ライフサイエンスコーパス: meromyosin

1 sphorylated but not thiophosphorylated heavy meromyosin.

2 osin rod and, to a lesser extent, with light meromyosin.

3 the regulatory domain of smooth muscle heavy meromyosin.

4 the intact RLC bound to the two-headed heavy meromyosin.

5 tent with cross-linking two RLC to one light meromyosin.

6 on 23 of the regulatory light chain of heavy meromyosin.

7 folded) transition in unphosphorylated heavy meromyosin.

8 roscopy of two-dimensional crystals of heavy meromyosin.

9 nphosphorylated but not phosphorylated heavy meromyosin.

10 at a dimer of Myo5c-HMM (double-headed heavy meromyosin 5c) has a 6-fold lower Km for actin filaments

11 ments comparing the subfragment-1 with heavy meromyosin (a two-headed subfragment).

12 Myosin 5 heavy meromyosin, a constitutively active fragment lacking the

13 Smooth muscle heavy meromyosin, a double-headed proteolytic fragment of myos

14 ed regulatory light chain N termini in heavy meromyosin, a double-headed subfragment with an intact r

15 The apparent affinity of acto-heavy meromyosin (acto-HMM) for MgATP was reduced by the prese

16 of MgATP-induced dissociation of acto-heavy meromyosin (acto-HMM) were virtually identical for the t

17 that one head of the unphosphorylated heavy meromyosin-ADP complex bound to actin and that the partn

18 adhesion and cytolysis, whereas mutations in meromyosin affect cytoskeletal function.

19 ers such as alpha-actinin, fascin, and heavy meromyosin alter the mechanical response independent of

20 or unphosphorylated and phosphorylated heavy meromyosin and for S1, approximately 50% of the molecule

21 and the smaller force produced by the heavy meromyosin and I341A actin system.

22 maximal MgATPase activity of wild type heavy meromyosin and moves actin filaments at half the wild ty

23 ntous forms of Acanthamoeba myosin II, heavy meromyosin and myosin subfragment 1, have actin-activate

24 binant calponin shows interaction with heavy meromyosin and myosin subfragment 2 but not subfragment

25 de release by an equal factor for both heavy meromyosin and subfragment 1, thus only indirectly influ

26 Using recombinant beta-cardiac heavy meromyosin and subfragment 1, which cannot form the inte

27 t bond to form between actin and rigor heavy meromyosin and the load-dependent durations of those bon

28 e the qualitatively similar effects of heavy meromyosin and tropomyosin on the conformational dynamic

29 monomers, the short-tailed subfragment heavy meromyosin, and SMM filaments.

30 Recombinant heavy meromyosin- and subfragment-1 (S1)-like constructs for b

31 We have shown that unphosphorylated heavy meromyosin appears to adopt a special state in the prese

32 ce of ADP based upon analysis of actin-heavy meromyosin association rate constants.

33 -linked between the RLC of one head to light meromyosin between leucine 1554 and glutamate 1583, adja

34 nd NM2C and monomeric, non-filamentous heavy meromyosin bind to liposomes containing one or more acid

35 thiophosphorylated or unphosphorylated heavy meromyosin bind very strongly to actin (K(d) < 10 nM) in

36 cleavage of the head-tail junction of heavy meromyosin by papain and chymotrypsin, suggesting it is

37 Here, smooth muscle heavy meromyosin C-loop chimeras were constructed with skeleta

38 Nucleotide binding to unphosphorylated heavy meromyosin caused a decrease in exposure and an increase

39 vitro sliding of thin filaments over a heavy meromyosin-coated surface.

40 duced dissociation of the pyrene-actin-heavy meromyosin complex, and (iii) amplitudes of the associat

41 For the actin-heavy meromyosin complex, cross-links were formed in both de-

42 osphorylated recombinant nonmuscle IIA heavy meromyosin constructs.

43 and neutron scattering measurements of heavy meromyosin containing all three light chains (LC(1-3)) i

44 lations of heterodimeric smooth muscle heavy meromyosins containing heads with different properties.

