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1                 The carboxylation process is vitamin K dependent, and current evidence suggests that
2 support by genetically engineered 3T3 is not vitamin K dependent, and soluble recombinant GAS6 does n
3                The Drosophila carboxylase is vitamin K-dependent, and it has a K(m) toward a model pe
4                       Protein C, a secretory vitamin K-dependent anticoagulant serine protease, inact
5                                          The vitamin K-dependent biosynthesis of gamma-carboxyglutami
6 domain, a membrane-anchoring domain found on vitamin K-dependent blood coagulation and regulatory pro
7                             Some recombinant vitamin K-dependent blood coagulation factors (factors V
8 the bloodstream, Ad vectors can bind several vitamin K-dependent blood coagulation factors, which con
9 d mechanism, which involves virus binding to vitamin K-dependent blood coagulation factors.
10 arboxylase gene, and hence the regulation of vitamin K-dependent blood coagulation protein synthesis.
11                             Prothrombin is a vitamin K-dependent blood coagulation protein that under
12 ntial post-translational modification of the vitamin K-dependent blood coagulation proteins, the regu
13 n amino acid critical to the function of the vitamin K-dependent blood coagulation proteins.
14       Human factor X is a two-chain, 58-kDa, vitamin K-dependent blood coagulation zymogen.
15      This domain is strongly conserved among vitamin K-dependent blood proteins and, in addition to a
16 rboxyglutamic acid-containing regions of the vitamin K-dependent blood-clotting proteins.
17  properties of matrix Gla protein (MGP) as a vitamin K-dependent calcification inhibitor.
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
20          Assay of hagfish liver demonstrated vitamin K-dependent carboxylase activity in this hemicho
21                                          The vitamin K-dependent carboxylase also catalyzes the epoxi
22 us is the sole invertebrate wherein both the vitamin K-dependent carboxylase and its product, gamma-c
23                                              Vitamin K-dependent carboxylase catalyzes the post-trans
24                                          The vitamin K-dependent carboxylase catalyzes the posttransl
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
28                                          The vitamin K-dependent carboxylase is an integral membrane
29                                          The vitamin K-dependent carboxylase modifies and renders act
30 odendrocytes nor neurons possess significant vitamin K-dependent carboxylase or epoxidase activity.
31                                          The vitamin K-dependent carboxylase was located in the endop
32                            Incubation of the vitamin K-dependent carboxylase with the sulfhydryl-reac
33                                          The vitamin K-dependent carboxylase, a constituent of the en
34                            Using recombinant vitamin K-dependent carboxylase, purified in the absence
35  only known invertebrate with a demonstrated vitamin K-dependent carboxylase.
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
43              The propeptide sequences of the vitamin K-dependent clotting factors serve as a recognit
44 quired for posttranslational modification of vitamin K-dependent clotting factors.
45 gs have been encountered in association with vitamin K-dependent coagulation factor deficiency, an au
46 ings with characteristic features of PXE and vitamin K-dependent coagulation factor deficiency.
47 e novel insight into mechanisms by which the vitamin K-dependent coagulation factors are regulated.
48                                              Vitamin K-dependent coagulation factors deficiency is a
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
51 structural features that distinguish it from vitamin K-dependent coagulation proteases.
52 yme complex formation with gla variants of a vitamin K-dependent coagulation protein and provides evi
53                              Factor VII is a vitamin K-dependent coagulation protein essential for pr
54 evaluate Ca2+-specific adsorption of several vitamin K-dependent coagulation proteins to monolayers t
55 se of decreased biological activities of all vitamin K-dependent coagulation proteins.
56 nism confirmed by in vitro reconstitution of vitamin K-dependent disulphide bridge formation.
57 bit calcification requires the activity of a vitamin K-dependent enzyme, which mediates MGP carboxyla
58 vitamin K-dependent carboxylase activity and vitamin K-dependent epoxidase activity.
59                                  Analyses of vitamin K-dependent factors in 6 cancer patients with av
60                                              Vitamin K-dependent factors protect against vascular and
61 and < 1% on warfarin, at a point where other vitamin K-dependent factors were at 30-40% activity leve
62 ogical role for these two new members of the vitamin K-dependent family of proteins.
