|June 29, 2022
GGCX mutants that impair hemostasis reveal the importance of processivity and full carboxylation to VKD protein functionMark A Rishavy, Kevin W Hallgren, Lee A Wilson, et al.
The Journal of Biological Chemistry|August 3, 2005
The vitamin K-dependent carboxylase has been acquired by Leptospira pathogens and shows altered activity that suggests a role other than protein carboxylationMark A Rishavy, Kevin W Hallgren, Anna V Yakubenko, et al.
Pageof 4

Showing results (21-30 of 36) with videos related to

Sort By:
Pageof 4
Biochemistry|April 26, 2006
r-VKORC1 expression in factor IX BHK cells increases the extent of factor IX carboxylation but is limited by saturation of another carboxylation component or by a shift in the rate-limiting stepKevin W Hallgren, Wen Qian, Anna V Yakubenko, et al.
Nature Cell Biology|July 15, 2009
A two-step model for senescence triggered by a single critically short telomerePauline Abdallah, Pierre Luciano, Kurt W Runge, et al.
Nature Genetics|March 18, 2003
Sir3p phosphorylation by the Slt2p pathway effects redistribution of silencing function and shortened lifespanAlo Ray, Ronald E Hector, Nilanjan Roy, et al.
Blood|March 30, 2018
Warfarin alters vitamin K metabolism: a surprising mechanism of VKORC1 uncoupling necessitates an additional reductaseMark A Rishavy, Kevin W Hallgren, Lee Wilson, et al.
Chromosoma|February 1, 2012
Mec1p associates with functionally compromised telomeresRonald E Hector, Alo Ray, Bo-Ruei Chen, et al.
Molecular and Cellular Biology|May 23, 2018
A Heterochromatin Domain Forms Gradually at a New Telomere and Is Dynamic at Stable TelomeresJinyu Wang, Jessica R Eisenstatt, Julien Audry, et al.
The Journal of Biological Chemistry|August 7, 2013
The vitamin K oxidoreductase is a multimer that efficiently reduces vitamin K epoxide to hydroquinone to allow vitamin K-dependent protein carboxylationMark A Rishavy, Kevin W Hallgren, Lee A Wilson, et al.
Biochemistry|November 1, 2006
Brønsted analysis reveals Lys218 as the carboxylase active site base that deprotonates vitamin K hydroquinone to initiate vitamin K-dependent protein carboxylationMark A Rishavy, Kevin W Hallgren, Anna V Yakubenko, et al.
Blood|June 29, 2022
GGCX mutants that impair hemostasis reveal the importance of processivity and full carboxylation to VKD protein functionMark A Rishavy, Kevin W Hallgren, Lee A Wilson, et al.
The Journal of Biological Chemistry|August 3, 2005
The vitamin K-dependent carboxylase has been acquired by Leptospira pathogens and shows altered activity that suggests a role other than protein carboxylationMark A Rishavy, Kevin W Hallgren, Anna V Yakubenko, et al.
Pageof 4