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1 ilizing the closed switch 2 structure of the myosin head.
2 , indicating considerable flexibility in the myosin head.
3 interact with the ATP hydrolysis site in the myosin head.
4 bound and exerted chaperone activity on the myosin head.
5 ied by a disorder-to-order transition of the myosin head.
6 n and reveals an unusual conformation of the myosin head.
7 rIA-labeled RLC is functionally bound to the myosin head.
8 rminal UCS domain known to interact with the myosin head.
9 al orientation and rotational motions of the myosin head.
10 ally due to drag forces from weakly attached myosin heads.
11 ar to be due to the longitudinal addition of myosin heads.
12 e to an axial perturbation of some levels of myosin heads.
13 f the resistive population of strongly bound myosin heads.
14 on of lever arm angles of the actin-attached myosin heads.
15 the 14.5 nm axial spacing between crowns of myosin heads.
16 n is partially available for weak binding of myosin heads.
17 of myosin head domains or the orientation of myosin heads.
18 hich reciprocally affects the motions of the myosin heads.
19 o transitions in the dynamics of interacting myosin heads.
20 insert can affect the cooperativity between myosin heads.
21 tween the functional behavior of MRP and MHC myosin heads.
22 c packing but is enforced by elements of the myosin heads.
23 acterized the motions of these force-bearing myosin heads.
24 ed, directly demonstrating signaling between myosin heads.
25 n intact, a distortion must occur within the myosin heads.
26 ls an asymmetric interaction between the two myosin heads.
27 tile filament array alter the motions of the myosin heads.
28 ted with a conformational equilibrium of the myosin heads.
29 where Tpm shields actin from the binding of myosin heads.
30 ulated thin filaments even in the absence of myosin heads.
31 s and cooperative interactions between bound myosin heads.
32 duce an M-region (bare zone) that is free of myosin heads.
35 ed changes in X-ray reflections arising from myosin heads, actin filaments, troponin, and tropomyosin
37 even more dramatic, in that at all levels of myosin head/actin, phosphorylation was necessary to affe
38 ta suggest that the regulatory domain of the myosin head acts as a single mechanically rigid body, co
39 M3 reflection from the regular repeat of the myosin heads along the filaments decreased in proportion
40 confirmed the axial tilt; but strongly bound myosin heads also showed an unexpected azimuthal slew of
42 The peak angle between the lever axis of the myosin head and the fiber or actin filament axis was 100
43 conserved interactions between the 'blocked' myosin head and the myosin tail, which may contribute to
44 erable flexibility in the orientation of the myosin head and the position of the S1-S2 junction is ne
45 of myofibrillogenesis are independent of the myosin head and these processes are regulated by the myo
47 defined interactions sites between adjacent myosin heads and associated protein partners, and then a
48 f two rich layer-line patterns, one from the myosin heads and based on a 429 A axial repeat, and one
49 meridional reflections come from unattached myosin heads and from backbone components of the myosin
50 sociated with the quasi-helical order of the myosin heads and myosin binding protein C (MyBP-C) decre
51 iled alpha-helix at the junction between the myosin heads and S2, and the dependence of regulation on
52 eloped a cross-bridge model with independent myosin heads and strain-dependent interstate transition
53 ure directly affects the conformation of the myosin heads and that they need to be in a particular co
54 explore how coupled motions between the two myosin heads and the dimerization domain (S2) in smooth
55 ype filament reveals the conformation of the myosin heads and the organization of titin and MyBP-C at
57 e absence of Ca, the interaction between the myosin heads and the thin filaments was most likely the
58 he structures of thick filaments had ordered myosin heads and were distinguishable from each other by
59 a hinge in the coiled coil, allowing the two myosin 'heads' and their motor domains to interact with
60 elastic distortion of the RLC region of the myosin head, and during the subsequent rapid force recov
64 in) of around 16%, but most of the remaining myosin heads are also actin-attached even at moderate ac
66 ric contraction either less than 17 % of the myosin heads are attached to actin, or that heads can de
67 aximal shortening velocity, only 10 % of the myosin heads are attached to the thin filaments at any o
71 in label probes showed that dephosphorylated myosin heads are highly ordered in the relaxed fibers an
