ライフサイエンスコーパス: actomyosin ATPase

1 l systems and (2) the calcium sensitivity of actomyosin ATPase.

2 lays a major role in the changed kinetics of actomyosin ATPase.

3 and an increased calcium sensitivity of the actomyosin ATPase.

4 actin and the V(max) and K(m) parameters of actomyosin ATPase.

5 omyosin in a position on actin that inhibits actomyosin ATPase.

6 independently, TnI is capable of inhibiting actomyosin ATPase.

7 core sequence for CaD-induced inhibition of actomyosin ATPase.

8 en for full-length CaD) of inhibition of the actomyosin ATPase.

9 ibute to tropomyosin-dependent inhibition of actomyosin ATPase: a central segment [747-767 (690-710 i

10 aining HSSTnT1, -2, and -3 did not alter the actomyosin ATPase activation and inhibition in the prese

11 ts were hyposensitive to Ca(2+) in regulated actomyosin ATPase activities.

12 cTnT isoforms all yielded different maximal actomyosin ATPase activities.

13 le EMD 57033 has been shown to stimulate the actomyosin ATPase activity and contractility of myofilam

14 oth D75Y and E59D are required to reduce the actomyosin ATPase activity and maximal force in muscle f

15 the actin-binding protein caldesmon inhibits actomyosin ATPase activity and might in this way take pa

16 ic cardiomyopathy-causing mutations in cTnI, actomyosin ATPase activity and skinned fiber studies wer

17 nT1 DCM mutations strongly decreased maximal actomyosin ATPase activity as compared with TnT1-WT.

18 e CaM-mediated reversal of the inhibition of actomyosin ATPase activity by CaD and for the functional

19 and flexibility of crossbridges may regulate actomyosin ATPase activity by modifying the kinetics of

20 r results suggest that a decrease in maximal actomyosin ATPase activity in conjunction with decreased

21 ere examined by monitoring the time-resolved actomyosin ATPase activity in COPD and non-COPD fibres t

22 sensitivity, while simultaneously measuring actomyosin ATPase activity in situ by a fluorimetric tec

23 ard smooth muscle caldesmon (CaD) to inhibit actomyosin ATPase activity is due mainly to an inhibitor

24 Ca(2+)-activated actomyosin ATPase activity showed that cTnI-ND myofibril

25 etter predictor of the calcium dependence of actomyosin ATPase activity than that of TnC or the Tn co

26 elin increases isometric force and decreases actomyosin ATPase activity thus increasing the economy o

27 Analysis of actin binding and inhibition of actomyosin ATPase activity using these mutants identifie

28 Ca(2+)-dependent actomyosin ATPase activity was also decreased; however,

29 rabeculae with intact endothelial cells, but actomyosin ATPase activity was increased.

30 Actomyosin ATPase activity was measured as a function of

31 l isoforms) had a reduced ability to inhibit actomyosin ATPase activity when compared with cTnT3 (adu

32 ponent of the troponin complex that inhibits actomyosin ATPase activity, and Ca(2+) binding to the tr

33 dothelin-1 raised isometric force, decreased actomyosin ATPase activity, and decreased unloaded short

34 tivities of the thin filament, reconstituted actomyosin ATPase activity, and force generation in skin

35 s purified co-sediments with actin, inhibits actomyosin ATPase activity, and interacts with Ca2+/calm

36 Isometric force, actomyosin ATPase activity, and unloaded shortening velo

37 e or release, sarcolemmal Na+/Ca2+ exchange, actomyosin ATPase activity, L-type Ca2+ channel current,

38 which inhibits tropomyosin's potentiation of actomyosin ATPase activity, moves tropomyosin in one dir

39 dium, particularly through a decrease in the actomyosin ATPase activity.

40 r, augmenting maximal force without altering actomyosin ATPase activity.

41 a decrease in the ability of cTnI to inhibit actomyosin ATPase activity.

42 th muscle caldesmon binds actin and inhibits actomyosin ATPase activity.

43 e caldesmon (CaD) binds F-actin and inhibits actomyosin ATPase activity.

44 , TnT, that is responsible for inhibition of actomyosin ATPase activity.

45 n C (TnC), actin-tropomyosin (actin-Tm), and actomyosin ATPase activity.

46 ect on either actin-binding or inhibition of actomyosin ATPase activity.

