ライフサイエンスコーパス: crossbridge

1 with the structural "backbone" of the myosin crossbridge.

2 to index the lifetime of the prerigor, AMADP crossbridge.

3 ioether linkages in addition to the cofactor crossbridge.

4 to the compliance known to be present in the crossbridge.

5 he amino group of the pentaglycine cell wall crossbridge.

6 ing the aggregate number of force-generating crossbridges.

7 results from rotation of actin-bound myosin crossbridges.

8 ggesting that it arose from actively cycling crossbridges.

9 of ATP, enough only for a single turnover of crossbridges.

10 reonine (T) and the amino group of cell-wall crossbridges.

11 y affects the number of attached and cycling crossbridges.

12 e used by SR-Ca2+ pumps and the remainder by crossbridges.

13 promote strong binding of endogenous myosin crossbridges.

14 o reductions in the number of strong-binding crossbridges.

15 ridges, and decreased the flexibility of the crossbridges.

16 dent on feedback effects of force-generating crossbridges.

17 to some extent, with that of cycling myosin crossbridges.

18 hat rear bridges are more strained than lead crossbridges.

19 realignment to fit into both types of rigor crossbridges.

20 f myofilaments powered by the cycling myosin crossbridges.

21 ow double-headed lead and single-headed rear crossbridges.

22 have a nonhelical, side-polar arrangement of crossbridges.

23 nd exposes a tethering segment of S2 in many crossbridges.

24 ting in cooperative binding of other cycling crossbridges.

25 de-linked to the amino group of pentaglycine crossbridges.

26 on is primarily determined by strong cycling crossbridges.

27 ted using a five-step kinetic scheme for the crossbridge/A-MATPase cycle where the force generating c

28 in skinned fibres by reducing the number of crossbridges able to productively bind to the thin filam

29 e, may serve as a swing-out adapter allowing crossbridge access to actin, as the elastic component of

30 ight into the modulation mechanism of strong crossbridge and cTnI phosphorylation in cardiac thin fil

31 access to actin, as the elastic component of crossbridges and as part of a phosphorylation-regulated

32 -MHC-containing filaments did not extend the crossbridges and did not alter degree of order or flexib

33 echanisms: having a small number of attached crossbridges and probably utilizing intracellular Ca2+ b

34 ), as well more complex interactions between crossbridges and regulatory units (XB-RU interactions).

35 consists of paired rigor-like and non-rigor crossbridges and suggests possible transitions in the my

36 rises from increasing strain of all attached crossbridges and that the first transition reflects the

37 activated filaments requires strongly bound crossbridges, and (3) that crossbridges are bound to the

38 tation, increased the degree of order of the crossbridges, and decreased the flexibility of the cross

39 that do not average the repeating motifs of crossbridges, and thereby retain information on variabil

40 ch of six fn3 domains, and that the last two crossbridges are at the level of the first two groups of

41 ion of muscle and muscle fibres, most myosin crossbridges are attached to actin during isometric cont

42 es strongly bound crossbridges, and (3) that crossbridges are bound to the periphery of actin, at a s

43 verse lines in a portion of the A band where crossbridges are found (C zone).

44 tead, new non-rigor forms of variably angled crossbridges are found bound to actin sites not labeled

45 at in resting vascular smooth muscle, active crossbridges are inhibited by caldesmon.

46 In transverse view, AMPPNP "lead" crossbridges are less azimuthally bent than rigor.

47 This suggests that many crossbridges are weakly attached to actin, possibly at t

48 ising from radial forces exerted by attached crossbridges, are fast enough to occur during the power

49 ructure and argue against a bipolar, helical crossbridge arrangement.

50 axing position on actin that inhibits myosin-crossbridge association.

51 trained, relaxing position to inhibit myosin-crossbridge association.

52 order meridional reflection from the myosin crossbridges, at 14.56 nm) at each of a number of quick

53 mp enhances an early step in the actomyosin (crossbridge) ATPase cycle before Pi-release.

54 that a T-jump promotes an early step in the crossbridge-ATPase cycle that generates force.

55 measure of changes in the numbers of myosin crossbridges attached to actin during Ca2+ activation.

