ライフサイエンスコーパス: myosin A

1 of the cell and is present in a complex with myosin A.

2 H Plasmodium falciparum MTIP in complex with Myosin A adopts a compact conformation, with its two dom

3 ence and immunoelectron microscopy show that myosins A and B are scrambled, in contrast to their asse

4 tagenesis studies show that H810 and K813 of Myosin A are key players in the formation of the compact

5 A short peptide derived from the tail of myosin A (C-MyoA) bound to MTIP and was able to disrupt

6 involved in motility (myosin light chain 1, myosin A), cell morphology (PhIL1), and host cell invasi

7 m expresses a simple complement of MyTH/FERM myosins, a class VII (M7) myosin required for cell-subst

8 ies to MTIP were used to immobilise the MTIP-myosin A complex, allowing actin binding and motility to

9 players in the formation of the compact MTIP:Myosin A complex.

10 actors necessary for the complete folding of myosin, a cytoplasmic extract was prepared from myotubes

11 ed by fourfold to sixfold, whereas nonmuscle myosin A decreased to 30% of control.

12 They had abundant vimentin filaments but no myosin, a discontinuous basal lamina, sparse rough endop

13 ain of caldesmon binds to the neck region of myosin, a dissociated NH2 domain may account for caldesm

14 the src-homology 3 (SH3) domain in class II myosins, a distinct beta-barrel structure, remains unkno

15 Here, we show that class I myosins, a family of membrane-binding, actin-based motor

16 rved two lifetimes for nucleotide release by myosin: a fast component with a lifetime of approximatel

17 nately affect the mechanics of double-headed myosin, a finding relevant to our understanding of heter

18 sins, a second member of the class III/ninaC myosins, a gene similar to the class XV deafness myosin,

19 gene, is one member of the mammalian class I myosins, a group of small, calmodulin-binding mechanoche

20 Only the unprotonated state of Myosin A-H810 is compatible with the compact complex.

21 Toxoplasma gondii myosin A has been implicated in this process, but direct

22 Cardiac myosin, a heart autoantigen, induced experimental autoim

23 A complex containing the myosin-A heavy chain, a myosin light chain, and the acce

24 able to disrupt the association of MTIP and myosin A in parasite lysates.

25 ptidomimetic compounds that disrupt the MTIP-myosin A interaction are predicted to inhibit parasite m

26 prevent a compact conformation of MTIP with Myosin A, it actually appears to be essential for the fo

27 Most surprisingly, every side-chain atom of Myosin A-K813 is engaged in contacts with MTIP.

28 Myosins, a large family of actin-based motors, have one

29 ecreased the actin-translocating activity of myosin a little, but the phosphorylation-dependent regul

30 calcium-troponin (Ca-Tn) binding or by actin-myosin (A-M) strong binding.

31 , but was not required for the expression of myosin, a marker of differentiation.

32 include the heavy chain of myosin-Va (dilute myosin), a motor protein thought to be involved in vesic

33 Nonmuscle myosin A mRNA decreased to 50% of control after 3 hours

34 e interaction between the C-terminal tail of myosin A (MyoA) and its light chain, myosin A tail domai

35 Myosin A (MyoA) is a Class XIV myosin implicated in glid

36 Myosin A (MyoA), the other class XIV myosin in Plasmodiu

37 ring precursor nodes containing formins and myosin, a new study shows that formin-mediated polymeriz

38 s a 23-kDa isoform of one of the subunits of myosin, a protein involved in muscle contraction.

39 he capture and pulling of actin filaments by myosin, a result that has broad implications for cellula

40 ment of actin filament velocities powered by myosin A revealed a velocity of 3.51 microm s(-1), a spe

41 myosins-I, three new class II (conventional) myosins, a second member of the class III/ninaC myosins,

42 1 reduced the S100A4 inhibition of nonmuscle myosin A self-association and phosphorylation in vitro.

43 ate that unlike any previously characterized myosin a single-headed myosin V spends most of its kinet

44 tail of myosin A (MyoA) and its light chain, myosin A tail domain interacting protein (MTIP), is an e

45 o substrates of Plasmodium falciparum CDPK1: myosin A tail domain-interacting protein (MTIP) and glid

46 ex proteins, including the MyoA light chain, myosin A tail domain-interacting protein (MTIP).

47 The MTIP-myosin A tail interaction has a Kd of 235 nM and calcium

48 h its two domains completely surrounding the Myosin A-tail helix, dramatically different from previou

49 The Myosin A-tail interacting protein (MTIP) of the malaria

50 Toxoplasma gondii myosin-A (TgM-A) is a remarkably small approximately 93

51 of the class XIVa family, Toxoplasma gondii myosin A (TgMyoA), is a monomeric unconventional myosin

52 in SM-1 was enhanced 10-fold, and nonmuscle myosin A was reduced to 40% of control.

53 rally and immunologically similar to cardiac myosin, a well-known mediator of inflammatory heart dise