戻る
「早戻しボタン」を押すと検索画面に戻ります。 [閉じる]

コーパス検索結果 (１語後でソート)

通し番号をクリックするとPubMedの該当ページを表示します
1 M induces a continuous activation in resting myosin ATPase.
2  unexpected from standard kinetic schemes of myosin ATPase.
3  rigor actin binding and actin-activation of myosin ATPase.
4 ct sensor initiating actin activation of the myosin ATPase.
5 m actin, thus triggering actin-activation of myosin ATPase.
6 ng actomyosin binding or actin-activation of myosin ATPase.
7 the ability of filamentous actin to activate myosin ATPase.
8 ributing to affinity and actin regulation of myosin ATPase.
9 e kinase, phosphatidylinositol 3-kinase, and myosin ATPase.
10 ed by inhibitors of actin polymerization and myosin ATPase.
11 thick filament OFF state and inhibiting acto-myosin ATPase.
12 ibition of actin activation of smooth muscle myosin ATPase.
13 time and increases ejection fraction through myosin ATPase activation.
14  investigated its kinase, actin binding, and myosin ATPase activities.
15  destabilize the cytoskeleton, or inhibiting myosin ATPase activity also resulted in MLC20 dephosphor
16 in binds to actin and inhibits activation of myosin ATPase activity and force production of striated
17  of Ca(2+) sensitivity of human beta-cardiac myosin ATPase activity are consistent with the hypothesi
18  reduced the rate of actin-activated cardiac myosin ATPase activity but had no effect on correspondin
19 experiments show the exon 7 domain modulates myosin ATPase activity but has no effect on actin filame
20         Caldesmon inhibits the activation of myosin ATPase activity by actin-tropomyosin.
21 nsus on the mechanism of inhibition of actin-myosin ATPase activity by caldesmon.
22 lecular level, we show that Ca(2+) increases myosin ATPase activity by shifting mavacamten-stabilized
23  Ca2+, myosin light chain phosphorylation or myosin ATPase activity during contractile stimulation.
24                    TA1 increased the rate of myosin ATPase activity in isolated bovine myofibrils and
25  Ca2+, myosin light chain phosphorylation or myosin ATPase activity in response to contractile stimul
26             The super-relaxed (SRX) state of myosin ATPase activity is critical for striated muscle f
27 -relaxed state of myosin (SRX), in which the myosin ATPase activity is strongly inhibited, has been o
28 , and the mechanism by which actin catalyses myosin ATPase activity is unclear.
29 vision, which has been shown to decrease the myosin ATPase activity of a number of myosins.
30 ne and synapse formation, whereas inhibiting myosin ATPase activity results in decreased spine and sy
31         No reduction in total CK activity or myosin ATPase activity was detected.
32 - tion-dependent regulation of smooth muscle myosin ATPase activity was investigated by forming two-
33                  However, 84% and 58% of the myosin ATPase activity was maintained when it was incuba
34  partial inhibition of the actin-tropomyosin-myosin ATPase activity was observed in the absence of Ca
35 not NM-IIB, independent of the inhibition of myosin ATPase activity with blebbistatin.
36                 After analyzing EPR spectra, myosin ATPase activity, and available structural informa
37 hair bundles, confirmed that bundles display myosin ATPase activity, and shown that the work performe
38 f actin and the steady-state actin-activated myosin ATPase activity.
39  with and without an allosteric modulator of myosin ATPase activity.
40  exhibiting substantial ATPase activity, and myosin ATPase activity.
41 oth muscle that inhibits actin activation of myosin ATPase activity.
42 erved in the maximal rate of actin-activated myosin ATPase activity.
43 -muscle myosins to wild-type Tau depended on myosin ATPase activity.
44 the same maximal actin-tropomyosin-activated myosin ATPase activity.
45 to bind to actin and inhibit actin-activated myosin ATPase activity; 1 mol of peptide is bound per ac
46  to regulate actin-tropomyosin(Tm)-activated myosin-ATPase activity.
47 ion and the inhibition of actin-Tm-activated myosin-ATPase activity.
48 chemical studies, that blebbistatin inhibits myosin ATPase and actin interaction by stabilizing the c
49 rotational flexibility of myosin S1 enhances myosin ATPase and actin sliding.
50 stantial inhibitory effects on activation of myosin ATPase and in vitro motility of F-actin: (1) bind
51 ta-cardiac myosin eliminates actin-activated myosin ATPase and reduces actomyosin affinity in rigor m
52 ctin-actin interaction for the activation of myosin ATPase and the polymerization of actin by S1.
53  C-loop, was recently demonstrated to affect myosin ATPase and was indirectly implicated in the actom
54                         Inhibitors of muscle myosin ATPases are needed to treat conditions that could
