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1  major substrates are myosin light chain and myosin phosphatase.
2 th siRNA prevented ATP-induced activation of myosin phosphatase.
3 phatase, indicating that it does not inhibit myosin phosphatase.
4 eased phosphatase activity of phosphorylated myosin phosphatase.
5 ated and converted to a potent inhibitor for myosin phosphatase.
6 eloped two reagents with opposing effects on myosin phosphatase.
7  mutant of MBS that constitutively activates myosin phosphatase.
8 ion with the myosin-binding subunit (MBS) of myosin phosphatase.
9 ther TIMAP/PP1cbeta could also function as a myosin phosphatase.
10 ified a novel interaction between Nkx2.5 and myosin phosphatase.
11 cell cluster through localized inhibition of myosin phosphatase.
12 elium to show the consequences of modulating myosin phosphatase.
13 t dependent on myosin light chain kinase and myosin phosphatase.
14 tance vessels by influencing the activity of myosin phosphatase.
15 osphorylation and subsequent inactivation of myosin phosphatase.
16                          We demonstrate that Myosin phosphatase, a complex of Protein phosphatase 1 a
17 7) and Ser(854)-Thr(855) phosphorylations on myosin phosphatase activity and contraction are unknown.
18               After 20 min of nitroprusside, myosin phosphatase activity had declined to basal levels
19                         Thus, TIMAP inhibits myosin phosphatase activity in ECs by competing with MYP
20 rial contractility is governed by regulating myosin phosphatase activity in response to agonist stimu
21 ation of nitroprusside at the same time that myosin phosphatase activity increased, suggesting that t
22                                              Myosin phosphatase activity is critical to the regulatio
23 atase in cell division, the possibility that myosin phosphatase activity may be altered during cell d
24                   In vitro SMTNL1 suppresses myosin phosphatase activity through a substrate-directed
25 30-kDa subunit and resulted in inhibition of myosin phosphatase activity was not identified.
26 oprusside, when force declined, increases in myosin phosphatase activity, concurrent with cGMP-mediat
27 hat regulate actin cytoskeleton dynamics and myosin phosphatase activity, including focal adhesion ki
28                                              Myosin phosphatase activity, myosin light chain phosphor
29 e-dependent protein kinases had no effect on myosin phosphatase activity, whereas phosphorylation at
30  explain Ca2+ sensitization is inhibition of myosin phosphatase activity.
31 on of cGMP and a large transient increase in myosin phosphatase activity.
32 hospho-CPI-17 contributed to the increase in myosin phosphatase activity.
33 af-1 in the regulation of pathways involving myosin phosphatase activity.
34 antibody against MBS that is able to inhibit myosin phosphatase activity.
35             We have previously reported that myosin phosphatase also controls mitosis, apparently by
36 dressed how CPI-17 could selectively inhibit myosin phosphatase among other protein phosphatase-1 (PP
37 etion of the myosin binding subunit (Mbs) of myosin phosphatase, an antagonist of myosin II activatio
38 rotein-coupled receptor agonists can inhibit myosin phosphatase and cause smooth muscle cell contract
39 hoA/Rho kinase, whereas NO/cGMP can activate myosin phosphatase and cause smooth muscle cell relaxati
40  in situ, thereby regulating the activity of myosin phosphatase and contraction.
41 ectly bound to the Myosin-binding subunit of Myosin phosphatase and decreased Myosin dephosphorylatio
42 ooth muscle cells (VSMCs) via stimulation of myosin phosphatase and inhibition of Rho kinase activity
43 orylates the myosin binding subunit (MBS) of myosin phosphatase and inhibits the phosphatase activity
44                               Par-1 binds to myosin phosphatase and phosphorylates it at a known inac
45 e, we describe the association of Raf-1 with myosin phosphatase and phosphorylation of the regulatory
46 tly binds both the myosin binding subunit of myosin phosphatase and RhoA and is localized to actin-my
47 6-kDa human protein that interacts with both myosin phosphatase and RhoA.
48  is a phosphorylation-dependent inhibitor of myosin phosphatase and, in response to agonists, Thr-38
49 ation was associated with high expression of myosin phosphatase and/or reduced myosin light-chain kin
50  targeting subunit (MYPT1) by the endogenous myosin phosphatase-associated kinase, MYPT1 kinase.
51 tase, suggesting that ROCK not only inhibits myosin phosphatase but also phosphorylates MLC directly
52 ed phosphorylation of myosin light chain and myosin phosphatase, but not LIM kinase, suggesting that
53 e regulatory myosin-binding subunit (MBS) of myosin phosphatase by Raf-1.
