ライフサイエンスコーパス: myosin filament

1 that there are six titin molecules per half myosin filament.

2 s at opposite ends, analogous to a miniature myosin filament.

3 thus propelling the actin filament past the myosin filament.

4 in the proximity of the helical track of the myosin filament.

5 ms to be located close to the surface of the myosin filament.

6 end and side-by-side arrays of small bipolar myosin filaments.

7 sarcomeric unit, parallel with the actin and myosin filaments.

8 ns of the regulatory domain in reconstituted myosin filaments.

9 in polymerization and contractility of actin/myosin filaments.

10 fibers through incorporation into endogenous myosin filaments.

11 gnetic resonance in reconstituted, synthetic myosin filaments.

12 n S1SA) inhibits cosedimentation of CaP with myosin filaments.

13 myosin head region that links the actin and myosin filaments.

14 on microscopy suggest that Mts1 destabilizes myosin filaments.

15 for binding to a discrete number of sites in myosin filaments.

16 sent at M lines where it surrounds the thick myosin filaments.

17 understanding the molecular organization of myosin filaments.

18 l fashion to yield the bridge regions of the myosin filaments.

19 res overlap between uniform-length actin and myosin filaments.

20 n may play a role in length determination of myosin filaments.

21 as the assembly of Z-bodies and nonstriated myosin filaments.

22 whether this structure is present in native myosin filaments.

23 sliding were explored in isolated actin and myosin filaments.

24 tile apparatus, and ability to interact with myosin filaments.

25 both the sidepolar and bipolar smooth muscle myosin filaments.

26 egular aggregates containing large sidepolar myosin filaments.

27 l arrangement of the thin (actin) and thick (myosin) filaments.

28 r KD values, exhibited some stabilization of myosin filaments against ATP depolymerization in vitro,

29 en (i.e. the velocity of sliding between the myosin filament and the actin filament under zero load,

30 en (i.e. the velocity of sliding between the myosin filament and the actin filament under zero load,

31 ne of the simplest explanations is that both myosin filaments and actin filaments are stabilized (e.g

32 required for maintaining the organization of myosin filaments and internal components of the M-line d

33 are hybrids, containing striated muscle-like myosin filaments and smooth muscle-like actin filaments

34 KRP binds to unphosphorylated smooth muscle myosin filaments and stabilizes them against ATP-induced

35 ation of interactions between the cortex and myosin filaments and that the motor domain is dispensabl

36 Calculations included both the myosin filaments and the actin filaments of the muscle c

37 The structure of cardiac myosin filaments and the alterations caused by HCM mutat

38 he concepts of the double array of actin and myosin filaments and, later, the overlapping filament mo

39 s assembled near those sites (both actin and myosin filaments) and moved towards the centre of the no

40 in heads and from backbone components of the myosin filaments, and the interaction of these with the

41 Dynamic MV, myosin filaments, and their associated actin filaments f

42 n-6 localization closely resembles where new myosin filaments appear at the cortex by de novo assembl

43 t before titin is organized the first muscle myosin filaments are about half the length of the 1.6 mu

44 to study the structural changes induced when myosin filaments are activated by Ca2+.

45 ures consisting solely of MyHC, and that the myosin filaments are compacted in the presence of MyBP.

46 Smooth muscle myosin filaments are exponentially distributed with appr

47 Mammalian myosin filaments are helically ordered only at higher te

48 Here we show that intact nonmuscle myosin filaments are required for the synthesis of heter

49 Self-assembled myosin filaments are shown here to be asymmetric in phys

50 he ATP analogues AMP-PNP or ADP.BeF(x)() the myosin filaments are substantially ordered at higher tem

51 e NM myosin regulatory light chain (RLC), NM myosin filament assembly and contraction, although it di

52 1943A, in SM tissues inhibits ACh-induced NM myosin filament assembly and SM contraction, and also in

53 nd NM RLC phosphorylation is required for NM myosin filament assembly and SM contraction.