55           (1) In actin-tropomyosin-activated myosin ATPase assays at pCa 9, wild-type troponin caused
56 se activity in reconstituted actin-activated myosin ATPase assays was similar for all three TnT mutan
57 lost at 60 degrees C the ability to activate myosin ATPase at a 100-fold slower rate and unfolded in
58 tors of actin filaments (cytochalasin D) and myosin ATPase (butanedione monoxime), indicating that th
59 in the study of the kinetic mechanism of the myosin ATPase by fluorescence spectroscopy.
60 how that BS inhibits contractility and actin-myosin ATPase by stabilizing the OFF state of the thick
61 nsure tight reciprocal coupling between this myosin ATPase cycle and the macroscopic cardiac cycle.
62                  Modeling the complete actin.myosin ATPase cycle has always been limited by the lack
63  is not known which kinetic step in the acto-myosin ATPase cycle limits contraction speed in unloaded
64 at these compounds affect early steps of the myosin ATPase cycle to different extents.
65 P) to weakly (ATP) actin-bound states of the myosin ATPase cycle.
66 inding with nucleotide hydrolysis during the myosin ATPase cycle.
67 re controlled by the same steps in the actin-myosin ATPase cycle.
68 is maintained throughout the actin-activated myosin ATPase cycle.
69 in and throughout the entire actin-activated myosin ATPase cycle.
70 in orientations are coupled to force and the myosin ATPase cycle.
71  to elucidate key structural features of the myosin ATPase cycle.
72  levels of activation by disrupting the acto-myosin ATPase cycle.
73 onsistent with this idea, inhibiting ROCK or myosin ATPase disrupted myosin localization/organization
74 ated into protein expression, would decrease myosin ATPase enzyme velocity and slow speed of contract
75 e mechanisms by which ATP is supplied to the myosin ATPase, for muscle contraction, requires a highly
76                                     By using myosin ATPase histochemistry and anti-myosin heavy chain
77 na pipiens anterior tibialis muscle based on myosin ATPase histochemistry, size and location.
78 n with and without ADP, intermediates in the myosin ATPase hydrolytic pathway, are effective regulato
79 n, could inhibit actin-tropomyosin-activated myosin ATPase in the absence of Ca(2+), and two of them
80      Maximal activation of actin-tropomyosin-myosin ATPase in the presence of Ca(2+) was also decreas
81 e N509K relay mutation suppressed defects in myosin ATPase, in vitro motility, myofibril stability, a
82 in light chain kinase inhibitor ML-7 and the myosin ATPase inhibitor 2,3-butanedione-2-monoxime pertu
83      Inhibition of cell contraction with the myosin ATPase inhibitor blebbistatin attenuated oxidativ
84                                  Mavacamten, myosin ATPase inhibitor recently approved by the US Food
85                                   Adding the myosin ATPase inhibitor, 2,3-butanedione monoxide abolis
86                                          The myosin ATPase inhibitor, butanedione monoxime (BDM), rev
87  a slow phase, while butanedione monoxime, a myosin ATPase inhibitor, inhibited both the slow and fas
88 tility that can be reversed by mavacamten, a myosin ATPase inhibitor.
89  the structure-function relationships of two myosin ATPase inhibitors, mavacamten and para-nitroblebb
90 proteins involved in cell signaling than the myosin ATPase involved in cellular motility.
91 vator of myosin, we found that inhibition of myosin ATPase, myosin light chain kinase (MLCK), and the
92  of the dependence of the hydrolytic step of myosin ATPase on temperature and the requirement that hy
93 alcium concentration by disrupting the actin-myosin ATPase pathway.
94 O(4)3- complexes with specific states of the myosin-ATPase pathway.
95                      The correlation of acto-myosin ATPase rate with tension redevelopment kinetics (
96 Fenn effect that energy liberation (and acto-myosin ATPase rate) in muscle are increased during short
97  states with biochemical states in the actin-myosin ATPase reaction, and showed that a small shift in
98 but is not coupled to a specific step in the myosin ATPase reaction.
99 nhibition of actin-tropomyosin activation of myosin ATPase requires less than one peptide per seven a
100 f actomyosin contractility (specifically, of myosin ATPase, Rho kinase, or myosin light-chain kinase
101 ion of the actin activation of smooth muscle myosin ATPase since CaD-(1-717) caused only 30% of the i
102 some muscles, fibre types were determined by myosin ATPase staining following alkali pre-incubation.
103 le abnormalities in R58Q vs. wild-type mice, myosin ATPase staining revealed a decreased proportion o
104 tin is necessary for actin activation of the myosin ATPase, this finding explains the low metabolic c

 
Page Top