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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 nome-wide CRISPR-Cas9 knockout screen with a vitamin K-dependent apoptotic reporter cell line.
6                                          The vitamin K-dependent biosynthesis of gamma-carboxyglutami
7 VKOR) drives the vitamin K cycle, activating vitamin K-dependent blood clotting factors.
8 domain, a membrane-anchoring domain found on vitamin K-dependent blood coagulation and regulatory pro
9                             Some recombinant vitamin K-dependent blood coagulation factors (factors V
10 the bloodstream, Ad vectors can bind several vitamin K-dependent blood coagulation factors, which con
11 d mechanism, which involves virus binding to vitamin K-dependent blood coagulation factors.
12 arboxylase gene, and hence the regulation of vitamin K-dependent blood coagulation protein synthesis.
13                             Prothrombin is a vitamin K-dependent blood coagulation protein that under
14 ntial post-translational modification of the vitamin K-dependent blood coagulation proteins, the regu
15 n amino acid critical to the function of the vitamin K-dependent blood coagulation proteins.
16       Human factor X is a two-chain, 58-kDa, vitamin K-dependent blood coagulation zymogen.
17      This domain is strongly conserved among vitamin K-dependent blood proteins and, in addition to a
18 rboxyglutamic acid-containing regions of the vitamin K-dependent blood-clotting proteins.
19  properties of matrix Gla protein (MGP) as a vitamin K-dependent calcification inhibitor.
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
22          Assay of hagfish liver demonstrated vitamin K-dependent carboxylase activity in this hemicho
23                                          The vitamin K-dependent carboxylase also catalyzes the epoxi
24 us is the sole invertebrate wherein both the vitamin K-dependent carboxylase and its product, gamma-c
25                                              Vitamin K-dependent carboxylase catalyzes the post-trans
26                                          The vitamin K-dependent carboxylase catalyzes the posttransl
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
30                                          The vitamin K-dependent carboxylase is an integral membrane
31                                          The vitamin K-dependent carboxylase modifies and renders act
32 odendrocytes nor neurons possess significant vitamin K-dependent carboxylase or epoxidase activity.
33                                          The vitamin K-dependent carboxylase was located in the endop
34                            Incubation of the vitamin K-dependent carboxylase with the sulfhydryl-reac
35                                          The vitamin K-dependent carboxylase, a constituent of the en
36                            Using recombinant vitamin K-dependent carboxylase, purified in the absence
37  only known invertebrate with a demonstrated vitamin K-dependent carboxylase.
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
43 l ferroptosis, displays strong inhibition of vitamin K-dependent carboxylation.
44 el to the function of FSP1, does not support vitamin K-dependent carboxylation.
45         In addition, VKOR variants can cause vitamin K-dependent clotting factor deficiency or alter
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
49              The propeptide sequences of the vitamin K-dependent clotting factors serve as a recognit
50 quired for posttranslational modification of vitamin K-dependent clotting factors.
51 gs have been encountered in association with vitamin K-dependent coagulation factor deficiency, an au
52 ings with characteristic features of PXE and vitamin K-dependent coagulation factor deficiency.
53 e novel insight into mechanisms by which the vitamin K-dependent coagulation factors are regulated.
54                                              Vitamin K-dependent coagulation factors deficiency is a
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
57 structural features that distinguish it from vitamin K-dependent coagulation proteases.
58 yme complex formation with gla variants of a vitamin K-dependent coagulation protein and provides evi
59                              Factor VII is a vitamin K-dependent coagulation protein essential for pr
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
62 se of decreased biological activities of all vitamin K-dependent coagulation proteins.
63 nism confirmed by in vitro reconstitution of vitamin K-dependent disulphide bridge formation.
64 bit calcification requires the activity of a vitamin K-dependent enzyme, which mediates MGP carboxyla
65 vitamin K-dependent carboxylase activity and vitamin K-dependent epoxidase activity.
66                                  Analyses of vitamin K-dependent factors in 6 cancer patients with av
67                                              Vitamin K-dependent factors protect against vascular and
68 and < 1% on warfarin, at a point where other vitamin K-dependent factors were at 30-40% activity leve
69 ogical role for these two new members of the vitamin K-dependent family of proteins.
70 inhibit the overall activity of the complete vitamin K-dependent g-carboxylation system.
