ライフサイエンスコーパス: gamma-carboxyglutamic acid

1 II), and by a decreased urinary excretion of gamma-carboxyglutamic acid.

2 e concomitant conversion of glutamic acid to gamma-carboxyglutamic acid.

3 itamin K-dependent carboxylation to generate gamma-carboxyglutamic acid.

4 translational conversion of glutamic acid to gamma-carboxyglutamic acid, an amino acid critical to th

5 fully carboxylated as demonstrated by direct gamma-carboxyglutamic acid analysis of the alkaline hydr

6 alcin (ucOC)], plasma phylloquinone, urinary gamma-carboxyglutamic acid, and plasma undercarboxylated

7 The vitamin K-dependent biosynthesis of gamma-carboxyglutamic acid appears to be a highly conser

8 ulation and regulatory proteins that contain gamma-carboxyglutamic acid are a part of a unique class

9 n underestimate of the true contributions of gamma-carboxyglutamic acid at these positions.

10 Upon binding of Ca2+ to gamma-carboxyglutamic acid, conantokin G undergoes a con

11 Conantokin G is a gamma-carboxyglutamic acid-containing conotoxin from the

12 The removal of the gamma-carboxyglutamic acid-containing domain from the fX

13 s transmembrane proteins with amino-terminal gamma-carboxyglutamic acid-containing domains preceded b

14 ions, Ca2+, Mg2+, and Zn2+, to the synthetic gamma-carboxyglutamic acid-containing neuroactive peptid

15 cation, characterization, and structure of a gamma-carboxyglutamic acid-containing peptide, conotoxin

16 ylation system that converts the proteins to gamma-carboxyglutamic acid-containing proteins.

17 its structure to other conotoxins and to the gamma-carboxyglutamic acid-containing regions of the vit

18 sma (IXNP); each protein had the same Mr and gamma-carboxyglutamic acid content.

19 Urinary gamma-carboxyglutamic acid did not change in response to

20 e amino-terminus of the Ca(2+)-bound form of gamma-carboxyglutamic acid domain (GD) of human protein

21 I, we expressed wild-type PZ, PZ lacking the gamma-carboxyglutamic acid domain (GD-PZ), and a chimeri

22 The effect of replacing the gamma-carboxyglutamic acid domain of activated protein C

23 Deletion of the gamma-carboxyglutamic acid domain of APC, a region criti

24 s like PC/PS vesicles bind to the N-terminal gamma-carboxyglutamic acid domain of APC, and that one m

25 ally inactive and lacks the membrane-binding gamma-carboxyglutamic acid domain of native fXa but reta

26 nic PF4 to the anionic, vitamin K- dependent gamma-carboxyglutamic acid domain of protein C.

27 The gamma-carboxyglutamic acid domain substitution therefore

28 constants (Ki) toward a factor IX propeptide/gamma-carboxyglutamic acid domain substrate.

29 d mutagenesis of the 40 N-terminal residues (gamma-carboxyglutamic acid domain) of blood clotting fac

30 Each protein contains an N-terminal gamma-carboxyglutamic acid domain, followed by EGF1 and

31 ates of the protein C derivative lacking the gamma-carboxyglutamic acid domain, which is required for

32 Unlike the gamma-carboxyglutamic acid domain-containing proteins of

33 tructure of NAP5 bound at the active site of gamma-carboxyglutamic acid domainless factor Xa (des-fXa

34 -and-tight ligand of the exosites of FXa and gamma-carboxyglutamic acid domainless FXa (des-Gla-FXa),

35 e have constructed a protein C mutant in the gamma-carboxyglutamic acid-domainless form in which the

36 teocalcin, plasma phylloquinone, and urinary gamma-carboxyglutamic acid excretion appear to be sensit

37 n, we report the synthesis of N-alpha-Fmoc-L-gamma-carboxyglutamic acid gamma,gamma'-tert-butyl ester

38 inhibitors of mineralization, such as matrix gamma-carboxyglutamic acid Gla protein, fetuin, and oste

