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1                                              MLCP activity may arise from functionally shared roles b
2                                              MLCP dephosphorylated phosphoserine 19, phosphothreonine
3                                              MLCP dephosphorylates pCPI-17 at a slow rate that is, no
4                                              MLCP with its regulatory subunit MYPT2 bound tightly to
5 ity is regulated by the phosphorylation of a MLCP-specific inhibitor, CPI17 at Thr38 and MBS (myosin
6 stration mechanism through which pCPI-17 and MLCP interact inhibition by unfair competition: MLCP pro
7 scle depend on myosin light chain kinase and MLCP activities without changes in constitutive MYPT1 ph
8 th muscle appear to be dependent on MLCK and MLCP activities without changes in constitutive MYPT1 ph
9 osphatase (MLCP) targeting subunit MYPT1 and MLCP inhibitor protein CPI-17 were examined.
10 ent tissues may be similar to the attenuated MLCP activity in wild-type tissues resulting from consti
11 ficient tissues may be similar to attenuated MLCP activity in wild-type tissues resulting from consti
12 PP1delta) from MYPT1 and inhibition of basal MLCP activity.
13 delta from MYPT1, and thereby restored basal MLCP activity leading to a decrease in phospho-MLC.
14                                      Because MLCP activity is regulated by the phosphorylation of a M
15  for phosphorylation by a soluble cMLCK, but MLCP activity limits the amount of constitutive RLC phos
16 lation rate of serine 19 and threonine 18 by MLCP.
17 of RLC in the dephosphorylation of myosin by MLCP.
18 irming that RLC-phosphorylation regulated by MLCP, enhances cardiac performance in vivo.
19 uclear transport factors, and is reversed by MLCP.
20 h MYPT2 as the regulatory subunit of cardiac MLCP, distinct from the ubiquitously expressed canonical
21  limited information is available on cardiac MLCP.
22 nockout mice to biochemically define cardiac-MLCP proteins and developed a cardiac myofibrillar phosp
23  that the main catalytic subunit for cardiac-MLCP is PP1cbeta, and maintenance of RLC phosphorylation
24 ntribute to our understanding of the cardiac-MLCP in vivo.
25      Previously, the identity of the cardiac-MLCP was biochemically shown to be similar to the smooth
26 P interact inhibition by unfair competition: MLCP protects pCPI-17 from other phosphatases, while pCP
27  the myosin light chain phosphatase complex (MLCP).
28 pCPI-17 dephosphorylation and the consequent MLCP activation during muscle relaxation.
29 h muscle contractility because the effective MLCP activity is not changed.
30                                  A model for MLCP regulation via its regulatory MYPT1 subunit and int
31 , while pCPI-17 blocks other substrates from MLCP's active site.
32                                 Furthermore, MLCP activity may arise from functionally shared roles b
33 muscle with a relatively low CPI-17 and high MLCP content.
34 rylation of p-MYPT1, consequently increasing MLCP activity and thus decreasing p-MRLC.
35 okin is to modulate force through increasing MLCP activity and that this effect is further potentiate
36 on toward dephosphorylation, thus increasing MLCP activity.
37 l esters and diacylglycerol can also inhibit MLCP by phosphorylating and thereby activating CPI-17, a
38 osphorylation, which is predicted to inhibit MLCP activity in isolated ileal smooth muscle tissues, w
39 ist-induced MYPT1 phosphorylation to inhibit MLCP activity.
40 Ca(2+) sensitizing mechanisms for inhibiting MLCP besides phosphorylation of MYPT1 and CPI-17.
41 ed CPI-17 specifically and potently inhibits MLCP in vitro and in situ and is activated when phosphor
42 ed in beating hearts at a site that inhibits MLCP activity.
43                                     Instead, MLCP itself is the critical enzyme for pCPI-17 dephospho
44 ial smooth muscle with a high CPI-17 and low MLCP expression generated greater force and MLC phosphor
45 ly by low cMLCK activity in balance with low MLCP activity.
