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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 thick filament OFF state and inhibiting acto-myosin ATPase.
5 ct sensor initiating actin activation of the myosin ATPase.
6 m actin, thus triggering actin-activation of myosin ATPase.
7 ng actomyosin binding or actin-activation of myosin ATPase.
8 the ability of filamentous actin to activate myosin ATPase.
9 ributing to affinity and actin regulation of myosin ATPase.
10 e kinase, phosphatidylinositol 3-kinase, and myosin ATPase.
11 ed by inhibitors of actin polymerization and myosin ATPase.
12 ibition of actin activation of smooth muscle myosin ATPase.
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
22 Ca2+, myosin light chain phosphorylation or myosin ATPase activity during contractile stimulation.
23 Ca2+, myosin light chain phosphorylation or myosin ATPase activity in response to contractile stimul
24 -relaxed state of myosin (SRX), in which the myosin ATPase activity is strongly inhibited, has been o
26 ne and synapse formation, whereas inhibiting myosin ATPase activity results in decreased spine and sy
28 - tion-dependent regulation of smooth muscle myosin ATPase activity was investigated by forming two-
30 partial inhibition of the actin-tropomyosin-myosin ATPase activity was observed in the absence of Ca
33 hair bundles, confirmed that bundles display myosin ATPase activity, and shown that the work performe
38 to bind to actin and inhibit actin-activated myosin ATPase activity; 1 mol of peptide is bound per ac
41 chemical studies, that blebbistatin inhibits myosin ATPase and actin interaction by stabilizing the c
43 stantial inhibitory effects on activation of myosin ATPase and in vitro motility of F-actin: (1) bind
44 ta-cardiac myosin eliminates actin-activated myosin ATPase and reduces actomyosin affinity in rigor m
45 ctin-actin interaction for the activation of myosin ATPase and the polymerization of actin by S1.
46 C-loop, was recently demonstrated to affect myosin ATPase and was indirectly implicated in the actom
48 se activity in reconstituted actin-activated myosin ATPase assays was similar for all three TnT mutan
49 lost at 60 degrees C the ability to activate myosin ATPase at a 100-fold slower rate and unfolded in
50 tors of actin filaments (cytochalasin D) and myosin ATPase (butanedione monoxime), indicating that th
52 how that BS inhibits contractility and actin-myosin ATPase by stabilizing the OFF state of the thick
54 is not known which kinetic step in the acto-myosin ATPase cycle limits contraction speed in unloaded
63 ated into protein expression, would decrease myosin ATPase enzyme velocity and slow speed of contract
64 e mechanisms by which ATP is supplied to the myosin ATPase, for muscle contraction, requires a highly
67 n with and without ADP, intermediates in the myosin ATPase hydrolytic pathway, are effective regulato
68 n, could inhibit actin-tropomyosin-activated myosin ATPase in the absence of Ca(2+), and two of them
70 e N509K relay mutation suppressed defects in myosin ATPase, in vitro motility, myofibril stability, a
71 in light chain kinase inhibitor ML-7 and the myosin ATPase inhibitor 2,3-butanedione-2-monoxime pertu
75 a slow phase, while butanedione monoxime, a myosin ATPase inhibitor, inhibited both the slow and fas
77 vator of myosin, we found that inhibition of myosin ATPase, myosin light chain kinase (MLCK), and the
78 of the dependence of the hydrolytic step of myosin ATPase on temperature and the requirement that hy
82 Fenn effect that energy liberation (and acto-myosin ATPase rate) in muscle are increased during short
83 states with biochemical states in the actin-myosin ATPase reaction, and showed that a small shift in
85 nhibition of actin-tropomyosin activation of myosin ATPase requires less than one peptide per seven a
86 ion of the actin activation of smooth muscle myosin ATPase since CaD-(1-717) caused only 30% of the i
87 some muscles, fibre types were determined by myosin ATPase staining following alkali pre-incubation.
88 tin is necessary for actin activation of the myosin ATPase, this finding explains the low metabolic c
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