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2 support by genetically engineered 3T3 is not vitamin K dependent, and soluble recombinant GAS6 does n
8 domain, a membrane-anchoring domain found on vitamin K-dependent blood coagulation and regulatory pro
10 the bloodstream, Ad vectors can bind several vitamin K-dependent blood coagulation factors, which con
12 arboxylase gene, and hence the regulation of vitamin K-dependent blood coagulation protein synthesis.
14 ntial post-translational modification of the vitamin K-dependent blood coagulation proteins, the regu
20 mma-carboxylases argue for conservation of a vitamin K-dependent carboxylase across animal species an
21 is cDNA in COS cells or insect cells yielded vitamin K-dependent carboxylase activity and vitamin K-d
24 us is the sole invertebrate wherein both the vitamin K-dependent carboxylase and its product, gamma-c
27 g [(3)H]-N-ethylmaleimide indicated that the vitamin K-dependent carboxylase contains two or three fr
28 ian vitamin K-dependent carboxylases and the vitamin K-dependent carboxylase from Conus textile, a ma
29 ts demonstrate the broad distribution of the vitamin K-dependent carboxylase gene, including a highly
32 odendrocytes nor neurons possess significant vitamin K-dependent carboxylase or epoxidase activity.
38 Given the functional similarity of mammalian vitamin K-dependent carboxylases and the vitamin K-depen
39 KORC1L1 reduces vitamin K epoxide to support vitamin K-dependent carboxylation as efficiently as does
40 he diversity of animal species that maintain vitamin K-dependent carboxylation to generate gamma-carb
41 ements beyond the Gla domain of factor IX in vitamin K-dependent carboxylation, we have examined the
42 reductase (VKOR) is an essential enzyme for vitamin K-dependent carboxylation, while the physiologic
46 here for protein C have general relevance to vitamin K-dependent clotting factors containing epiderma
47 rrhage and normal functional activity of the vitamin K-dependent clotting factors IX, X, and prothrom
48 ited capacity, and cell lines overexpressing vitamin K-dependent clotting factors produce only a frac
51 gs have been encountered in association with vitamin K-dependent coagulation factor deficiency, an au
53 e novel insight into mechanisms by which the vitamin K-dependent coagulation factors are regulated.
55 including the binding of Ad to platelets and vitamin K-dependent coagulation factors, but we found th
56 In this study, we examined whether other vitamin K-dependent coagulation protease zymogens can mo
58 yme complex formation with gla variants of a vitamin K-dependent coagulation protein and provides evi
60 carboxylase (GGCX) results in production of vitamin K-dependent coagulation proteins (FII and FX) wi
61 evaluate Ca2+-specific adsorption of several vitamin K-dependent coagulation proteins to monolayers t
64 bit calcification requires the activity of a vitamin K-dependent enzyme, which mediates MGP carboxyla
68 and < 1% on warfarin, at a point where other vitamin K-dependent factors were at 30-40% activity leve
71 binding of the cationic PF4 to the anionic, vitamin K- dependent gamma-carboxyglutamic acid domain o
72 sidues is catalyzed by the membrane-embedded vitamin K-dependent gamma-carboxylase (VKGC), which typi
74 between the Conus carboxylase and vertebrate vitamin K-dependent gamma-carboxylases argue for conserv
75 anticoagulant factor protein S is a secreted vitamin K-dependent gamma-carboxylated protein that is m
76 Human osteocalcin (OC) undergoes reversible, vitamin K-dependent gamma-carboxylation at three glutami
77 ding has been shown to be dependent upon the vitamin K-dependent gamma-carboxylation modification of
82 ngineering of cells containing a recombinant vitamin K-dependent gamma-carboxylation system with enha
83 d vitamin K cofactor-producing enzyme of the vitamin K-dependent gamma-carboxylation system, produced
85 in place of Gla is a poor substrate for the vitamin K-dependent gamma-glutamyl carboxylase (apparent
86 s to gamma-carboxyglutamic acid (Gla) by the vitamin K-dependent gamma-glutamyl carboxylase (gamma-ca
94 xin epsilon-TxIX and used in assays with the vitamin K-dependent gamma-glutamyl carboxylase from C. t
97 (residues 1-345 and residues 346-758) of the vitamin K-dependent gamma-glutamyl carboxylase, a glycop
98 n K antagonists such as warfarin inhibit the vitamin K-dependent gamma-glutamyl carboxylation during
99 cate impairment of the functional, secreted, vitamin K-dependent, gamma-carboxylated form of periosti
100 emonstrate the evolutionary emergence of the vitamin K-dependent Gla domain before the divergence of
106 inalis as a model organism for investigating vitamin K-dependent physiological phenomena, which may b
114 in the endoplasmic reticulum (ER), catalyzes vitamin K-dependent posttranslational modification of gl
116 ormation, expression, and propagation of the vitamin K-dependent procoagulant complexes and extends o
118 rfarin resistance to rat chromosome 1 and of vitamin K-dependent protein deficiencies to the syntenic
119 utamic acid protein (MGP) is a member of the vitamin K-dependent protein family with unique structura
121 in K antagonists on the functionality of the vitamin K-dependent protein produced by extrahepatic tis
122 anin-A[rs9658644], Cystatin-C[rs2424577] and Vitamin K-Dependent Protein S[rs6123] in the schizophren
123 equired for carboxylase activity, called the vitamin K-dependent protein site of interaction (VKS).
