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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
18 lized by the covalent attachment of a cobalt redox buffer and used as a new solid contact for ion-sel
19 zed and reduced species of a redox couple as redox buffer and used them to make SC-ISEs that exhibite
28 s surface-attached CIM-ph-Tpy-Co(III/II)-Tpy redox buffer as a solid contact were tested as K(+) sens
29 emerged as key species involved in cellular redox buffering as well as RSS generation, translocation
30 is not only an important intracellular thiol redox buffer but also a cofactor for several redox activ
31 med that cysteine is the major intracellular redox buffer by showing that T. vaginalis contains high
32 V) dissolution at S/Fe = 0.112 is due to the redox buffer capacity of FeS, which is evidenced by the
33 rations in this pathway could compromise the redox buffering capacity of cells, which may in turn be
35 es its contribution to glutathione-dependent redox-buffering capacity under ex vivo conditions in bra
36 , and that the rate of electron flux through redox buffering circuits is directly linked to changes i
37 s-induced JH(2)O(2) production to NNT-linked redox buffering circuits provides a potential means of i
38 is reduced to H(2)O by electrons drawn from redox buffering circuits supplied by NADPH, and that the
40 ized PVC membranes, along with a hydrophilic redox buffer composed of ferrocyanide and ferricyanide t
41 s intermediate layer based on the lipophilic redox buffer consisting of the Co(III) and Co(II) comple
42 HCY regulate spare respiratory capacity, the redox buffer cystathionine, lipid and amino acid metabol
43 cs and lipidomics revealed elevations in the redox buffers cystathionine, hexosylceramides, and gluco
44 ioxidants (e.g., ascorbic acid) and cellular redox buffers (e.g., glutathione), and the Abeta-Cu(I) c
46 environment without reducing agents and in a redox-buffered environment by adding redox mediator 9,10
49 wever, the effects of the composition of the redox buffer, GSSG and GSH, on folding has not been exte
51 e disulphide (GSSG) forms the most important redox buffer in organisms responsible for detoxification
52 he host is cysteine, which acts as the major redox buffer in the blood by transitioning between reduc
55 inhibit isomerization and oxidize PDI when a redox buffer is not present to maintain the PDI redox st
58 e-containing proteins is slow and involves a redox buffer of glutathione and glutathione disulfide.
59 r study reveals that spermine metabolism via redox buffering of the ER underpins appressorial adhesio
68 cohols to afford benzyl ethers, enabled by a redox-buffering strategy that maintains the activity of
70 added back to alkali-treated microsomes in a redox buffer that reflected conditions found in the lume
73 w rate and the addition of hydroquinone as a redox buffer to the spray solvent were found to decrease
74 recursors to both guanidine denaturation and redox buffer unfolding are similar, as are in vitro fold
76 h agents manipulate the cellular glutathione redox buffer, we conclude that the observed effects of E
80 cult-to-handle modifications to the cellular redox buffer which can impair proper cellular function.
83 t catalyzes protein disulfide formation in a redox buffer with an initial velocity that is 30-fold fa