ライフサイエンスコーパス: myosin rod

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1 ents where it is likely to interact with the myosin rod.

2 vidence suggesting it is associated with the myosin rod.

3 between components of the two heads and the myosin rod.

4 myosin heads interact with a segment of the myosin rod.

5 nd (3) an alternative tail at the end of the myosin rod.

6 he difference in tightness of packing of the myosin rods.

7 ized fragment of the scallop striated-muscle myosin rod adjacent to the head-rod junction.

8 re that corresponds well to the pitch of the myosin rod alpha-helix along the thick filament axis.

9 ead and these processes are regulated by the myosin rod and tailpiece.

10 d is different from those of skeletal muscle myosin rod and tropomyosin, for which non-two-state ther

11 nus with the light meromyosin section of the myosin rod and with titin.

12 ken gizzard alpha-calponin co-sediments with myosin rod and, to a lesser extent, with light meromyosi

13 1776 residue occupies a core position in the myosin rod at which the substitution of glycine is extre

14 est the hypothesis that perturbations in the myosin rod can disturb normal sarcomeric uniformity and,

15 so fit well to the [ATP] dependence of V for myosin-rod cofilaments at three fixed N.

16 Taken together, these data indicate that myosin rod domains are the key structures giving SHG fro

17 Using the coding sequence for the myosin rod domains as a molecular clock, we estimate tha

18 orylation may reinforce interactions between myosin rod domains, enhance thick filament connections t

19 carboxy terminus of an assembly-incompetent myosin rod fragment.

20 Two CaP binding sites on smooth muscle myosin rod have been recently described.

21 ther an embryonic or an adult isoform of the myosin rod in their indirect flight muscles.

22 To examine the role of the myosin rod in this process, we determined the minimal si

23 athy, the mechanism whereby mutations in the myosin rod influences mechanical function is less clear.

24 Thick filaments assemble when the myosin rod is expressed in mutant indirect flight muscle

25 77), the C-terminal proteolytic peptide from myosin rod, is a 900 A coiled-coil that contains two pai

26 the sequence that encodes the alpha-helical myosin rod, is extremely low.

27 Hinge B was previously shown to increase myosin rod length, increase A-band and sarcomere length,

28 anner consistent with this region increasing myosin rod length.

29 residues in the heptad repeat of the mutant myosin rods likely alters interactions that stabilize co

30 These results suggest that the myosin rod mediates specific interactions with the head

31 Our imaging results indicate that myosin rod mutations likely disturb production and/or pr

32 in the light meromyosin (LMM) region of the myosin rod, nor would these be expected to directly affe

33 4 residues and the coiled-coil domain of the myosin rod of 1086 residues).

34 Myosin rod protein (MRP) is a naturally occurring 155 kD

35 Myosin rod protein (MRP), a 155 kDa protein encoded by a

36 e effects of four MYH9-like mutations in the myosin rod-R1171C, D1430N, D1847K and R1939X-which occur

37 due repeat and the 7-residue repeat found in myosin rod sequence, both myosin mutants showed a stable

38 bly, segments of the human fast IId skeletal myosin rod were expressed in Escherichia coli and examin

39 on two criteria, the tightness of packing of myosin rods within the backbone of the filament and the

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