Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Mark A. Rishavy"'
Autor:
Mark A. Rishavy, Kevin W. Hallgren, Lee A. Wilson, James M. Hiznay, Kurt W. Runge, Kathleen L. Berkner
Publikováno v:
Blood. 140:1710-1722
γ-Glutamyl carboxylase (GGCX) generates multiple carboxylated Glus (Glas) in vitamin K–dependent (VKD) proteins that are required for their functions. GGCX is processive, remaining bound to VKD proteins throughout multiple Glu carboxylations, and
Autor:
Kevin W. Hallgren, Savita Singh, Kurt W. Runge, Kathleen L. Berkner, Lee Wilson, Mark A. Rishavy
Publikováno v:
Blood. 131:2826-2835
The anticoagulant warfarin inhibits the vitamin K oxidoreductase (VKORC1), which generates vitamin K hydroquinone (KH2) required for the carboxylation and consequent activation of vitamin K-dependent (VKD) proteins. VKORC1 produces KH2 in 2 reactions
Vitamin K-dependent (VKD) protein activities require carboxylated Glus (Glas) generated by the gamma-glutamyl carboxylase. Some carboxylase mutations cause severe bleeding, while others cause pseudoxanthoma elasticum (PXE)-like associated with excess
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9fc5564bfc5fef3fccbfd45f0071160f
Publikováno v:
J Thromb Haemost
Essentials A carboxylase mutation that impairs splicing to delete exon 2 sequences was previously reported. We found that the mutant was inactive for vitamin K-dependent (VKD) protein carboxylation. An incomplete splicing defect likely accounts for V
Vertebrates possess 2 proteins with vitamin K oxidoreductase (VKOR) activity: VKORC1, whose vitamin K reduction supports vitamin K-dependent (VKD) protein carboxylation, and VKORC1-like 1 (VKORC1L1), whose function is unknown. VKD proteins include li
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::efa5830a0a3be010ba2208392189d886
https://europepmc.org/articles/PMC5821188/
https://europepmc.org/articles/PMC5821188/
Autor:
Kurt W. Runge, Lee Wilson, Aisulu Usubalieva, Kevin W. Hallgren, Mark A. Rishavy, Kathleen L. Berkner
Publikováno v:
Journal of Biological Chemistry. 288:31556-31566
The vitamin K oxidoreductase (VKORC1) recycles vitamin K to support the activation of vitamin K-dependent (VKD) proteins, which have diverse functions that include hemostasis and calcification. VKD proteins are activated by Glu carboxylation, which d
Publikováno v:
Journal of Biological Chemistry. 286:7267-7278
The vitamin K oxidoreductase (VKOR) reduces vitamin K to support the carboxylation and consequent activation of vitamin K-dependent proteins, but the mechanism of reduction is poorly understood. VKOR is an integral membrane protein that reduces vitam
Autor:
Alison J. Whelan, Qiaoli Li, Nicole L. Armstrong, Jouni Uitto, Kathleen L. Berkner, Kevin W. Hallgren, Leon J. Schurgers, Mark A. Rishavy, Qiujie Jiang, Maria Yadira Hurley, Dorothy K. Grange
Publikováno v:
Journal of Investigative Dermatology. 129:553-563
A characteristic feature of classic pseudoxanthoma elasticum (PXE), an autosomal recessive disorder caused by mutations in the ABCC6 gene, is aberrant mineralization of connective tissues, particularly the elastic fibers. Here, we report a family wit
Autor:
Mark A. Rishavy, Kathleen L. Berkner
Publikováno v:
Biochemistry. 47:9836-9846
Vitamin K-dependent (VKD) proteins become activated by the VKD carboxylase, which converts Glu’s to carboxylated Glu’s (Gla’s) in their Gla domains. The carboxylase uses vitamin K epoxidation to drive Glu carboxylation, and the two half-reactio
Autor:
Kurt W. Runge, Richard L. Zuerner, Kevin W. Hallgren, Anna V. Yakubenko, Mark A. Rishavy, Kathleen L. Berkner
Publikováno v:
Journal of Biological Chemistry. 280:34870-34877
Leptospirosis is an emerging infectious disease whose pathology includes a hemorrhagic response, and sequencing of the Leptospira interrogans genome revealed an ortholog of the vitamin K-dependent (VKD) carboxylase as one of several hemostatic protei