125 Activation of Axl by its ligand Gas6, a vitamin K-dependent protein, is inhibited at doses of wa
126 his contrasts with bone Gla protein, another vitamin K-dependent protein, which appears not to requir
129 at factor-X-encoding cDNA revealed that this vitamin-K-dependent protein has a dibasic Arg-Arg sequen
130 ilic ligand, Gas6, a member of the family of vitamin K dependent proteins that is preferentially expr
131 frozen plasma (mFFP), PCC, mixtures of human vitamin K-dependent proteins (VKDP) (prothrombin, FVII,
132 ults suggest features of membrane binding by vitamin K-dependent proteins and provide reagents that m
133 physiological consequences in the levels of vitamin K-dependent proteins and the biochemical mechani
136 ities of synthetic propeptides of nine human vitamin K-dependent proteins by determining the inhibiti
142 in individuals with combined deficiencies of vitamin K-dependent proteins have a mutation, L394R, in
144 itamin K actions, the potential functions of vitamin K-dependent proteins in cancer, and observationa
146 e cancer cells, and an altered expression of vitamin K-dependent proteins in prostate tumors has been
147 presence of activation peptides (AP) of the vitamin K-dependent proteins in the phlebotomy blood of
149 r gamma-carboxyglutamic acid modification of vitamin K-dependent proteins includes gamma-carboxylase
150 dent carboxylase modifies and renders active vitamin K-dependent proteins involved in hemostasis, cel
152 modification of the membrane contact site of vitamin K-dependent proteins may enhance the membrane af
157 peptide and the propeptides of the mammalian vitamin K-dependent proteins show no obvious sequence ho
159 istent with studies on prothrombin and other vitamin K-dependent proteins that have been modified or
164 tion is strongly dependent on the binding of vitamin K-dependent proteins to cell membranes containin
166 hat the affinities of the propeptides of the vitamin K-dependent proteins vary over a considerable ra
168 raction by prothrombin, protein Z, and other vitamin K-dependent proteins were studied to determine t
169 tion of select glutamic acid residues of the vitamin K-dependent proteins which are important for coa
170 ated Glu (Gla) to activate a large number of vitamin K-dependent proteins with diverse functions, and
171 ding properties of human and bovine forms of vitamin K-dependent proteins Z, S, and C were characteri
172 ree new factors interpreted as inflammation, vitamin K-dependent proteins, and procoagulant activity.
173 s involved in the gamma-carboxylation of the vitamin K-dependent proteins, and vitamin K epoxide is a
174 e carboxylation and consequent activation of vitamin K-dependent proteins, but the mechanism of reduc
175 e to the analogous sequence present in other vitamin K-dependent proteins, contains a disproportionat
176 sible for post-translational modification of vitamin K-dependent proteins, converting them to Gla-con
177 shared to some degree by factor X and other vitamin K-dependent proteins, most notably prothrombin.
194 activated by gamma-glutamyl carboxylation, a vitamin K-dependent reaction, to serve in an anti-minera
196 nd 2 are the founding members of a family of vitamin K-dependent single-pass integral membrane protei
197 fication of select glutamate residues of its vitamin K-dependent substrates to gamma-carboxyglutamate
198 terrogans genome revealed an ortholog of the vitamin K-dependent (VKD) carboxylase as one of several
205 nts governing the modification of individual vitamin K-dependent (VKD) proteins by the carboxylase ha
206 sttranslational carboxylation of a number of vitamin K-dependent (VKD) proteins involved in a wide va
211 nerates multiple carboxylated Glus (Glas) in vitamin K-dependent (VKD) proteins that are required for
213 ycles vitamin K to support the activation of vitamin K-dependent (VKD) proteins, which have diverse f
216 of the coagulation cascade, the multidomain vitamin-K-dependent zymogen prothrombin is converted to