Pages that link to "Q74190477"

The following pages link to The putative vitamin K-dependent gamma-glutamyl carboxylase internal propeptide appears to be the propeptide binding site (Q74190477):

Displaying 17 items.

• Structural and functional insights into enzymes of the vitamin K cycle (Q28086880) (← links)
• Identification of the gene for vitamin K epoxide reductase (Q28242592) (← links)
• The vitamin K cycle (Q28274345) (← links)
• Vitamin K-dependent carboxylation (Q28274354) (← links)
• Vitamin K-dependent gamma-glutamylcarboxylation: an ancient posttranslational modification (Q28274366) (← links)
• Warfarin Pharmacogenetics: New Life for an Old Drug (Q28468726) (← links)
• Transmembrane domain interactions and residue proline 378 are essential for proper structure, especially disulfide bond formation, in the human vitamin K-dependent gamma-glutamyl carboxylase. (Q33607356) (← links)
• Pharmacogenetics of warfarin: challenges and opportunities (Q33819050) (← links)
• Mutations in the GGCX and ABCC6 genes in a family with pseudoxanthoma elasticum-like phenotypes (Q33979143) (← links)
• Gla-rich protein (GRP), a new vitamin K-dependent protein identified from sturgeon cartilage and highly conserved in vertebrates (Q34845780) (← links)
• Vitamin K-dependent proteins in Ciona intestinalis, a basal chordate lacking a blood coagulation cascade (Q35127469) (← links)
• Characterization of vitamin K-dependent carboxylase mutations that cause bleeding and nonbleeding disorders (Q36800446) (← links)
• Identification of the N-linked glycosylation sites of vitamin K-dependent carboxylase and effect of glycosylation on carboxylase function (Q37640662) (← links)
• A conformational investigation of propeptide binding to the integral membrane protein γ-glutamyl carboxylase using nanodisc hydrogen exchange mass spectrometry (Q38569603) (← links)
• Characteristics of recombinant W501S mutated human gamma-glutamyl carboxylase (Q40564169) (← links)
• Insight into the coupling mechanism of the vitamin K-dependent carboxylase: mutation of histidine 160 disrupts glutamic acid carbanion formation and efficient coupling of vitamin K epoxidation to glutamic acid carboxylation (Q41879585) (← links)
• Binding of the factor IX gamma-carboxyglutamic acid domain to the vitamin K-dependent gamma-glutamyl carboxylase active site induces an allosteric effect that may ensure processive carboxylation and regulate the release of carboxylated product (Q44683481) (← links)