ライフサイエンスコーパス: gamma-glutamylcysteine

1 24-180-fold increases in the K(m) values for gamma-glutamylcysteine.

2 ione, dimercaptosuccinate, penicillamine, or gamma-glutamylcysteine.

3 of GSH1 and elevating the cellular levels of gamma-glutamylcysteine.

4 in the aerobic phototrophic halobacteria is gamma-glutamylcysteine.

5 .w. thiol bound to S-thiolated proteins, but gamma-glutamylcysteine and cysteine were also bound.

6 ceptibility of gshA and gshB mutants lacking gamma-glutamylcysteine and glutathione synthetases to NO

7 5, however increases in the thiols cysteine, gamma-glutamylcysteine and glutathione were observed.

8 hiosulfate increased more than did cysteine, gamma-glutamylcysteine and glutathione.

9 step in the biosynthesis of glutathione from gamma-glutamylcysteine and glycine in an ATP-dependent m

10 n of the ubiquitous peptide glutathione from gamma-glutamylcysteine and glycine.

11 accumulated sulfite, thiosulfate, cysteine, gamma-glutamylcysteine, and glutathione.

12 cumulation of glutathione and its precursor, gamma-glutamylcysteine, and significant depletion of 1 o

13 The first contains GSH1, indicating that gamma-glutamylcysteine can functionally replace GSH if i

14 , grow poorly as the dipeptide intermediate, gamma-glutamylcysteine, can partially substitute for GSH

15 In contrast, binding of either glycine or gamma-glutamylcysteine causes a 6.7-fold decrease in bin

16 latin (PC) synthase has been assumed to be a gamma-glutamylcysteine dipeptidyl transpeptidase (EC 2.3

17 tathione and related thiols by the action of gamma-glutamylcysteine dipeptidyl transpeptidases (phyto

18 The dependence of phytochelatin synthase (gamma-glutamylcysteine dipeptidyltranspeptidase (PCS), E

19 rsenic treatment, the root concentrations of gamma-glutamylcysteine (EC), PC2, and PC3 peptides in a

20 phytochelatins consist of repeating units of gamma-glutamylcysteine followed by a C-terminal Gly, Ser

21 yme catalyzes the ATP-dependent formation of gamma-glutamylcysteine from glutamate (Km = 9.1 mm) and

22 Since GSH2 is responsible for converting gamma-glutamylcysteine (gamma-EC) to glutathione (GSH) i

23 t instead accumulates the precursor compound gamma-glutamylcysteine (gamma-EC).

24 e liquid chromatography (HPLC) assessment of gamma-glutamylcysteine (gamma-GC) product formation.

25 utathione and accumulates only its precursor gamma-glutamylcysteine (gamma-GC).

26 Phytochelatin (PC) synthases are gamma-glutamylcysteine (gamma-Glu-Cys) dipeptidyl transp

27 ax) hGS in three states: apoenzyme, bound to gamma-glutamylcysteine (gammaEC), and with hGSH, ADP, an

28 Within the gamma-glutamylcysteine/glutathione-binding site, the S15

29 ar redox environment and is synthesized from gamma-glutamylcysteine, glycine, and ATP by glutathione

30 The binding of either ATP or gamma-glutamylcysteine increased the binding affinity of

31 gamma-Glutamylcysteine is the major low-molecular weight

32 Regulation of gamma-glutamylcysteine ligase (GCL), the rate-controllin

33 city, we measured the levels and activity of gamma-glutamylcysteine ligase (GCL), the rate-controllin

34 also caused increases in mRNA expression of gamma-glutamylcysteine ligase catalytic subunit and NQO1

35 us glutamine and had increased expression of gamma-glutamylcysteine ligase relative to WT MEFs.