39 The missing gamma-carboxyglutamic acid (GLA) and part of epidermal g

40 e carboxylation of glutamic acid residues to gamma-carboxyglutamic acid (Gla) by the vitamin K-depend

41 he independent importance of the propeptide, gamma-carboxyglutamic acid (Gla) domain and elements bey

42 ey are bound, multiple glutamic acids in the gamma-carboxyglutamic acid (Gla) domain are carboxylated

43 First, the gamma-carboxyglutamic acid (Gla) domain binds C6PS only

44 stimulatory effect requires presence of the gamma-carboxyglutamic acid (Gla) domain in protein C and

45 uivalent in terms of the manner in which the gamma-carboxyglutamic acid (Gla) domain of each protein

46 The glutamic acid-rich gamma-carboxyglutamic acid (Gla) domain of factor IX is

47 othelial cells and that its occupancy by the gamma-carboxyglutamic acid (Gla) domain of protein C/APC

48 Residue K5 in factor IX gamma-carboxyglutamic acid (Gla) domain participates in

49 +)), have three of seven Ca(2+) sites in the gamma-carboxyglutamic acid (Gla) domain replaced by Mg(2

50 hain of factor X consists of an NH2-terminal gamma-carboxyglutamic acid (Gla) domain, followed by a f

51 loop Lys159-Lys165, are near the factor VIIa gamma-carboxyglutamic acid (Gla) domain, suggesting that

52 Factor VIIa (FVIIa) consists of a gamma-carboxyglutamic acid (Gla) domain, two epidermal g

53 helial protein C receptor (EPCR) through its gamma-carboxyglutamic acid (Gla) domain, with unknown he

54 Four of these encode gamma-carboxyglutamic acid (Gla) domain-containing prote

55 (PC) rely on the presence of the N-terminal gamma-carboxyglutamic acid (Gla) domain.

56 acids (G4-Q11) exposed on the surface of the gamma-carboxyglutamic acid (Gla) domain.

57 ranes containing phosphatidylserine (PS) via gamma-carboxyglutamic acid (Gla) domains is one of the e

58 nhanced function requires interaction of the gamma-carboxyglutamic acid (Gla) domains of factor IXa a

59 To assess the role of gamma-carboxyglutamic acid (Gla) domains of FX and FIX i

60 ranes containing phosphatidylserine (PS) via gamma-carboxyglutamic acid (Gla) domains.

61 mic acids on these proteins are converted to gamma-carboxyglutamic acid (Gla) in a reaction that requ

62 rage tumor acidity, and replacing Asp14 with gamma-carboxyglutamic acid (Gla) increases the sharpness

63 L-gamma-Carboxyglutamic acid (Gla) is an uncommon amino ac

64 ovel membrane proteins have an extracellular gamma-carboxyglutamic acid (Gla) protein domain and cyto

65 The proline-rich gamma-carboxyglutamic acid (Gla) proteins (PRGPs) 1 and

66 s one of four known vertebrate transmembrane gamma-carboxyglutamic acid (Gla) proteins.

67 We investigated the functional role of gamma-carboxyglutamic acid (Gla) residue 21 of human fac

68 s property seemed to correlate with an extra gamma-carboxyglutamic acid (Gla) residue at position 11

69 The 17-residue peptide, which contains five gamma-carboxyglutamic acid (Gla) residues and an amidate

70 gely governed by the periodic positioning of gamma-carboxyglutamic acid (Gla) residues within the pri

71 tidine within the intercysteine-loop and two gamma-carboxyglutamic acid (Gla) residues, formed by pos

72 idue polypeptide containing five residues of gamma-carboxyglutamic acid (Gla), and conantokin-T (con-

73 aturally occurring amino acid analogues of l-gamma-carboxyglutamic acid (Gla), appropriately protecte

74 the x-ray crystallographic structure of the gamma-carboxyglutamic acid (Gla)-domainless activated fo

75 reacts with CO(2) and glutamate to generate gamma-carboxyglutamic acid (Gla).

