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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                     Also, OM reduces maximum actin-activated ATPase 2-fold in F764L, compared with 4-
5 sured basal ATPase, V(max), and K(ATPase) of actin-activated ATPase, actin-sliding velocities, rigor
6                                          The actin-activated ATPase activities (Vmax) of asymmetric H
7  We found that, based upon the change in the actin-activated ATPase activities and actin translocatin
8 tions in a manner that reflects the relative actin-activated ATPase activities of the donor myosins.
9                                   Similarly, actin-activated ATPase activities of the mutant and wild
10                          We have studied the actin-activated ATPase activities of three mutations in
11 e domain sequence switch conferred beta-like actin-activated ATPase activities to the chimeric myosin
12                                              Actin-activated ATPase activities were also reduced.
13 chains of amoeba myosins I, increasing their actin-activated ATPase activities.
14 n vitro motility (2.7-fold), and the Vmax of actin-activated ATPase activity (up to 2-fold), the prop
15 n comprising an N-terminal motor domain with actin-activated ATPase activity and a C-terminal globula
16  these cells exhibited 4-5-fold reduction in actin-activated ATPase activity and a decrease in motor
17    We found calcium moderately increases the actin-activated ATPase activity and completely inhibits
18 lated Myo2 were obtained that exhibited high actin-activated ATPase activity and in vitro actin filam
19  defective properties in vitro, particularly actin-activated ATPase activity and sliding velocity.
20 ila, mouse, and human myosin 18A (M18A) lack actin-activated ATPase activity and the ability to trans
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 tation does not significantly change maximum actin-activated ATPase activity but slows actin sliding
25  Mg(2+) modulated actin-sliding velocity and actin-activated ATPase activity by changing the rate of
26 2C, A397D, and E450Q mutations abolished the actin-activated ATPase activity completely.
27                                 The K(m) for actin-activated ATPase activity decreased 15-fold, but V
28 ve for both actin-translocating activity and actin-activated ATPase activity in the dephosphorylated
29 bed here, we have found that the kcat of the actin-activated ATPase activity is changed by the loop 2
30                             Muscle myosin-II actin-activated ATPase activity is significantly higher
31      Therefore, the Mg(2+) inhibition of the actin-activated ATPase activity observed in class II myo
32                                          The actin-activated ATPase activity of Acanthamoeba myosin I
33                                          The actin-activated ATPase activity of all constructs except
34 ion significantly decreased the K(m) for the actin-activated ATPase activity of both alpha- and beta-
35 e been shown previously to down-regulate the actin-activated ATPase activity of both the full-length
36                                Inhibition of actin-activated ATPase activity of fast skeletal and car
37                                          The actin-activated ATPase activity of full-length mammalian
38 t exogenous GTD is capable of inhibiting the actin-activated ATPase activity of GTD-deleted myosin Va
39                   V(max) and K(actin) of the actin-activated ATPase activity of HuM5B were 9.7 +/- 0.
40 o suggest a reciprocal shift, with basal and actin-activated ATPase activity of IFI-3a showing reduce
41                  V(max) and K(ATPase) of the actin-activated ATPase activity of M10IQ1 were 13.5 s(-1
42              We demonstrate that the maximum actin-activated ATPase activity of M2beta-S1 is slowed m
43                                 In EGTA, the actin-activated ATPase activity of MD(2IQ) was 7.4 +/- 1
44 ation significantly decreased the Km for the actin-activated ATPase activity of MHC isoforms.
45 , RLC phosphorylation does not influence the actin-activated ATPase activity of Myo2p.
46                           Interestingly, the actin-activated ATPase activity of MYO3A 2IQ is slightly
47 at the inhibitory action of caldesmon on the actin-activated ATPase activity of myosin in solution an
48                                          The actin-activated ATPase activity of myosin increased sign
49 und that melanophilin directly activates the actin-activated ATPase activity of myosin Va and thus it
50        ADP did not significantly inhibit the actin-activated ATPase activity of myosin X, suggesting
51                             The steady-state actin-activated ATPase activity of NMIIB S1 was decrease
52 tern blot analysis (116 kDa) and inhibit the actin-activated ATPase activity of purified adrenal myos
53                                          The actin-activated ATPase activity of smooth muscle myosin
54 ingly, the tail domain markedly inhibits the actin-activated ATPase activity of tailless DM7A at low
55               On the other hand, the maximum actin-activated ATPase activity of the chimeric myosin w
56 om the wild-type ABL significantly increased actin-activated ATPase activity of the dephosphorylated
57        Recent studies have revealed that the actin-activated ATPase activity of the full-length myosi
58                                          The actin-activated ATPase activity of the melanocyte-type m
59 large as that of the monomer form, while the actin-activated ATPase activity of the two forms was ide
60 a as determined by (i) the dependence of its actin-activated ATPase activity on heavy-chain phosphory
61 e E56G mutation has no significant effect on actin-activated ATPase activity or actomyosin affinity i
62 ble for USH1B cause the complete loss of the actin-activated ATPase activity or the reduction of duty
63  (1) Both the actin sliding activity and the actin-activated ATPase activity showed phosphorylation d