56 -dependent changes are independent of strong crossbridge attachment and likely arise from alterations

57 itch locomotory fibers, but surprisingly the crossbridge attachment rate has remained unchanged.

58 ve neighbor interactions or length-dependent crossbridge attachment, contributed unique features to t

59 These kinetics result in very few crossbridges being attached during contraction of superf

60 The role of dityrosine as a fluorescent crossbridge between adjacent calmodulin molecules within

61 single microtubules, but forms well-defined crossbridges between antiparallel filaments.

62 otic flagella the dynein motor proteins form crossbridges between the outer doublet microtubules.

63 The structure reveals flexible crossbridges between the two protofilaments, and subunit

64 structuring of axoplasm through intra-axonal crossbridging between adjacent neurofilaments or to othe

65 dergo dynamic rearrangement concomitant with crossbridge binding in the A band.

66 tivation and relaxation rates of tropomyosin/crossbridge binding kinetics differ most significantly b

67 ng to the thin filaments recruits additional crossbridge binding to actin as well as increased Ca2+ b

68 Our results also predicted crossbridge binding to be slowest in human and fastest i

69 highly cooperative process in which initial crossbridge binding to the thin filaments recruits addit

70 thought to involve switch-like regulation of crossbridge binding to the thin filaments.

71 Another class of glycol-PNP crossbridge binds outside the rigor actin target zone.

72 very oxygen consumption in the presence of a crossbridge blocker, N-benzyl-p-toluene sulphonamide (BT

73 put is mediated by alterations in numbers of crossbridges bound to the thin filament.

74 to aggregate and the filaments are maximally crossbridged by fascin.

75 under cellular conditions, unphosphorylated crossbridges can slowly cycle.

76 NP-N that becomes rigidified 1,000-fold upon crossbridging CENP-A and its adjacent nucleosomal DNA.

77 econstruction of AMPPNP fibers show only one crossbridge class, in the position of the rigor lead bri

78 The portion of the crossbridge close to the thick filament appears broader

79 Our findings suggest that at least 62% of crossbridge compliance is associated with the tail domai

80 dence of the peak tension suggest that a non-crossbridge component increasingly develops tension thro

81 In order to visualize the changes in crossbridge conformation and distribution that give rise

82 Crossbridges consist of the globular N-terminal catalyti

83 filament-associated protein localized to the crossbridge-containing C zones of striated muscle sarcom

84 To determine the fraction of crossbridges contributing to tension and the structural

85 sion rise is reduced to 30-40%, the peak non-crossbridge contribution and the residual force enhancem

86 ion is reduced to approximately 15%, and the crossbridge contribution to stretch-induced tension rise

87 nd some single-headed "lead" bridges but few crossbridges corresponding to the rear bridges of rigor.

88 rther study, physiological regulation of the crossbridge cycle by calponin.

89 The findings aid our understanding of the crossbridge cycle by showing that it may not be necessar

90 investigate the regulation of the actomyosin crossbridge cycle in cardiac muscles, the effects of ATP

91 ously developed mechano-kinetic model of the crossbridge cycle in frog muscle to simulate the tempera

92 Thereafter, the crossbridge cycle is largely truncated, with prepower st

93 herefore, the effect of CP on the actomyosin crossbridge cycle is proposed to occur through a functio

94 In contrast, when crossbridge cycle kinetics were slowed by lowering [ATP]

95 this may be due, at least in part, to faster crossbridge cycle kinetics.

96 tes, in part, by speeding the step(s) in the crossbridge cycle that limit loaded shortening rates, an

97 To investigate the kinetic parameters of the crossbridge cycle that regulate force and shortening in

98 Two processes characterize intermediate crossbridge cycle transitions, B (work producing) and C

99 d that the tension-generating step(s) in the crossbridge cycle was highly endothermic and was therefo

100 urrent models for the Ca2+ activation of the crossbridge cycle, but these models do not explain the s

101 an extra step in the attached pathway of the crossbridge cycle, perhaps located on a parallel pathway

102 ase perturb different molecular steps in the crossbridge cycle.

103 yosin binding site, at an early stage of the crossbridge cycle.

104 uring the prepowerstroke state of the dynein crossbridge cycle.

105 a full understanding of the operation of the crossbridge cycle.

