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1 on of diacylglycerol by dephosphorylation of phosphatidate).
2 removes the beta phosphate from DGPP to form phosphatidate.
3 holipid synthesis through its consumption of phosphatidate.
4 tant (Vmax/Km) 10-fold greater than that for phosphatidate.
5 vators was to cause a decrease in the Km for phosphatidate.
6 nt phosphorylation of diacylglycerol to form phosphatidate.
7 e that uses CTP, instead of ATP, to generate phosphatidate.
8 diacylglycerol pyrophosphate (0.6 mol %) and phosphatidate (1.4 mol %) were found in the vacuole memb
9 d), phosphatidylethanolamine (1.3-fold), and phosphatidate (2-fold) and a decrease in the synthesis o
10 yzes both phospholipid hydrolysis to produce phosphatidate and a transphosphatidylation reaction usin
11 hatidate phosphatase, controls the levels of phosphatidate and diacylglycerol for phospholipid synthe
12 ng the relative proportions of its substrate phosphatidate and its product diacylglycerol.
13 tion of diacylglycerol pyrophosphate to form phosphatidate and Pi.
14 ation of the beta phosphate of DGPP to yield phosphatidate and Pi.
15 glycerol kinase indicated that alteration in phosphatidate and/or diacylglycerol levels might be the
16        Because diacylglycerol pyrophosphate, phosphatidate, and diacylglycerol have roles as lipid si
17 te from diacylglycerol pyrophosphate to form phosphatidate, and it then removes the phosphate from ph
18 sin increases levels of the lipin substrate, phosphatidate, and reduces the product, diacylglycerol.
19 hosphatidate binding site abolished dioleoyl phosphatidate- and insulin-induced translocation of KSR1
20  unaffected, suggesting that the short-chain phosphatidates are receptor subtype-specific lysophospha
21 rginines located in the core of the putative phosphatidate binding site abolished dioleoyl phosphatid
22    Our results demonstrate that a functional phosphatidate binding site is necessary for Raf-1 functi
23  (KSR) contains a sequence homologous to the phosphatidate binding site of Raf-1.
24 tase also catalyzed the dephosphorylation of phosphatidate, but this dephosphorylation was subsequent
25 d (Ki = 0.35 mol %) the dephosphorylation of phosphatidate by a competitive mechanism whereas phospha
26  accumulation of [3H]-cytidine monophosphate phosphatidate (CMP-PA) after incubation with [3H]-cytidi
27 uence (UASINO), a cis-acting element for the phosphatidate-controlled Henry (Ino2-Ino4/Opi1) regulato
28 d levels of diacylglycerol pyrophosphate and phosphatidate correlated with the induced expression of
29 phatidate by a competitive mechanism whereas phosphatidate did not inhibit the dephosphorylation of D
30  our previous work, suggest the formation of phosphatidate-enriched membrane microdomains that contai
31 rexpression of DGK1 causes the appearance of phosphatidate-enriched membranes around the nucleus and
32 rt triacylglycerol-derived diacylglycerol to phosphatidate for phospholipid synthesis.
33 rol and simultaneously controls the level of phosphatidate for the synthesis of phospholipids.
34 major role in controlling the utilization of phosphatidate for the synthesis of triacylglycerol or me
35 on of IgE-receptor-stimulated, PLD-catalysed phosphatidate formation suppressed secretion of granule
36 inase enzyme that catalyzes the formation of phosphatidate from diacylglycerol.
