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1 on of diacylglycerol by dephosphorylation of phosphatidate).
2 removes the beta phosphate from DGPP to form phosphatidate.
3 tant (Vmax/Km) 10-fold greater than that for phosphatidate.
4 vators was to cause a decrease in the Km for phosphatidate.
5 holipid synthesis through its consumption of 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
15 glycerol kinase indicated that alteration in phosphatidate and/or diacylglycerol levels might be the
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
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
30 phatidate by a competitive mechanism whereas phosphatidate did not inhibit the dephosphorylation of D
31 our previous work, suggest the formation of phosphatidate-enriched membrane microdomains that contai
32 rexpression of DGK1 causes the appearance of phosphatidate-enriched membranes around the nucleus and
35 major role in controlling the utilization of phosphatidate for the synthesis of triacylglycerol or me
36 on of IgE-receptor-stimulated, PLD-catalysed phosphatidate formation suppressed secretion of granule
38 Butan-1-ol, which acts as an acceptor of phosphatidate generated by the PLD pathway, blocked LPA-
41 ellular level, PLD and its reaction product, phosphatidate, interact with a large number of protein p
42 phosphatase cascade largely controls whether phosphatidate is partitioned into the storage lipid tria
47 ycerol synthesis and simultaneously controls phosphatidate levels for phospholipid synthesis, is subj
52 e levels of diacylglycerol pyrophosphate and phosphatidate on the cytosolic face of the vacuole membr
54 composed of pure phosphatidylserine (PS) or phosphatidate (PA) and mixtures of PA with phosphatidylc
55 alyze the dephosphorylation of DGPP to yield phosphatidate (PA) and then catalyze the dephosphorylati
56 lyzes the dephosphorylation of DGPP to yield phosphatidate (PA) and then catalyzes the dephosphorylat
59 encodes the protein lipin 1, which possesses phosphatidate (PA) phosphatase (3-sn-phosphatidate phosp
60 been primarily characterized by a defect in phosphatidate (PA) phosphatase activity and also exhibit
61 me accounts for half of the Mg2+-independent phosphatidate (PA) phosphatase activity in Saccharomyces
62 This JBC Review on the discoveries of yeast phosphatidate (PA) phosphatase genes is dedicated to Dr.
66 t Saccharomyces cerevisiae, the PAH1-encoded phosphatidate (PA) phosphatase plays a major role in the
68 The Saccharomyces cerevisiae PAH1-encoded phosphatidate (PA) phosphatase, which catalyzes the deph
70 The Saccharomyces cerevisiae PAH1-encoded phosphatidate (PA) phosphatase, which catalyzes the Mg(2
71 is inhibited by 1% ethanol, indicating that phosphatidate (PA) produced by phospholipase D (PLD) act
72 App1p, which catalyzes the conversion of phosphatidate (PA) to diacylglycerol, is unique among Mg
75 rol kinase, which converts diacylglycerol to phosphatidate, partially suppressed the pah1Delta-mediat
76 Saccharomyces cerevisiae membrane-associated phosphatidate phosphatase (3-sn-phosphatidate phosphohyd
78 The Saccharomyces cerevisiae PAH1-encoded phosphatidate phosphatase (PAP) catalyzes the penultimat
81 The family of three lipin proteins act as phosphatidate phosphatase (PAP) enzymes required for gly
82 re evolutionarily conserved Mg(2+)-dependent phosphatidate phosphatase (PAP) enzymes with essential r
83 -1, lipin-2, and lipin-3) are Mg2+-dependent phosphatidate phosphatase (PAP) enzymes, which catalyze
89 h a modulator of transcription factors and a phosphatidate phosphatase (PAP1), is known to play impor
90 myces cerevisiae PAH1-encoded Mg2+-dependent phosphatidate phosphatase (PAP1, 3-sn-phosphatidate phos
92 was performed to determine the mechanism of phosphatidate phosphatase activation by anionic phosphol
93 biosynthesis of triacylglycerol through its phosphatidate phosphatase activity and also acts as a tr
94 positively charged sphingoid base, inhibited phosphatidate phosphatase activity and antagonized the a
