ライフサイエンスコーパス: myosin subfragment

1 beta-cardiac myosin subfragment 1 (betaS1) tertiary structure and dyn

2 We studied the regulation of fluorescent myosin subfragment 1 (fS1) binding to rigor myofibrils o

3 We expressed and purified human beta-cardiac myosin subfragment 1 (M2beta-S1) containing a C-terminal

4 ce and presence of N-ethylmaleimide-modified myosin subfragment 1 (NEM-S1) at both short and long SLs

5 The binding of N-ethylmaleimide-treated myosin subfragment 1 (NEM-S1) to actin filaments mimics

6 f fibers with a strong binding derivative of myosin subfragment 1 (NEM-S1).

7 striated muscle contraction, the effects of myosin subfragment 1 (S-1) on the actin binding of cardi

8 erimental data on the equilibrium binding of myosin subfragment 1 (S-1) to regulated actin filaments

9 arent KM or the Vmax for MgATP hydrolysis by myosin subfragment 1 (S1) alone, nor did it affect the v

10 AP-actin binds to skeletal myosin subfragment 1 (S1) and forms a homogeneous comple

11 y bound to single-headed fragments of muscle myosin subfragment 1 (S1) and non-muscle myosin V (MV).

12 intensity difference between rabbit skeletal myosin subfragment 1 (S1) and nucleotide-bound or trappe

13 tional similarity to the extensively studied myosin subfragment 1 (S1) and their accessibility to mol

14 Myosin subfragment 1 (S1) and tropomyosin inhibited the

15 The regulation of myosin subfragment 1 (S1) binding to actin by Tm has bee

16 ionic strength dependence of skeletal muscle myosin subfragment 1 (S1) binding to actin in the presen

17 model predict very similar binding traces of myosin subfragment 1 (S1) binding to regulated actin fil

18 active site (near or at Trp 130) of skeletal myosin subfragment 1 (S1) by using luminescence resonanc

19 ) and SH2 (Cys697) groups on rabbit skeletal myosin subfragment 1 (S1) can be cross-linked by using r

20 Myosin subfragment 1 (S1) can be specifically modified a

21 in (Tn), and weakens Tm binding to the actin-myosin subfragment 1 (S1) complex (acto-S1).

22 The reactive SH1 (Cys-707) group of the myosin subfragment 1 (S1) has been used frequently as an

23 Past biochemical work on myosin subfragment 1 (S1) has shown that the bent alpha-

24 The conformation of myosin subfragment 1 (S1) in the vicinity of the ATP sen

25 510 (Trp510) fluorescence in rabbit skeletal myosin subfragment 1 (S1) indicates the conformation of

26 premixing actin with the NA3 prior to adding myosin subfragment 1 (S1) inhibits the rate of actoS1 as

27 Surmises of how myosin subfragment 1 (S1) interacts with actin filaments

28 n of the reactive lysine (Lys84) in skeletal myosin subfragment 1 (S1) introduces a chiral probe (TNP

29 When smooth muscle myosin subfragment 1 (S1) is bound to actin filaments in

30 The Mg-ATPase activity of skeletal muscle myosin subfragment 1 (S1) is reversibly eliminated when

31 Myosin subfragment 1 (S1) is the ATP catalyzing motor pr

32 The myosin subfragment 1 (S1) MgATPase rate was measured usi

33 o result from an angular displacement of the myosin subfragment 1 (S1) tail domain with respect to th

34 Here, we show that the addition of myosin subfragment 1 (S1) to TFs reconstituted with thes

35 tudied in the absence and in the presence of myosin subfragment 1 (S1) using multifrequency phase/mod

36 ilon-ADP) release from cleaved and uncleaved myosin subfragment 1 (S1) was examined.

