ライフサイエンスコーパス: redox buffer

1 w that glutathione acts as the main cellular redox buffer.

2 oxidative perturbation of the ER glutathione redox buffer.

3 ithout any added oxidized PDI or glutathione redox buffer.

4 y similar to when hydroquinone was used as a redox buffer.

5 e presence of 0.5 M guanidine and a suitable redox buffer.

6 n the reducing capacity of the extracellular redox buffer.

7 tored by circular dichroism in a glutathione redox buffer.

8 ation, even in the presence of a glutathione redox buffer.

9 essive copper entry, which is deleterious to redox buffers.

10 n be followed in the presence of glutathione redox buffers.

11 ore versatile than classical aliphatic thiol redox buffers.

12 th the disulfide-scrambled state in the same redox buffers.

13 binds to melanin and cooperatively increases redox buffering.

14 in thiol redox signaling and acts as a major redox buffer against reactive oxygen species, helping to

15 l-glycine, GSH) has vital functions as thiol redox buffer and cofactor of antioxidant and detoxificat

16 M may preserve Fe(II) by functioning both as redox buffer and complexant, which may help explain the

17 omises production of glutathione, a critical redox buffer and enzymatic cofactor.

18 zed and reduced species of a redox couple as redox buffer and used them to make SC-ISEs that exhibite

19 The metabolites that function in thiol redox buffering and homeostasis in Bacillus are not well

20 logens accelerate the redox equilibration of redox buffers and [Fe(4)S(4)](B) during catalysis.

21 ature, as evidenced by precursor behavior in redox buffers and by thermodynamic calculations.

22 ridyl, which makes it possible to extend the redox buffer approach to ionophore-based ISEs.

23 is not only an important intracellular thiol redox buffer but also a cofactor for several redox activ

24 med that cysteine is the major intracellular redox buffer by showing that T. vaginalis contains high

25 V) dissolution at S/Fe = 0.112 is due to the redox buffer capacity of FeS, which is evidenced by the

26 rations in this pathway could compromise the redox buffering capacity of cells, which may in turn be

27 ll size, limited hydraulic conductivity, and redox buffering capacity.

28 es its contribution to glutathione-dependent redox-buffering capacity under ex vivo conditions in bra

29 s intermediate layer based on the lipophilic redox buffer consisting of the Co(III) and Co(II) comple

30 ioxidants (e.g., ascorbic acid) and cellular redox buffers (e.g., glutathione), and the Abeta-Cu(I) c

31 ivity and was positively associated with the redox-buffering efficiency of tannins.

32 To create a more efficient redox buffer for the in vitro folding of disulfide conta

33 This application of redox buffers for controlled doping provides a new metho

34 wever, the effects of the composition of the redox buffer, GSSG and GSH, on folding has not been exte

35 This redox buffer has also been successfully applied to sodiu

36 e disulphide (GSSG) forms the most important redox buffer in organisms responsible for detoxification

37 A glutathione redox buffer increases the kcat for single-cysteine muta

38 Due to the high redox buffer intensity of heterogeneous mixed valent iro

39 inhibit isomerization and oxidize PDI when a redox buffer is not present to maintain the PDI redox st

40 chronic oxidative stress condition through a redox-buffering mechanism.

41 e-containing proteins is slow and involves a redox buffer of glutathione and glutathione disulfide.

42 In this study we tested the effect of redox buffer on platelet aggregation and the effect of r

43 Kinetic studies suggest that the redox buffer participates as the nucleophile and/or the

44 lecting compensatory increases in alterative redox-buffering pathways.

45 Here we report on an improved redox buffer platform based on equimolar amounts of the

46 ded proteins in the ER depends on an optimum redox buffer ratio.

47 In redox buffers, rLIN-12.1 forms only one disulfide isomer

48 ase in the ratio of the reduced and oxidized redox buffer species.

49 Glutathione and GSSG form the principle redox buffering system in the cell, with the endoplasmic

50 added back to alkali-treated microsomes in a redox buffer that reflected conditions found in the lume

51 In the absence of either QSOX or redox buffer, the fastest refolding of RfBP is accomplis

52 In the absence of a redox buffer, these steady-state reduction-oxidation cyc

53 w rate and the addition of hydroquinone as a redox buffer to the spray solvent were found to decrease

54 recursors to both guanidine denaturation and redox buffer unfolding are similar, as are in vitro fold

55 The refolding performed in glutathione redox buffer was quenched at different time points by ad

56 h agents manipulate the cellular glutathione redox buffer, we conclude that the observed effects of E

57 By reacting at this electrode, redox buffers were able to maintain electrode potentials

58 Several redox buffers were introduced for controlling electroche

59 Two types of redox buffers were used.

60 cult-to-handle modifications to the cellular redox buffer which can impair proper cellular function.

61 Melanin is a fungal extracellular redox buffer which, in principle, can neutralize antimic

62 Many of these reactions include a redox buffer, which is a mixture of a thiol (RSH) and th

63 t catalyzes protein disulfide formation in a redox buffer with an initial velocity that is 30-fold fa