54 at PP1 phosphatase, the catalytic subunit of myosin phosphatase, can regulate PDE5 dephosphorylation.
55 ify PPP1R12A and PPP1CB, two subunits of the myosin phosphatase complex that antagonizes actomyosin c
56 e-Rho interacting protein as a member of the myosin phosphatase complex that directly binds both the
57 ing subunit 1 (MYPT1), two components of the myosin phosphatase complex, as HDAC7-associated proteins
58 ial association of MYPT1 with PP1beta in the myosin phosphatase complex.
59 n, and efficient operation of multimolecular myosin phosphatase complexes that include myosin IIA, pr
60 ctly dephosphorylating SA2, and the other is myosin phosphatase counteracting PLK1.
61                                              Myosin phosphatase dephosphorylates HDAC7 and promotes i
62 phila melanogaster myosin binding subunit of myosin phosphatase (DMYPT) in both processes.
63                            The activation of myosin phosphatase during mitosis would enhance dephosph
64    Histamine stimulus triggers inhibition of myosin phosphatase-enhanced phosphorylation of myosin an
65               We find that by inhibiting the myosin phosphatase, ERK and RSK promote myosin II-mediat
66                            The inhibition of myosin phosphatase evokes smooth muscle contraction in t
67                                              Myosin phosphatase from smooth muscle consists of a cata
68 phosphatase catalytic subunit (PP1c) and the myosin phosphatase holoenzyme (MBP) were compared using
69 tein phosphatase 1 subunit PP1cbeta, forming myosin phosphatase holoenzymes.
70 ase) and MEL-11 (a myosin-binding subunit of myosin phosphatase), impairs ovulation.
71                   To explore the function of myosin phosphatase in cell division, the possibility tha
72 f a unique positive regulatory mechanism for myosin phosphatase in cell division.
73 induced by agents that inhibit smooth muscle myosin phosphatase in the absence of Ca2+ may be mediate
74 ds directly to the myosin binding subunit of myosin phosphatase in vivo in vascular smooth muscle cel
75             On the other hand, inhibition of myosin phosphatase increased MLC phosphorylation and blo
76     Consistent with this model, depletion of myosin phosphatase increased the velocity of ring moveme
77               Concurrently, AMPK inactivates Myosin Phosphatase, increasing Myosin II-dependent amoeb
78  phosphorylate the myosin binding subunit of myosin phosphatase, indicating that it does not inhibit
79  light chain phosphorylation or depletion of myosin phosphatase inhibit Myo-II contractile pulses, di
80 ROCK) Ca(2+)-sensitizing pathways leading to myosin phosphatase inhibition are critically involved in
81 on and inhibition of myosin phosphatase, the myosin phosphatase inhibitor CPI17, or direct phosphoryl
82                                    CPI-17, a myosin phosphatase inhibitor phosphoprotein, is phosphor
83 -targeting protein MYPT1 and increase in the myosin phosphatase inhibitor protein CPI-17.
84  subunit 1, and protein kinase C-potentiated myosin phosphatase inhibitor) and integrins were reduced
85 rough which phorbol esters and smooth muscle myosin phosphatase inhibitors can induce contraction of
86                              We propose that Myosin phosphatase is a crucial and tightly controlled r
87                                              Myosin phosphatase is a heterotrimeric holoenzyme consis
88                                Inhibition of myosin phosphatase is critical for agonist-induced contr
89                                              Myosin phosphatase is localized not only at actin-myosin
90                      The mechanisms by which myosin phosphatase is targeted to these loci are incompl
91                                              Myosin phosphatase is the primary effector of smooth mus
92  Myosin light chains are dephosphorylated by myosin phosphatase, leading to vascular smooth muscle re
93 KG I and its subsequent dephosphorylation by myosin phosphatase may be key steps in the regulation of
94 n response to vasoconstrictors by inhibiting myosin phosphatase (MLCP) activity and increasing myosin
95                                              Myosin phosphatase (MLCP) plays a critical regulatory ro
96 y is through inhibition of the smooth muscle myosin phosphatase (MLCP) that dephosphorylates the RLC
97 kinase I (PKG-Ialpha)-mediated activation of myosin phosphatase (MLCP).