37 Lys-553 of skeletal muscle myosin subfragment 1 (S1) was specifically labeled with

38 Tm) on ATPase and on the binding kinetics of myosin subfragment 1 (S1) were studied to clarify the me

39 The interaction of myosin subfragment 1 (S1) with actin-tropomyosin-troponi

40 ns of Cys-697 and Cys-707 of skeletal muscle myosin subfragment 1 (S1) with N,N'-p-phenylenedimaleimi

41 Myosin subfragment 1 (S1) with SH1 (Cys(707)) and SH2 (C

42 n was used for monitoring the interaction of myosin subfragment 1 (S1) with the His-40-Gly-42 site in

43 yosin was studied by comparing the effect of myosin subfragment 1 (S1) with two other structural pert

44 For myosin subfragment 1 (S1), the degree of lever arm rotat

45 psin made it possible to isolate homogeneous myosin subfragment 1 (S1), uncontaminated by endogenous

46 (2+) concentration conditions: inhibition of myosin subfragment 1 (S1)-thin filament MgATPase activit

47 Labeled RLC was reconstituted onto myosin subfragment 1 (S1).

48 nd Cys(697) (SH2) in the catalytic domain of myosin subfragment 1 (S1).

49 along with R403Q, to facilitate isolation of myosin subfragment 1 (S1).

50 anges in actin that are then communicated to myosin subfragment 1 (S1).

51 king of known atomic structures of actin and myosin subfragment 1 (S1; the head and neck region of my

52 In analogy to SH1-labeled myosin subfragment 1 (SH1-S1), SH2-labeled S1 (SH2-S1) a

53 , MgADP, and smooth muscle (chicken gizzard) myosin subfragment 1 (smS1).

54 Myosin subfragment 1 and a series of nucleoside triphosp

55 omic model of acto-S1, the complex formed by myosin subfragment 1 and actin, reveals that the regulat

56 nd the C-terminal long alpha-helix domain of myosin subfragment 1 as well as myosin subfragment 2 (Gl

57 Fitting the acto-myosin subfragment 1 atomic structure into the tomogram

58 It inhibits acto-myosin subfragment 1 ATPase (acto-S-1 ATPase) and filame

59 CA(2+)-sensitive regulation of thin filament-myosin subfragment 1 ATPase activity, or the CA2+ concen

60 was 41 s-1 in the first turnover based on a myosin subfragment 1 concentration of 150 microM.

61 er with the reconstituted thin filament, but myosin subfragment 1 decreased the transfer, consistent

62 Both C0 and C1 compete with myosin subfragment 1 for binding to F-actin and effectiv

63 Myosin subfragment 1 hydrophobicity was found to be sens

64 -ATP (1b, enf-ATP) to act as a substrate for myosin subfragment 1 in the presence and absence of acti

65 cs of their interaction with rabbit skeletal myosin subfragment 1 in the presence and absence of acti

66 I-troponin was inhibitory in a thin filament-myosin subfragment 1 MgATPase assay.

67 he tropomyosin deletion suppressed the actin-myosin subfragment 1 MgATPase rate and the in vitro slid

68 tation resulted in a decreased thin filament-myosin subfragment 1 MgATPase rate.

69 While mutations in the myosin subfragment 1 motor domain can directly disrupt t

70 onship when actin filaments are propelled by myosin subfragment 1 or full-length myosin.

71 Superposition of the structures of ncd and myosin subfragment 1 reveals that the labeled cysteine i

72 tropomyosin to actin, cooperative binding of myosin subfragment 1 to the thin filament, CA(2+)-sensit

73 The interaction with skeletal myosin subfragment 1 was measured in the absence and pre

74 e examined the interactions of smooth muscle myosin subfragment 1 with ADP to see if this additional

75 e incubated with a wide range of fluorescent myosin subfragment 1(fS1) at pCa 9 or pCa 4 with or with

76 Atomic structures of scallop myosin subfragment 1(S1) with the bound MgADP, MgAMPPNP,

77 Irradiation of the stable myosin subfragment 1(S1).MgADP.orthovanadate (Vi) comple

78 ring the first turnover (based on 180 microM myosin subfragment 1).

79 plakinolide-induced filaments decorated with myosin subfragment 1, demonstrating unequivocally that t

80 Acanthamoeba myosin II, heavy meromyosin and myosin subfragment 1, have actin-activated MgATPase that

81 cooperativity in the equilibrium binding of myosin subfragment 1, to actin but the binding curves di

82 In contrast to rabbit skeletal myosin subfragment 1, where the mant group is protected

83 tion greatly weakened tropomyosin binding to myosin subfragment 1-decorated actin, with the full-leng

84 Myosin subfragment 1-fragment decoration demonstrated th

85 dues had no effect on Ca2+-activation of the myosin subfragment 1-thin filament MgATPase rate and did

86 ubstituted it for the VELC of bovine cardiac myosin subfragment 1.