37     Butan-1-ol, which acts as an acceptor of phosphatidate generated by the PLD pathway, blocked LPA-
38               Insulin and exogenous dioleoyl phosphatidate induced a rapid translocation of a mouse K
39                                              Phosphatidate inhibits differentiation of cultured adipo
40 ellular level, PLD and its reaction product, phosphatidate, interact with a large number of protein p
41 P was synthesized from phosphatidate via the phosphatidate kinase reaction.
42                The dependence of activity on phosphatidate (Km = 2.2 mol %) was cooperative (Hill num
43          Two screens for novel regulators of phosphatidate led to the identification of DGK1.
44                      Mutations that decrease phosphatidate levels decrease nuclear membrane growth in
45 ycerol synthesis and simultaneously controls phosphatidate levels for phospholipid synthesis, is subj
46  PAH1 at the nuclear envelope by controlling phosphatidate levels.
47                              We propose that phosphatidate metabolism is a critical factor determinin
48  by barium arachidate and barium dimyristoyl phosphatidate on a Si substrate.
49 e levels of diacylglycerol pyrophosphate and phosphatidate on the cytosolic face of the vacuole membr
50                     The addition of dioleoyl phosphatidate or insulin increased the co-localization o
51  composed of pure phosphatidylserine (PS) or phosphatidate (PA) and mixtures of PA with phosphatidylc
52 alyze the dephosphorylation of DGPP to yield phosphatidate (PA) and then catalyze the dephosphorylati
53 lyzes the dephosphorylation of DGPP to yield phosphatidate (PA) and then catalyzes the dephosphorylat
54                                              Phosphatidate (PA) is a central metabolite of lipid meta
55                             Mg(2+)-dependent phosphatidate (PA) phosphatase (3-sn-phosphatidate phosp
56 encodes the protein lipin 1, which possesses phosphatidate (PA) phosphatase (3-sn-phosphatidate phosp
57  been primarily characterized by a defect in phosphatidate (PA) phosphatase activity and also exhibit
58 me accounts for half of the Mg2+-independent phosphatidate (PA) phosphatase activity in Saccharomyces
59                             The PAH1-encoded phosphatidate (PA) phosphatase in Saccharomyces cerevisi
60                   We show that the conserved phosphatidate (PA) phosphatase Pah1, which generates dia
61  is inhibited by 1% ethanol, indicating that phosphatidate (PA) produced by phospholipase D (PLD) act
62     App1p, which catalyzes the conversion of phosphatidate (PA) to diacylglycerol, is unique among Mg
63                                              Phosphatidate (PA), whose cellular levels are controlled
64 ylcholine, generating the putative messenger phosphatidate (PA).
65 rol kinase, which converts diacylglycerol to phosphatidate, partially suppressed the pah1Delta-mediat
66 Saccharomyces cerevisiae membrane-associated phosphatidate phosphatase (3-sn-phosphatidate phosphohyd
67                                              Phosphatidate phosphatase (PAP) catalyzes the dephosphor
68    The Saccharomyces cerevisiae PAH1-encoded phosphatidate phosphatase (PAP) catalyzes the penultimat
69                       Lipin-1 functions as a phosphatidate phosphatase (PAP) enzyme in the glycerol 3
70                              The three lipin phosphatidate phosphatase (PAP) enzymes catalyze a step
71    The family of three lipin proteins act as phosphatidate phosphatase (PAP) enzymes required for gly
72 re evolutionarily conserved Mg(2+)-dependent phosphatidate phosphatase (PAP) enzymes with essential r
73 -1, lipin-2, and lipin-3) are Mg2+-dependent phosphatidate phosphatase (PAP) enzymes, which catalyze
74                    Pah1p, which functions as phosphatidate phosphatase (PAP) in the yeast Saccharomyc
75           Early work indicates a role of the phosphatidate phosphatase (PAP) in this metabolism; the
76                                              Phosphatidate phosphatase (PAP) plays diverse roles in l
77                             Yeast App1p is a phosphatidate phosphatase (PAP) that associates with end
78                             The PAH1-encoded phosphatidate phosphatase (PAP), which catalyzes the com
79 myces cerevisiae PAH1-encoded Mg2+-dependent phosphatidate phosphatase (PAP1, 3-sn-phosphatidate phos