98                        This study identifies myosin phosphatase (MP) holoenzyme consisting of protein
99                                              Myosin phosphatase (MP) is a key regulator of myosin lig
100                  The phosphatase activity of myosin phosphatase (MP) that dephosphorylates MLC is ina
101             Dephosphorylation is mediated by myosin phosphatase (MP), a complex that consists of a ca
102 This reaction is catalyzed by the holoenzyme myosin phosphatase (MP), which includes the catalytic su
103 activation involves PIP(2) hydrolysis and/or myosin phosphatase (MP).
104                                          The myosin phosphatase (MP)/protein arginine methyltransfera
105                             Neither cellular myosin phosphatase, myosin light chain kinase, nor RhoA
106 myosin (pMLC), and the regulatory subunit of myosin phosphatase (MYPT1) were determined by Western bl
107  proteins, PP-1bp55, was homologous to human myosin phosphatase, MYPT2.
108  kinase C-potentiated inhibitory protein for myosin phosphatase of 17 kDa (CPI-17), prostate apoptosi
109          Furthermore, both overexpression of myosin phosphatase or inhibition of the myosin light-cha
110  with measurements of myosin light chain and myosin phosphatase phosphorylation.
111                             We show that the myosin phosphatase Pp1 complex, which inhibits non-muscl
112 ignificantly enhanced the phosphorylation of myosin phosphatase, promoted assembly of stress fibers,
113 BS, suggesting that M-RIP may play a role in myosin phosphatase regulation by RhoA.
114                            A mutation in the myosin phosphatase regulator mypt1 results in a small ve
115 escued by depletion of the YAP/TAZ-dependent myosin phosphatase regulator, NUAK2, or by inhibition of
116 xpress the phosphatase inhibitor CPI-17, the myosin phosphatase regulatory (MYPT-1) and catalytic (PP
117 nd vasodilator pathways inhibit and activate myosin phosphatase, respectively.
118                              Among them, the myosin phosphatase rho-interacting protein (MPRIP) links
119 BFOX2-regulated splicing events, such as via myosin phosphatase RHO-interacting protein (MPRIP), is a
120               This reduction in stress fiber myosin phosphatase-Rho interacting protein and myosin bi
121                       We recently identified myosin phosphatase-Rho interacting protein as a member o
122 NA interference to silence the expression of myosin phosphatase-Rho interacting protein in human vasc
123                                              Myosin phosphatase-Rho interacting protein silencing red
124                                 Furthermore, myosin phosphatase-Rho interacting protein silencing res
125  kinase, nor RhoA activities were changed by myosin phosphatase-Rho interacting protein silencing.
126                         We hypothesized that myosin phosphatase-Rho interacting protein targets myosi
127         These data support the importance of myosin phosphatase-Rho interacting protein-dependent tar
128                                         This myosin phosphatase-RhoA interacting protein, or M-RIP, i
129  translocation via a previously unrecognized myosin phosphatase-RhoA-interacting protein-dependent pa
130  adenosine or ATPgammaS downstream effector, myosin phosphatase, significantly attenuated the E. coli
131                  Regulation of smooth muscle myosin phosphatase (SMPP-1M) is thought to be a primary
132 nd catalytic, 37-kDa, PP1c) of smooth muscle myosin phosphatase (SMPP-1M), we determined, in Triton-X
133            5-HT increased phosphorylation of myosin phosphatase subunit 1 (Mypt-1), a known ROCK targ
134 .5 from differentiating cells identified the myosin phosphatase subunits protein phosphatase 1beta an
135 CK activity in addition to the inhibition of myosin phosphatase, suggesting that ROCK not only inhibi
136 t PP1 regulatory subunit and a member of the myosin phosphatase target (MYPT) protein family.
137  inhibited the consequent phosphorylation of myosin phosphatase target subunit (MYPT1) and the expres
138 osin light chain phosphatase (MLCP) subunits myosin phosphatase target subunit 1 (MYPT1) and protein
139 iation between NF2 and its activator MYPT-1 (myosin phosphatase target subunit 1) in cardiomyocytes,
140 ractile response (myosin light chain kinase, myosin phosphatase target subunit 1, and protein kinase
141                                 We show that myosin phosphatase target subunit 1- protein phosphatase
142 is balance is achieved by interaction of the myosin phosphatase target subunit of myosin phosphatase
143 f myosin binding subunit 85 (MBS85), another myosin phosphatase targeting subunit (MYPT) family membe
144                       We have found that the myosin phosphatase targeting subunit (MYPT) undergoes mi
145 We are using the tissue-specific splicing of myosin phosphatase targeting subunit (MYPT1) as a model
146 ho-associated kinase, that phosphorylate the myosin phosphatase targeting subunit (MYPT1) at Thr(697)
147    Alternative splicing of the smooth muscle myosin phosphatase targeting subunit (Mypt1) exon 23 (E2
148 on of MLCP induced by the phosphorylation of myosin phosphatase targeting subunit (MYPT1), a regulato
149 ooth muscle express distinct isoforms of the myosin phosphatase targeting subunit (MYPT1), and the is
150 phosphorylation and dephosphorylation of the myosin phosphatase targeting subunit (MYPT1).