36 rgets, the xCT cystine/glutamate antiporter, gamma-glutamylcysteine ligase, and glutathione peroxidas

37 ere observed for S-glutathione (S-GSH) and S-gamma-glutamylcysteine (S-gamma-GluCys), both of which w

38 uch as the NAD(P)H quinone oxidase 1 (NQO1), gamma glutamylcysteine synthase heavy unit (gammaGCSH),

39 te metabolism - adenylyl transferase (GlnE), gamma-glutamylcysteine synthase (GshA), UDP-N-acetylmura

40 de hydrolase, glutathione S-transferase, and gamma-glutamylcysteine synthase, whose expression is ind

41 presumably with feedback over-stimulation of gamma-glutamylcysteine synthesis and its subsequent conv

42 osynthesis inhibitor propargylglycine or the gamma-glutamylcysteine synthesis inhibitor buthionine su

43 A modified bacterial gamma-glutamylcysteine synthetase (ECS) gene, S1ptECS, w

44 plants expressing the E. coli gene encoding gamma-glutamylcysteine synthetase (gamma-ECS) from a str

45 ress the Escherichia coli gshI gene encoding gamma-glutamylcysteine synthetase (gamma-ECS), targeted

46 , concomitant with a significant increase in gamma-glutamylcysteine synthetase (gamma-GCS) activity a

47 mononuclear cell and colon mRNA content for gamma-glutamylcysteine synthetase (gamma-GCS) and DT-dia

48 Gamma-glutamylcysteine synthetase (gamma-GCS) and glutat

49 y the sequential action of distinct enzymes, gamma-glutamylcysteine synthetase (gamma-GCS) and GSH sy

50 f this stress response, the up-regulation of gamma-glutamylcysteine synthetase (gamma-GCS) and the pr

51 gamma-Glutamylcysteine synthetase (gamma-GCS) catalyzes

52 gamma-Glutamylcysteine synthetase (gamma-GCS) catalyzes

53 drug resistance-associated protein (MRP) and gamma-glutamylcysteine synthetase (gamma-GCS) heavy subu

54 Gamma-glutamylcysteine synthetase (gamma-GCS) mRNA expre

55 th factor-beta(1) (TGF-beta(1)) can modulate gamma-glutamylcysteine synthetase (gamma-GCS) mRNA level

56 We found that gamma-glutamylcysteine synthetase (gamma-GCS) was induce

57 -Px/GSSG-R) functions, protein expression of gamma-glutamylcysteine synthetase (gamma-GCS), and total

58 state RNA levels of the catalytic subunit of gamma-glutamylcysteine synthetase (gamma-GCS), the rate-

59 sis is regulated by the rate-limiting enzyme gamma-glutamylcysteine synthetase (gamma-GCS).

60 e and thereby trypanothione, is catalyzed by gamma-glutamylcysteine synthetase (gamma-GCS).

61 Gamma-glutamylcysteine synthetase (gamma-GCS, glutamate-

62 Inhibition of gamma-glutamylcysteine synthetase (gammaGCS) by buthioni

63 o delete in P. falciparum the genes encoding gamma-glutamylcysteine synthetase (gammaGCS) or glutathi

64 by trypanothione, is catalyzed by the enzyme gamma-glutamylcysteine synthetase (gammaGCS).

65 targeted disruption of the heavy subunit of gamma-glutamylcysteine synthetase (gammaGCS-HS(tm1)), an

66 increased liver GSH, both cysteine level and gamma-glutamylcysteine synthetase (GCS) activity were si

67 mRNA expression of gamma-glutamylcysteine synthetase (GCS) large subunit an

68 of two subunits of the rate-limiting enzyme gamma-glutamylcysteine synthetase (GCS) was examined aft

69 tic (GCSh) and regulatory (GCS1) subunits of gamma-glutamylcysteine synthetase (GCS) which catalyzes

70 e in the de novo synthesis of glutathione is gamma-glutamylcysteine synthetase (GCS), a heterodimer c

71 GSH) and cysteine, and increased activity of gamma-glutamylcysteine synthetase (GCS), the rate-limiti

72 ase (NQO1), glutathione S-transferase (GST), gamma-glutamylcysteine synthetase (GCS), UDP-glucuronosy

73 the rate-limiting enzyme for GSH synthesis, gamma-glutamylcysteine synthetase (GCS), were also deter

74 nd the activity of the rate-limiting enzyme, gamma-glutamylcysteine synthetase (GCS).