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
73 lanogaster cDNA clone encodes a protein with vitamin K-dependent gamma-carboxylase activity.
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
78                                          The vitamin K-dependent gamma-carboxylation of glutamate to
79                                          The vitamin K-dependent gamma-carboxylation system in the en
80                                          The vitamin K-dependent gamma-carboxylation system is respon
81                The eukaryotic cell harbors a vitamin K-dependent gamma-carboxylation system that conv
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
84 mental approaches aimed at understanding the vitamin K-dependent gamma-carboxylation system.
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
87                                          The vitamin K-dependent gamma-glutamyl carboxylase binds an
88                                          The vitamin K-dependent gamma-glutamyl carboxylase catalyzes
89                                          The vitamin K-dependent gamma-glutamyl carboxylase catalyzes
90                                          The vitamin K-dependent gamma-glutamyl carboxylase catalyzes
91                                          The vitamin K-dependent gamma-glutamyl carboxylase catalyzes
92                                          The vitamin K-dependent gamma-glutamyl carboxylase catalyzes
93                                              Vitamin K-dependent gamma-glutamyl carboxylase catalyzes
94 xin epsilon-TxIX and used in assays with the vitamin K-dependent gamma-glutamyl carboxylase from C. t
95                        The expression of the vitamin K-dependent gamma-glutamyl carboxylase gene in l
96                                              Vitamin K-dependent gamma-glutamyl carboxylase is a 758
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
101                               Protein C is a vitamin K-dependent glycoprotein synthesized in the live
102                               Protein S is a vitamin K-dependent glycoprotein, which, besides its ant
103         CDP is also related to disruption of vitamin K-dependent metabolism, causing secondary effect
104                                     Inactive vitamin K-dependent MGP (desphospho-uncarboxylated [dp-u
105                                     Inactive vitamin K-dependent MGP (dp-ucMGP) and prothrombin (PIVK
106 inalis as a model organism for investigating vitamin K-dependent physiological phenomena, which may b
107              Protein Z (PZ) is a multidomain vitamin K-dependent plasma protein that functions as a c
108                          Protein Z (PZ) is a vitamin K-dependent plasma protein whose function has be
109         Human protein Z (PZ) is a 62,000-Mr, vitamin K-dependent plasma protein whose structure is si
110               Activated protein C (APC) is a vitamin K-dependent plasma serine protease which down-re
111  and defines a novel precursor structure for vitamin K-dependent polypeptides.
112                             Because of their vitamin K-dependent post-translational modification, the
113                Matrix Gla protein (MGP) is a vitamin K-dependent post-translationally modified protei
114 in the endoplasmic reticulum (ER), catalyzes vitamin K-dependent posttranslational modification of gl
115 rowth, seen in osteoarthritis (OA), may be a vitamin K-dependent process.
116 ormation, expression, and propagation of the vitamin K-dependent procoagulant complexes and extends o
117                        The affinities of the vitamin K-dependent propeptides for the gamma-carboxylas
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
120 oduce functional forms of all members of the vitamin K-dependent protein family.
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).
124                   Protein Z (PZ) is a plasma vitamin K-dependent protein that functions as a cofactor
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
127         However, two anticoagulant proteins, vitamin K-dependent protein-S (p < 0.0001) and heparin c
128 r for the membrane-binding conformation of a vitamin K-dependent protein.
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
134                 Overall, membrane binding by vitamin K-dependent proteins appeared consistent with th
135                           Propeptides of the vitamin K-dependent proteins bind to an exosite on gamma
136 ities of synthetic propeptides of nine human vitamin K-dependent proteins by determining the inhibiti
137                       The propeptides of the vitamin K-dependent proteins contain a gamma-carboxylati
138 l implications for overproducing recombinant vitamin K-dependent proteins for therapeutic use.
139                                              Vitamin K-dependent proteins function as calcification i
140        TAM receptors can be activated by the vitamin K-dependent proteins Gas6 and protein S.
141            Comparison of naturally occurring vitamin K-dependent proteins has provided possible bases
142 in individuals with combined deficiencies of vitamin K-dependent proteins have a mutation, L394R, in
143            Two human cDNAs that encode novel vitamin K-dependent proteins have been cloned and sequen
144 itamin K actions, the potential functions of vitamin K-dependent proteins in cancer, and observationa
145                         Severe deficiency of vitamin K-dependent proteins in patients not maintained
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
148                                              Vitamin K-dependent proteins in vascular tissue affect v
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
151                       Gamma-carboxylation of vitamin K-dependent proteins is dependent on formation o
152 modification of the membrane contact site of vitamin K-dependent proteins may enhance the membrane af
153 ic acid to gamma-carboxyglutamic acid in the vitamin K-dependent proteins of blood and bone.