64 ATPase activity for 2-3-fold but reduced the actin-activated ATPase activity to 50% of the wild type.
65 urements at the same temperature showed that actin-activated ATPase activity was 2.9-fold greater for
66 slocating activity of myosin VI although the actin-activated ATPase activity was not affected by Ca(2
67                                          The actin-activated ATPase activity was reduced at Ca(2+) co
68                   K(actin) and K(ATP) of the actin-activated ATPase activity were significantly highe
69 the 50-20K sequence specifically affects the actin-activated ATPase activity while the 25-50K sequenc
70 Q mutant myosin demonstrated 2.3-fold higher actin-activated ATPase activity, 2.2-fold greater averag
71 IFI relay domain, we find a 50% reduction in actin-activated ATPase activity, a significant increase
72 nd actin in an ATP-sensitive manner, exhibit actin-activated ATPase activity, and generate force and
73 unts for the low actin-sliding velocity, low actin-activated ATPase activity, and high duty ratio.
74 ted the overall shape of a myosin, exhibited actin-activated ATPase activity, and moved actin filamen
75     We subsequently found that piglet had an actin-activated ATPase activity, colocalized with actin
76 he N-dependence of actin sliding velocities, actin-activated ATPase activity, force generation agains
77                             I455M has normal actin-activated ATPase activity, Pi burst, and ATP-induc
78 nine and glutamic acid substitutions reduced actin-activated ATPase activity, slowed the in vitro sli
79 n the other hand, ADP markedly inhibited the actin-activated ATPase activity, suggesting a high affin
80    All three mutants, however, have impaired actin-activated ATPase activity, with apparent second-or
81  of motility and nearly 5-fold regulation of actin-activated ATPase activity.
82 es for inhibitors of the recombinant motor's actin-activated ATPase activity.
83 main constructs (amino acids 1-800) featured actin-activated ATPase activity.
84 influence actin binding and thereby modulate actin-activated ATPase activity.
85 ), which was comparable to the V(max) of the actin-activated ATPase activity.
86                   ADP markedly inhibited the actin-activated ATPase activity.
87 ng protein that possesses calcium-stimulated actin-activated ATPase activity.
88 ffects ADP release, while loop 2 affects the actin-activated ATPase activity.
89  with actin, and display wild-type levels of actin-activated ATPase activity.
90 phorylated and dephosphorylated MIC(IQ) show actin-activated ATPase activity; however, HCP increases
91 ed for both actin-translocating activity and actin-activated ATPase activity; however, these activiti
92              Both 546- and 625-MDE exhibited actin-activated ATPase and actin-binding activities simi
93                  W546- and V413W-MDE display actin-activated ATPase and actin-binding properties simi
94 atic increase in intrinsic motor properties, actin-activated ATPase and in vitro actin gliding veloci
95                 Despite similar steady-state actin-activated ATPase and unloaded in vitro motility-sl
96 ep (ADP release) in the smooth muscle myosin-actin-activated ATPase cycle that is modulated by regula
97 atalytic motor domain, and characterized its actin-activated ATPase cycle using quantitative equilibr
98 DP release is the rate-limiting step for the actin-activated ATPase cycle.
99 DP release is the rate-limiting step for the actin-activated ATPase cycle; thus, HuM5B is a high duty
100 king strokes, the MYH7b isoforms have slower actin-activated ATPase cycles and actin sliding velociti
101            She3p does not affect the maximal actin-activated ATPase in solution or the velocity of mo
102 lly decreased in vitro motility velocity and actin-activated ATPase, in contrast to other MYH7 mutati
103                               In both cases, actin-activated ATPase inhibition is indicated mainly by
104                 At nanomolar calcium levels, actin-activated ATPase is low and the molecule is folded
105                                 Steady-state actin-activated ATPase measurements revealed a V(max) of
106                                              Actin-activated ATPase measurements using the expressed
107 ct the Vmax, and increased the Km values for actin-activated ATPase of HMM.
108 hat is responsible for the inhibition of the actin-activated ATPase of myosin.
109                            Regulation of the actin-activated ATPase of smooth muscle myosin II is kno
110                                              Actin-activated ATPases of SMM and XL-Rh-SMM were simila
111 sence of 14-3-3beta had little effect on the actin-activated ATPase or motile activities of Myo1c.
112                                  The maximum actin activated ATPase rate (V(max)) and the actin conce
113 indicate that it has a 2-fold higher maximum actin-activated ATPase rate (kcat = 1.5 +/- 0.1 s-1) and
114 , V0 is linearly correlated with the maximal actin-activated ATPase rate (vmax), which is limited by
115 t sliding velocity, whereas Loop 2 modulates actin-activated ATPase rate in Dictyostelium myosin, but
116                                  The maximum actin-activated ATPase rate is relatively slow (k(cat) =
117 ate of actin filament sliding or the maximal actin-activated ATPase rate of S1 or HMM constructs.
118 D515N mutation had no effect on steady-state actin-activated ATPase rate or load-dependent detachment
119  found, surprisingly, that in vitro solution actin-activated ATPase rates were increased (higher Vmax
120 tion, which increases activity of the myosin actin-activated ATPase, resulting in contraction.
121 ity and doubles myosin in vitro motility and actin-activated ATPase velocities, thereby involving a c
122                             K(ATPase) of the actin-activated ATPase was 62 microm, which is much high

 
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