ライフサイエンスコーパス: myristoylated alanine-rich C kinase substrate

1 cific subunits of AMPA or NMDA receptors and myristoylated alanine-rich C kinase substrate).

2 imilar to the phosphorylation site domain of myristoylated alanine-rich C kinase substrate, a conserv

3 C) activity and of phosphorylated (inactive) myristoylated alanine-rich C-kinase substrate, a PKC tar

4 DeltaDAKAP200 appears to be a myristoylated alanine-rich C kinase substrate analog.

5 The release of phosphorylated myristoylated alanine-rich C kinase substrate and its su

6 mbrane and calmodulin binding domains of the myristoylated alanine-rich C kinase substrate and neurom

7 ral biologically important peripheral (e.g., myristoylated alanine-rich C kinase substrate) and integ

8 porters, actin binding proteins (radixin and myristoylated alanine-rich C kinase substrate), and Rab

9 ortant regulatory molecules as Raf-1 kinase, myristoylated alanine-rich C kinase substrate, and SOS.

10 the major protein kinase C substrate MARCKS (myristoylated alanine-rich C kinase substrate) as a pote

11 We show that phosphorylation of myristoylated alanine-rich C kinase substrate by membran

12 Strikingly, the lipid ligand MED (myristoylated alanine-rich C kinase substrate effector d

13 We investigated the role of MARCKS (myristoylated, alanine-rich C-kinase substrate) in dendr

14 The MARCKS protein (myristoylated alanine-rich C kinase substrate) is an act

15 MARCKS (myristoylated alanine-rich C-kinase substrate) is a majo

16 We report here that macrophage-enriched myristoylated alanine-rich C kinase substrate (MacMARCKS

17 he protein kinase C substrate domains of the myristoylated alanine rich C kinase substrate (MARCKS) a

18 , and protein kinase C binding domain of the myristoylated alanine rich C kinase substrate (MARCKS) w

19 switch that controls membrane binding of the myristoylated alanine-rich C kinase substrate (MARCKS) [

20 Here, we identify myristoylated alanine-rich C kinase substrate (MARCKS) a

21 ased phosphorylations of PKC at Thr(514) and myristoylated alanine-rich C kinase substrate (MARCKS) a

22 The myristoylated alanine-rich C kinase substrate (MARCKS) a

23 Ca(2+)-PKC) is hypothesized to phosphorylate myristoylated alanine-rich C kinase substrate (MARCKS) a

24 basic (+13), unstructured effector domain of myristoylated alanine-rich C kinase substrate (MARCKS) b

25 Myristoylated alanine-rich C kinase substrate (MARCKS) i

26 Myristoylated alanine-rich C kinase substrate (MARCKS) i

27 Myristoylated alanine-rich C kinase substrate (MARCKS) i

28 Direct evidence is provided that the myristoylated alanine-rich C kinase substrate (MARCKS) i

29 The myristoylated alanine-rich C kinase substrate (MARCKS) i

30 pe and phosphorylation and redistribution of myristoylated alanine-rich C kinase substrate (MARCKS) i

31 The myristoylated alanine-rich C kinase substrate (MARCKS) i

32 ions of membrane-associated proteins such as myristoylated alanine-rich C kinase substrate (MARCKS) m

33 The present study reveals that myristoylated alanine-rich C kinase substrate (MARCKS) p

34 al studies by Gay et al. demonstrated that a myristoylated alanine-rich C kinase substrate (MARCKS) p

35 utrophil elastase-induced phosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS) p

36 eviously that a peptide corresponding to the myristoylated alanine-rich C kinase substrate (MARCKS) p

37 Membrane binding of the myristoylated alanine-rich C kinase substrate (MARCKS) r

38 corresponding to the effector region of the myristoylated alanine-rich C kinase substrate (MARCKS) s

39 ptide comprising the effector domain (ED) of myristoylated alanine-rich C kinase substrate (MARCKS) w

40 Myristoylated Alanine-Rich C Kinase Substrate (MARCKS),

41 We previously found the myristoylated alanine-rich C kinase substrate (MARCKS),

42 uggest that the basic effector domain of the myristoylated alanine-rich C kinase substrate (MARCKS),

43 The basic effector domain of myristoylated alanine-rich C kinase substrate (MARCKS),

44 egulating the cellular concentrations of the myristoylated alanine-rich C kinase substrate (MARCKS),

45 ein with subunits containing a COOH-terminal myristoylated alanine-rich C kinase substrate (MARCKS)-r

46 MacMARCKS (also known as myristoylated alanine-rich C kinase substrate (MARCKS)-r

47 lable 12 amino acid peptide derived from the myristoylated alanine-rich C kinase substrate (MARCKS-PS

48 next identified that the phosphorylation of Myristoylated alanine-rich C-kinase substrate (MARCKS) a

49 Here, we identify the actin-binding protein myristoylated alanine-rich C-kinase substrate (MARCKS) a

50 Myristoylated alanine-rich C-kinase substrate (MARCKS) a

51 from the lipid binding domain of the protein myristoylated alanine-rich C-kinase substrate (MARCKS) b

52 two actin-associated proteins, myosin II and myristoylated alanine-rich C-kinase substrate (MARCKS) i

53 Because PKCalpha can phosphorylate the myristoylated alanine-rich C-kinase substrate (MARCKS) m

54 tide derived from the effector domain of the myristoylated alanine-rich C-kinase substrate (MARCKS) p

55 crease in a poorly-characterized MK protein, myristoylated alanine-rich C-kinase substrate (MARCKS),

56 The effector domain of the myristoylated alanine-rich C-kinase substrate (MARCKS-ED

57 The effector domain of myristoylated alanine-rich C-kinase substrate (MARCKS-ED

58 e ubiquitinated after rapid preconditioning: myristoylated, alanine-rich C-kinase substrate (MARCKS)

59 and that the major PKC epsilon target is the myristoylated, alanine-rich C-kinase substrate (MARCKS).

60 The myristoylated alanine-rich C kinase substrate, or MARCKS

61 Mice lacking the myristoylated alanine-rich C-kinase substrate, or MARCKS

62 Phosphorylation of myristoylated alanine-rich C kinase substrate (phospho-M

63 PKC-dependent myristoylated alanine-rich C kinase substrate phosphoryl

64 pears to be the detachment of phosphorylated myristoylated alanine-rich C kinase substrate (pMARCKS)

65 st that DeltaDAKAP200 is a new member of the myristoylated alanine-rich C kinase substrate protein fa

66 lly mobile, chimeric A kinase anchor protein-myristoylated alanine-rich C kinase substrate protein th

67 s determined by translocation of eGFP-tagged myristoylated alanine-rich C kinase substrate protein) r

68 eoxybalanol, inhibits phosphorylation of the myristoylated alanine-rich C kinase substrate protein, a

69 Here, we demonstrate in mice that the myristoylated alanine-rich C-kinase substrate protein (M

70 al phosphorylation site domain of vertebrate myristoylated alanine-rich C kinase substrate proteins.

71 We could demonstrate that Lck and myristoylated alanine-rich C kinase substrate, two main

72 Consequently, phosphorylation of myristoylated alanine-rich C kinase substrate was decrea