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1 -sulfoxide reductase) and MsrB (methionine-R-sulfoxide reductase).
2 ide reductase, peroxiredoxin, and methionine sulfoxide reductase.
3 rsed by coexpression with peptide methionine sulfoxide reductase.
4 d by a ubiquitous enzyme, peptide methionine sulfoxide reductase.
5 ersed by treating the enzyme with methionine sulfoxide reductase.
6 idized protein was incubated with methionine sulfoxide reductase.
7 f stereospecific enzymes known as methionine sulfoxide reductases.
8 that are catalyzed by endogenous methionine sulfoxide reductases.
9 of glutathione peroxidase 1 and methionine-R-sulfoxide reductase 1 in the liver, suggesting partial s
11 KII inhibition, overexpression of methionine sulfoxide reductase A (an enzyme that reduces oxidized C
18 ant form of M. genitalium lacking methionine sulfoxide reductase A (MsrA), an antioxidant enzyme whic
19 CaMKII oxidation is reversed by methionine sulfoxide reductase A (MsrA), and MsrA-/- mice show exag
20 be reversed through the action of methionine sulfoxide reductase A (MsrA), which is implicated in oxi
22 strate almost absent catalase and methionine sulfoxide reductase A and B protein expression via immun
23 ) method for the determination of methionine sulfoxide reductase A and methionine sulfoxide reductase
27 led the redox relay mechanisms of methionine sulfoxide reductase A of the pathogen Corynebacterium di
28 uctase, glutathione reductase and methionine sulfoxide reductase A proteins were significantly up-reg
29 of only glutathione reductase and methionine sulfoxide reductase A proteins were significantly up-reg
30 ling by targeting the antioxidant methionine sulfoxide reductase A to modulate liposarcoma cell survi
31 cted transgenic overexpression of methionine sulfoxide reductase A, an enzyme that reduces oxidized C
32 oxide dismutase (SOD2), catalase, methionine sulfoxide reductase A, and the 20S proteasome subunits P
33 ues of diverse targets, including methionine sulfoxide reductase A, myosin light chain kinase, and Ru
34 er-expression of a repair enzyme, methionine sulfoxide reductase A, rendered them resistant, suggesti
36 idues in proteins is catalyzed by methionine sulfoxide reductases A (MSRA) and B (MSRB), which act in
37 In normal healthy human skin, methionine sulfoxide reductases A and B specifically reduce methion
41 ional selenoproteins, including methionine-S-sulfoxide reductase, a selenoprotein specific to Chlamyd
42 iform selenium deficiency because methionine sulfoxide reductase activities were similar in mice and
43 cleus and exhibited the highest methionine-R-sulfoxide reductase activity because of the presence of
44 y, the soluble 83-kDa enzyme retained biotin sulfoxide reductase activity using reduced methyl violog
45 ) were essential for MoCo-dependent dimethyl sulfoxide reductase activity, suggesting that these prot
47 nsible for this function: MsrA (methionine-S-sulfoxide reductase) and MsrB (methionine-R-sulfoxide re
48 e reductase, Rhodobacter capsulatus dimethyl sulfoxide reductase, and Shewanella massilia trimethylam
53 hionine sulfoxide reductase A and methionine sulfoxide reductase B activities in mouse liver is descr
55 onjunction with Mical proteins, methionine-R-sulfoxide reductase B1 (MsrB1) regulates mammalian actin
57 lamine-N-oxide reductase (TMAOR), and biotin sulfoxide reductase (BSOR) are members of a class of bac
58 cter sphaeroides f. sp. denitrificans biotin sulfoxide reductase (BSOR) catalyzes the reduction of d-
60 d that expression of yeast free methionine-R-sulfoxide reductase can fully compensate for this defici
61 cter sphaeroides f. sp. denitrificans biotin sulfoxide reductase catalyzes the reduction of d-biotin
62 Enzymes belonging to the bacterial dimethyl sulfoxide reductase (DMSOR) family contain a metal-bis-p
65 tic intermediate in the reaction of dimethyl sulfoxide reductase (DMSOR) with (CH(3))(3)NO has been p
68 plastidial thiol peroxidases and methionine sulfoxide reductases employing a single cysteine residue
71 gnificant homology to the peptide methionine sulfoxide reductase family of enzymes, specifically MsrA