63 inhibit the overall activity of the complete vitamin K-dependent g-carboxylation system.
64  binding of the cationic PF4 to the anionic, vitamin K- dependent gamma-carboxyglutamic acid domain o
65 lanogaster cDNA clone encodes a protein with vitamin K-dependent gamma-carboxylase activity.
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
69                                          The vitamin K-dependent gamma-carboxylation of glutamate to
70                                          The vitamin K-dependent gamma-carboxylation system in the en
71                                          The vitamin K-dependent gamma-carboxylation system is respon
72                The eukaryotic cell harbors a vitamin K-dependent gamma-carboxylation system that conv
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
75 mental approaches aimed at understanding the vitamin K-dependent gamma-carboxylation system.
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
78                                          The vitamin K-dependent gamma-glutamyl carboxylase binds an
79                                          The vitamin K-dependent gamma-glutamyl carboxylase catalyzes
80                                          The vitamin K-dependent gamma-glutamyl carboxylase catalyzes
81                                          The vitamin K-dependent gamma-glutamyl carboxylase catalyzes
82                                          The vitamin K-dependent gamma-glutamyl carboxylase catalyzes
83                                          The vitamin K-dependent gamma-glutamyl carboxylase catalyzes
84                                              Vitamin K-dependent gamma-glutamyl carboxylase catalyzes
85 xin epsilon-TxIX and used in assays with the vitamin K-dependent gamma-glutamyl carboxylase from C. t
86                        The expression of the vitamin K-dependent gamma-glutamyl carboxylase gene in l
87                                              Vitamin K-dependent gamma-glutamyl carboxylase is a 758
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
91                               Protein C is a vitamin K-dependent glycoprotein synthesized in the live
92                               Protein S is a vitamin K-dependent glycoprotein, which, besides its ant
93         CDP is also related to disruption of vitamin K-dependent metabolism, causing secondary effect
94 inalis as a model organism for investigating vitamin K-dependent physiological phenomena, which may b
95              Protein Z (PZ) is a multidomain vitamin K-dependent plasma protein that functions as a c
96                          Protein Z (PZ) is a vitamin K-dependent plasma protein whose function has be
97         Human protein Z (PZ) is a 62,000-Mr, vitamin K-dependent plasma protein whose structure is si
98               Activated protein C (APC) is a vitamin K-dependent plasma serine protease which down-re
99  and defines a novel precursor structure for vitamin K-dependent polypeptides.
100                             Because of their vitamin K-dependent post-translational modification, the
101 in the endoplasmic reticulum (ER), catalyzes vitamin K-dependent posttranslational modification of gl
102 rowth, seen in osteoarthritis (OA), may be a vitamin K-dependent process.
103 ormation, expression, and propagation of the vitamin K-dependent procoagulant complexes and extends o
104                        The affinities of the vitamin K-dependent propeptides for the gamma-carboxylas
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
107 oduce functional forms of all members of the vitamin K-dependent protein family.
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).
111                   Protein Z (PZ) is a plasma vitamin K-dependent protein that functions as a cofactor
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
114 r for the membrane-binding conformation of a vitamin K-dependent protein.
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
119                 Overall, membrane binding by vitamin K-dependent proteins appeared consistent with th
120                           Propeptides of the vitamin K-dependent proteins bind to an exosite on gamma
121 ities of synthetic propeptides of nine human vitamin K-dependent proteins by determining the inhibiti
122                       The propeptides of the vitamin K-dependent proteins contain a gamma-carboxylati
123 l implications for overproducing recombinant vitamin K-dependent proteins for therapeutic use.
124        TAM receptors can be activated by the vitamin K-dependent proteins Gas6 and protein S.
125            Comparison of naturally occurring vitamin K-dependent proteins has provided possible bases
126 in individuals with combined deficiencies of vitamin K-dependent proteins have a mutation, L394R, in
127            Two human cDNAs that encode novel vitamin K-dependent proteins have been cloned and sequen
128                         Severe deficiency of vitamin K-dependent proteins in patients not maintained
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
132                       Gamma-carboxylation of vitamin K-dependent proteins is dependent on formation o
133 modification of the membrane contact site of vitamin K-dependent proteins may enhance the membrane af
134 ic acid to gamma-carboxyglutamic acid in the vitamin K-dependent proteins of blood and bone.
