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1  Consistently, ADP decreased K(actin) of the actin-activated ATPase.
2 ctin binding, ATP-induced actin release, and actin-activated ATPase.
3 C to study structural correlates of myosin's actin-activated ATPase.
4 sured basal ATPase, V(max), and K(ATPase) of actin-activated ATPase, actin-sliding velocities, rigor
5                                          The actin-activated ATPase activities (Vmax) of asymmetric H
6  We found that, based upon the change in the actin-activated ATPase activities and actin translocatin
7 tions in a manner that reflects the relative actin-activated ATPase activities of the donor myosins.
8                                   Similarly, actin-activated ATPase activities of the mutant and wild
9                          We have studied the actin-activated ATPase activities of three mutations in
10 e domain sequence switch conferred beta-like actin-activated ATPase activities to the chimeric myosin
11                                              Actin-activated ATPase activities were also reduced.
12 chains of amoeba myosins I, increasing their actin-activated ATPase activities.
13 n vitro motility (2.7-fold), and the Vmax of actin-activated ATPase activity (up to 2-fold), the prop
14 n comprising an N-terminal motor domain with actin-activated ATPase activity and a C-terminal globula
15  these cells exhibited 4-5-fold reduction in actin-activated ATPase activity and a decrease in motor
16    We found calcium moderately increases the actin-activated ATPase activity and completely inhibits
17 lated Myo2 were obtained that exhibited high actin-activated ATPase activity and in vitro actin filam
18  defective properties in vitro, particularly actin-activated ATPase activity and sliding velocity.
19 ila, mouse, and human myosin 18A (M18A) lack actin-activated ATPase activity and the ability to trans
20                                     Both the actin-activated ATPase activity and the actin translocat
21                                     Both the actin-activated ATPase activity and the actin translocat
22                                     Both the actin-activated ATPase activity and the actin-translocat
23     The Ala and Asn mutants had the same low actin-activated ATPase activity as unphosphorylated wild
24  Mg(2+) modulated actin-sliding velocity and actin-activated ATPase activity by changing the rate of
25 2C, A397D, and E450Q mutations abolished the actin-activated ATPase activity completely.
26                                 The K(m) for actin-activated ATPase activity decreased 15-fold, but V
27 ve for both actin-translocating activity and actin-activated ATPase activity in the dephosphorylated
28 bed here, we have found that the kcat of the actin-activated ATPase activity is changed by the loop 2
29                             Muscle myosin-II actin-activated ATPase activity is significantly higher
30      Therefore, the Mg(2+) inhibition of the actin-activated ATPase activity observed in class II myo
31                                          The actin-activated ATPase activity of Acanthamoeba myosin I
32                                          The actin-activated ATPase activity of all constructs except
33 ion significantly decreased the K(m) for the actin-activated ATPase activity of both alpha- and beta-
34 e been shown previously to down-regulate the actin-activated ATPase activity of both the full-length
35                                          The actin-activated ATPase activity of full-length mammalian
36 t exogenous GTD is capable of inhibiting the actin-activated ATPase activity of GTD-deleted myosin Va
37                   V(max) and K(actin) of the actin-activated ATPase activity of HuM5B were 9.7 +/- 0.
38                  V(max) and K(ATPase) of the actin-activated ATPase activity of M10IQ1 were 13.5 s(-1
39              We demonstrate that the maximum actin-activated ATPase activity of M2beta-S1 is slowed m
40                                 In EGTA, the actin-activated ATPase activity of MD(2IQ) was 7.4 +/- 1
41 ation significantly decreased the Km for the actin-activated ATPase activity of MHC isoforms.
42 , RLC phosphorylation does not influence the actin-activated ATPase activity of Myo2p.
43                           Interestingly, the actin-activated ATPase activity of MYO3A 2IQ is slightly
44 at the inhibitory action of caldesmon on the actin-activated ATPase activity of myosin in solution an
45                                          The actin-activated ATPase activity of myosin increased sign
46 und that melanophilin directly activates the actin-activated ATPase activity of myosin Va and thus it
47        ADP did not significantly inhibit the actin-activated ATPase activity of myosin X, suggesting
48                             The steady-state actin-activated ATPase activity of NMIIB S1 was decrease
49 tern blot analysis (116 kDa) and inhibit the actin-activated ATPase activity of purified adrenal myos
50                                          The actin-activated ATPase activity of smooth muscle myosin
51 ingly, the tail domain markedly inhibits the actin-activated ATPase activity of tailless DM7A at low
52               On the other hand, the maximum actin-activated ATPase activity of the chimeric myosin w
53 om the wild-type ABL significantly increased actin-activated ATPase activity of the dephosphorylated
54        Recent studies have revealed that the actin-activated ATPase activity of the full-length myosi
55                                          The actin-activated ATPase activity of the melanocyte-type m
56 large as that of the monomer form, while the actin-activated ATPase activity of the two forms was ide
57 a as determined by (i) the dependence of its actin-activated ATPase activity on heavy-chain phosphory
58 e E56G mutation has no significant effect on actin-activated ATPase activity or actomyosin affinity i
59 ble for USH1B cause the complete loss of the actin-activated ATPase activity or the reduction of duty
60  (1) Both the actin sliding activity and the actin-activated ATPase activity showed phosphorylation d