45 ction, we prepared five well regulated heavy meromyosins containing single-cysteine mutants of the hu

46 Expressed chimeric smooth muscle heavy meromyosins containing skeletal muscle myosin heavy chai

47 s the motilities of both actins at low heavy meromyosin densities but potentiates only the motility o

48 e motility of the mutant actin at high heavy meromyosin densities.

49 50) decreased by 0.12-0.18 when either heavy meromyosin density was reduced to approximately 60% or t

50 d but reduced the isometric force that heavy meromyosin exerted on regulated thin filaments.

51 t a greater percentage of NEM-modified heavy meromyosin (external load) was required for arresting th

52 a fluorescently labeled double-headed heavy meromyosin form showed no processive movements along act

53 A recombinant myosin V heavy meromyosin fragment that is missing the distal portion o

54 analysis, one-head thiophosphorylated heavy meromyosin had a similar K(m) value for actin but a V(ma

55 This heavy meromyosin has only 4% of the maximal MgATPase activity

56 rofiles were best fit by models of the heavy meromyosin head-tail junction in which the angular separ

57 nce methods that monitor the number of heavy meromyosin heads that bind to pyrene-actin: (i) amplitud

58 The subfragment 2/light meromyosin "hinge" region has been proposed to significa

59 The subfragment 2/light meromyosin "hinge" region of the MHC rod, located in the

60 of noninserted and inserted NMHC II-C heavy meromyosin (HMM II-C/HMM II-C1) resulted in significant

61 Since the junction between the heavy meromyosin (HMM) and light meromyosin (LMM) regions is e

62 een using shorter myosin subfragments, heavy meromyosin (HMM) and myosin subfragment 1 (S1).

63 he effect of H(2)O(2) on smooth muscle heavy meromyosin (HMM) and subfragment 1 (S1) was examined.

64 We have used two myosin fragments, heavy meromyosin (HMM) and Subfragment 1 (S1), to look at the

65 ucleotide complexes of skeletal muscle heavy meromyosin (HMM) and subfragment 1 (S1).

66 We find that wild-type and zippered heavy meromyosin (HMM) are able to bind by both heads to actin

67 tin filaments when they were placed on heavy meromyosin (HMM) attached to a glass surface.

68 in filaments) when they were placed on heavy meromyosin (HMM) attached to a glass surface.

69 osin for that of gizzard smooth muscle heavy meromyosin (HMM) causes activation of the dephosphorylat

70 mechanical properties of an expressed heavy meromyosin (HMM) construct with only one of its RLCs pho

71 ty chromatography were used to isolate heavy meromyosin (HMM) containing one phosphorylated and one d

72 ctin required higher concentrations of heavy meromyosin (HMM) for its sliding than did the rabbit act

73 ed nonlinearly with reduced density of heavy meromyosin (HMM) for regulated (and unregulated) F-actin

74 ed and wild-type baculovirus-expressed heavy meromyosin (HMM) II-B and II-C.

75 yosin IIs, baculovirus-expressed mouse heavy meromyosin (HMM) II-C2 demonstrates no requirement for r

76 the motor function of SH1 spin-labeled heavy meromyosin (HMM) in the in vitro motility assays and (ii

77 ible interactions between the heads of heavy meromyosin (HMM) in the presence and absence of calcium

78 ents are propelled by surface-adsorbed heavy meromyosin (HMM) motor fragments.

79 s as a mechanical lever, smooth muscle heavy meromyosin (HMM) mutants were expressed with shorter or

80 Measurements of actin-activated heavy meromyosin (HMM) NTPase, the rates of NTP binding to myo

81 d and thiophosphorylated smooth muscle heavy meromyosin (HMM) on positively charged lipid monolayers.

82 into the assay and at low densities of heavy meromyosin (HMM) on the cover slip.

83 Scallop heavy meromyosin (HMM) preparation obtained by a new improved

84 y-state hydrolytic activity of cardiac heavy meromyosin (HMM) showed that PTU treatment resulted in >

85 sin and rabbit skeletal myosin and its heavy meromyosin (HMM) subfragment.