75 Analysis of these data suggests that two myosin heads are required to activate the thin filament.
79 n rigor (in the absence of ATP, when all the myosin heads are rigidly bound to the thin filament), a
80 that during isometric contraction 29% of the myosin heads are strongly bound to actin within the myof
81 viously suggested that the helical tracks of myosin heads are zigzagged, short diagonal ridges being
82 the analysis of interference effects between myosin head arrays in the two halves of the thick filame
83 *ATP state, the orientations of the attached myosin heads assume a wide range of azimuthal and axial
84 nergy transfer experiment confirmed that the myosin head assumes a more compact conformation in the p
85 age isometric force exerted by each attached myosin head at 5 degrees C, 4.5 pN, and the maximum slid
86 rearrangements of actin, tropomyosin and the myosin heads at different stages of actomyosin cycle in
87 rast, actin-bound caldesmon was not moved by myosin heads at low head/actin ratios, as uncovered by f
89 after rapid freezing, show binding of single myosin heads at varying angles that is largely restricte
94 and electron microscopy revealed that mutant myosin heads bear a dramatic propensity to collapse and
96 ated myosin filaments, the helically ordered myosin heads become disordered and project further from
100 own by three independent approaches to track myosin head binding to the thin filament, but is absent
101 s been shown that skeletal and smooth muscle myosin heads binding to actin results in the movement of
102 ed the largest variation indicating that the myosin head binds MgATP more tightly in the order IIA (8
106 ges, active cross-bridges are usually single myosin heads, bound preferentially to actin target zones
107 hat the azimuth of S2 origins of those rigor myosin heads, bound to the actin target zone of actively
108 rder requires the closed conformation of the myosin head but is not dependent on the hydrolysis of AT
109 We have measured the step size of individual myosin heads by fusing an enhanced green fluorescent pro
110 measured the number and position of attached myosin heads by tracing cross-bridges through the three-
112 e S1-S2 junction is necessary, such that the myosin head can bind to a nearby actin whereas the tail
113 ational results of a half sarcomere with 150 myosin heads can explain the experimentally measured for
114 alytic and lever arm domains of noncompetent myosin heads change angle on actin, whereas lever arm mo
116 sm of muscle activation in the thin filament-myosin head complex under physiological conditions.
118 termined the structure of the intact scallop myosin head, containing both the motor domain and the le
119 is possible that this pliant junction in the myosin head contributes to the compliance known to be pr
120 harp meridional reflections, signifying that myosin heads (cross-bridges) are distributed in a well-o
121 M-band (M6', M4', M1, M4 and M6) and in the myosin head crowns (P1, P2 and P3) at the M-region edges
122 The mechanism of force generation by the myosin head depends on the relationship between cross-br
124 e with the contributions from actin-attached myosin heads determines the behavior of these reflection
125 The 3.1-A x-ray structure of the scallop myosin head domain (subfragment 1) in the ADP-bound near
127 fully accounted for by the compliance of the myosin head domain, 0.38 +/- 0.06 nm pN(-1), obtained fr
129 the OFF state of the thick filament in which myosin head domains are more parallel to the filament ax
130 functional rhodamine probes on the cRLC: the myosin head domains became more perpendicular to the fil
132 is not affected by either the proportion of myosin head domains or the orientation of myosin heads.
133 ive information about axial movements of the myosin heads during contraction with sub-nanometer resol
134 2-fold change of the global dynamics of the myosin head, effected by decreasing the interactions wit
136 d structure had narrow shafts and disordered myosin heads extending at different angles from the back
137 availability of the majority fraction of the myosin heads for contraction is controlled in part by th
140 e to those of the corresponding RLC lobes in myosin head fragments bound to isolated actin filaments
141 iological; it may function to make activated myosin heads freer to contact actin filaments during mus
142 hree-dimensional structures of the truncated myosin head from Dictyostelium discoideum myosin II comp
143 the sliding velocity of actin filaments past myosin heads from 9.0 +/- 1.3 to 5.7 +/- 1.0 mum/s at 0.
