It is thought that each myosin head functions as a contractile machinery unit, because each head shows ATPase activity and binds to F-actin. A still unsolved question is whether or not the two heads of a myosin molecule interact with each other during their cyclic interaction with F-actin. ...
During a part of the hydrolytic cycle, myosin head (S1) carries no nucleotide and binds strongly to an actin filament forming a rigor bond. At saturating concentration of S1 in rigor, S1 is well known to form 1:1 complex with actin. However, we have provided evidence that under certain ...
mixing in stopped flow apparatus directly demonstrated that myosin head initially binds through the loop 635-647 to the N-terminus of one actin and then through the loop 567-574 to the N-terminus of the second actin (Andreev {\&} Reshetnyak, 2007, J. Mol. Biol. 365(3), 551-554). ...
In vitro under unloaded conditions, a single myosin molecule is capable of executing a power stroke on actin filament as force generated by a single head is greater than the drag experienced by the actin filament. For a low duty molecular motor such as myosin II, it has been a longstanding...
We have shown that vesicles in the axoplasm of the squid giant axon move on actin filaments and that movement is inhibited by myosin V-specific antibodies ... BJ Molyneaux,MK Mulcahey,P Stafford,... - 《Cell Motility & the Cytoskeleton》 被引量: 36发表: 2010年 Head-to-tail regulation is...
Single-headed myosin S-1 binds to actin at a given angle relative to the actin filament. The bound single head (both motor and neck domains) often extends towards the plus end of actin at least in the nucleotide-free and ADP-bound conditions (Rayment et al.1993b; Jontes et al.1995)....
actin and the actin nucleation complex Arp2/3. We found that myosin 1b controls the formation of secretory granules and the associated regulated secretion in both neuroendocrine cells and chromogranin A-expressing COS7 cells used as a simplified model of induced secretion. We show that F-actin ...
Interestingly, the tail domain markedly inhibits the actin-activated ATPase activity of tailless DM7A at low Ca but not high Ca. By examining various deletion constructs, we found that deletion of the distal IQ domain, the C-terminal region of the tail, and the N-terminal region of the ...
The glutaraldehyde-induced cross-linking of the F-actin-myosin head (S1) complex, previously described [Bertrand et al. (1988) Biochemistry 27, 5728-5736], was investigated in the presence of tropomyosin (Tm) alone or associated with troponin (Tn), at a Tm-Tn/actin/S1 molar ratio of 1:...
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