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2 support by genetically engineered 3T3 is not vitamin K dependent, and soluble recombinant GAS6 does n
6 domain, a membrane-anchoring domain found on vitamin K-dependent blood coagulation and regulatory pro
8 the bloodstream, Ad vectors can bind several vitamin K-dependent blood coagulation factors, which con
10 arboxylase gene, and hence the regulation of vitamin K-dependent blood coagulation protein synthesis.
12 ntial post-translational modification of the vitamin K-dependent blood coagulation proteins, the regu
18 mma-carboxylases argue for conservation of a vitamin K-dependent carboxylase across animal species an
19 is cDNA in COS cells or insect cells yielded vitamin K-dependent carboxylase activity and vitamin K-d
22 us is the sole invertebrate wherein both the vitamin K-dependent carboxylase and its product, gamma-c
25 g [(3)H]-N-ethylmaleimide indicated that the vitamin K-dependent carboxylase contains two or three fr
26 ian vitamin K-dependent carboxylases and the vitamin K-dependent carboxylase from Conus textile, a ma
27 ts demonstrate the broad distribution of the vitamin K-dependent carboxylase gene, including a highly
30 odendrocytes nor neurons possess significant vitamin K-dependent carboxylase or epoxidase activity.
36 Given the functional similarity of mammalian vitamin K-dependent carboxylases and the vitamin K-depen
37 KORC1L1 reduces vitamin K epoxide to support vitamin K-dependent carboxylation as efficiently as does
38 he diversity of animal species that maintain vitamin K-dependent carboxylation to generate gamma-carb
39 ements beyond the Gla domain of factor IX in vitamin K-dependent carboxylation, we have examined the
40 reductase (VKOR) is an essential enzyme for vitamin K-dependent carboxylation, while the physiologic
41 rrhage and normal functional activity of the vitamin K-dependent clotting factors IX, X, and prothrom
42 ited capacity, and cell lines overexpressing vitamin K-dependent clotting factors produce only a frac
45 gs have been encountered in association with vitamin K-dependent coagulation factor deficiency, an au
47 e novel insight into mechanisms by which the vitamin K-dependent coagulation factors are regulated.
49 including the binding of Ad to platelets and vitamin K-dependent coagulation factors, but we found th
50 In this study, we examined whether other vitamin K-dependent coagulation protease zymogens can mo
52 yme complex formation with gla variants of a vitamin K-dependent coagulation protein and provides evi
54 evaluate Ca2+-specific adsorption of several vitamin K-dependent coagulation proteins to monolayers t
57 bit calcification requires the activity of a vitamin K-dependent enzyme, which mediates MGP carboxyla
61 and < 1% on warfarin, at a point where other vitamin K-dependent factors were at 30-40% activity leve
64 binding of the cationic PF4 to the anionic, vitamin K- dependent gamma-carboxyglutamic acid domain o
66 between the Conus carboxylase and vertebrate vitamin K-dependent gamma-carboxylases argue for conserv
67 anticoagulant factor protein S is a secreted vitamin K-dependent gamma-carboxylated protein that is m
68 ding has been shown to be dependent upon the vitamin K-dependent gamma-carboxylation modification of
73 ngineering of cells containing a recombinant vitamin K-dependent gamma-carboxylation system with enha
74 d vitamin K cofactor-producing enzyme of the vitamin K-dependent gamma-carboxylation system, produced
76 in place of Gla is a poor substrate for the vitamin K-dependent gamma-glutamyl carboxylase (apparent
77 s to gamma-carboxyglutamic acid (Gla) by the vitamin K-dependent gamma-glutamyl carboxylase (gamma-ca
85 xin epsilon-TxIX and used in assays with the vitamin K-dependent gamma-glutamyl carboxylase from C. t
88 (residues 1-345 and residues 346-758) of the vitamin K-dependent gamma-glutamyl carboxylase, a glycop
89 n K antagonists such as warfarin inhibit the vitamin K-dependent gamma-glutamyl carboxylation during
90 emonstrate the evolutionary emergence of the vitamin K-dependent Gla domain before the divergence of
94 inalis as a model organism for investigating vitamin K-dependent physiological phenomena, which may b
101 in the endoplasmic reticulum (ER), catalyzes vitamin K-dependent posttranslational modification of gl
103 ormation, expression, and propagation of the vitamin K-dependent procoagulant complexes and extends o
105 rfarin resistance to rat chromosome 1 and of vitamin K-dependent protein deficiencies to the syntenic
106 utamic acid protein (MGP) is a member of the vitamin K-dependent protein family with unique structura
108 in K antagonists on the functionality of the vitamin K-dependent protein produced by extrahepatic tis
109 anin-A[rs9658644], Cystatin-C[rs2424577] and Vitamin K-Dependent Protein S[rs6123] in the schizophren
110 equired for carboxylase activity, called the vitamin K-dependent protein site of interaction (VKS).