80       This was accompanied by a reduction in phosphatidate phosphatase 1 (PAP1) activity.
81  was performed to determine the mechanism of phosphatidate phosphatase activation by anionic phosphol
82  biosynthesis of triacylglycerol through its phosphatidate phosphatase activity and also acts as a tr
83 positively charged sphingoid base, inhibited phosphatidate phosphatase activity and antagonized the a
84                          Lipin proteins have phosphatidate phosphatase activity and catalyze the form
85 genase-like domains of Pah1 are required for phosphatidate phosphatase activity and the in vivo funct
86 ese results suggested that the activation of phosphatidate phosphatase activity by anionic phospholip
87 growth phase-mediated inductions of PAH1 and phosphatidate phosphatase activity do not correlate with
88 also abrogates the nuclear translocation and phosphatidate phosphatase activity of lipin-1.
89              Anionic phospholipids activated phosphatidate phosphatase activity whereas zwitterionic
90 se A, which cause a significant reduction in phosphatidate phosphatase activity, the phosphorylation
91 nositol were mixed competitive activators of phosphatidate phosphatase activity.
92 tase resulted in the stimulation (6-fold) of phosphatidate phosphatase activity.
93 f Pah1 regulate its subcellular location and phosphatidate phosphatase activity.
94 ane expansion, which occurs in cells lacking phosphatidate phosphatase activity.
95                                      Loss of phosphatidate phosphatase also resulted in the derepress
96 mation of diacylglycerol by the PAH1-encoded phosphatidate phosphatase and by channeling diacylglycer
97                                 PAH1-encoded phosphatidate phosphatase catalyzes the penultimate step
98 neither a substrate nor an inhibitor of pure phosphatidate phosphatase from S. cerevisiae.
99                                 Lipin-1 is a phosphatidate phosphatase in glycerolipid biosynthesis a
100                                         Pah1 phosphatidate phosphatase in Saccharomyces cerevisiae ca
101                                  Pah1 is the phosphatidate phosphatase in the yeast Saccharomyces cer
102                           Yeast PAH1-encoded phosphatidate phosphatase is the enzyme responsible for
103 al loss-of-function mutation in the gene for phosphatidate phosphatase Lpin1 and a truncation mutatio
104                            The dependence of phosphatidate phosphatase on phosphatidate was cooperati
105 reviously that the activity of the conserved phosphatidate phosphatase Pah1p/Smp2p regulates nuclear
106               This result confirmed the role phosphatidate phosphatase plays in phosphatidylcholine s
107 doplasmic reticulum membrane to catalyze the phosphatidate phosphatase reaction.
108                           Yeast Pah1p is the phosphatidate phosphatase that catalyzes the penultimate
109 ingle lipin homolog in yeast, Smp2, exhibits phosphatidate phosphatase type-1 (PAP1) activity, which
110 e showed that the expression of PAH1-encoded phosphatidate phosphatase was induced by zinc deficiency
111 his enzyme, in conjunction with PAH1-encoded phosphatidate phosphatase, controls the levels of phosph
112  including phosphatidylinositol synthase and phosphatidate phosphatase, were not affected in the cki1
113                Saccharomyces cerevisiae Pah1 phosphatidate phosphatase, which catalyzes the conversio
114            In Saccharomyces cerevisiae, Pah1 phosphatidate phosphatase, which catalyzes the dephospho
115                                 PAH1-encoded phosphatidate phosphatase, which catalyzes the dephospho
116                              The yeast Pah1p phosphatidate phosphatase, which catalyzes the penultima
117  degradation was conserved for human lipin 1 phosphatidate phosphatase.