47 bfragment-2 portion of myosin, which reduces actomyosin ATPase activity; phosphorylation abolishes th

48 hift the distribution of crossbridges in the actomyosin ATPase (AMATPase) to increase the relative po

49 act as a tether still have an effect on the actomyosin ATPase and (b) as to why the myosin head posi

50 It inhibits actomyosin ATPase and filament severing in vitro, and is

51 Phosphorylation at these sites inhibits the actomyosin ATPase and inhibits phosphorylation of S19 on

52 uce the activity of TnI in the inhibition of actomyosin ATPase and result in cardiac muscle malfuncti

53 17 is responsible for the weak inhibition of actomyosin ATPase and reveal that the inhibitory determi

54 We performed actomyosin ATPase and spectroscopic solution studies to

55 domains of CaD involved in the regulation of actomyosin ATPase and the binding of actin, tropomyosin,

56 osin to assume a second position, initiating actomyosin ATPase and thus permitting contraction to pro

57 ient for tropomyosin-dependent inhibition of actomyosin ATPase; and two actin binding segments N-term

58 paring wild-type (WT) and mutant proteins in actomyosin ATPase assays and in troponin-replaced rabbit

59 E), or weaker (R145W) than wild-type cTnI in actomyosin ATPase assays in the absence of Ca2+.

60 Reconstituted actomyosin ATPase assays with 50% cTnC-A31S:50% cTnC-WT

61 n skinned fiber studies and in reconstituted actomyosin ATPase assays.

62 onin-tropomyosin and therefore inhibition of actomyosin ATPase by caldesmon-tropomyosin and by tropon

63 that of troponin and therefore inhibition of actomyosin ATPase by calponin and troponin cannot be str

64 ges may help explain how force modulates the actomyosin ATPase cycle and thus the physiology and ener

65 ent kinetic data show that most steps of the actomyosin ATPase cycle are slowed down compared with ot

66 rm movement with respect to the steps in the actomyosin ATPase cycle has not been determined.

67 ng-to-weak structural transitions during the actomyosin ATPase cycle in an isoform-dependent manner,

68 ng that myosin Vc spends the majority of the actomyosin ATPase cycle in weak actin-binding states, un

69 n is qualitatively predicted by a simplified actomyosin ATPase cycle where a pre-phosphate release, f

70 d an increase in the maximum velocity of the actomyosin ATPase cycle, and our transient-kinetics expe

71 late the kinetics of individual steps of the actomyosin ATPase cycle.

72 ct showed little effect on most steps of the actomyosin ATPase cycle.

73 f weakly bound myosin S1 on actin during the actomyosin ATPase cycle.

74 load-dependent step and/or transition in the actomyosin ATPase cycle.

75 getics of the biochemical transitions in the actomyosin ATPase cycle.

76 s the rate-limiting step in the steady-state actomyosin ATPase cycle.

77 brium states that mimic intermediates in the actomyosin ATPase cycle.

78 ic constants for each step in the myosin and actomyosin ATPase cycles of recombinant wild-type S1 and

79 site, is required for full inhibition of the actomyosin ATPase in the absence of calcium.

80 mutants were defective in activation of the actomyosin ATPase in the presence of Ca2+.

81 Using phosphomimics, measurements of actomyosin ATPase in vitro and force generation in demem

82 atory protein of smooth muscle that inhibits actomyosin ATPase in vitro.

83 r calmodulin (CaM) binding and actin-binding/actomyosin ATPase inhibition are present in the region b

84 e adjacent weak actin-binding sites and weak actomyosin ATPase inhibitory determinants.

85 jacent to one of the major actin binding and actomyosin ATPase inhibitory domains.

86 oes the heated CaD; its inhibitory action on actomyosin ATPase is reversed by a much lesser amount of

87 D89A and alpha h89A activated the regulated actomyosin ATPase poorly in the presence of Ca2+ (24 +/-

88 The contractile and actomyosin ATPase properties of single fibres were exami

89 e of the fundamental mechanochemistry of the actomyosin ATPase reaction under a minimal load and serv

90 gh most of the mutants were able to activate actomyosin ATPase similarly to wild-type cTnI, L144Q had

91 Ac2--4, and dAc3--5) all fully inhibited the actomyosin ATPase (+Tn) in EGTA.

92 ion of actomyosin affinity and regulation of actomyosin ATPase velocity.

93 ed the troponin activation properties of the actomyosin ATPase when Ca(2+) was present.

94 a significant increase in the activation of actomyosin ATPase with either CTnI or SSTnI, whereas HCT

95 assayed for actin binding, regulation of the actomyosin ATPase with troponin, cooperative myosin S1-i

96 s the mutant increased the activation of the actomyosin ATPase without affecting the inhibitory quali