96 phosphorylation of Pah1 stimulated both its phosphatidate phosphatase activity and its subsequent ph
97 genase-like domains of Pah1 are required for phosphatidate phosphatase activity and the in vivo funct
98 ese results suggested that the activation of phosphatidate phosphatase activity by anionic phospholip
99 growth phase-mediated inductions of PAH1 and phosphatidate phosphatase activity do not correlate with
102 se A, which cause a significant reduction in phosphatidate phosphatase activity, the phosphorylation
108 mation of diacylglycerol by the PAH1-encoded phosphatidate phosphatase and by channeling diacylglycer
109 is a protein phosphatase that activates Pah1 phosphatidate phosphatase at the nuclear-endoplasmic ret
119 al loss-of-function mutation in the gene for phosphatidate phosphatase Lpin1 and a truncation mutatio
121 reviously that the activity of the conserved phosphatidate phosphatase Pah1p/Smp2p regulates nuclear
124 anding of how phosphorylation of lipin 1beta phosphatidate phosphatase regulates its interaction with
126 c reticulum membrane localization of Pah1, a phosphatidate phosphatase that produces diacylglycerol f
127 ingle lipin homolog in yeast, Smp2, exhibits phosphatidate phosphatase type-1 (PAP1) activity, which
128 e showed that the expression of PAH1-encoded phosphatidate phosphatase was induced by zinc deficiency
129 his enzyme, in conjunction with PAH1-encoded phosphatidate phosphatase, controls the levels of phosph
130 hat catalyzes the dephosphory-lation of Pah1 phosphatidate phosphatase, required for its translocatio
131 including phosphatidylinositol synthase and phosphatidate phosphatase, were not affected in the cki1
136 in lipid metabolism as an activator of Pah1 phosphatidate phosphatase, which produces diacylglycerol
141 Similarly, other phospholipids derived from phosphatidate, phosphatidylglycerol and cardiolipin, wer
147 regulation of COX-2 expression and implicate phosphatidate phosphohydrolase 1 as a key regulatory com
148 l, which is an effective inhibitor of type 1 phosphatidate phosphohydrolase activities and is only mo
149 owed that Sph inhibited protein kinase C and phosphatidate phosphohydrolase activities paving the way
151 e-associated phosphatidate phosphatase (3-sn-phosphatidate phosphohydrolase, EC 3.1.3.4) activity by
152 endent phosphatidate phosphatase (PAP1, 3-sn-phosphatidate phosphohydrolase, EC 3.1.3.4) catalyzes th
153 pendent phosphatidate (PA) phosphatase (3-sn-phosphatidate phosphohydrolase, EC 3.1.3.4) catalyzes th
154 nversion to corresponding diacylglycerols by phosphatidate phosphohydrolase, since diacylglycerols we
155 EL) suicide substrate, but BEL also inhibits phosphatidate phosphohydrolase-1 and a group VIB phospho
157 release for prostacyclin production via the phosphatidate phosphohydrolase/diacylglycerol lipase pat
158 ssesses phosphatidate (PA) phosphatase (3-sn-phosphatidate phosphohydrolase; EC 3.1.3.4) activity.
160 -deficient mice, there is an accumulation of phosphatidate species containing a range of medium chain
161 ding any role for phospholipase-D or de novo phosphatidate synthesis in the dopaminergic response.
162 nositide signaling is independent of de novo phosphatidate synthesis, and that the widely used enzyme
163 se in the levels of [3H]delta4Ach-containing phosphatidate that is directly correlated with a decreas
166 osphatase, which catalyzes the conversion of phosphatidate to diacylglycerol for triacylglycerol synt
167 gene expression and to enzymatically convert phosphatidate to diacylglycerol, an essential precursor
171 se, which catalyzes the dephosphorylation of phosphatidate to produce diacylglycerol at the endoplasm
172 sphatase catalyzing the dephosphorylation of phosphatidate to produce diacylglycerol, is one of the m
175 se, which catalyzes the dephosphorylation of phosphatidate to yield diacylglycerol, plays a crucial r
180 a negative regulatory effect on the level of phosphatidate used for the de novo synthesis of membrane
182 e dependence of phosphatidate phosphatase on phosphatidate was cooperative (n approximately 2.2) in t