ライフサイエンスコーパス: barbed end of

1 They attach to the barbed end of a filament and prevent polymerization, lea

2 profilin will block subunit addition at the barbed end of a filament.

3 characterized myosin motors move towards the barbed (+) end of actin filaments.

4 sis shows how the binding of profilin to the barbed end of actin causes a rotation of the small domai

5 heads swing forward alternately towards the barbed end of actin driven by ATP hydrolysis.

6 formin, AtFH14, processively attaches to the barbed end of actin filaments as a dimer and slows their

7 s, function as homodimers that bind with the barbed end of actin filaments through a ring-like struct

8 tin capping protein (CP), which binds to the barbed end of actin filaments to prevent the addition or

9 CP binds with high affinity to the barbed end of actin filaments, blocking the addition and

10 ng protein, purified Cdc12(FH1FH2)p caps the barbed end of actin filaments, preventing subunit additi

11 cing the capping protein CapZ at the growing barbed end of actin filaments.

12 , HPO-30 ICD directly binds to the sides and barbed end of actin filaments.

13 of the actin cytoskeleton by binding to the barbed end of actin filaments.

14 Myosin V, a motor that moves toward the barbed end of actin, is processive, undergoing multiple

15 Actin capping protein (CapZ) binds the barbed ends of actin at sarcomeric Z-lines.

16 d that dissociates capping proteins from the barbed ends of actin filaments [14] [15] [16], they are

17 he cell allow capping protein to bind to the barbed ends of actin filaments and Arp2/3 complex to bin

18 Myosin XVa localization overlaps with the barbed ends of actin filaments and extends to the apical

19 units for subsequent polymerization steps at barbed ends of actin filaments and has been shown to par

20 Profilin interacts with the barbed ends of actin filaments and is thought to facilit

21 ate between the low affinity of profilin for barbed ends of actin filaments and its high affinity for

22 rized and discontinuous distribution of free barbed ends of actin filaments and of beta-actin protein

23 concentration of capping protein, which caps barbed ends of actin filaments and prevents elongation,

24 pping protein (CP) binds the rapidly growing barbed ends of actin filaments and prevents the addition

25 muscles near or on sarcomere Z lines, where barbed ends of actin filaments are anchored.

26 ia revealed that the relative levels of free barbed ends of actin filaments are reduced by over 30% i

27 ing proteins bind to and dissociate from the barbed ends of actin filaments by observing single muscl

28 the closer to the front of the cell the more barbed ends of actin filaments face forward.

29 The Bni1 FH2 domain protects growing barbed ends of actin filaments from vast excesses of cap

30 The barbed ends of actin filaments in striated muscle are an

31 CP binds to the barbed ends of actin filaments in vitro and controls act

32 e interaction of N-WASP with GRB2 and/or the barbed ends of actin filaments increases its exchange ra

33 Capping the barbed ends of actin filaments is a critical step for re

34 echanism by which capping protein (CP) binds barbed ends of actin filaments is not understood, and th

35 model to investigate how competition for the barbed ends of actin filaments might influence this proc

36 min proteins associate processively with the barbed ends of actin filaments through many rounds of ac

37 and tightly associate with the fast growing barbed ends of actin filaments to allow insertional grow

38 Actin capping protein (CP) binds barbed ends of actin filaments to regulate actin assembl

39 ive activity of lamellipodia, depends on the barbed ends of actin filaments, and requires both the LI

40 also demonstrate that Aip1 does not cap the barbed ends of actin filaments, as was previously though

41 nucleation, and growth by polymerization of barbed ends of actin filaments, as well as capping and d

42 his interaction weakens the binding of CP to barbed ends of actin filaments, lessening the ability of

43 VASP induces and maintains clustering of the barbed ends of actin filaments, which putatively corresp

44 nding inhibited the ability of CP to cap the barbed ends of actin filaments.

45 oteins move processively with the elongating barbed ends of actin filaments.

46 unction of CP is presumed to involve binding barbed ends of actin filaments.

47 ) uncaps a small number of the fast-growing (barbed) ends of actin filaments, thereby eliciting slow

48 P promotes depolymerization at the opposite (barbed) ends of actin filaments.

49 the cleft separating domains 1 and 3 at the barbed-end of actin.

50 AIP1 also caps the barbed end of ADF/cofilin-bound actin filament.

51 The very high affinity of gelsolin for the barbed end of an actin filament drives the binding react

52 number as it severs F-actin and to cover the barbed end of an actin filament, which otherwise might c

53 ittle effect on Capu once it is bound to the barbed end of an elongating filament.

54 cture may allow formins to stair-step on the barbed end of an elongating nascent filament.

55 The alpha/beta-heterodimer caps the barbed ends of an actin filament and restricts its growt

56 is slow, predicting a half-life for a capped barbed end of approximately 30 min.