86 al domains of MyBP-C on the ability of heavy meromyosin (HMM) to support movement of actin filaments

87 oke sizes of single- and double-headed heavy meromyosin (HMM) were each ~6 nm.

88 c digestions of myosin, which produced heavy meromyosin (HMM) with different percentages of molecules

89 een heads, we examined the kinetics of heavy meromyosin (HMM) with one thiophosphorylated head.

90 xpressed a smooth muscle heterodimeric heavy meromyosin (HMM) with one wild-type head, and the other

91 MBP bound to dephosphorylated myosin, heavy meromyosin (HMM), and subfragment 1.

92 ead motif (IHM) where the two heads of heavy meromyosin (HMM), or myosin, fold back onto each other a

93 nts of human cardiac myosin, including heavy meromyosin (HMM), the S1 subfragment, and two light mero

94 this question, we produced asymmetric heavy meromyosin (HMM), which is composed of a wild-type (WT)

95 neered and characterized smooth muscle heavy meromyosin (HMM), which is composed of one entire HMM he

96 Heavy meromyosin (HMM), which lacks two-thirds of the tail, cl

97 ere visualized gliding over a skeletal heavy meromyosin (HMM)-coated surface.

98 >/= 0.25 mM, the flexural rigidity of heavy meromyosin (HMM)-propelled actin filaments is similar (w

99 density of the adsorbed motor protein (heavy meromyosin, HMM) using quartz crystal microbalance; and

100 enesis and baculovirus expression of a heavy meromyosin- (HMM-) like fragment of human nonmuscle myos

101 One of the expressed heavy meromyosins (HMMexp) consists of two 150-kDa myosin heav

102 ee recombinant constructs of nonmuscle heavy meromyosin IIB containing 1) two complete heads, 2) one

103 nt movement over a surface coated with heavy meromyosin in in vitro motility assays.

104 domains of double-headed smooth muscle heavy meromyosin, including the N terminus of the regulatory l

105 a single-species homology model of two heavy meromyosin interacting-heads motifs (IHMs).

106 copy was used to determine whether the heavy meromyosin IQ molecules were capable of processive movem

107 in-activated MgATPase of smooth muscle heavy meromyosin is activated by thiophosphorylation of two re

108 The stabilizing effect of heavy meromyosin is cooperative.

109 When the subfragment 2 domain of heavy meromyosin is oriented as it would be in an actomyosin f

110 tin velocity generated by minus-insert heavy meromyosin is significantly influenced, but not limited,

111 ved for the Q15C mutant on a truncated heavy meromyosin lacking both catalytic domains.

112 ms in 10 S and not in unphosphorylated heavy meromyosin (lacking the light meromyosin), suggesting a

113 hypothesis we have expressed myosin V heavy meromyosin-like fragments containing 6IQ motifs, as well

114 assay to characterize the mechanics of heavy meromyosin-like fragments of myosin V (M5(HMM)) expresse

115 e two mutations were engineered into a heavy meromyosin-like recombinant fragment of nonmuscle myosin

116 Double-headed (heavy meromyosin-like) and single-headed (subfragment 1-like)

117 Light meromyosin (LMM 77), the C-terminal proteolytic peptide

118 The dimerization specificity of the light meromyosin (LMM) domain of chicken neonatal and adult my

119 sin (HMM), the S1 subfragment, and two light meromyosin (LMM) peptides containing amino acid sequence

120 (cMyBP-C(C10mut)), which binds to the light meromyosin (LMM) region of the myosin heavy chain, the u

121 tations have not been described in the light meromyosin (LMM) region of the myosin rod, nor would the

122 between the heavy meromyosin (HMM) and light meromyosin (LMM) regions is expected to disrupt the alph

123 od, located in the C-terminal third of heavy meromyosin, may form a less stable coiled-coil than flan

124 chanochemistry of single smooth muscle heavy meromyosin molecules lacking a seven-amino acid insert i

125 Comparison with studies of single heavy meromyosin molecules suggests that an increased mobility

126 egulation, we engineered smooth muscle heavy meromyosin molecules that contained one complete head an

127 Leu-25 to Lys-53 bound both myosin and heavy meromyosin more strongly and was capable of displacing c

128 eveal that at nanomolar calcium levels heavy meromyosin moves robustly on actin filaments whereas few

129 light chain of each head of a skeletal heavy meromyosin, near the head-rod junction (positions 2, 73,

130 uals reacted with distinctly different light meromyosin peptides.