112 Activation of Axl by its ligand Gas6, a vitamin K-dependent protein, is inhibited at doses of wa
113 his contrasts with bone Gla protein, another vitamin K-dependent protein, which appears not to requir
115 at factor-X-encoding cDNA revealed that this vitamin-K-dependent protein has a dibasic Arg-Arg sequen
116 ilic ligand, Gas6, a member of the family of vitamin K dependent proteins that is preferentially expr
117 ults suggest features of membrane binding by vitamin K-dependent proteins and provide reagents that m
118 physiological consequences in the levels of vitamin K-dependent proteins and the biochemical mechani
121 ities of synthetic propeptides of nine human vitamin K-dependent proteins by determining the inhibiti
126 in individuals with combined deficiencies of vitamin K-dependent proteins have a mutation, L394R, in
129 presence of activation peptides (AP) of the vitamin K-dependent proteins in the phlebotomy blood of
130 r gamma-carboxyglutamic acid modification of vitamin K-dependent proteins includes gamma-carboxylase
131 dent carboxylase modifies and renders active vitamin K-dependent proteins involved in hemostasis, cel
133 modification of the membrane contact site of vitamin K-dependent proteins may enhance the membrane af
138 peptide and the propeptides of the mammalian vitamin K-dependent proteins show no obvious sequence ho
140 istent with studies on prothrombin and other vitamin K-dependent proteins that have been modified or
145 tion is strongly dependent on the binding of vitamin K-dependent proteins to cell membranes containin
147 hat the affinities of the propeptides of the vitamin K-dependent proteins vary over a considerable ra
149 raction by prothrombin, protein Z, and other vitamin K-dependent proteins were studied to determine t
150 tion of select glutamic acid residues of the vitamin K-dependent proteins which are important for coa
151 ated Glu (Gla) to activate a large number of vitamin K-dependent proteins with diverse functions, and
152 ding properties of human and bovine forms of vitamin K-dependent proteins Z, S, and C were characteri
153 ree new factors interpreted as inflammation, vitamin K-dependent proteins, and procoagulant activity.
154 s involved in the gamma-carboxylation of the vitamin K-dependent proteins, and vitamin K epoxide is a
155 e carboxylation and consequent activation of vitamin K-dependent proteins, but the mechanism of reduc
156 sible for post-translational modification of vitamin K-dependent proteins, converting them to Gla-con
157 shared to some degree by factor X and other vitamin K-dependent proteins, most notably prothrombin.
174 activated by gamma-glutamyl carboxylation, a vitamin K-dependent reaction, to serve in an anti-minera
176 nd 2 are the founding members of a family of vitamin K-dependent single-pass integral membrane protei
177 fication of select glutamate residues of its vitamin K-dependent substrates to gamma-carboxyglutamate
178 terrogans genome revealed an ortholog of the vitamin K-dependent (VKD) carboxylase as one of several
185 nts governing the modification of individual vitamin K-dependent (VKD) proteins by the carboxylase ha
191 ycles vitamin K to support the activation of vitamin K-dependent (VKD) proteins, which have diverse f
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