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1 ), Bach1, cystine/glutamate transporter, and glutamate cysteine ligase.
2 ough an increase in the rate-limiting enzyme glutamate cysteine ligase.
3 tase (NQO1), glutathione S-transferases, and glutamate-cysteine ligase.
4 in its de novo biosynthesis is catalyzed by glutamate cysteine ligase, a broadly expressed enzyme fo
5 ed that loss of MLK3 increased expression of glutamate cysteine ligase, accelerated hepatic GSH recov
7 Because people are known to vary in their glutamate-cysteine ligase activity, this enzyme may also
8 suggest that Nrf2, through up-regulation of glutamate-cysteine ligase and increase of GSH levels, pr
9 C57Bl/6 mice that conditionally overexpress glutamate-cysteine ligase, and report here their resista
11 and those that were stably transfected with glutamate cysteine ligase catalytic subunit (GCLC), a ra
12 , and upregulation of Nrf2-regultated genes, glutamate cysteine ligase catalytic subunit (GCLC), and
13 otypic Nrf2-regulated enzymes, including the glutamate-cysteine ligase catalytic and modifier subunit
14 of genes encoding heme oxygenase 1 (Hmox1), glutamate-cysteine ligase catalytic subunit (Gclc) and p
15 disease and a functional polymorphism in the glutamate-cysteine ligase catalytic subunit (GCLC) gene.
18 quinone exposure as well as the induction of glutamate-cysteine ligase catalytic subunit and 14-3-3si
19 drogenase, quinone 1, glutathione reductase, glutamate-cysteine ligase catalytic subunit, ABCC1, pero
20 2-dependent genes, such as heme oxygenase-1, glutamate-cysteine ligase catalytic subunit, and NAD(P)H
23 so induced the oxidant stress response genes glutamate-cysteine ligase, catalytic subunit, and NAD(P)
24 Male transgenic mice induced to overexpress glutamate-cysteine ligase exhibited resistance to acetam
25 H9c2 cells, or overexpression of either the glutamate cysteine ligase (GCL) catalytic subunit (GCLC)
30 ovo GSH biosynthesis pathway is catalyzed by glutamate cysteine ligase (GCL), a heterodimer, composed
32 further demonstrate a rhythm in activity of glutamate cysteine ligase (GCL), the rate-limiting enzym
33 roach (i.e. post-translational activation of glutamate cysteine ligase (GCL), the rate-limiting enzym
34 ncrease cellular GSH levels, the activity of glutamate cysteine ligase (GCL), the rate-limiting enzym
37 enzyme in the glutathione synthetic pathway [glutamate cysteine ligase (GCL)] were found to be induce
38 reatment was observed to promote the loss of glutamate cysteine ligase (GCL, rate-limiting enzyme in
39 ssion of genes downstream of Nrf2, including glutamate-cysteine ligase (GCL) and glutathione S-transf
47 xamined the response of Arabidopsis thaliana glutamate-cysteine ligase (GCL) to changes in redox envi
48 ymes for glutathione synthesis, particularly glutamate-cysteine ligase (GCL), and metabolism as well
49 se in glutathione S-transferase-P1 (GST-P1), glutamate-cysteine ligase (GCL), and NAD(P)H:quinone oxi
50 on the activity of the rate-limiting enzyme glutamate-cysteine ligase (GCL), consisting of a catalyt
53 e (GSH) and its de novo rate-limiting enzyme glutamate-cysteine ligase (GCL), which consists of a cat
56 occurs via two enzymatic steps catalyzed by glutamate-cysteine ligase (GCL, made up of two subunits)
58 l gene targeting of the catalytic subunit of glutamate cysteine ligase (Gclc) blocked GSH production
59 very that combining inhibitors of mTORC1 and glutamate cysteine ligase (GCLC) can selectively and eff
60 , due to deletion of the modifier subunit of glutamate cysteine ligase (Gclm), the rate-limiting enzy
61 ransporter xCT and the regulatory subunit of glutamate-cysteine ligase (GCLM) in a hypoxia-inducible
66 nobacteria, we generated deletion mutants of glutamate-cysteine ligase (gshA) and glutathione synthet
68 ional response and an increased formation of glutamate cysteine ligase holoenzyme, as shown using a h
69 ergistic lethality with heme oxygenase-1 and glutamate-cysteine ligase inhibitors against CLL cells.
71 /c-Myc phosphorylation, nuclear Nrf2 levels, glutamate cysteine ligase levels, GSH concentration and
72 f glutathione through knock-out of the GCLM (glutamate-cysteine ligase modifier subunit) also did not
74 defense because basal levels of glutathione, glutamate cysteine ligase modulatory subunit, catalase,
75 out (KO) of the key GSH-synthesizing enzyme, glutamate-cysteine ligase modulatory subunit (GCLM).
76 d the structures of Saccharomyces cerevisiae glutamate cysteine ligase (ScGCL) in the presence of glu
78 (Nrf2) that down-regulate the expression of glutamate cysteine ligase, the rate limiting enzyme for
80 eated male mice carrying, but not expressing glutamate-cysteine ligase transgenes, or to female gluta
82 amma-glutamylcysteine synthetase (gamma-GCS, glutamate-cysteine ligase), which catalyzes the first an
83 e-(S,R)-sulfoximine, a specific inhibitor of glutamate-cysteine ligase, which is a rate-limiting enzy
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