46 sion patterns, phasic muscles contained more MLCP myosin-targeting subunit than tonic tissues.
47 lly shown to be similar to the smooth muscle MLCP, which is a well-characterized trimeric protein com
48 iquitously expressed canonical smooth muscle MLCP.
49 ly bound to myosin, thus facilitating myosin/MLCP interaction.
50 ed inhibition and cGMP-induced activation of MLCP.
51 esting conditions, predicting attenuation of MLCP activity.
52 -696 and Thr-853 causes an autoinhibition of MLCP that accounts for Ca(2+) sensitization of smooth mu
53 n depend upon the relative concentrations of MLCP compared to CPI-17, and the specific activities of
54 ting conditions, predicting a high extent of MLCP phosphatase inhibition.
55 ic acid may also contribute to inhibition of MLCP acting, at least in part, through the Rho/Rho-kinas
56 itor protein CPI-17 results in inhibition of MLCP activity.
57         This implicates CPI-17 inhibition of MLCP as an important component in modulating vascular mu
58 ant role in G-protein-mediated inhibition of MLCP in tonic arterial smooth muscle.
59 d the mechanism underlying the inhibition of MLCP induced by the phosphorylation of myosin phosphatas
60 Thr(38) may contribute towards inhibition of MLCP while the phasic visceral VD, which has a low CPI-1
61 he dual activation of MLCK and inhibition of MLCP.
62 omain of the myosin binding subunit (MBS) of MLCP are localized in the C terminus of MBS.
63 re in accord with literature measurements of MLCP and CPI-17 phosphorylation states during agonist st
64 n important role in substrate recognition of MLCP.
65 the mechanism of ROCK-mediated regulation of MLCP are not well understood.
66       The effects of the different routes of MLCP regulation depend upon the relative concentrations
67 gments docked directly at the active site of MLCP, and this was blocked by a PP1/PP2A inhibitor micro
68                               Specificity of MLCP toward the various phosphorylation sites of RLC was
69 ion between PKG and the targeting subunit of MLCP (MYPT1) is not fully understood.
70 hat phosphorylates the regulatory subunit of MLCP and inhibits phosphatase activity.
71  at Thr38 and MBS (myosin binding subunit of MLCP) at Thr696, we examined the effect of 8-Br-cGMP on
72 ing subunit (MYPT1), a regulatory subunit of MLCP, at Thr-696 and Thr-853 using glutathione S-transfe
73 nd directly to the myosin binding subunit of MLCP, yet both ROCK isoforms regulated MLCP and myosin l
74 was also found with the catalytic subunit of MLCP.
75 ctivated the myosin light chain phosphatase (MLCP) activity of the holoenzyme.
76  decrease in myosin light-chain phosphatase (MLCP) activity, which was reflected in a significant lef
77  increase in myosin light chain phosphatase (MLCP) activity.
78 elaxation by myosin light chain phosphatase (MLCP) containing regulatory (MYPT1) and catalytic (PP1cd
79 terotrimeric myosin light chain phosphatase (MLCP) has been assigned as a physiological phosphatase t
80 egulation of myosin light chain phosphatase (MLCP) in response to agonist stimulation and cAMP/cGMP s
81              Myosin light chain phosphatase (MLCP) plays a pivotal role in smooth muscle contraction
82 entified the myosin light chain phosphatase (MLCP) subunits myosin phosphatase target subunit 1 (MYPT
83 tion of RLC, myosin light chain phosphatase (MLCP) targeting subunit MYPT1 and MLCP inhibitor protein
84 n kinase and myosin light chain phosphatase (MLCP), is fundamental to the biochemical and physiologic
85 on levels of myosin light chain phosphatase (MLCP), the MLCP inhibitor phosphoprotein CPI-17, and the
86 n kinase and myosin light chain phosphatase (MLCP), which contains a regulatory subunit MYPT1 bound t
87 horylated by myosin light chain phosphatase (MLCP).