57 These data suggest the barbed end of Arp2 is exposed, but Arp2 and Arp3 are not

58 ivation the first actin monomer binds at the barbed end of Arp2.

59 NPFs, Arpin has a C-helix that binds at the barbed end of Arp3.

60 These results suggest that the barbed ends of Cdc42-induced filaments are protected fro

61 motility is driven by actin assembly at the barbed ends of core bundles, which in turn is linked to

62 ently inhibits nucleation and binding to the barbed end of elongating filaments by the C-terminal hal

63 INF2 and two of DIA1 bound to the middle and barbed end of F-actin.

64 brin inhibits depolymerization mainly at the barbed end of F-actin.

65 n the same strand but probably closer to the barbed end of F-actin.

66 ments like swinholide A; rather, it caps the barbed end of F-actin.

67 Myosin-5 walks toward the barbed ends of F-actin, traveling to sites of actin poly

68 threefold longer processive runs on trailing barbed ends of fascin-bundled F-actin.

69 Moreover, enhanced processivity on trailing barbed ends of fascin-bundled filaments is an evolutiona

70 We conclude that XAip1 caps the barbed end of filaments severed by cofilin.

71 It binds to the barbed end of filaments with high affinity and modulates

72 elerate elongation, although it binds to the barbed end of filaments.

73 ctin elongates either the pointed end or the barbed end of filaments.

74 Aip1 does not cap the barbed ends of filaments severed by cofilin.

75 Formins bind the barbed ends of filaments via their dimeric FH2 domains,

76 on through a processive interaction with the barbed ends of filaments.

77 pFH1FH2 remained associated with the growing barbed ends of filaments.

78 in monomer incorporation at the fast-growing barbed ends of filaments.

79 2 domains form dimers that bind actin at the barbed end of growing filaments and remain attached as n

80 ofilin-actin from the cellular pool onto the barbed end of growing filaments.

81 Capping protein (CP) binds to barbed ends of growing actin filaments and inhibits elon

82 quent recruitment of fascin to the clustered barbed ends of Lambda-precursors initiated filament bund

83 atory factors IRTKS and EPS8 localize to the barbed ends of motile microvilli, where they control the

84 %) associate for approximately 25 s with the barbed end of preassembled filaments, inhibiting their e

85 ucleated new actin filaments or captured the barbed ends of preformed actin filaments that grew by in

86 The probe angle relative to the barbed end of the actin (beta) averaged 128 degrees whil

87 ghtly caps (K(d) approximately 0.1-1 nM) the barbed end of the actin filament (the end favored for po

88 expressed, 62-kDa heterodimer that binds the barbed end of the actin filament with approximately 0.1

89 heterodimeric 62-kDa protein that binds the barbed end of the actin filament with high affinity to b

90 nucleate and processively cap the elongating barbed end of the actin filament, and Bud6 and profilin

91 and the molecular basis for how CP binds the barbed end of the actin filament, we have used a combina

92 ty to block monomer addition and loss at the barbed end of the actin filament.

93 fidelity of information communicated at the barbed end of the actin filament.

94 ced dynamics at the edge oriented toward the barbed end of the actin filament.

95 and cell motility by binding tightly to the barbed end of the actin filament.

96 Villin wraps around and caps the barbed end of the actin trimer.

97 ne on Arp3, delivering actin subunits at the barbed end of the Arps to initiate branch elongation.

98 Subunits at the barbed end of the filament are likely to be in this favo

99 Rapid treadmilling, where the barbed end of the filament grows and the pointed end shr

100 Conversely, the barbed end of the filament takes on a conformation nearl

101 rmin Homology 2 (FH2) domain dimers with the barbed end of the filament, allowing subunit addition wh

102 P interacts with both actin protomers at the barbed end of the filament, and the amphipathic helix at

103 in complexes into contact with the FH2-bound barbed end of the filament, thereby enabling direct tran

104 units between the immobilized formin and the barbed end of the filament.

105 in is proposed to be in position to join the barbed end of the growing filament concurrently with the

106 tes actin filaments and remains bound to the barbed end of the growing filament.

107 merization at the pointed end as well as the barbed end of the monomer.

108 ctin polymerization and protects the growing barbed ends of the actin fibers from capping proteins.

109 ngly, a loss of the uniform alignment of the barbed ends of the actin filaments.

110 e presence of magnesium, suggesting that the barbed ends of the erythrocyte actin filaments are cappe

111 To test directly whether the barbed ends of the erythrocyte actin filaments were alre

112 ion due to addition of actin monomers to the barbed ends of the filaments.

113 ing nurse cell dumping, Enabled localizes to barbed ends of the nurse cell actin filaments, suggestin

114 Localization of Fhos to the barbed-ends of the arrays, achieved via a novel N-termin

115 ex nucleation in vitro, but uncapping of the barbed ends of these actin filaments restores their abil

116 ed rat cardiac myofibrils at the pointed and barbed ends of thin filaments, respectively.