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1 r characterized myosins (e.g., myosin-II and myosin-V).
2 grain structure of the dimeric, linear motor myosin V.
3 ead promotes highly selective and processive myosin V.
4 ein independently of its putative linkage to myosin V.
5 n intensity when bound to the active site of myosin V.
6 consistent with a 37-nm forward step size of myosin V.
7 IQ4, allowed building a model of the LCBD of myosin V.
8 he transport of multiple distinct cargoes by myosin V.
9 is essential for processive myosins, such as myosin V.
10 n, regulation, and molecular interactions of myosin V.
11 We also used SHREC to study the motion of myosin V.
12 he leading lever arm in the waiting state of myosin V.
13 increase the degree of processive motion of myosin V.
14 processive motor from the myosin superfamily myosin V.
15 DdMII), and nonmuscle myosin IIA, as well as myosin V.
16 tch II with the gamma phosphate of ATP, into myosin V.
17 changes in the force-generating lever arm in myosin V.
18 ormational changes at the nucleotide site of myosin V.
19 and contrast the motility of myosin-VI with myosin-V.
20 and cytoplasmic dynein, and an actin motor, myosin-V.
21 ermined by competition between kinesin-1 and myosin-V.
22 sity but was not affected by the presence of myosin-V.
25 icted Cdk1 sites in other organelle-specific myosin V adaptors suggests that the inheritance of other
29 rate of the hydrolysis step (myosin V-ATP-->myosin V-ADP-Pi) were all approximately 10-fold slower i
32 itching can be tuned via combinations of 1-4 myosin V and 1-4 dynein-dynactin engaged motors through
33 nalyzing the properties of chimeras of mouse myosin V and a non-processive class V myosin from yeast
34 Time courses of MgmantADP dissociation from myosin V and actomyosin V are biphasic with fast observe
35 The [Mg(2+)] dependence of ADP binding to myosin V and actomyosin V was measured from the fluoresc
37 ch transcribes varying DNA sequences, and to myosin V and cytoplasmic dynein, which may advance by va
41 ar to or slightly faster in S217A than in WT myosin V and mechanochemical gating of the rates of diss
43 ell short of the 36-nm step-size observed in myosin V and myosin VI that corresponds to the actin pse
44 developing photoreceptors and asked here if myosin V and the Drosophila Rab11 interacting protein, d
45 ectly observe Smy1-3GFP being transported by myosin V and transiently pausing at the neck in a manner
46 8-A cryoEM reconstruction of this state for myosin V and used molecular dynamics flexed fitting for
48 ectory, shapes for scaffolds containing both myosin V and VI are dominated by the myosin with a stiff
53 two-dimensional actin-myosin interface using myosin V and VI precisely patterned on DNA nanostructure
57 myosin and formin) and membrane trafficking (myosin-V and exocyst) were dynamic during cytokinesis.
58 lated protein can function intimately with a myosin-V and its receptor in the transport of a specific
59 ral studies show several differences between myosin-V and VI, including a significant difference in t
61 approximately 8-10 times slower than that of myosin V, and its step size is 30 nm, which is consisten
62 transition, and the processive run length of myosin V, and thus, it is important to understand how ca
63 al dwell-time distributions of single-headed myosin V, and were able to use a single kinetic scheme t
67 have shown how the structure and kinetics of myosin V are specialized to produce a highly processive
69 cule experiments indicate that myosin-VI and myosin-V are processive molecular motors, but travel tow
70 tubule motor, kinesin-1, and an actin motor, myosin-V, are essential for osk mRNA posterior localizat
72 -ADP-Pi and the rate of the hydrolysis step (myosin V-ATP-->myosin V-ADP-Pi) were all approximately 1
73 re dependence of the maximum actin-activated myosin V ATPase rate is similar to the pocket opening st
75 ze the central position of the CR and resist myosin V-based forces to promote the fidelity of cell di
77 ion is not as robust as that of kinesin-1 or myosin-V because dynein moves only a limited distance (a
78 alog increases when the MV.SLADP complex (MV=myosin V) binds to actin, implying an opening of the act