106 hat causes actin filaments, and hence myosin-crossbridge cycling and contraction, to switch on and of

107 Da myosin light chain (MLC), which activates crossbridge cycling and the polymerization of a pool of

108 is indicates that dATP increased the rate of crossbridge cycling in cardiac muscle.

109 ry determinant in controlling the actomyosin crossbridge cycling kinetics of cardiac muscles, because

110 Crossbridge cycling kinetics were studied by measuring k

111 including thin filament on-off kinetics and crossbridge cycling kinetics with interactions within an

112 tretch activation response are indicators of crossbridge cycling kinetics.

113 d phosphorylation also accelerated isometric crossbridge cycling kinetics.

114 This steric effect controls myosin-crossbridge cycling on actin that drives contraction.

115 n by C-protein is mediated by the effects of crossbridge cycling on the Ca2+ affinity of troponin C.

116 intrinsic length component increases loaded crossbridge cycling rates at short SL and beta-MyHC myoc

117 stent with contraction cost being minimized (crossbridge cycling), in contrast to the contractile cos

118 n important parameter in setting the rate of crossbridge cycling, and (2) C protein-mediated control

119 0 kDa light chain of myosin, which activates crossbridge cycling, as well as the polymerization of a

120 tified substance(s) that inhibits myocardial crossbridge cycling, independent of Ca2+ or other second

121 ATPase activity by modifying the kinetics of crossbridge cycling.

122 ing a tropomyosin conformation that prevents crossbridge cycling.

123 tion, resulting in release of the "brake" on crossbridge cycling.

124 sed, redeveloped force, demonstrating active crossbridge cycling; strips containing normal h-caldesmo

125 ge force generation and faster (post-stroke) crossbridge detachment by negative strain.

126 tation that the Ca(2+)-dissociation rate and crossbridge detachment rate are similar in fast-twitch s

127 f Ca(2+) from troponin C (TnC) and decreased crossbridge detachment rate on the time course of relaxa

128 bladder fibers have evolved a 10-fold faster crossbridge detachment rate than fast-twitch locomotory

129 and very fast calcium transient, (ii) a fast crossbridge detachment rate, and (iii) probably a fast k

130 hat does not alter the rate-limiting step of crossbridge detachment.

131 and regulatory domains of the new non-rigor crossbridges differ from those in the atomic model of ac

132 )) and of force redevelopment after forcible crossbridge dissociation (k(act)) were similar and were

133 Calcium- and copper-crossbridged domains of synthetic block copolymers or na

134 g sites on actin, thereby controlling myosin crossbridge dynamics and consequently muscle contraction

135 (2+) binding at neighbouring Tn sites and/or crossbridge feedback effects on Ca(2+) binding affinity.

136 hanged the myofilament characteristics via a crossbridge feedback mechanism.

137 These results suggest that (1) crossbridge flexibility is an important parameter in set

138 locity is increased, probably enhancement of crossbridge force generation and faster (post-stroke) cr

139 was to investigate the strain sensitivity of crossbridge force generation in muscle.

140 a characteristic rise in force showing that crossbridge force generation is endothermic (heat absorb

141 Thus the crossbridge force generation step in muscle is both temp

142 dial force-frequency relation, and increased crossbridge force-time integral (FTI).

143 structural changes are further modulated by crossbridge formation and fine-tuned by phosphorylation

144 re, Tmods are novel regulators of actomyosin crossbridge formation and muscle contractility, and futu

145 ation, thin filament lengths, and actomyosin crossbridge formation in skeletal muscle fibers.

146 s critical to the inhibition of actin-myosin crossbridge formation when intracellular calcium is low.

147 n actin polymerization, fimbrin binding, and crossbridge formation, presumably achieved by a feedback

148 X-ray diagrams, suggesting that the average crossbridge forms in the reconstruction reflect the nati

149 force is associated with a transition of the crossbridges from a state in which they are nonspecifica

150 f C protein by protein kinase A extended the crossbridges from the backbone of the filament, changed

151 nism for the previously observed increase in crossbridge FTI.