76 mily have glutamic acid residues modified to gamma-carboxyglutamic acids (Gla) by a specific gamma-ca

77 Conantokin G is a gamma-carboxyglutamic acid- (Gla-) containing conotoxin

78 min K-dependent carboxylase and its product, gamma-carboxyglutamic acid, have been identified.

79 translational conversion of glutamic acid to gamma-carboxyglutamic acid in precursor proteins contain

80 arboxylated osteocalcin (%ucOC), and urinary gamma-carboxyglutamic acid in response to 5 d of supplem

81 To investigate the role of gamma-carboxyglutamic acid in the calcium-induced struct

82 To gain insight into the role of gamma-carboxyglutamic acid in the structure of this pept

83 anslational modification of glutamic acid to gamma-carboxyglutamic acid in the vitamin K-dependent pr

84 doplasmic reticulum membrane responsible for gamma-carboxyglutamic acid modification of vitamin K-dep

85 boxylation system with enhanced capacity for gamma-carboxyglutamic acid modification.

86 Matrix gamma-carboxyglutamic acid protein (MGP) is a member of

87 Matrix gamma-carboxyglutamic acid protein (MGP) is a mineral-bi

88 fibrosis and calcification and found matrix gamma-carboxyglutamic acid protein, decorin, periostin,

89 gen production and gene expression of matrix gamma-carboxyglutamic acid protein, recently shown to pl

90 a substitution based on the sequence in bone gamma-carboxyglutamic acid protein.

91 ing a family of proteins termed proline-rich gamma-carboxyglutamic acid (PRRG) proteins were identifi

92 thesis that stapling can effectively replace gamma-carboxyglutamic acid residues in stabilizing the h

93 tive patch created by the side chains of two gamma-carboxyglutamic acid residues that extend outward

94 These peptides contain gamma-carboxyglutamic acid residues typically spaced at

95 dified residues: four cysteine residues, two gamma-carboxyglutamic acid residues, and one residue eac

96 17-residue polypeptide, which contains five gamma-carboxyglutamic acid residues, is a N-methyl-d-asp

97 ogen factor X as well as derivatives lacking gamma-carboxyglutamic acid residues.

98 -PAGE, active site titration, and content of gamma-carboxyglutamic acid residues.

99 fies precursors of these proteins to contain gamma-carboxyglutamic acid residues.

100 pancy of the metal binding sites, defined by gamma-carboxyglutamic acids, results in formation of a c

101 rginine substitution at amino acid 12 in the gamma-carboxyglutamic acid rich (Gla) domain of the matu

102 ydrophobic omega-loop within the prothrombin gamma-carboxyglutamic acid-rich (Gla) domain is importan

103 stabilize the structural orientation of the gamma-carboxyglutamic acid-rich (Gla) domain relative to

104 od coagulation is mediated by the N-terminal gamma-carboxyglutamic acid-rich (Gla) domain, a membrane

105 This binding is mediated by the n-terminal gamma-carboxyglutamic acid-rich domain of this protein.

106 particular interest are the interactions of gamma-carboxyglutamic acid-rich domain-containing clotti

107 compared with individual modules because the gamma-carboxyglutamic acid-rich module and the thrombin-

108 a designed "microprotein S," comprising the gamma-carboxyglutamic acid-rich module, the thrombin-sen

109 heral proteins by using the membrane anchor (gamma-carboxyglutamic-acid-rich domain; GLA domain) of h

110 across animal species and the importance of gamma-carboxyglutamic acid synthesis in diverse biologic

111 Twenty-four-hour ratios of urinary gamma-carboxyglutamic acid to creatinine were unchanged

112 To examine its biosynthesis of gamma-carboxyglutamic acid, we studied the carboxylase f

113 oute for the preparation of Fmoc-protected l-gamma-carboxyglutamic acid, which is amenable to large-s

114 this reaction, glutamic acid is converted to gamma-carboxyglutamic acid while vitamin KH2 is converte