135                                    All known vitamin K-dependent proteins possess a conserved eightee
136                       gamma-Carboxylation of vitamin K-dependent proteins requires a functional vitam
137                The enzymatic activity of the vitamin K-dependent proteins requires the post-translati
138 peptide and the propeptides of the mammalian vitamin K-dependent proteins show no obvious sequence ho
139                           The propeptides of vitamin K-dependent proteins stimulate gamma-carboxylase
140 istent with studies on prothrombin and other vitamin K-dependent proteins that have been modified or
141  and dissociation kinetics relative to other vitamin K-dependent proteins that have been tested.
142                          Therefore, the five vitamin K-dependent proteins that were examined were equ
143 ropeptide is the primary binding site of the vitamin K-dependent proteins to carboxylase.
144                                   Binding of vitamin K-dependent proteins to cell membranes containin
145 tion is strongly dependent on the binding of vitamin K-dependent proteins to cell membranes containin
146                                          The vitamin K-dependent proteins undergo a conformational tr
147 hat the affinities of the propeptides of the vitamin K-dependent proteins vary over a considerable ra
148                  No binding of PTX2 to other vitamin K-dependent proteins was observed.
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.
158 , a required cofactor for g-carboxylation of vitamin K-dependent proteins.
159 is not attributable to the Gla domain of all vitamin K-dependent proteins.
160  amino acid propeptide sequence found in all vitamin K-dependent proteins.
161 ed for the posttranslational modification of vitamin K-dependent proteins.
162 underlie membrane binding behaviors of other vitamin K-dependent proteins.
163 tamin K that is required for modification of vitamin K-dependent proteins.
164 n/phospholipid binding) for a Gla residue in vitamin K-dependent proteins.
165 ylation of certain glutamic acid residues in vitamin K-dependent proteins.
166 in post-translational gamma-carboxylation of vitamin K-dependent proteins.
167 t-translational modification of a variety of vitamin K-dependent proteins.
168 he sea squirt Ciona intestinalis that encode vitamin K-dependent proteins.
169 increased cellular production of recombinant vitamin K-dependent proteins.
170 ey regulatory protein in synthesis of active vitamin K-dependent proteins.
171 erent than in Gla domain structures of other vitamin K-dependent proteins.
172 cerning regulation of gamma-carboxylation of vitamin K-dependent proteins.
173 propeptide cleavage site, as occurs in other vitamin-K-dependent proteins.
174 activated by gamma-glutamyl carboxylation, a vitamin K-dependent reaction, to serve in an anti-minera
175               Central to this pathway is the vitamin K-dependent serine protease, APC, and its precur
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
179                                          The vitamin K-dependent (VKD) carboxylase binds VKD proteins
180                                          The vitamin K-dependent (VKD) carboxylase converts clusters
181                                          The vitamin K-dependent (VKD) carboxylase converts Glu's to
182                                          The vitamin K-dependent (VKD) carboxylase uses the oxygenati
183                                              Vitamin K-dependent (VKD) proteins are modified by the V
184                                              Vitamin K-dependent (VKD) proteins become activated by t
185 nts governing the modification of individual vitamin K-dependent (VKD) proteins by the carboxylase ha
186                             Carboxylation of vitamin K-dependent (VKD) proteins is required for their
187                                Vitamin K and vitamin K-dependent (VKD) proteins may be involved in re
188                                              Vitamin K-dependent (VKD) proteins require carboxylation
189                                              Vitamin K-dependent (VKD) proteins require modification
190                                 For 16 known vitamin K-dependent (VKD) proteins, we evaluated the rel
191 ycles vitamin K to support the activation of vitamin K-dependent (VKD) proteins, which have diverse f
192 a-carboxylase for gamma-carboxylation of all vitamin K-dependent (VKD) proteins.
193                              Factor VII is a vitamin K-dependent zymogen of a serine protease that pa

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