ライフサイエンスコーパス: carboxyglutamic

1 The missing gamma-carboxyglutamic acid (GLA) and part of epidermal growth

2 oxylation of glutamic acid residues to gamma-carboxyglutamic acid (Gla) by the vitamin K-dependent ga

3 ependent importance of the propeptide, gamma-carboxyglutamic acid (Gla) domain and elements beyond th

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

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

6 latory effect requires presence of the gamma-carboxyglutamic acid (Gla) domain in protein C and is en

7 nt in terms of the manner in which the gamma-carboxyglutamic acid (Gla) domain of each protein pertur

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

9 Similar to FX, the gamma-carboxyglutamic acid (Gla) domain of FII binds within th

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

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

12 ave three of seven Ca(2+) sites in the gamma-carboxyglutamic acid (Gla) domain replaced by Mg(2+) at

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

14 ys159-Lys165, are near the factor VIIa gamma-carboxyglutamic acid (Gla) domain, suggesting that the f

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

16 protein C receptor (EPCR) through its gamma-carboxyglutamic acid (Gla) domain, with unknown hemostat

17 Four of these encode gamma-carboxyglutamic acid (Gla) domain-containing proteins, w

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

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

20 containing phosphatidylserine (PS) via gamma-carboxyglutamic acid (Gla) domains is one of the essenti

21 d function requires interaction of the gamma-carboxyglutamic acid (Gla) domains of factor IXa and fac

22 To assess the role of gamma-carboxyglutamic acid (Gla) domains of FX and FIX in FVII

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

24 ids on these proteins are converted to gamma-carboxyglutamic acid (Gla) in a reaction that requires v

25 umor acidity, and replacing Asp14 with gamma-carboxyglutamic acid (Gla) increases the sharpness of pH

26 L-gamma-Carboxyglutamic acid (Gla) is an uncommon amino acid tha

27 embrane proteins have an extracellular gamma-carboxyglutamic acid (Gla) protein domain and cytosolic

28 The proline-rich gamma-carboxyglutamic acid (Gla) proteins (PRGPs) 1 and 2 are

29 of four known vertebrate transmembrane gamma-carboxyglutamic acid (Gla) proteins.

30 We investigated the functional role of gamma-carboxyglutamic acid (Gla) residue 21 of human factor IX

31 erty seemed to correlate with an extra gamma-carboxyglutamic acid (Gla) residue at position 11 of pro

32 7-residue peptide, which contains five gamma-carboxyglutamic acid (Gla) residues and an amidated C-te

33 overned by the periodic positioning of gamma-carboxyglutamic acid (Gla) residues within the primary s

34 within the intercysteine-loop and two gamma-carboxyglutamic acid (Gla) residues, formed by post-tran

35 olypeptide containing five residues of gamma-carboxyglutamic acid (Gla), and conantokin-T (con-T), a

36 ly occurring amino acid analogues of l-gamma-carboxyglutamic acid (Gla), appropriately protected for

37 -ray crystallographic structure of the gamma-carboxyglutamic acid (Gla)-domainless activated form.

38 s with CO(2) and glutamate to generate gamma-carboxyglutamic acid (Gla).

39 family of proteins termed proline-rich gamma-carboxyglutamic acid (PRRG) proteins were identified and

40 BMP9 and their inhibitors MGP (matrix gamma-carboxyglutamic acid [Gla] protein) and CV2 (crossveinle

41 carboxylated as demonstrated by direct gamma-carboxyglutamic acid analysis of the alkaline hydrolysat

42 The auxiliary gamma-carboxyglutamic acid and epidermal growth factor domains

43 he vitamin K-dependent biosynthesis of gamma-carboxyglutamic acid appears to be a highly conserved fu

44 n and regulatory proteins that contain gamma-carboxyglutamic acid are a part of a unique class of mem

45 restimate of the true contributions of gamma-carboxyglutamic acid at these positions.

46 XNP); each protein had the same Mr and gamma-carboxyglutamic acid content.

47 Urinary gamma-carboxyglutamic acid did not change in response to suppl

48 o-terminus of the Ca(2+)-bound form of gamma-carboxyglutamic acid domain (GD) of human protein C (PC)

49 expressed wild-type PZ, PZ lacking the gamma-carboxyglutamic acid domain (GD-PZ), and a chimeric PZ m

50 Mutagenesis of the FVIIa 4-carboxyglutamic acid domain and dose titrations with FX

51 The effect of replacing the gamma-carboxyglutamic acid domain of activated protein C (APC)

52 Deletion of the gamma-carboxyglutamic acid domain of APC, a region critical fo

53 PC/PS vesicles bind to the N-terminal gamma-carboxyglutamic acid domain of APC, and that one mechani

54 nactive and lacks the membrane-binding gamma-carboxyglutamic acid domain of native fXa but retains th

55 4 to the anionic, vitamin K- dependent gamma-carboxyglutamic acid domain of protein C.