54 myosin heavy chain on Ser1943 and causes NM myosin filament assembly at the SM cell cortex.

55 mechanisms of disease pathogenesis involving myosin filament assembly or interaction with thick filam

56 Stimulation with ACh caused NM myosin filament assembly, as assessed by a Triton solubi

57 However, this movement is inhibited by myosin filament assembly, because whole myosin was delay

58 ting NM myosin Ser1943 phosphorylation or NM myosin filament assembly.

59 cells show increased expression of Myh11 and myosin filament-associated contractile genes at the mess

60 eously activate the myosin heads of adjacent myosin filaments at a distance of >or=40 nm.

61 osin-binding protein-C on the surface of the myosin filament backbone.

62 hat remain fixed in position relative to the myosin filament backbone.

63 yosin II heavy chain, driving disassembly of myosin filaments both in vitro and in vivo.

64 quired for the Rho-induced assembly of actin-myosin filament bundles, or for vinculin association wit

65 each 14.5 nm repeat in native smooth muscle myosin filaments by scanning transmission electron micro

66 It is known that myosin filaments can assemble and disassemble in nonmusc

67 on pillars demonstrates that submicron scale myosin filaments can cause these local contractions.

68 cally within the hexagonal A-band lattice of myosin filaments, can redistribute through the I-band to

69 Phosphorylation of smooth muscle myosin filaments caused a small increase in the amplitud

70 newly discovered extensibility of actin and myosin filaments challenges the foundation of the theory

71 Cardiac myosin filaments consist of the molecular motor myosin I

72 We conclude that native smooth muscle myosin filaments contain four myosin molecules at each 1

73 does not colocalize with large, needle-like myosin filaments containing MYO-3, a striated-muscle myo

74 While accumulating at the equator, myosin filaments disappear from the poles of the cell, a

75 (MHCK A) has been shown previously to drive myosin filament disassembly in vitro and in vivo.

76 Here, we show that artificial myosin filaments, engineered using a DNA nanotube scaffo

77 s in the micromolar region could disassemble myosin filaments even at resting levels of cytoplasmic [

78 hermore, the head configuration critical for myosin filament formation (extended or folded) was uncha

79 cal tail piece, of myosin II is critical for myosin filament formation both in vitro and in vivo.

80 genous NM myosin Ser1943 phosphorylation, NM myosin filament formation, the assembly of membrane adhe

81 g cells at a conserved site that can lead to myosin-filament formation and contraction of actomyosin

82 single-particle analysis of the M-region of myosin filaments from goldfish skeletal muscle under rel

83 nd three-dimensional image reconstruction of myosin filaments from horseshoe crab (Limulus) muscle.

84 Myosin filaments from many muscles are activated by phos

85 veloped a simple method for purifying native myosin filaments from muscle filament suspensions.

86 mensional reconstructions of relaxed, native myosin filaments from tarantula striated muscle, suggest

87 Here we have studied the structure of myosin filaments from the smooth muscles of the human pa

88 determine the three-dimensional structure of myosin filaments from wild-type mouse cardiac muscle and

89 urements of mobility of these two domains in myosin filaments give strong support for this notion.

90 precise mode of binding of C-protein to the myosin filament has not been determined.

91 Vertebrate striated muscle myosin filaments have a 3-fold rotational symmetry aroun

92 Since there are two actin filaments per half myosin filament in a half sarcomere, this means that the

93 ns provide key insights into the role of the myosin filament in cardiac contraction, assembly, and di

94 We conclude that myosin filaments in all smooth muscles, regardless of fu

95 9 activates RHO-1 GTPase for organization of myosin filaments in C. elegans muscle cells.

96 Of all the myosin filaments in muscle, the most important in terms

97 motifs and that regulate the organization of myosin filaments in muscle.