151                Isoforms of the smooth muscle myosin phosphatase targeting subunit 1 (MYPT1) are gener
152 atase subunits protein phosphatase 1beta and myosin phosphatase targeting subunit 1 (Mypt1) as novel
153 ase inhibitor protein of 17 kDa (CPI-17) and myosin phosphatase targeting subunit 1 (MYPT1) phosphory
154 otein phosphatase 1 (PP1) regulatory subunit myosin phosphatase targeting subunit 1 (MYPT1) to activa
155 s I and II, and the total and phosphorylated myosin phosphatase targeting subunit 1 (MYPT1) were asse
156               One Cyclin A/Cdk1 substrate is myosin phosphatase targeting subunit 1 (MYPT1), and we s
157 tify protein phosphatase 1beta (PP1beta) and myosin phosphatase targeting subunit 1 (MYPT1), two comp
158 l adhesion kinase, myosin light chain 2, and myosin phosphatase targeting subunit 1 in primary human
159                                       MYPT1 (myosin phosphatase targeting subunit 1) is responsible f
160 osphatase found in cardiac myocytes contains Myosin Phosphatase Targeting Subunit 2 (MYPT2).
161 es phosphorylation of both myosin II and the myosin phosphatase targeting subunit MYPT1 to synergisti
162 tion is due to the binding of p116Rip to the myosin phosphatase targeting subunit MYPT1.
163 en PP1 and a 34-kDa N-terminal domain of the myosin phosphatase targeting subunit MYPT1.
164 tein phosphatase 1c, PP1c), a large subunit (myosin phosphatase targeting subunit, MYPT), and a small
165  SMTNL1 deletion was associated with loss of myosin phosphatase-targeting protein MYPT1 and increase
166 cell lines and found that RSK phosphorylates myosin phosphatase-targeting subunit 1 (MYPT1) at Ser-50
167                                              Myosin phosphatase-targeting subunit 1 (MYPT1) binds to
168 is a heterotrimeric holoenzyme consisting of myosin phosphatase-targeting subunit 1 (MYPT1), a cataly
169  (CPI-17), prostate apoptosis response-4, or myosin phosphatase-targeting subunit 1 (MYPT1), all of w
170 rmation of a signaling complex of RhoA/ROCK2/myosin phosphatase-targeting subunit 1 (MYPT1).
171 ry target gene of SMTNL1 in these muscles is myosin phosphatase-targeting subunit 1 (MYPT1).
172  myosin IIA, protein phosphatase 1delta, and myosin phosphatase-targeting subunit 1, BIG1 and BIG2 se
173  been impaired, the levels of phosphorylated myosin phosphatase-targeting subunit 1, the regulatory s
174 rgeting subunit 1, the regulatory subunit of myosin phosphatase that is inhibited by Rho-kinase, were
175                                              Myosin phosphatase, the key enzyme controlling myosin li
176 ugh either phosphorylation and inhibition of myosin phosphatase, the myosin phosphatase inhibitor CPI
177 e regulated by myosin light-chain kinase and myosin phosphatase through phosphorylation and dephospho
178 o interacting protein-dependent targeting of myosin phosphatase to stress fibers for regulating myosi
179                                 Targeting of myosin phosphatase to the cell membrane precedes the dis
180  phosphatase-Rho interacting protein targets myosin phosphatase to the contractile apparatus to depho
181 the epithelium must ;relax', via activity of myosin phosphatase, to allow for normal hindbrain morpho
182 ntracellular Ca2+, but involve activation of myosin phosphatase via a novel G-protein-coupled mechani
183 y and microtubule acetylation is mediated by myosin phosphatase via controlled activation and deactiv
184 ro experiments showing the activation of the myosin phosphatase via heterophilic leucine zipper inter
185              The MYPT1 regulatory subunit of myosin phosphatase was concentrated only in the fraction
186                 Furthermore, the activity of myosin phosphatase was increased more than twice and it
187        The regulatory subunit (MYPT1) of the myosin phosphatase was phosphorylated in PC3 cells and H
188  of the myosin phosphatase target subunit of myosin phosphatase with either myosin light chain or HDA

 
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