56 The gamma-carboxyglutamic acid domain substitution therefore lower

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

58 genesis of the 40 N-terminal residues (gamma-carboxyglutamic acid domain) of blood clotting factor VI

59 Each protein contains an N-terminal gamma-carboxyglutamic acid domain, followed by EGF1 and EGF2 d

60 f the protein C derivative lacking the gamma-carboxyglutamic acid domain, which is required for bindi

61 Unlike the gamma-carboxyglutamic acid domain-containing proteins of the b

62 re of NAP5 bound at the active site of gamma-carboxyglutamic acid domainless factor Xa (des-fXa) has

63 ight ligand of the exosites of FXa and gamma-carboxyglutamic acid domainless FXa (des-Gla-FXa), incre

64 e additional roles by interacting with the 4-carboxyglutamic acid domains of procoagulant coagulation

65 cin, plasma phylloquinone, and urinary gamma-carboxyglutamic acid excretion appear to be sensitive me

66 report the synthesis of N-alpha-Fmoc-L-gamma-carboxyglutamic acid gamma,gamma'-tert-butyl ester (Fmoc

67 tors of mineralization, such as matrix gamma-carboxyglutamic acid Gla protein, fetuin, and osteoponti

68 ational conversion of glutamic acid to gamma-carboxyglutamic acid in precursor proteins containing th

69 lated osteocalcin (%ucOC), and urinary gamma-carboxyglutamic acid in response to 5 d of supplementati

70 To investigate the role of gamma-carboxyglutamic acid in the calcium-induced structural t

71 To gain insight into the role of gamma-carboxyglutamic acid in the structure of this peptide, w

72 ional modification of glutamic acid to gamma-carboxyglutamic acid in the vitamin K-dependent proteins

73 mic reticulum membrane responsible for gamma-carboxyglutamic acid modification of vitamin K-dependent

74 tion system with enhanced capacity for gamma-carboxyglutamic acid modification.

75 Matrix gamma-carboxyglutamic acid protein (MGP) is a member of the vi

76 Matrix gamma-carboxyglutamic acid protein (MGP) is a mineral-binding

77 sis and calcification and found matrix gamma-carboxyglutamic acid protein, decorin, periostin, and th

78 oduction and gene expression of matrix gamma-carboxyglutamic acid protein, recently shown to play a r

79 titution based on the sequence in bone gamma-carboxyglutamic acid protein.

80 that stapling can effectively replace gamma-carboxyglutamic acid residues in stabilizing the helical

81 atch created by the side chains of two gamma-carboxyglutamic acid residues that extend outward from a

82 These peptides contain gamma-carboxyglutamic acid residues typically spaced at i,i+4

83 residues: four cysteine residues, two gamma-carboxyglutamic acid residues, and one residue each of 6

84 sidue polypeptide, which contains five gamma-carboxyglutamic acid residues, is a N-methyl-d-aspartate

85 recursors of these proteins to contain gamma-carboxyglutamic acid residues.

86 actor X as well as derivatives lacking gamma-carboxyglutamic acid residues.

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

88 e substitution at amino acid 12 in the gamma-carboxyglutamic acid rich (Gla) domain of the mature pro

89 s animal species and the importance of gamma-carboxyglutamic acid synthesis in diverse biological sys

90 Twenty-four-hour ratios of urinary gamma-carboxyglutamic acid to creatinine were unchanged with t

91 eaction, glutamic acid is converted to gamma-carboxyglutamic acid while vitamin KH2 is converted to v

92 ational conversion of glutamic acid to gamma-carboxyglutamic acid, an amino acid critical to the func

93 (ucOC)], plasma phylloquinone, urinary gamma-carboxyglutamic acid, and plasma undercarboxylated proth

94 Upon binding of Ca2+ to gamma-carboxyglutamic acid, conantokin G undergoes a conformat

95 dependent carboxylase and its product, gamma-carboxyglutamic acid, have been identified.

96 To examine its biosynthesis of gamma-carboxyglutamic acid, we studied the carboxylase from Co

97 or the preparation of Fmoc-protected l-gamma-carboxyglutamic acid, which is amenable to large-scale p

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

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

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

101 smembrane proteins with amino-terminal gamma-carboxyglutamic acid-containing domains preceded by the

102 Ca2+, Mg2+, and Zn2+, to the synthetic gamma-carboxyglutamic acid-containing neuroactive peptides, co

103 , characterization, and structure of a gamma-carboxyglutamic acid-containing peptide, conotoxin epsil

104 n system that converts the proteins to gamma-carboxyglutamic acid-containing proteins.

105 ructure to other conotoxins and to the gamma-carboxyglutamic acid-containing regions of the vitamin K

106 constructed a protein C mutant in the gamma-carboxyglutamic acid-domainless form in which the P1 Arg

107 obic omega-loop within the prothrombin gamma-carboxyglutamic acid-rich (Gla) domain is important in m

108 lize the structural orientation of the gamma-carboxyglutamic acid-rich (Gla) domain relative to EGF-1

109 gulation is mediated by the N-terminal gamma-carboxyglutamic acid-rich (Gla) domain, a membrane-ancho

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

111 cular interest are the interactions of gamma-carboxyglutamic acid-rich domain-containing clotting pro

112 ed with individual modules because the gamma-carboxyglutamic acid-rich module and the thrombin-sensit

113 igned "microprotein S," comprising the gamma-carboxyglutamic acid-rich module, the thrombin-sensitive

114 nd by a decreased urinary excretion of gamma-carboxyglutamic acid.

115 omitant conversion of glutamic acid to gamma-carboxyglutamic acid.

116 K-dependent carboxylation to generate gamma-carboxyglutamic acid.

117 proteins by using the membrane anchor (gamma-carboxyglutamic-acid-rich domain; GLA domain) of human c

118 ave glutamic acid residues modified to gamma-carboxyglutamic acids (Gla) by a specific gamma-carboxyl

119 of the metal binding sites, defined by gamma-carboxyglutamic acids, results in formation of a calcium

120 s 1-116 of protein S and including the gamma-carboxyglutamic-rich domain, the thrombin-sensitive regi