144 ection (M6) and the equilibrium positions of myosin heads from the fourth myosin layer line peak posi
145 skeletal muscle can be increased by shifting myosin heads from the super-relaxed state (SRX), with a
150 ilament lattice spacing, the majority of the myosin heads have their light chain domains in IHM-like
153 e we compare the overall organization of the myosin head in these three states and show how the confo
157 in active, isometric muscle, the fraction of myosin heads in any given biochemical state is independe
158 tation of the dephosphorylated RLC region of myosin heads in cardiac muscle is primarily determined b
159 n the two lobes of the RLC to actin-attached myosin heads in muscle fibers, and suggest that such ben
161 ffect of temperature on the helical order of myosin heads in rabbit psoas muscle in the presence of n
162 onformation of the light chain domain of the myosin heads in relaxed demembranated fibers from rabbit
163 en adjacent actin binding sites and adjacent myosin heads in response to cross-bridge attachment/deta
165 only about 17 % of the concentration of the myosin heads in the fibre, suggesting that during isomet
166 te similar behavior of SH1- and SH2-modified myosin heads in the in vitro motility assays despite som
170 25 degrees C, where approximately 95% of the myosin heads in the skinned rabbit psoas muscle contain
171 viding further support for the proposal that myosin heads in the SRX are also in the interacting-head
174 ADP, induce the "closed" conformation of the myosin head (in which the gamma phosphate pocket is clos
176 n upon addition of skeletal or smooth muscle myosin heads, indicating a movement of the whole tropomy
177 cules suggests that an increased mobility of myosin heads induced by Ca2+ binding underlies the chang
179 close to the actin-binding interface of the myosin head influence actin binding and thereby modulate
180 by an asymmetric interaction between the two myosin heads, inhibiting their actin binding or ATPase a
181 We conclude that in the "off" state, scallop myosin heads interact with each other, forming a rigid s
183 ecent models suggesting a pre-cocking of the myosin head involving an enormous rotation between the l
184 eorientation of the regulatory domain of the myosin head is a feature of all current models of force
186 of rabbit shows that stiffness of the rabbit myosin head is only approximately 62% of that in frog.
187 telium myosin motor domain revealed that the myosin head is required to bend at residues Ile-455 and
188 productive blebbistatin-binding site of the myosin head is within the aqueous cavity between the nuc
189 hat upon stretch the fraction of actin-bound myosin heads is higher than during isometric contraction
190 we predict that the average number of bound myosin heads is regulated by the external force and nucl
191 ta show that a small fraction of actin-bound myosin heads is sufficient for supporting the O-state an
193 direct information about the position of the myosin head lever arm; they are, in fact, reporting rela
194 the attached A*M*ATP cross-bridges while the myosin heads maintain some degree of helical distributio
196 nique attachment configuration: the "primed" myosin heads may function as "transient struts" when att
197 Small-angle x-ray diffraction indicates that myosin heads move increasingly toward the thin filament
198 m series compliance; force drops faster when myosin heads move relative to actin during relaxation.
201 d to F-actin and simultaneously activate the myosin heads of adjacent myosin filaments at a distance
202 ange in orientation of the RLC region of the myosin heads on activation of cardiac muscle is small; t
203 ving changes in both the organisation of the myosin heads on its surface and the axial periodicity of
205 d/superrelaxed quasi-helical ordering of the myosin heads on the filament surface, whereas phosphoryl
206 n head.We have modelled the surface array of myosin heads on the filaments using as a building block
208 correlation between the conformation of the myosin heads on the surface of the thick filaments and t
209 ing of Ca(2+) to, or phosphorylation of, the myosin heads on the surface of the thick filaments.
210 of muscle involves the cyclic interaction of myosin heads on the thick filaments with actin subunits
213 racterized by helical packing of most of the myosin head or motor domains on the thick filament surfa
215 y of cross-bridge formation remains high for myosin heads originating within 8 nm axially of the targ
216 callop) filaments reveals a helical array of myosin head-pair motifs above the filament surface.
