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1 oteins containing an active site cysteine or cysteine sulfenic acid.
2 served cysteine residue to the corresponding cysteine-sulfenic acid, and perhaps to higher oxidation
8 As a posttranslational protein modification, cysteine sulfenic acid (Cys-SOH) is well established as
9 4-nitrobenzo-2-oxa-1,3-diazole to identify a cysteine sulfenic acid (Cys-SOH) modification that forms
11 for more than 20 years that unusually stable cysteine-sulfenic acid (Cys-SOH) derivatives can be intr
17 e have examined the importance of reversible cysteine sulfenic acid formation in naive CD8(+) T cell
18 r, these results demonstrate that reversible cysteine sulfenic acid formation is an important regulat
20 To examine the contribution of reversible cysteine sulfenic acid formation to T cell activation, i
22 ion reaction and the subsequent reactions of cysteine sulfenic acid have been studied by stopped-flow
27 a-1, 3-diazole (NBD-Cl), it was shown that a cysteine sulfenic acid intermediate (Cys-SOH) is formed
29 of reaction intermediates and implicate the cysteine-sulfenic acid ligand as the catalytic nucleophi
30 nds and is sensitive to oxidation; thus, the cysteine sulfenic acid may play a role in the regulation
31 ith increased oxidant damage, which led to a cysteine sulfenic acid modification in endothelin B rece
32 r substitution at position 420 that mimics a cysteine sulfenic acid results in a ~4-fold increase in
33 In contrast, the E18D mutation stabilizes a cysteine-sulfenic acid that is readily reduced to the th
34 t reaction suggests that the condensation of cysteine sulfenic acid to give cysteine thiosulfinate es
35 emonstrated that the reversible formation of cysteine sulfenic acid was critical for ERK1/2 phosphory
37 lowed by rate-limiting comproportionation of cysteine sulfenic acid with cysteinate to give cystine.
38 lowed by rate-limiting comproportionation of cysteine sulfenic acid with cysteinate to give cystine.
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