98 at the same time as the sliding of actin and myosin filaments in response to muscle length or force s

99 Adjacent myosin filaments in striated muscle A-bands are cross-li

100 bipolar, helical structure characteristic of myosin filaments in striated muscle has not been disprov

101 ic domains in unphosphorylated smooth muscle myosin filaments in the absence of nucleotides.

102 smitin may play a central role in organizing myosin filaments in the contractile apparatus and perhap

103 indicates the presence of a superlattice of myosin filaments in the Drosophila A-band.

104 The in vivo structure of the myosin filaments in vertebrate smooth muscle is unknown.

105 cts with two configurations of smooth muscle myosin filaments in vitro.

106 by increased calcium sensitization of actin-myosin filaments, involving Rho-kinase.

107 of the actin filament is maximal, while the myosin filament is in the OFF state characterized by mos

108 ms after the start of stimulation, when the myosin filament is still in the OFF state.

109 , suggesting that KRP's ability to stabilize myosin filaments is commensurate with its myosin binding

110 association of collagen mRNAs with nonmuscle myosin filaments is necessary to coordinately synthesize

111 tron micrograph images of negatively stained myosin filaments isolated from human cardiac muscle in t

112 tically different pattern of sampling of the myosin filament layer-lines, which indicates the presenc

113 Myosin filament mechanosensing determines the efficiency

114 KEY POINTS: Myosin filament mechanosensing determines the efficiency

115 dynamics of green fluorescent protein-tagged myosin filaments, microtubules, and Kinesin-6 (which car

116 the number of actin-attached motors per half-myosin filament (n) during V0 shortening imposed either

117 diated through the polarization of actin and myosin filament networks.

118 Regulation of muscle contraction via the myosin filaments occurs in vertebrate smooth and many in

119 cycling cross-bridges linking the actin and myosin filaments of a relaxed skeletal muscle.

120 We have observed smooth muscle myosin filaments of different length and head number (N)

121 Myosin filaments of muscle are regulated either by phosp

122 xactly as expected if adjacent four-stranded myosin filaments, of repeat 116 nm, are axially shifted

123 tween nuclei are unable to stably accumulate myosin filaments or suppress actin-filled ruffles.

124 ptor agonists has been shown to induce actin-myosin filament organization.

125 on depends on interactions between actin and myosin filaments organized into sarcomeres, but the mech

126 e a simple mechanism of contraction based on myosin filaments pulling neighboring bundles together in

127 nteraction between single isolated actin and myosin filaments, raising the question whether all of th

128 similar interaction switches off activity in myosin filaments regulated by Ca(2+) binding.

129 periodicity (about 435A) than the intrinsic myosin filament repeat of 429A.

130 Dissociation of nonmuscle myosin filaments results in secretion of collagen alpha1

131 sin, and as a consequence, the rate of actin-myosin filament sliding.

132 vital role in assembly of contractile actin-myosin filaments (stress fibers) and of associated focal

133 gments, but little is known about effects of myosin filament structure on mechanochemistry.

134 and a disordered population with respect to myosin filament structure.

135 found that the release of the heads from the myosin filament surface by reduction of electrostatic ch

136 been visualized in a wide variety of native myosin filaments, testifying to the generality of these

137 inds to the heads of relaxed Ca2+ -regulated myosin filaments, the helically ordered myosin heads bec

138 n molecules overlap at the centre of bipolar myosin filaments to produce an M-region (bare zone) that

139 of vinculin and UNC-89 as well as actin and myosin filaments to these in vivo focal adhesion analogs

140 The mass-per-length of myosin filaments was 159 kDa/nm, corresponding to 4.38(+

141 The mobility of the regulatory domain in myosin filaments was characterized by an effective rotat

142 loss of protein kinase activity when native myosin filaments were used as the substrate.

143 Moreover, addition of myosin filaments, which contract the actin mesh, allowed

144 ozen and then freeze substituted, shows many myosin filaments with a square backbone in transverse pr