ライフサイエンスコーパス: thioltransferase

1 hich can be reactivated by dithiothreitol or thioltransferase.

2 With substantially more thioltransferase (100 nM) Cys-67-SSG was partially deglu

3 ically and efficiently by glutaredoxin (GRx, thioltransferase), a thioldisulfide oxidoreductase.

4 In addition, glutathione level, thioltransferase activity, m-calpain activity, and m-cal

5 effect of Grx1 on Bim is dependent on Grx1's thioltransferase activity.

6 Grx (C22S), demonstrating a requirement for thioltransferase activity.

7 redoxins, O2L and G4L, both of which exhibit thioltransferase and dehydroascorbate reductase activiti

8 fied Y55.7 protein had glutathione-dependent thioltransferase and dehydroascorbate reductase activiti

9 The role of thioltransferase and glutathione reductase in the cellul

10 Thioltransferase and GSSG reductase in situ displayed si

11 ibited the isolated component enzymes of the thioltransferase and thioredoxin systems, consistent wit

12 the thioltransferase system, consistent with thioltransferase being the primary intracellular catalys

13 ponding to a putative N-acetyltransferase or thioltransferase catalytic site.

14 es a GSH-dependent pathway, likely involving thioltransferase-catalyzed reduction of the oxidation-se

15 Moreover, transfection with antisense thioltransferase cDNA was incompatible with cell surviva

16 At low thioltransferase concentrations (5 nM), deglutathionylat

17 nalysis of HIV-1MN virus with an antibody to thioltransferase detected a band co-migrating with recom

18 lone was not an effective reductant, whereas thioltransferase displayed differential catalysis toward

19 els along with the glutathione reductase and thioltransferase enzyme activities.

20 ggest that the relative participation of the thioltransferase (glutaredoxin) and thioredoxin systems

21 be catalyzed in vitro by the cellular enzyme thioltransferase (glutaredoxin) coupled to GSH and GSSG

22 ar event is protein S-glutathionylation, and thioltransferase (glutaredoxin) is a specific and effici

23 y the glutathione-specific dethiolase enzyme thioltransferase (glutaredoxin), indicating that the ina

24 95A, Cys-67-SSG) as potential substrates for thioltransferase (glutaredoxin).

25 t are specifically reversed by the cytosolic thioltransferase, glutaredoxin-1 (Glrx).

26 The structurally homologous thioredoxins and thioltransferases/glutaredoxins possess a solvent-expose

27 Collectively, these data suggest that thioltransferase has a vital role in sulfhydryl homeosta

28 icinal dithiol nature of their active sites: thioltransferase (IC(50) approximately 1 micrometer), GS

29 Our results implicate thioltransferase in the regulation and/or maintenance of

30 The structure of human thioltransferase is characterized by a thioredoxin-like

31 Glutaredoxin (thioltransferase) is a thiol-disulfide oxidoreductase th

32 Glutaredoxin (GRx, thioltransferase) is implicated in cellular redox regula

33 Human glutaredoxin (GRx), also known as thioltransferase, is a 12 kDa thiol-disulfide oxidoreduc

34 Accordingly, the catalytic cycle of thioltransferase itself involves a covalent glutathionyl

35 ide exchange reactions characteristic of the thioltransferases lies in the relative reactivity of the

36 ment of the diglutathionylated protease with thioltransferase not only restored protease activity but

37 Thioltransferase (or Grx) belongs to the oxidoreductase

38 sible function of the recombinant human lens thioltransferase (RHLT).

39 reductase activity of recombinant pig liver thioltransferase (RPLTT) was investigated.

40 , and this correlated with inhibition of the thioltransferase system, consistent with thioltransferas

41 etected a band co-migrating with recombinant thioltransferase that persisted following subtilisin tre

42 study was undertaken to investigate whether thioltransferase (TTase) exhibits dehydroascorbate (DHA)

43 To clone the human lens thioltransferase (TTase) gene and to purify, characteriz

44 study the possible physiological function of thioltransferase (TTase) in combating oxidative damage i

45 Human thioltransferase (TTase) is a 12 kDa thiol-disulfide oxi

46 arent pKa for the active site thiol of human thioltransferase (TTase) is about 3.5, but the pH depend

47 A new redox regulating enzyme, thioltransferase (TTase), has been found in the lens.

48 n view of the important antioxidant roles of thioltransferase (TTase), thioredoxin (Trx), and thiored

49 Disruption of the vicinal dithiol on thioltransferase (via oxidation to C22-SS-C25; or C25S m

50 Comparison of the human thioltransferase with other thiol-disulfide oxidoreducta

51 ilisin treatment, indicating the presence of thioltransferase within HIV-1.