87 n either MgADP.BeFx.SlDc or chicken skeletal myosin subfragment 1.

88 ore typical, long filaments upon addition of myosin subfragment 1.

89 , and to a lesser degree, thin filament with myosin subfragment 1.

90 t various times after rapidly mixing ATP and myosin subfragment 1.

91 ulation of the interaction between actin and myosin subfragment 1: evidence for three states of the t

92 Purified wild-type and mutant myosin subfragments 1 (S1), expressed in Dictyostelium,

93 e binding of actin to rabbit skeletal muscle myosin subfragment-1 (a single-headed subfragment) can b

94 -binding, non-force-generating derivative of myosin subfragment-1 (NEM-S1) in chemically skinned myoc

95 activation with Ca(2+) and N-ethyl-maleimide myosin subfragment-1 (NEM-S1), a non-tension-generating,

96 fter addition of N-ethylmaleimide-conjugated myosin subfragment-1 (NEM-S1), a strongly binding myosin

97 trong-binding, nonforce-generating analog of myosin subfragment-1 (NEM-S1).

98 measurements of the binding stoichiometry of myosin subfragment-1 (S-1) to the RTF.

99 anine reduced the strong binding of actin to myosin subfragment-1 (S1) 9-fold compared to wild-type a

100 Atomic models of myosin subfragment-1 (S1) and the actin filament are doc

101 Neither acto-myosin subfragment-1 (S1) ATPase activity nor the trypti

102 When myosin subfragment-1 (S1) binds to actin, these lysines

103 calcium affinity in regulated thin filament-myosin subfragment-1 (S1) MgATPase assays, a 20% decreas

104 ng constant for DNEQ and delta-DSE actins to myosin subfragment-1 (S1) relative to that of wild type

105 The proximity of skeletal myosin subfragment-1 (S1) to actin, and its orientation

106 The binding curve of myosin subfragment-1 (S1) to F-actin is not a simple hyp

107 Myosin subfragment-1 (S1) was labeled with NPM in the pr

108 mide, and the labeled ELC was exchanged into myosin subfragment-1 (S1).

109 ansfer between the regulatory light chain on myosin subfragment-1 and the C-terminus of actin was mea

110 onin T inhibited actin-tropomyosin-activated myosin subfragment-1 ATPase activity to the same extent

111 actin and WT troponin and beta-TM, activated myosin subfragment-1 ATPase in a calcium-dependent, coop

112 nylyl-imidodiphosphate) binding to wild-type myosin subfragment-1 enhanced tryptophan fluorescence by

113 ation of myosin observed in chicken skeletal myosin subfragment-1 is unable to hydrolyze ATP and most

114 mation observed here and in chicken skeletal myosin subfragment-1 is unable to hydrolyze ATP and repr

115 The force-extension curve of single myosin subfragment-1 molecules, interacting in the rigor

116 th nucleotide binding to the skeletal muscle myosin subfragment-1.

117 ures are similar to that of chicken skeletal myosin subfragment-1.

118 ix domain of myosin subfragment 1 as well as myosin subfragment 2 (Gly773-Ser1104) and light chains o

119 levels and have modeled the organization of myosin subfragment 2 and the possible locations of the 3

120 shows interaction with heavy meromyosin and myosin subfragment 2 but not subfragment 1.

121 sted by measuring separation distances among myosin subfragment-2, the nucleotide site, and the regul

122 wo intact myosin heads because single-headed myosin subfragments are always active.

123 degree to which competitive displacement of myosin subfragment binding to actin is responsible for t

124 The actin-myosin subfragment S1 ATPase activity was greater for th

125 Rigor and weak (in the presence of ATP) myosin subfragment (S1) binding and acto-S1 ATPase did n

126 Competition binding experiments of myosin subfragment (S1) to cross-linked dimers in the pr

127 by the active sites of expressed myosin and myosin subfragments, which are not available in sufficie

128 Expressed smooth muscle myosin subfragments with as many as 100 amino acids of t