217 uction shows axial and azimuthal (no radial) myosin head perturbations within the 429-A axial repeat,
218 osin position on actin by phosphorylation of myosin heads plays a key role in the regulation of smoot
219 the actomyosin ATPase and (b) as to why the myosin head positions in phosphorylated wild-type mice a
220 e fish muscle A-band lattice relative to the myosin head positions, and that these newly observed X-r
221 into a strong, stereo-specific complex, the myosin heads push Tpm strand to the open, or O, state al
222 ine the dynamics of the proximal part of the myosin head (regulatory domain) which accompany the chan
223 rovides a measure of the distance over which myosin heads remain attached to actin as they go through
227 correlation and the biochemical state of the myosin heads required to obtain the helical array has no
230 the catalytic and regulatory domains of the myosin head (S1) is likely to be the force generating co
231 with a phosphorescent probe at C374, and the myosin head (S1) was separated into isoenzymes S1A1 and
233 of weakly (+ATP) and strongly (no ATP) bound myosin heads (S1) on the microsecond dynamics of actin l
236 nce fringes (which measures the shift of the myosin heads scattering mass towards the center of the s
237 d-flow studies suggested that strongly bound myosin head significantly increased the Ca2+ sensitivity
238 This appears to ensure proper folding of myosin heads so that they can perform their ATP-dependen
239 ion results showed a 1.0 to 1.5% increase in myosin head spacing with activation; however, this incre
241 similar to those in frog, while the average myosin head stiffness of dogfish (1.98 +/- 0.31 pN nm(-1
243 s actin movement against the viscous drag of myosin heads strongly bound to actin (Hill's dashpot).
248 the domains bind to distinct subsites on the myosin head, suggesting distinct roles in forming the my
250 erturb the orientations of the population of myosin heads that are attached to actin, and thereby cha
251 pling of regulated binding sites and cycling myosin heads that are induced by interfilamentary moveme
252 tential for interaction between troponin and myosin heads that bind near it along the thin filament r
253 of wild type, supporting the hypothesis that myosin heads that lack phosphorylated RLC remain close t
254 conclude that the loosening of the array of myosin heads that occurs on activation is real and physi
255 chanical characteristics of myofilaments and myosin heads that underpin refined models of the acto-my
256 ions with the filament surface (or the other myosin head), the coupling of the intradomain dynamics r
257 Analysis of the interactions between the myosin heads, the cardiac isoform of myosin-binding prot
258 ucture, and function (ATPase motor) to other myosin heads, the organization of the tail has been less
259 the filament and the degree of order of the myosin heads, thick filaments isolated from a control gr
261 presence of both Ca2+ and strong binding of myosin head to actin was required to achieve a fully ope
264 n and the slow rate of ADP release helps the myosin head to remain attached to actin for a large frac
270 of muscle contraction the initial binding of myosin heads to the actin thin filament contributes to s
271 red here correlates well with the binding of myosin heads to the core of the thick filament in a stru
272 gment 2 (S2), the segment that links the two myosin heads to the thick filament backbone, may serve a
273 ructural studies to stabilize the binding of myosin heads to the thick filament, and here we have uti
275 a complementary role in moving and orienting myosin heads toward actin target sites, thereby increasi
279 actin and myosin and between residues of the myosin head underlies the mechanism of force generation.
281 hanical characteristics of the filaments and myosin heads vary in muscles of different animals we app
282 maximum axial movement of the distal part of myosin head was modeled using FRET distance changes with
284 ra density, reflecting weakly bound, cycling myosin heads, was also detected, on the extreme peripher
285 eature approximately the size and shape of a myosin head.We have modelled the surface array of myosin
286 he inner domain of actin, and strongly bound myosin heads were now observed over the junction of the
287 he mutation decreased also the amount of the myosin heads which bound strongly to actin at high Ca(2+
288 moves tropomyosin in one direction, whereas myosin heads, which enhance potentiation, move tropomyos
291 oth the UCS and the Central domains bind the myosin head with high affinity, only the UCS domain disp
295 These results imply that the interaction of myosin heads with actin within an intact sarcomere chang
296 are close to those expected for actin-bound myosin heads with their light chain domains in a pre-pow
298 ults and examine the fraction of actin-bound myosin heads within the myofilament lattice during calci
299 tric force is a larger fraction of the total myosin head working stroke in the dogfish than in the fr
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