80 n XI shares a similar structure with that of myosin V, but has evolved plant-specific cargo binding m
81 e studied the structural dynamics of chicken myosin V by combining the localization power of fluoresc
82 ch actin accelerates the release of ADP from myosin V by reducing the magnesium affinity of a myosin
83 the dynamics of the actin binding region of myosin V by using fluorescence resonance energy transfer
84 onal perturbation of the switch 1 structure, myosin V can be converted into a low duty ratio motor th
85 The kinetics of detachment indicate that myosin V can detach from actin at two distinct points in
86 The enzymatic and mechanical functions of myosin V can, therefore, be modulated both by calcium-de
92 he upper 50-kDa domain (residues 292-297) of myosin V containing a single IQ domain (MV 1IQ), allowin
93 the result of the energetics of the complete myosin-V cycle and is not the source of directional moti
94 with simulations and is applied to in vitro myosin V data where a small 10 nm population of steps is
96 Direct measurements of phosphate release in myosin V demonstrate that Mg(2+) reduces actin affinity
97 Our comparison between vertebrate and fly myosin V demonstrates that the well preserved function o
99 a critical step in the spatial regulation of myosin V-dependent organelle transport and may reveal co
100 I-dependent), contractile vacuole activity (myosin V-dependent), and phagocytosis (myosin VII-depend
103 tes the processive run length of full-length myosin V (dFull) and a truncated dimeric construct (dHMM
107 cular interactions including the motion of a myosin-V dimer "walking" on an actin fibre, RNA stem-loo
108 gation complex") and one with kinesin II and myosin V ("dispersion complex"), and that the removal of
111 There are three distinct members of the myosin V family in vertebrates, and each isoform is invo
112 een unknown as to whether all members of the myosin V family share a common, evolutionarily conserved
116 ed to correspondingly change the affinity of myosin V for actin in the weak binding state, without ch
117 long microtubules and then shifts control to myosin V for delivery on actin filaments to the cell mem
131 cultured Xenopus melanophores is mediated by myosin V, heterotrimeric kinesin-2, and cytoplasmic dyne
132 te of product release from the double-headed myosin V-HMM using a new ATP analogue, 3'-(7-diethylamin
133 tion strategy halting growth by immobilizing myosin V in a newly described state on selectively stabi
135 reconstructions provide the atomic models of myosin V in both weak and strong actin bound states.
137 Thus, spatial and temporal regulation of myosin V in vivo by a head-to-tail interaction is critic
139 strong support for a straight-neck model of myosin V in which the lever arm of the leading head is t
140 Here we define the in vivo delivery cycle of myosin-V in its essential function of secretory vesicle
150 These data demonstrate that the step-size of myosin V is affected by the length of its neck and is no
155 of chemical energy to directional motion in myosin V is examined by careful simulations that include
170 tionality of the motor core, we attached the myosin V lever arm to myosin VI, with and without the un
171 myosin VI lever arm for the relatively rigid myosin V lever increases trajectory skewness, and vice v
179 ws, our results show that the two heads of a myosin V molecule communicate, not through any one mecha
180 d constructs reveal that a single Drosophila myosin V molecule spends most of its mechanochemical cyc
181 s approach, the individual heads of a single myosin V molecule were observed taking 72-nm steps as th
182 forward or backward force on a single-headed myosin V molecule, hypothesized to simulate forces exper
184 y to study the structural dynamics of single myosin V molecules that had been labeled with bifunction
185 s at the molecular level, we observed single myosin V molecules that were differentially labeled with
186 this coordination, processive runs of single myosin V molecules were perturbed by varying nucleotide
188 is mediated by interaction between the yeast myosin V motor Myo2 and organelle-specific adaptors.
