Enhanced gamma-carboxylation of recombinant factor X using a chimeric construct containing the prothrombin propeptide.
about
Regulated cleavage of prothrombin by prothrombinase: repositioning a cleavage site reveals the unique kinetic behavior of the action of prothrombinase on its compound substrateRatcheting of the substrate from the zymogen to proteinase conformations directs the sequential cleavage of prothrombin by prothrombinase.The N-terminal epidermal growth factor-like domain in factor IX and factor X represents an important recognition motif for binding to tissue factor.The vitamin K cycle.Restricted active site docking by enzyme-bound substrate enforces the ordered cleavage of prothrombin by prothrombinase.Post-translational modifications in the context of therapeutic proteins.Characterization of vitamin K-dependent carboxylase mutations that cause bleeding and nonbleeding disorders.Industrial production of clotting factors: Challenges of expression, and choice of host cells.A cluster of basic amino acids in the factor X serine protease mediates surface attachment of adenovirus/FX complexes.Functional expression of the human coagulation factor IX using heterologous signal peptide and propeptide sequences in mammalian cell line.Biological Insights into Therapeutic Protein Modifications throughout Trafficking and Their Biopharmaceutical Applications.Stable and high-level production of recombinant Factor IX in human hepatic cell line.The conformational switch from the factor X zymogen to protease state mediates exosite expression and prothrombinase assembly.Galectin 3-binding protein is a potential contaminant of recombinantly produced factor IX.Binding of substrate in two conformations to human prothrombinase drives consecutive cleavage at two sites in prothrombin.Prothrombinase assembly and S1 site occupation restore the catalytic activity of FXa impaired by mutation at the sodium-binding site.Nematode anticoagulant protein c2 reveals a site on factor Xa that is important for macromolecular substrate binding to human prothrombinase.Engineered factor Xa variants retain procoagulant activity independent of direct factor Xa inhibitors.Fate of membrane-bound reactants and products during the activation of human prothrombin by prothrombinase.The endothelial protein C receptor enhances hemostasis of FVIIa administration in hemophilic mice in vivo.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.Thrombin-activable factor X re-establishes an intrinsic amplification in tenase-deficient plasmas.Effect of propeptide amino acid substitution in γ-carboxylation, activity and expression of recombinant human coagulation factor IX.The elusive role of the potential factor X cation-binding exosite-1 in substrate and inhibitor interactions.Formation of factors IXa and Xa by the extrinsic pathway: differential regulation by tissue factor pathway inhibitor and antithrombin III.A rapid pro-hemostatic approach to overcome direct oral anticoagulants.Truncated gamma-glutamyl carboxylase in rambouillet sheep.
P2860
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P2860
Enhanced gamma-carboxylation of recombinant factor X using a chimeric construct containing the prothrombin propeptide.
description
2000 nî lūn-bûn
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2000年の論文
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2000年学术文章
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2000年学术文章
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2000年学术文章
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@zh-sg
2000年學術文章
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name
Enhanced gamma-carboxylation o ...... ng the prothrombin propeptide.
@en
type
label
Enhanced gamma-carboxylation o ...... ng the prothrombin propeptide.
@en
prefLabel
Enhanced gamma-carboxylation o ...... ng the prothrombin propeptide.
@en
P2093
P356
P1433
P1476
Enhanced gamma-carboxylation o ...... ng the prothrombin propeptide.
@en
P2093
P304
14322-14329
P356
10.1021/BI001074Q
P407
P577
2000-11-01T00:00:00Z