72 s protein is the only member of the dimethyl sulfoxide reductase family of molybdopterin enzymes that
73 ydrogenase is a novel member of the dimethyl sulfoxide reductase family of molybdopterin-containing e
75 tudies of the molybdenum-containing dimethyl sulfoxide reductase from Rhodobacter sphaeroides have yi
76 eversion of knockout mutations in the biotin sulfoxide reductase gene, bisC, has 64% base sequence id
77 cter sphaeroides f. sp. denitrificans biotin sulfoxide reductase has been heterologously expressed in
78 sely related MGD-containing enzyme, dimethyl sulfoxide reductase, has indicated a number of conserved
80 and oxidized apoA-I treated with methionine sulfoxide reductase implicate oxidation of specific tyro
81 expression of Rhodobacter sphaeroides biotin sulfoxide reductase in Escherichia coli were modified, r
83 repair of oxidized calmodulin by methionine sulfoxide reductase induces comparable changes in alpha-
85 the active site cysteine of mouse methionine sulfoxide reductase is 7.2 even in the absence of substr
86 methionine residues performed by methionine sulfoxide reductase is important for the gastric pathoge
89 cepted, primarily from studies on methionine sulfoxide reductase (Msr) A, that the biological reducin
93 phaS are excellent substrates for methionine sulfoxide reductase (Msr), thereby providing an efficien
95 the reducing requirement for the methionine sulfoxide reductases (Msr), we have shown that thioredox
99 pair oxidized residues, including methionine sulfoxide reductases MsrA and MsrB, which reduce methion
100 reduced back to methionines by methionine-S-sulfoxide reductase (MsrA) and methionine-R-sulfoxide re
101 in proteins can be repaired by methionine-S-sulfoxide reductase (MsrA) and methionine-R-sulfoxide re
102 ulting methionine sulfoxides by methionine-S-sulfoxide reductase (MsrA) and methionine-R-sulfoxide re
105 have investigated the ability of methionine sulfoxide reductase (MsrA) to maintain optimal calmoduli
109 carboxyl terminus of the peptide-methionine sulfoxide reductase (MsrA), a repair enzyme, from Helico
110 nrelated protein known as peptide methionine sulfoxide reductase (MsrA), an antioxidant repair enzyme
111 in cytochrome c peroxidase (ccp), methionine sulfoxide reductase (msrA), or the metal-binding protein
112 lpha/beta-type SASP with peptidyl methionine sulfoxide reductase (MsrA), which can reduce methionine
113 med this compound by import and methionine-S-sulfoxide reductase (MsrA)-dependent reduction, but meth
120 S) elements, one of which was a methionine-R-sulfoxide reductase (MsrB) homolog from Metridium senile
125 reversible through the action of methionine sulfoxide reductases (MSRs), which play key roles in lif
128 a model, we show that of the two methionine sulfoxide reductases (MXR1, MXR2), deletion of mitochond
130 he ycbX- and yiiM-dependent pathways, biotin sulfoxide reductase plays also a role in the detoxificat
133 ants and a mutant lacking peptide methionine sulfoxide reductase (pmsr2-1) showed increased protein o
134 1 cells expressing a yeast free methionine-R-sulfoxide reductase proliferated in the presence of eith
135 y evolved Sec-containing forms of methionine sulfoxide reductases reflect catalytic advantages provid
138 g the structures for R. sphaeroides dimethyl sulfoxide reductase, Rhodobacter capsulatus dimethyl sul
139 e intracellular and extracellular methionine sulfoxide reductases (SpMsrAB1 and SpMsrAB2, respectivel
141 n-Benson-Bassham, dinitrogenase and dimethyl sulfoxide reductase systems, were probed in strains grow
143 UGA) of Mycoplasma pneumoniae and methionine sulfoxide reductase (two UGAs) of Mycoplasma genitalium.
144 eins involving the enzyme peptide methionine sulfoxide reductase type A (MSRA) is postulated to serve
145 man spectra previously reported for dimethyl sulfoxide reductase, vibrational modes associated with a
147 (MsrA)-dependent reduction, but methionine-R-sulfoxide reductases were not involved in this process,
150 Reduction back to methionine by methionine sulfoxide reductases would allow the antioxidant system
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