61 ATPase activity for 2-3-fold but reduced the actin-activated ATPase activity to 50% of the wild type.
62 urements at the same temperature showed that actin-activated ATPase activity was 2.9-fold greater for
63 slocating activity of myosin VI although the actin-activated ATPase activity was not affected by Ca(2
64                                          The actin-activated ATPase activity was reduced at Ca(2+) co
65                   K(actin) and K(ATP) of the actin-activated ATPase activity were significantly highe
66 the 50-20K sequence specifically affects the actin-activated ATPase activity while the 25-50K sequenc
67 Q mutant myosin demonstrated 2.3-fold higher actin-activated ATPase activity, 2.2-fold greater averag
68 IFI relay domain, we find a 50% reduction in actin-activated ATPase activity, a significant increase
69 nd actin in an ATP-sensitive manner, exhibit actin-activated ATPase activity, and generate force and
70 unts for the low actin-sliding velocity, low actin-activated ATPase activity, and high duty ratio.
71     We subsequently found that piglet had an actin-activated ATPase activity, colocalized with actin
72                             I455M has normal actin-activated ATPase activity, Pi burst, and ATP-induc
73 nine and glutamic acid substitutions reduced actin-activated ATPase activity, slowed the in vitro sli
74 n the other hand, ADP markedly inhibited the actin-activated ATPase activity, suggesting a high affin
75    All three mutants, however, have impaired actin-activated ATPase activity, with apparent second-or
76 main constructs (amino acids 1-800) featured actin-activated ATPase activity.
77 influence actin binding and thereby modulate actin-activated ATPase activity.
78 ), which was comparable to the V(max) of the actin-activated ATPase activity.
79                   ADP markedly inhibited the actin-activated ATPase activity.
80 ng protein that possesses calcium-stimulated actin-activated ATPase activity.
81 ffects ADP release, while loop 2 affects the actin-activated ATPase activity.
82  with actin, and display wild-type levels of actin-activated ATPase activity.
83  of motility and nearly 5-fold regulation of actin-activated ATPase activity.
84 phorylated and dephosphorylated MIC(IQ) show actin-activated ATPase activity; however, HCP increases
85 ed for both actin-translocating activity and actin-activated ATPase activity; however, these activiti
86              Both 546- and 625-MDE exhibited actin-activated ATPase and actin-binding activities simi
87                  W546- and V413W-MDE display actin-activated ATPase and actin-binding properties simi
88 ep (ADP release) in the smooth muscle myosin-actin-activated ATPase cycle that is modulated by regula
89 atalytic motor domain, and characterized its actin-activated ATPase cycle using quantitative equilibr
90 DP release is the rate-limiting step for the actin-activated ATPase cycle.
91 DP release is the rate-limiting step for the actin-activated ATPase cycle; thus, HuM5B is a high duty
92            She3p does not affect the maximal actin-activated ATPase in solution or the velocity of mo
93                               In both cases, actin-activated ATPase inhibition is indicated mainly by
94                 At nanomolar calcium levels, actin-activated ATPase is low and the molecule is folded
95                                 Steady-state actin-activated ATPase measurements revealed a V(max) of
96                                              Actin-activated ATPase measurements using the expressed
97 ct the Vmax, and increased the Km values for actin-activated ATPase of HMM.
98 hat is responsible for the inhibition of the actin-activated ATPase of myosin.
99                            Regulation of the actin-activated ATPase of smooth muscle myosin II is kno
100                                              Actin-activated ATPases of SMM and XL-Rh-SMM were simila
101                                  The maximum actin activated ATPase rate (V(max)) and the actin conce
102 indicate that it has a 2-fold higher maximum actin-activated ATPase rate (kcat = 1.5 +/- 0.1 s-1) and
103 , V0 is linearly correlated with the maximal actin-activated ATPase rate (vmax), which is limited by
104 t sliding velocity, whereas Loop 2 modulates actin-activated ATPase rate in Dictyostelium myosin, but
105                                  The maximum actin-activated ATPase rate is relatively slow (k(cat) =
106 ate of actin filament sliding or the maximal actin-activated ATPase rate of S1 or HMM constructs.
107  found, surprisingly, that in vitro solution actin-activated ATPase rates were increased (higher Vmax
108 tion, which increases activity of the myosin actin-activated ATPase, resulting in contraction.
109 ity and doubles myosin in vitro motility and actin-activated ATPase velocities, thereby involving a c
110                             K(ATPase) of the actin-activated ATPase was 62 microm, which is much high

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