193 -EPSC was via a mechanism dependent on actin/myosin V motor-based transport of AMPA receptors, which
197 Here we report how Spir actin nucleators and myosin V motors coordinate their specific membrane recru
198 hermore, we also see different velocities of myosin V motors in central regions of S2 cells, suggesti
199 nstrates that the well preserved function of myosin V motors in cytoplasmic transport can be accompli
201 tethering multiple myosin VI motors, but not myosin V motors, modifies their movement trajectories on
202 ontrast, tethering myosin VI motors, but not myosin V motors, progressively straightens the trajector
205 We investigate how the combined system of myosin-V motors plus actin filaments is used to transpor
206 udies have shown that melanosomes carried by myosin V move 35 nm in a stepwise fashion in which the s
211 of elevated levels to suppress a conditional myosin-V mutation (myo2-66), but its function with Myo2
212 f cells in late anaphase bearing exocyst and myosin V mutations show that both vesicle transport and
213 ated by binding a secretory vesicle and that myosin-V mutations that compromise vesicle binding rende
217 releases yeast vacuoles and peroxisomes from myosin V (Myo2) and terminates organelle transport from
219 min) depletes ATP levels and that the yeast myosin V, Myo2, responds by relocalizing to actin cables
222 hondrial inheritance: Arp2/3 complex and the myosin V Myo2p (together with its Rab-like binding partn
223 ted and characterized mutations in the yeast myosin V Myo2p to reveal that it is regulated by a head-
229 of an unconventional myosin-II (Myp2) and a myosin-V (Myo51) that are also present in the contractil
231 k suggested, however, that the fission yeast myosin-V (Myo52p) is a nonprocessive motor whose activit
237 e present a kinetic model for the walking of myosin V on actin under conditions of zero external forc
239 hat most secretory vesicles are delivered by myosin-V on linear actin cables in fission yeast cytokin
240 ow that, at realistic concentrations of ATP, myosin-V operates in the regime which maximizes motor ve
241 that Rab11 and the associated motor protein Myosin V play essential roles in both endogenous and ect
242 e eGFPs, confirm the hand-over-hand model of myosin V procession, and when combined with previous dat
243 an example, we consider the case of a single myosin-V protein transporting a cargo and show that, at
246 ted two mutations in the converter domain of myosin V (R712G and F750L) to examine how altering speci
248 ro motility assays, double-headed Drosophila myosin V requires high surface concentrations to exhibit
249 r in the S217A mutant than in wild type (WT) myosin V, resulting in a slower steady-state rate of bas
252 of the hand-over-hand model, thus confirming myosin V's mode of walking along an actin filament.
255 elease rate constant is reduced by Mg(2+) in myosin V, smooth muscle myosin, nonmuscle myosin IIA, CM
256 y using a dominant negative approach against myosin V, spine synapses became stronger compared to con
259 support a model in which the coordination of myosin V stepping is mediated by strain-generated inhibi
263 myosin Va than for nonprocessive Drosophila myosin V, suggesting that this elastic tether between th
264 sfer studies confirmed that Rab10 binding to myosin V tails in vivo required the alternatively splice
266 ning which of the several potential pathways myosin V takes in the process of ADP release and how act
268 tein complex containing actinin-4, BERP, and myosin V that is necessary for efficient TfR recycling b
276 the duty ratio from approximately 0.85 in WT myosin V to approximately 0.25 in S217A and produces a m
278 s or IAEDANS-labeled actin and FlAsH-labeled myosin V to examine the conformation of the nucleotide-
279 actin allows the detached head of a stepping myosin V to find its next actin binding site more quickl
280 main-swapping approach with the nonselective myosin V to identify the selectivity module of myosin X.
283 elements of myosin V work together to allow myosin V to step along actin for multiple ATPase cycles
284 ese data, we infer that P(i) release commits myosin V to undergo a highly load-dependent transition f
285 e test whether this feature is essential for myosin V to walk processively along an actin filament.
292 Single molecule experiments revealed that myosin-V walks in a stepwise fashion with occasional bac
294 tural changes associated with ADP release in myosin V, which is thought to be a strain-sensitive step
295 iple motors including kinesin-2, dynein, and myosin-V, which drive switching between microtubules and
297 uggest that PTC1 promotes the association of myosin-V with its organelle-specific adaptor proteins.
298 ndings reveal how the structural elements of myosin V work together to allow myosin V to step along a
299 ng FIRST/FRODA starting with three different myosin V X-ray crystal structures to examine intrinsic f
300 st motor domain on the neck and rod of mouse myosin V (Y-MD) showed longer run lengths than mouse wil