On a potential global role for vitamin K-dependent gamma-carboxylation in animal systems. Evidence for a gamma-glutamyl carboxylase in Drosophila.
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Protein stability: a crystallographer's perspectiveMolecular characterization of major cat allergen Fel d 1: expression of heterodimer by use of a baculovirus expression system.Characterization of the peptidylglycine α-amidating monooxygenase (PAM) from the venom ducts of neogastropods, Conus bullatus and Conus geographus.Evolution of matrix and bone gamma-carboxyglutamic acid proteins in vertebrates.gamma -Glutamyl carboxylation: An extracellular posttranslational modification that antedates the divergence of molluscs, arthropods, and chordates.The first gamma-carboxyglutamic acid-containing contryphan. A selective L-type calcium ion channel blocker isolated from the venom of Conus marmoreus.Gla-rich protein (GRP), a new vitamin K-dependent protein identified from sturgeon cartilage and highly conserved in vertebrates.The vitamin K-dependent carboxylase generates γ-carboxylated glutamates by using CO2 to facilitate glutamate deprotonation in a concerted mechanism that drives catalysis.Targeted mutagenesis by homologous recombination in D. melanogaster.Compound heterozygosity of novel missense mutations in the gamma-glutamyl-carboxylase gene causes hereditary combined vitamin K-dependent coagulation factor deficiencyA new model for vitamin K-dependent carboxylation: the catalytic base that deprotonates vitamin K hydroquinone is not Cys but an activated amine.Biochemical characterization of Drosophila gamma-glutamyl carboxylase and its role in fly development.Expression and characterization of recombinant vitamin K-dependent gamma-glutamyl carboxylase from an invertebrate, Conus textile.Identification of sequences within the gamma-carboxylase that represent a novel contact site with vitamin K-dependent proteins and that are required for activity.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.Multicomponent supramolecular systems: self-organization in coordination-driven self-assembly.The vitamin K-dependent carboxylase has been acquired by Leptospira pathogens and shows altered activity that suggests a role other than protein carboxylation.Identification of a gene encoding a typical gamma-carboxyglutamic acid domain in the tunicate Halocynthia roretzi.A conserved region of human vitamin K-dependent carboxylase between residues 393 and 404 is important for its interaction with the glutamate substrate.Successful synthesis of active human coagulation factor VII by co-expression of mammalian gamma-glutamyl carboxylase and modification of vit.K cycle in Drosophila Schneider S2 cells.
P2860
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P2860
On a potential global role for vitamin K-dependent gamma-carboxylation in animal systems. Evidence for a gamma-glutamyl carboxylase in Drosophila.
description
2000 nî lūn-bûn
@nan
2000 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
On a potential global role for ...... myl carboxylase in Drosophila.
@ast
On a potential global role for ...... myl carboxylase in Drosophila.
@en
type
label
On a potential global role for ...... myl carboxylase in Drosophila.
@ast
On a potential global role for ...... myl carboxylase in Drosophila.
@en
prefLabel
On a potential global role for ...... myl carboxylase in Drosophila.
@ast
On a potential global role for ...... myl carboxylase in Drosophila.
@en
P2093
P2860
P356
P1476
On a potential global role for ...... myl carboxylase in Drosophila.
@en
P2093
Bandyopadhyay PK
Olivera BM
P2860
P304
P356
10.1074/JBC.M009576200
P407
P577
2000-12-07T00:00:00Z