118                                   Lipins are phosphatidate phosphatases that generate diacylglycerol
119          Lipins are evolutionarily conserved phosphatidate phosphatases that perform key functions in
120  Similarly, other phospholipids derived from phosphatidate, phosphatidylglycerol and cardiolipin, wer
121                                 Lipin-1 is a phosphatidate phosphohydrolase (PAP) required for the ge
122                             Experiments with phosphatidate phosphohydrolase (PAPH) and phospholipase
123           BEL also inhibited islet cytosolic phosphatidate phosphohydrolase (PAPH), but the PAPH inhi
124                      Moreover, inhibitors of phosphatidate phosphohydrolase (propranolol) and diacylg
125 ound to be strikingly dependent on an active phosphatidate phosphohydrolase 1 (PAP-1).
126 regulation of COX-2 expression and implicate phosphatidate phosphohydrolase 1 as a key regulatory com
127 l, which is an effective inhibitor of type 1 phosphatidate phosphohydrolase activities and is only mo
128 as evidenced by studies using propranolol, a phosphatidate phosphohydrolase inhibitor.
129 e-associated phosphatidate phosphatase (3-sn-phosphatidate phosphohydrolase, EC 3.1.3.4) activity by
130 pendent phosphatidate (PA) phosphatase (3-sn-phosphatidate phosphohydrolase, EC 3.1.3.4) catalyzes th
131 endent phosphatidate phosphatase (PAP1, 3-sn-phosphatidate phosphohydrolase, EC 3.1.3.4) catalyzes th
132 nversion to corresponding diacylglycerols by phosphatidate phosphohydrolase, since diacylglycerols we
133 EL) suicide substrate, but BEL also inhibits phosphatidate phosphohydrolase-1 and a group VIB phospho
134 SH cells requires prior generation of DAG by phosphatidate phosphohydrolase.
135  release for prostacyclin production via the phosphatidate phosphohydrolase/diacylglycerol lipase pat
136 ssesses phosphatidate (PA) phosphatase (3-sn-phosphatidate phosphohydrolase; EC 3.1.3.4) activity.
137                            Here we show that phosphatidate promotes ERK phosphorylation in intact cel
138 -deficient mice, there is an accumulation of phosphatidate species containing a range of medium chain
139 ding any role for phospholipase-D or de novo phosphatidate synthesis in the dopaminergic response.
140 nositide signaling is independent of de novo phosphatidate synthesis, and that the widely used enzyme
141 se in the levels of [3H]delta4Ach-containing phosphatidate that is directly correlated with a decreas
142             Surprisingly, hepatic content of phosphatidate, the substrate of PAP-1 enzymes, was marke
143       This role was linked to the binding of phosphatidate to a specific polybasic site within the ki
144 osphatase, which catalyzes the conversion of phosphatidate to diacylglycerol for triacylglycerol synt
145 gene expression and to enzymatically convert phosphatidate to diacylglycerol, an essential precursor
146 glycerolipid biosynthesis, the conversion of phosphatidate to diacylglycerol.
147             The enzyme also dephosphorylates phosphatidate to form diacylglycerol and Pi.
148 date, and it then removes the phosphate from phosphatidate to form diacylglycerol.
149 se, which catalyzes the dephosphorylation of phosphatidate to produce diacylglycerol at the endoplasm
150                            Direct binding of phosphatidate to synthetic peptides derived from the seq
151  3.1.3.4) catalyzes the dephosphorylation of phosphatidate to yield diacylglycerol and Pi.
152 se, which catalyzes the dephosphorylation of phosphatidate to yield diacylglycerol, plays a crucial r
153 embrane to catalyze the dephosphorylation of phosphatidate to yield diacylglycerol.
154 ase (PAP) catalyzes the dephosphorylation of phosphatidate to yield diacylglycerol.
155 g2+-dependent activity that was specific for phosphatidate under the conditions employed.
156 esis and concurrently controls the levels of phosphatidate used for phospholipid synthesis.
157 a negative regulatory effect on the level of phosphatidate used for the de novo synthesis of membrane
158                    DGPP was synthesized from phosphatidate via the phosphatidate kinase reaction.
159 e dependence of phosphatidate phosphatase on phosphatidate was cooperative (n approximately 2.2) in t

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