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1 PC-PLC activation occurred at pH 7.0 and lower, but not
2 PC-PLC activation occurs in the acidified vacuolar envir
3 PC-PLC is made as a proenzyme whose maturation is mediat
4 PC-PLC is made as an inactive proenzyme whose activation
5 PC-PLC requires cleavage of an N-terminal propeptide for
6 PC-PLC secreted into infected cells was immunoprecipitat
7 PC-PLC, encoded by plcB, is a broad-range phospholipase,
10 ctivation of PC-PLC and that activation of a PC-PLC is an important component of macrophage activatio
15 in, Go, in the regulation of cell growth and PC-PLC-mediated hydrolysis of PC in IIC9 fibroblasts.
16 ology produced by pure HBL, and both HBL and PC-PLC were detected at toxic concentrations in infected
18 esults describe a novel function for LLO and PC-PLC and suggest that L. monocytogenes may use these v
19 A2 regulates compartmentalization of Mpl and PC-PLC, possibly by influencing cell wall properties and
23 ese data suggest that bacterially associated PC-PLC and Mpl localize at the cell wall-membrane interf
24 anthracis eliminated the activities of both PC-PLC and SPH, whereas introduction into B. anthracis o
27 ties of phosphatidylcholine-phospholipase C (PC-PLC) and protein kinase (PK) C and enhanced NO produc
28 hosphatidylcholine-specific phospholipase C (PC-PLC) and sphingomyelinase (SPH), encoded by the plc a
31 hosphatidylcholine-specific phospholipase C (PC-PLC) is a necessary intermediate in transducing apopt
32 atidylcholine (PC)-specific phospholipase C (PC-PLC) is linked to activation of the p42/44 (ERK) kina
35 hosphatidylcholine-specific phospholipase C (PC-PLC) of L. monocytogenes, is a potent inhibitor of in
36 idylcholine (PC)-preferring phospholipase C (PC-PLC) of Listeria monocytogenes plays a role in the ba
38 hosphatidylcholine-specific phospholipase C (PC-PLC) to the pathogenesis of experimental Bacillus end
39 hosphatidylcholine-specific phospholipase C (PC-PLC), inhibited Ca(2+)-induced 5-HT release to 50% of
40 tors of phosphatidylcholine phospholipase C (PC-PLC), PKC (including pseudosubstrate peptides, cheler
41 s is a secreted broad-range phospholipase C (PC-PLC), the activation of which requires processing of
42 ated in part by a bacterial phospholipase C (PC-PLC), whose activation requires cleavage of an N-term
50 shown that the broad-range phospholipase C, PC-PLC, promotes lysis of Henle 407 cell primary vacuole
51 assess the importance of compartmentalizing PC-PLC activity during infection, we created a mutant th
53 three Legionella enzymes and P. fluorescens PC-PLC share conserved domains also present in uncharact
54 nd Mpl-minus bacteria stained positively for PC-PLC, in contrast to less than 5% in untreated cells.
55 peculate that the additional requirement for PC-PLC activity is for lysis of secondary double-membran
56 nd Bacillus cereus PLC (PLCBc), we generated PC-PLC mutants with altered enzymatic activities and sub
58 armacological approach was used to implicate PC-PLC --> PKC --> NO signaling as being important for t
59 ibutes to B. cereus virulence and implicates PC-PLC and collagenase as additional virulence factors.
65 we demonstrate that, in the absence of LLO, PC-PLC activity is not only required for lysis of primar
67 observed that all three Mpl mutants mediate PC-PLC activation when bacteria are grown on semisolid m
71 tivates the ERK kinases is via activation of PC-PLC and that activation of a PC-PLC is an important c
72 slow response to 5-HT involves activation of PC-PLC by G alpha o to liberate diacylglycerol, which st
78 re, our results indicated that the amount of PC-PLC activity is critical for the efficiency of vacuol
81 ition, similarly to Mpl-mediated cleavage of PC-PLC propeptide, Mpl-mediated translocation of PC-PLC
83 . monocytogenes strain 10403S, expression of PC-PLC has to increase before or upon entry into human e
84 y can be increased by elevated expression of PC-PLC or Mpl, the enzyme required for proteolytic activ
90 In this study, the pH-dependent mechanism of PC-PLC activation was investigated by manipulating the i
91 ial cell wall and confirmed that the pool of PC-PLC associated with bacteria was efficiently activate
92 cellular growth, bacteria maintain a pool of PC-PLC that is not accessible to antibodies and that is
93 ormation of a bacterially associated pool of PC-PLC that would readily be accessible for activation a
95 2, indicating that neither the propeptide of PC-PLC nor PrsA2 is required for native folding of the c
96 stinct possibility that many of the roles of PC-PLC, especially in cell transformation, may be attrib
97 terize the mechanism regulating secretion of PC-PLC, the bacterial localization of PC-PLC and Mpl was
98 iated via the CDC28-dependent stimulation of PC-PLC activity in a novel cell cycle-regulated signalin
99 ages indicated that the rate of synthesis of PC-PLC exceeded the rate of translocation across the bac
101 LC propeptide, Mpl-mediated translocation of PC-PLC across the bacterial cell wall is pH sensitive.
102 membrane interface and that translocation of PC-PLC across the bacterial cell wall is rate limiting,
103 y, we showed that cell wall translocation of PC-PLC is inefficient, resulting in accumulation of PC-P
104 cted cells, rapid cell wall translocation of PC-PLC is triggered by a decrease in pH and correlates w
105 ide and of Mpl in cell wall translocation of PC-PLC, we generated a cleavage site mutant and a propep
107 hospholipases C (PLC), a broad spectrum PLC (PC-PLC) and a phosphatidylinositolspecific PLC (PI-PLC).
109 itionally, AEOW reduced LOX, lipase, PI-PLC, PC-PLC, and PLD activities, maintained higher levels of
111 ll, these results suggest that Mpl regulates PC-PLC translocation across the bacterial cell wall in a
112 er, TNF-alpha induced mPGES-1 by stimulating PC-PLC --> PKC --> NO --> cGMP --> PKG signal transducti
119 fficient translocation of the proform of the PC-PLC cleavage site mutant in a manner that was pH sens
120 oteins, we determined that processing of the PC-PLC propeptide by mature Mpl is also pH sensitive.
122 Substitutions D4E and H56Y remodeled the PC-PLC active site to more closely resemble the PLCBc ac
124 a is the conclusion that the members of this PC-PLC and phosphatase family possess a novel mechanism
126 e to gentamicin, suggesting that unregulated PC-PLC activity causes damage to host cell membranes.
127 -PLC is secreted in an active state, whereas PC-PLC is secreted as an inactive proenzyme (proPC-PLC)
128 LLO was sufficient for inducing FasL, while PC-PLC synergized with LLO for the induction of FasL exp