88 n kinase and myosin light chain phosphatase (MLCP).
89 e (MLCK) and myosin light chain phosphatase (MLCP).
90 nhibition of myosin light chain phosphatase (MLCP).
91 e (MLCK) and myosin light chain phosphatase (MLCP).
92 -17 inhibits myosin light-chain phosphatase (MLCP).
93 t (P-MBS) of myosin light chain phosphatase (MLCP).
94 ctivation of myosin light chain phosphatase (MLCP).
95 egulation of myosin light chain phosphatase (MLCP).
96 n kinase and myosin light chain phosphatase (MLCP).
97 ance between MLC kinase and MLC phosphatase (MLCP) activities.
98                             MLC phosphatase (MLCP) activity, once decreased by agonist-stimulation, r
99 ed by MLC kinase (MLCK) and MLC phosphatase (MLCP), the latter being a holoenzyme that involves inter
100 CK)-dependent inhibition of MLC phosphatase (MLCP), we examined the effects of cAMP on this pathway.
101 hibitory phosphorylation of MLC phosphatase (MLCP).
102  associated with decreased MRLC phosphatase (MLCP) activity, and increased Ca(2+) sensitivity of both
103 nstrictors by inhibiting myosin phosphatase (MLCP) activity and increasing myosin light chain phospho
104                          Myosin phosphatase (MLCP) plays a critical regulatory role in the Ca(2+) sen
105 ion of the smooth muscle myosin phosphatase (MLCP) that dephosphorylates the RLC in smooth muscle and
106 )-mediated activation of myosin phosphatase (MLCP).
107 Thr-696 and only Thr-853, inhibited purified MLCP (IC(50) = 1.6 and 60 nm, respectively) when they we
108      The rate of force relaxation reflecting MLCP activity, in the presence of 50 microM 8-Br-cGMP, w
109 hat although the ROCK isoforms both regulate MLCP and myosin light chain phosphorylation through diff
110 it of MLCP, yet both ROCK isoforms regulated MLCP and myosin light chain phosphorylation.
111  Despite that both ROCK1 and ROCK2 regulated MLCP, the ROCK isoforms had distinct and opposing effect
112  the RhoA signaling pathway, thus regulating MLCP activity and myosin phosphorylation in cells.
113 sphorylate and inactivate pCPI-17 to restore MLCP activity.
114 osphorylated MBS at Ser695 partially resumed MLCP activity inhibited by Thr696 phosphorylation.
115 pothesized that the striated muscle-specific MLCP regulatory subunit, MYPT2, targets the phosphatase
116 g muscle relaxation, phosphatases other than MLCP dephosphorylate and inactivate pCPI-17 to restore M
117                                          The MLCP is a trimeric enzyme with a catalytic, a 20-kDa and
118 f myosin light chain phosphatase (MLCP), the MLCP inhibitor phosphoprotein CPI-17, and the thin filam
119 (PP1alpha), a known catalytic subunit of the MLCP in VSMCs, as a potent repressor of MEF2 activity.
120 latory subunit (MYPT1) and at Thr(38) of the MLCP inhibitor protein CPI-17 results in inhibition of M
121 sted that phosphorylation at Thr(695) of the MLCP regulatory subunit (MYPT1) and at Thr(38) of the ML
122 e investigated the physiological role of the MLCP regulatory subunit MYPT1 in bladder smooth muscle c
123 e investigated the physiological role of the MLCP regulatory subunit MYPT1 in ileal smooth muscle in
124 of 8-Br-cGMP on the phosphorylation of these MLCP modulators.
125 e mechanism of NO-induced relaxation through MLCP deinhibition, we compared time-dependent changes in
126 clude that the expression ratio of CPI-17 to MLCP correlates with the Ca(2+) sensitivities of contrac
127 subunit (MYPT) family member, in addition to MLCP regulatory subunit MYPT1.
128 ion of MX2 by phosphorylation, together with MLCP-mediated dephosphorylation, balances the deleteriou

 
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