75 is the activity of the rate-limiting enzyme, gamma-glutamylcysteine synthetase (GCS).

76 Quantification of gamma-glutamylcysteine synthetase (GLCL) was determined

77 enomic structure of the catalytic subunit of gamma-glutamylcysteine synthetase (GLCLC) was determined

78 e-[S,R]-sulfoximine (L-BSO), an inhibitor of gamma-glutamylcysteine synthetase (the rate-limiting enz

79 thione (GSH) levels as well as depression of gamma-glutamylcysteine synthetase activity are factors t

80 These changes were accompanied by diminished gamma-glutamylcysteine synthetase activity in de novo gl

81 one levels was found to have a deficiency of gamma-glutamylcysteine synthetase activity.

82 tion of the genes for glutathione synthesis, gamma-glutamylcysteine synthetase and glutathione synthe

83 (PDTC) resulted in the up-regulation of the gamma-glutamylcysteine synthetase catalytic (GCS(h)) and

84 Gamma-glutamylcysteine synthetase catalyzes the first st

85 The nrc1 mutation was mapped to the gamma-glutamylcysteine synthetase gene and the nrc2 muta

86 Expression of the gamma-glutamylcysteine synthetase heavy subunit (gamma-G

87 GSH synthesis rate; and a 2-fold increase in gamma-glutamylcysteine synthetase heavy subunit (GCS-HS)

88 f glutathione S-transferases Pi (GST-Pi) and gamma-glutamylcysteine synthetase heavy subunit (GCSh) e

89 The overexpression of subunits of gamma-glutamylcysteine synthetase in combination complet

90 eriments confirm increased protein levels of gamma-glutamylcysteine synthetase in mouse lungs.

91 Expression of gamma-glutamylcysteine synthetase in the cisplatin-resis

92 hesis is not mediated by feedback control of gamma-glutamylcysteine synthetase in this system.

93 d resistance of ars1 is not abolished by the gamma-glutamylcysteine synthetase inhibitor l-buthionine

94 ncoding the heavy (catalytic) subunit of the gamma-glutamylcysteine synthetase is frequently elevated

95 es of Tat+ mice was accompanied by decreased gamma-glutamylcysteine synthetase regulatory subunit mRN

96 protein levels of glutathione synthetase and gamma-glutamylcysteine synthetase relative to wild-type

97 hich resulted in an increased sensitivity of gamma-glutamylcysteine synthetase to feedback inhibition

98 lutamate-cysteine ligase (GCL; also known as gamma-glutamylcysteine synthetase) is the rate-limiting

99 The inhibitor of gamma-glutamylcysteine synthetase, buthionine sulfoximin

100 expression of thiol-related genes including gamma-glutamylcysteine synthetase, gamma-glutamyl transp

101 e sulphoximine, an irreversible inhibitor of gamma-glutamylcysteine synthetase, increased PRIMA-1(Met

102 enzyme involved in glutathione biosynthesis, gamma-glutamylcysteine synthetase, is encoded by the GSH

103 dendritic cells via decreased expression of gamma-glutamylcysteine synthetase, the limiting enzyme f

104 as not due to an increase in the activity of gamma-glutamylcysteine synthetase, the rate-limiting enz

105 )-sulfoximine (BSO), a specific inhibitor of gamma-glutamylcysteine synthetase, the rate-limiting enz

106 one (GSH) concentrations and the activity of gamma-glutamylcysteine synthetase, which is a rate-limit

107 H synthesis is catalyzed by a single enzyme, gamma-glutamylcysteine synthetase-glutathione synthetase

108 n of both catalytic and modifier subunits of gamma-glutamylcysteine synthetase.

109 Other thiols measured included cysteine, gamma-glutamylcysteine, thiosulfate, coenzyme A, and sul

110 levels of the PC precursors, glutathione and gamma-glutamylcysteine, upon exposure to cadmium.