152 idal length perturbation analysis to compare crossbridge function in skinned left ventricular (LV) ep

153 lament is important for the formation of the crossbridge gap and thus the termination of the thick fi

154 dition, although 3-D visualization of myosin crossbridges has been possible in rigor, it has been dif

155 ontact interface with actin, while nontarget crossbridges have variable contact interfaces.

156 ion with a high-affinity toxin or disulphide crossbridge impedes the return of this voltage sensor to

157 Similar comparison using lead-type crossbridges in AMPPNP reveals departures from the rigor

158 The structure and function of myosin crossbridges in asynchronous insect flight muscle (IFM)

159 eflections generated by the arrays of myosin crossbridges in contracting muscle.

160 he possible roles of strongly binding myosin crossbridges in determining loaded shortening and power

161 Crossbridges in filaments with beta-MHC were less ordere

162 ure of chicken subfragment 1 (S1) to fit IFM crossbridges in lower-resolution electron microscopy tom

163 ed the three-dimensional structure of myosin crossbridges in situ in order to define the structural c

164 phosphorylation-regulated on-off switch for crossbridges in smooth muscle.

165 sphate (Pi) should shift the distribution of crossbridges in the actomyosin ATPase (AMATPase) to incr

166 In contrast to the rigor lead and rear crossbridges in the double chevrons, the averaged recons

167 hus reducing both the fraction of actomyosin crossbridges in the strongly bound state (-29%) and fibe

168 Comparison of in situ crossbridges in tomograms of rigor with atomic model of

169 Rather, it may be related to a decrease in crossbridge-induced activation of the thin filament at t

170 The relative flexibility of the crossbridges inferred from the optical diffraction patte

171 erties (M80Q sTnCF27W) did not affect strong crossbridge inhibition by 2,3-butanedione monoxime when

172 Effects of temperature, crossbridge inhibition, or variation in [MgATP] support

173 Muscle force is generated by myosin crossbridges interacting with actin.

174 uctural and kinetic effects of Ca2+ binding, crossbridge interaction, and protein kinase A phosphoryl

175 to an inhibitory position that blocks myosin-crossbridge interaction.

176 Acto-myosin (crossbridge) interaction was either inhibited using N-be

177 est known vertebrate muscle, we examined the crossbridge kinetic rates responsible for high contracti

178 , PKA phosphorylation of cMyBP-C accelerates crossbridge kinetics and loss of this regulation leads t

179 demonstrate that to achieve rapid actomyosin crossbridge kinetics bat and songbird SFM express myosin

180 Decreasing the rate of crossbridge kinetics by reducing intracellular inorganic

181 lel studies with intact muscles, we assessed crossbridge kinetics indirectly by determining f(min) (t

182 We examined the influences of Ca2+ and crossbridge kinetics on the maximum rate of force develo

183 loaded shortening velocity via regulation of crossbridge kinetics or crossbridge number, the shorteni

184 at the maximum relaxation rate is limited by crossbridge kinetics rather than by k(off).

185 yosin binding protein (cMyBP)-C may regulate crossbridge kinetics to modulate contraction.

186 Further, normal crossbridge kinetics were observed, demonstrating that m

187 may be mainly due to species differences in crossbridge kinetics.

188 ings are consistent with a lack of effect on crossbridge kinetics.

189 one in which stereospecifically bound myosin crossbridges label the actin helix.

190 tomograms of "glycol-stiff" sarcomeres show crossbridges large enough to contain only a single myosi

191 Crossbridge links between the central microtubule pair h

192 d control of the position and flexibility of crossbridges may regulate actomyosin ATPase activity by

193 phase during which ATP molecules soften the crossbridge-microtubule attachment at the cilium inflect

194 A new crossbridge motif identified in AMPPNP-treated muscle co

195 se in birefringence has been correlated with crossbridge movement away from the thick filaments.

196 birefringence response inverted, suggesting crossbridge movement similar to that of skeletal muscle.

197 Our data demonstrate that the gap of myosin crossbridges near the end of the thick filament closely

198 ty via regulation of crossbridge kinetics or crossbridge number, the shortening velocity was measured

199 at cleaves the stem peptide and pentaglycine crossbridge of the cell wall and alters processing and a

200 d that the ATPase domain of myosin forms the crossbridges of thick filaments that bind actin, and int

201 tion of cTnI were similar to those of strong crossbridges on structural changes in cTnI.