131 in the rod region, particularly to the light meromyosin portion of the rod.

132 ons spanning residues 1428-1571 in the light meromyosin portion of the tail, consistent with cross-li

133 single molecule can cross-link to the light meromyosin portion of the tail.

134 ehavior was found for native regulated heavy meromyosin prepared by proteolytic digestion of chicken

135 Different regions of light meromyosin produced valvulitis (residues 1685 to 1936) o

136 bolic [MgATP]-velocity relationship of heavy-meromyosin-propelled actin filaments in the in vitro mot

137 recognized synthetic peptides from the light meromyosin region of the human cardiac myosin molecule a

138 react with specific peptides from the light meromyosin region of the human cardiac myosin molecule.

139 2) region of the adult isoform and the light meromyosin region of the neonatal isoform.

140 binding sites in the subfragment 2 and light meromyosin regions of myosin, and that the region compri

141 itopes were demonstrated in the S2 and light meromyosin regions.

142 Proteolytic gizzard heavy meromyosin regulatory light chains were partially exchan

143 (1-153) increased the concentration of heavy meromyosin required to support in vitro sliding of thin

144 o motility assays with rabbit skeletal heavy meromyosin (rsHMM) or porcine cardiac myosin (pcMyosin).

145 nteractions at its C-terminus with the light meromyosin section of the myosin rod and with titin.

146 For SMM and heavy meromyosin, several sites showed two heterogeneous popul

147 SH2-labeled heavy meromyosin (SH2-HMM), similar to SH1-labeled HMM (SH1-HM

148 in over a surface coated with skeletal heavy meromyosin (sHMM) or full-length beta-cardiac myosin (MY

149 gy transfer measurements revealed that heavy meromyosin, similarly to tropomyosin, restores the formi

150 Smooth muscle myosin and smooth muscle heavy meromyosin (smHMM) are activated by regulatory light cha

151 e activity of smooth muscle myosin and heavy meromyosin (smHMM) is regulated by phosphorylation of th

152 ble portion of loop 2 of smooth muscle heavy meromyosin (smHMM).

153 Heavy meromyosin stabilizes the formin-nucleated actin filamen

154 aser trap, applied load slows myosin V heavy meromyosin stepping and increases the probability of bac

155 The folding pathway of the heavy meromyosin subfragment (HMM) of a skeletal muscle myosin

156 orylated heavy meromyosin (lacking the light meromyosin), suggesting a structural rearrangement withi

157 dephosphorylated or thiophosphorylated heavy meromyosin, suggesting positions outside the region of i

158 rylated inactive form of smooth muscle heavy meromyosin suitable for structural studies by electron c

159 novel conformations in human B-cardiac heavy meromyosin that diverge significantly from the hypotheti

160 th filamentous NM2 and non-filamentous heavy meromyosin; the addition of excess unbound RLC, but not

161 in-labeled skeletal actin and skeletal heavy meromyosin to propel the filaments.

162 p 2 specifically blocks the ability of heavy meromyosin to undergo a weak to strong binding transitio

163 changed each mutant onto smooth muscle heavy meromyosin, verified normal regulatory function, and use

164 howed that one-head thiophosphorylated heavy meromyosin was 46-120 times more active than unphosphory

165 n upon the actin binding properties of heavy meromyosin was investigated using three fluorescence met

166 y towards phosphorylated smooth muscle heavy meromyosin was proportional to the amount of PP1cdelta i

167 ffects of nucleotide on phosphorylated heavy meromyosin were the opposite.

168 (iii) amplitudes of the association of heavy meromyosin with pyrene-actin.

169 that two-head binding is a property of heavy meromyosin with uncleaved heavy chains.