ライフサイエンスコーパス: glutamylcysteine synthetase

1 oth catalytic and modifier subunits of gamma-glutamylcysteine synthetase.

2 (GSH) levels as well as depression of gamma-glutamylcysteine synthetase activity are factors that ar

3 changes were accompanied by diminished gamma-glutamylcysteine synthetase activity in de novo glutathi

4 vels was found to have a deficiency of gamma-glutamylcysteine synthetase activity.

5 f the genes for glutathione synthesis, gamma-glutamylcysteine synthetase and glutathione synthetase,

6 e 3 (Ring3), semaphorin subclass 4 member G, glutamylcysteine synthetase, and p45 NF erythroid 2 were

7 The inhibitor of gamma-glutamylcysteine synthetase, buthionine sulfoximine, als

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

9 Gamma-glutamylcysteine synthetase catalyzes the first step in

10 A modified bacterial gamma-glutamylcysteine synthetase (ECS) gene, S1ptECS, was exp

11 s expressing the E. coli gene encoding gamma-glutamylcysteine synthetase (gamma-ECS) from a strong co

12 he Escherichia coli gshI gene encoding gamma-glutamylcysteine synthetase (gamma-ECS), targeted to the

13 omitant with a significant increase in gamma-glutamylcysteine synthetase (gamma-GCS) activity and the

14 uclear cell and colon mRNA content for gamma-glutamylcysteine synthetase (gamma-GCS) and DT-diaphoras

15 Gamma-glutamylcysteine synthetase (gamma-GCS) and glutathione

16 sequential action of distinct enzymes, gamma-glutamylcysteine synthetase (gamma-GCS) and GSH syntheta

17 stress response, the up-regulation of gamma-glutamylcysteine synthetase (gamma-GCS) and the precedin

18 gamma-Glutamylcysteine synthetase (gamma-GCS) catalyzes the AT

19 gamma-Glutamylcysteine synthetase (gamma-GCS) catalyzes the fi

20 esistance-associated protein (MRP) and gamma-glutamylcysteine synthetase (gamma-GCS) heavy subunit ge

21 Gamma-glutamylcysteine synthetase (gamma-GCS) mRNA expression

22 tor-beta(1) (TGF-beta(1)) can modulate gamma-glutamylcysteine synthetase (gamma-GCS) mRNA levels in l

23 We found that gamma-glutamylcysteine synthetase (gamma-GCS) was induced in t

24 SG-R) functions, protein expression of gamma-glutamylcysteine synthetase (gamma-GCS), and total cellu

25 RNA levels of the catalytic subunit of gamma-glutamylcysteine synthetase (gamma-GCS), the rate-limiti

26 regulated by the rate-limiting enzyme gamma-glutamylcysteine synthetase (gamma-GCS).

27 thereby trypanothione, is catalyzed by gamma-glutamylcysteine synthetase (gamma-GCS).

28 Gamma-glutamylcysteine synthetase (gamma-GCS, glutamate-cystei

29 ssion of thiol-related genes including gamma-glutamylcysteine synthetase, gamma-glutamyl transpeptida

30 Inhibition of gamma-glutamylcysteine synthetase (gammaGCS) by buthionine sul

31 te in P. falciparum the genes encoding gamma-glutamylcysteine synthetase (gammaGCS) or glutathione sy

32 panothione, is catalyzed by the enzyme gamma-glutamylcysteine synthetase (gammaGCS).

33 ted disruption of the heavy subunit of gamma-glutamylcysteine synthetase (gammaGCS-HS(tm1)), an essen

34 sed liver GSH, both cysteine level and gamma-glutamylcysteine synthetase (GCS) activity were signific

35 mRNA expression of gamma-glutamylcysteine synthetase (GCS) large subunit and cata

36 o subunits of the rate-limiting enzyme gamma-glutamylcysteine synthetase (GCS) was examined after a 2

37 CSh) and regulatory (GCS1) subunits of gamma-glutamylcysteine synthetase (GCS) which catalyzes the ra

38 he de novo synthesis of glutathione is gamma-glutamylcysteine synthetase (GCS), a heterodimer consist

39 nd cysteine, and increased activity of gamma-glutamylcysteine synthetase (GCS), the rate-limiting enz

40 QO1), glutathione S-transferase (GST), gamma-glutamylcysteine synthetase (GCS), UDP-glucuronosyltrans

41 ate-limiting enzyme for GSH synthesis, gamma-glutamylcysteine synthetase (GCS), were also determined

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

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

44 The nrc1 mutation was mapped to the gamma-glutamylcysteine synthetase gene and the nrc2 mutation w

45 Quantification of gamma-glutamylcysteine synthetase (GLCL) was determined throug

46 structure of the catalytic subunit of gamma-glutamylcysteine synthetase (GLCLC) was determined, prov

47 ibition, 2-AAPA showed no inhibition against glutamylcysteine synthetase, glutathione synthetase, cat

48 hesis is catalyzed by a single enzyme, gamma-glutamylcysteine synthetase-glutathione synthetase (gamm

49 e mRNA levels of endogenous selenoprotein H, glutamylcysteine synthetase heavy and light chains, and

50 Expression of the gamma-glutamylcysteine synthetase heavy subunit (gamma-GCSh),

51 The mRNA levels of g-glutamylcysteine synthetase heavy subunit (GCS-HS) and G

52 nthesis rate; and a 2-fold increase in gamma-glutamylcysteine synthetase heavy subunit (GCS-HS) mRNA,

53 athione S-transferases Pi (GST-Pi) and gamma-glutamylcysteine synthetase heavy subunit (GCSh) express

54 The overexpression of subunits of gamma-glutamylcysteine synthetase in combination completely bl

55 ts confirm increased protein levels of gamma-glutamylcysteine synthetase in mouse lungs.

56 Expression of gamma-glutamylcysteine synthetase in the cisplatin-resistant c

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

58 hoximine, an irreversible inhibitor of gamma-glutamylcysteine synthetase, increased PRIMA-1(Met)-indu

59 stance of ars1 is not abolished by the gamma-glutamylcysteine synthetase inhibitor l-buthionine sulfo

60 g the heavy (catalytic) subunit of the gamma-glutamylcysteine synthetase is frequently elevated in ma

61 te-cysteine ligase (GCL; also known as gamma-glutamylcysteine synthetase) is the rate-limiting enzyme

62 involved in glutathione biosynthesis, gamma-glutamylcysteine synthetase, is encoded by the GSH1 gene

63 Tat+ mice was accompanied by decreased gamma-glutamylcysteine synthetase regulatory subunit mRNA and

64 n levels of glutathione synthetase and gamma-glutamylcysteine synthetase relative to wild-type cells.

65 ]-sulfoximine (L-BSO), an inhibitor of gamma-glutamylcysteine synthetase (the rate-limiting enzyme in

66 itic cells via decreased expression of gamma-glutamylcysteine synthetase, the limiting enzyme for GSH

67 oximine (BSO), a specific inhibitor of gamma-glutamylcysteine synthetase, the rate-limiting enzyme fo

68 due to an increase in the activity of gamma-glutamylcysteine synthetase, the rate-limiting enzyme fo

69 esulted in an increased sensitivity of gamma-glutamylcysteine synthetase to feedback inhibition by GS

70 SH) concentrations and the activity of gamma-glutamylcysteine synthetase, which is a rate-limiting en