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1 it is reversed by coexpression with peptide methionine sulfoxide reductase.
2 ion mediated by a ubiquitous enzyme, peptide methionine sulfoxide reductase.
3 s, in particular alkenal reductase PTGR1 and methionine sulfoxide reductase.
4 BC transporter solute-binding protein, and a methionine sulfoxide reductase.
5 ould be reversed by treating the enzyme with methionine sulfoxide reductase.
6 and the oxidized protein was incubated with methionine sulfoxide reductase.
7 ribonucleotide reductase, peroxiredoxin, and methionine sulfoxide reductase.
8 he action of stereospecific enzymes known as methionine sulfoxide reductases.
9 so observed that are catalyzed by endogenous methionine sulfoxide reductases.
10 thione peroxidase, ascorbate peroxidase, and methionine sulfoxide reductase 2) are slightly up-regula
11 cardial CaMKII inhibition, overexpression of methionine sulfoxide reductase A (an enzyme that reduces
14 o lower laying rate, egg mass, expression of methionine sulfoxide reductase A (MSRA) gene, and antiox
18 quitously expressed methionine repair enzyme methionine sulfoxide reductase A (MsrA) on the metabolic
20 that a mutant form of M. genitalium lacking methionine sulfoxide reductase A (MsrA), an antioxidant
23 n that can be reversed through the action of methionine sulfoxide reductase A (MsrA), which is implic
24 n-like domain (NT domain) is fused to tandem methionine sulfoxide reductase A and B domains (MsrA/B).
25 r, we demonstrate almost absent catalase and methionine sulfoxide reductase A and B protein expressio
26 horesis (CE) method for the determination of methionine sulfoxide reductase A and methionine sulfoxid
30 have unraveled the redox relay mechanisms of methionine sulfoxide reductase A of the pathogen Coryneb
31 quinone reductase, glutathione reductase and methionine sulfoxide reductase A proteins were significa
32 xpressions of only glutathione reductase and methionine sulfoxide reductase A proteins were significa
33 ecies signaling by targeting the antioxidant methionine sulfoxide reductase A to modulate liposarcoma
34 TARD3 as an in vivo binding partner of MSRA (methionine sulfoxide reductase A), an enzyme that reduce
35 dium-restricted transgenic overexpression of methionine sulfoxide reductase A, an enzyme that reduces
36 dants superoxide dismutase (SOD2), catalase, methionine sulfoxide reductase A, and the 20S proteasome
37 ysine residues of diverse targets, including methionine sulfoxide reductase A, myosin light chain kin
38 whereas over-expression of a repair enzyme, methionine sulfoxide reductase A, rendered them resistan
40 (MetO) residues in proteins is catalyzed by methionine sulfoxide reductases A (MSRA) and B (MSRB), w
42 S) can be repaired in the human epidermis by methionine sulfoxide reductases A and B, respectively.
45 ained by uniform selenium deficiency because methionine sulfoxide reductase activities were similar i
46 m Escherichia coli and the electron acceptor methionine sulfoxide reductase, also from E. coli, stron
52 tion of methionine sulfoxide reductase A and methionine sulfoxide reductase B activities in mouse liv
53 o binding MSRA, STARD3 binds all three MSRB (methionine sulfoxide reductase B), enzymes that reduce m
56 lly, we found that a cytosolic pool of human methionine sulfoxide reductase B2 (MsrB2) is strongly re
57 ne residues to methionine sulfoxide, and the methionine sulfoxide reductases catalyze their reduction
59 activity of plastidial thiol peroxidases and methionine sulfoxide reductases employing a single cyste
62 ossesses significant homology to the peptide methionine sulfoxide reductase family of enzymes, specif
64 a proof of principle, fluorogenic probes for methionine sulfoxide reductases have been developed.
65 these genes are fused to form a bifunctional methionine sulfoxide reductase (i.e., MsrBA) enzyme.
66 s of apoA-I and oxidized apoA-I treated with methionine sulfoxide reductase implicate oxidation of sp
68 ding or the repair of oxidized calmodulin by methionine sulfoxide reductase induces comparable change
70 e pK(a) of the active site cysteine of mouse methionine sulfoxide reductase is 7.2 even in the absenc
71 of oxidized methionine residues performed by methionine sulfoxide reductase is important for the gast
73 enerally accepted, primarily from studies on methionine sulfoxide reductase (Msr) A, that the biologi
76 presses antioxidant enzymes, among which are methionine sulfoxide reductase (Msr) enzymes, which are
78 Met5 of alphaS are excellent substrates for methionine sulfoxide reductase (Msr), thereby providing
80 nt study on the reducing requirement for the methionine sulfoxide reductases (Msr), we have shown tha
84 teins or repair oxidized residues, including methionine sulfoxide reductases MsrA and MsrB, which red
92 ty with the carboxyl terminus of the peptide-methionine sulfoxide reductase (MsrA), a repair enzyme,
93 ted by an unrelated protein known as peptide methionine sulfoxide reductase (MsrA), an antioxidant re
94 an mutants in cytochrome c peroxidase (ccp), methionine sulfoxide reductase (msrA), or the metal-bind
95 oxidized alpha/beta-type SASP with peptidyl methionine sulfoxide reductase (MsrA), which can reduce
106 s damage is reversible through the action of methionine sulfoxide reductases (MSRs), which play key r
110 versible and is regulated by the cytoplasmic methionine sulfoxide reductase Mxr1 (MsrA) and a previou
111 revisiae as a model, we show that of the two methionine sulfoxide reductases (MXR1, MXR2), deletion o
114 ild-type plants and a mutant lacking peptide methionine sulfoxide reductase (pmsr2-1) showed increase
116 sporadically evolved Sec-containing forms of methionine sulfoxide reductases reflect catalytic advant
118 rx2) and the intracellular and extracellular methionine sulfoxide reductases (SpMsrAB1 and SpMsrAB2,
121 hesin (one UGA) of Mycoplasma pneumoniae and methionine sulfoxide reductase (two UGAs) of Mycoplasma
122 ine in proteins involving the enzyme peptide methionine sulfoxide reductase type A (MSRA) is postulat