154                                    All known vitamin K-dependent proteins possess a conserved eightee
155                       gamma-Carboxylation of vitamin K-dependent proteins requires a functional vitam
156                The enzymatic activity of the vitamin K-dependent proteins requires the post-translati
157 peptide and the propeptides of the mammalian vitamin K-dependent proteins show no obvious sequence ho
158                           The propeptides of vitamin K-dependent proteins stimulate gamma-carboxylase
159 istent with studies on prothrombin and other vitamin K-dependent proteins that have been modified or
160  and dissociation kinetics relative to other vitamin K-dependent proteins that have been tested.
161                          Therefore, the five vitamin K-dependent proteins that were examined were equ
162 ropeptide is the primary binding site of the vitamin K-dependent proteins to carboxylase.
163                                   Binding of vitamin K-dependent proteins to cell membranes containin
164 tion is strongly dependent on the binding of vitamin K-dependent proteins to cell membranes containin
165                                          The vitamin K-dependent proteins undergo a conformational tr
166 hat the affinities of the propeptides of the vitamin K-dependent proteins vary over a considerable ra
167                  No binding of PTX2 to other vitamin K-dependent proteins was observed.
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.
178 , a required cofactor for g-carboxylation of vitamin K-dependent proteins.
179 is not attributable to the Gla domain of all vitamin K-dependent proteins.
180  amino acid propeptide sequence found in all vitamin K-dependent proteins.
181 ed for the posttranslational modification of vitamin K-dependent proteins.
182 underlie membrane binding behaviors of other vitamin K-dependent proteins.
183 tamin K that is required for modification of vitamin K-dependent proteins.
184 n/phospholipid binding) for a Gla residue in vitamin K-dependent proteins.
185 ylation of certain glutamic acid residues in vitamin K-dependent proteins.
186 in post-translational gamma-carboxylation of vitamin K-dependent proteins.
187 t-translational modification of a variety of vitamin K-dependent proteins.
188 he sea squirt Ciona intestinalis that encode vitamin K-dependent proteins.
189 increased cellular production of recombinant vitamin K-dependent proteins.
190 ey regulatory protein in synthesis of active vitamin K-dependent proteins.
191 erent than in Gla domain structures of other vitamin K-dependent proteins.
192 cerning regulation of gamma-carboxylation of vitamin K-dependent proteins.
193 propeptide cleavage site, as occurs in other vitamin-K-dependent proteins.
194 activated by gamma-glutamyl carboxylation, a vitamin K-dependent reaction, to serve in an anti-minera
195               Central to this pathway is the vitamin K-dependent serine protease, APC, and its precur
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
199                                          The vitamin K-dependent (VKD) carboxylase binds VKD proteins
200                                          The vitamin K-dependent (VKD) carboxylase converts clusters
201                                          The vitamin K-dependent (VKD) carboxylase converts Glu's to
202                                          The vitamin K-dependent (VKD) carboxylase uses the oxygenati
203                                              Vitamin K-dependent (VKD) proteins are modified by the V
204                                              Vitamin K-dependent (VKD) proteins become activated by t
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
207                             Carboxylation of vitamin K-dependent (VKD) proteins is required for their
208                                Vitamin K and vitamin K-dependent (VKD) proteins may be involved in re
209                                              Vitamin K-dependent (VKD) proteins require carboxylation
210                                              Vitamin K-dependent (VKD) proteins require modification
211 nerates multiple carboxylated Glus (Glas) in vitamin K-dependent (VKD) proteins that are required for
212                                 For 16 known vitamin K-dependent (VKD) proteins, we evaluated the rel
213 ycles vitamin K to support the activation of vitamin K-dependent (VKD) proteins, which have diverse f
214 a-carboxylase for gamma-carboxylation of all vitamin K-dependent (VKD) proteins.
215                              Factor VII is a vitamin K-dependent zymogen of a serine protease that pa
216  of the coagulation cascade, the multidomain vitamin-K-dependent zymogen prothrombin is converted to

 
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