202 he docking sites for weak and strongly bound crossbridges on thin filaments.

203 kbones and, in addition, reveal projections (crossbridges) on only two opposite sides of the square.

204 is determined primarily by strongly binding crossbridges or by [Ca(2+)] per se, which was done by me

205 Although bipolar tetramers were known to crossbridge pairs of microtubules, the mechanism for org

206 These results indicate that strongly binding crossbridges play a significant role in determining load

207 Divalent cations are shown here to crossbridge polyanionic amphiphiles, which thereby demix

208 bundles, time-dependent use of at least two crossbridging proteins, filament turnover, treadmilling,

209 (1,0)) indicate that PKA treatment increased crossbridge proximity to thin filaments under all condit

210 e is largely truncated, with prepower stroke crossbridges rapidly detaching at high strain and attach

211 hin filament binding sites (cTnI) or altered crossbridge recruitment (cMyBP-C/titin).

212 The ATP usage per twitch by the myosin crossbridges remains essentially constant at approximate

213 Correspondence analysis of 1831 38.7 nm crossbridge repeats grouped self-similar forms from whic

214 orescence originating from approximately 400 crossbridges residing in a small volume defined by a con

215 t with the strong binding of a single-myosin crossbridge, resulting in cooperative binding of other c

216 of actomyosin subfragment 1 to the averaged crossbridges shows that the detectable differences betwe

217 ) to increase the relative population of the crossbridge state prior to ADP release and Pi release, r

218 increases with temperature because attached crossbridge states bearing a relatively low force conver

219 thereby retain information on variability of crossbridge structure and distribution.

220 there is coupling between the RU and myosin crossbridges, the functional outcome of cardiomyopathy-r

221 t counterion entropy dominates electrostatic crossbridges, thus illustrating the insights gained into

222 position on the thin filament and binding of crossbridges to actin.

223 flight muscle the response of in situ rigor crossbridges to AMPPNP binding is not uniform.

224 the important contribution of strong binding crossbridges to cardiac muscle activation, likely mediat

225 romised, the relative contribution of strong crossbridges to maintain thin filament activation is inc

226 iated by cooperative recruitment of adjacent crossbridges to maximize force redevelopment against ext

227 ggest that myofibrillar-space calcium causes crossbridges to move away from the thick filaments witho

228 identically correlated, which indicated that crossbridge turnover was unaffected by Tm isoform switch

229 ion and the structural changes that attached crossbridges undergo when generating force, we monitored

230 e activation or the relative contribution of crossbridges versus Ca2+ to thin filament activation.

231 cing (b) and work-absorbing (c) steps of the crossbridge were less in alphaMHC403/+ strips than in wi

232 In thick filaments with alpha-MHC, crossbridges were clearly visible.

233 P utilization rates of the SR-Ca2+ pumps and crossbridges were measured using a coupled assay system

234 ve proportions used by SR-Ca2+ pumps and the crossbridges were similar to other muscles.

235 The crossbridges were synchronized by rapid photogeneration

236 scles and observed by negative staining show crossbridges with a 14.5-nm repeat projecting in opposit

237 probability of strong interactions of myosin crossbridges with actin, thereby decreasing cooperative

238 Crossbridges with an average 90 degrees axial angle cont

239 ant allosteric effects on the interaction of crossbridges with the thin filament.

240 the amino group of the m-diaminopimelic acid crossbridge within the listerial peptidoglycan.

241 ermit simultaneous examination of all myosin crossbridges within the unit cell and direct comparison

242 al link influenced the kinetics of activated crossbridges without affecting the aggregate number of f

243 butable to the reduced frequency b, at which crossbridge work is maximum.

244 tively, Ca2+ control of the number of active crossbridges would yield similar velocity-tension relati

245 Tm(H276N) slowed crossbridge (XB) detachment rate (g) by 19%.

246 The magnitude of length-mediated increase in crossbridge (XB) recruitment (E0) decreased by ~33% and

247 nI modulate muscle length-mediated effect on crossbridge (XB) recruitment dynamics, Ca(2+)-activated

248 ns between regulatory units (RU-RU), between crossbridges (XB-XB), as well more complex interactions