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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
12                                              Methionine sulfoxide reductase A (MsrA) catalyzes the re
13                           The enzyme peptide methionine sulfoxide reductase A (MSRA) catalyzes the re
14 o lower laying rate, egg mass, expression of methionine sulfoxide reductase A (MSRA) gene, and antiox
15                                              Methionine sulfoxide reductase A (MsrA) is an antioxidan
16                                              Methionine sulfoxide reductase A (MsrA) is an enzyme inv
17                                              Methionine sulfoxide reductase A (MsrA) maintains the fu
18 quitously expressed methionine repair enzyme methionine sulfoxide reductase A (MsrA) on the metabolic
19                                              Methionine sulfoxide reductase A (MsrA) repairs oxidized
20  that a mutant form of M. genitalium lacking methionine sulfoxide reductase A (MsrA), an antioxidant
21              CaMKII oxidation is reversed by methionine sulfoxide reductase A (MsrA), and MsrA-/- mic
22                         Here, we report that methionine sulfoxide reductase A (MSRA), which can reduc
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
27                                              Methionine sulfoxide reductase A is an essential enzyme
28                                              Methionine sulfoxide reductase A is an essential enzyme
29                                Lipidation of methionine sulfoxide reductase A occurs in the mouse, in
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
39  of myristoylated and nonmyristoylated mouse methionine sulfoxide reductase A.
40  (MetO) residues in proteins is catalyzed by methionine sulfoxide reductases A (MSRA) and B (MSRB), w
41                In normal healthy human skin, methionine sulfoxide reductases A and B specifically red
42 S) can be repaired in the human epidermis by methionine sulfoxide reductases A and B, respectively.
43                                       MSRAs (methionine sulfoxide reductases A) are enzymes that reve
44          Inactivation of HypT depends on the methionine sulfoxide reductases A/B.
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
47                Besides, higher expression of methionine sulfoxide reductase and cysteine peroxiredoxi
48                                              Methionine sulfoxide reductases are conserved enzymes th
49                                      Peptide methionine sulfoxide reductases are conserved enzymes th
50                                              Methionine sulfoxide reductases are key enzymes that rep
51                                              Methionine-sulfoxide reductases are unique, in that thei
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
54  fraction of inactivated GroEL by the enzyme methionine sulfoxide reductase B/A (MsrB/A).
55                   We further expressed mouse methionine sulfoxide reductase B1 (MsrB1), a selenoenzym
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
58                The enzymatic activity of the methionine sulfoxide reductase DmsABC helps Salmonella m
59 activity of plastidial thiol peroxidases and methionine sulfoxide reductases employing a single cyste
60                                              Methionine sulfoxide reductase enzymes MsrA and MsrB hav
61 liquid-like droplets in a manner reversed by methionine sulfoxide reductase enzymes.
62 ossesses significant homology to the peptide methionine sulfoxide reductase family of enzymes, specif
63                                      Here, a methionine sulfoxide reductase gene (AdMsrB1) was identi
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
67      This characteristic supports a role for methionine sulfoxide reductase in redox signaling.
68 ding or the repair of oxidized calmodulin by methionine sulfoxide reductase induces comparable change
69                 However, the identity of all methionine sulfoxide reductases involved, their cellular
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
72            Deletion or mutation in conserved methionine sulfoxide reductases leads to aging and sever
73 enerally accepted, primarily from studies on methionine sulfoxide reductase (Msr) A, that the biologi
74                                          The methionine sulfoxide reductase (MSR) enzyme converts Met
75                                              Methionine sulfoxide reductase (MSR) enzyme converts Met
76 presses antioxidant enzymes, among which are methionine sulfoxide reductase (Msr) enzymes, which are
77                                  The role of methionine sulfoxide reductase (Msr), a methionine repai
78  Met5 of alphaS are excellent substrates for methionine sulfoxide reductase (Msr), thereby providing
79 Met sulfoxide can be repaired back to Met by methionine sulfoxide reductase (Msr).
80 nt study on the reducing requirement for the methionine sulfoxide reductases (Msr), we have shown tha
81 f methionine sulfoxide (MetO) is mediated by methionine sulfoxide reductases (Msr).
82 ein functional changes through the action of methionine sulfoxide reductases (Msr).
83                           Here we used yeast methionine sulfoxide reductases MsrA and MsrB to address
84 teins or repair oxidized residues, including methionine sulfoxide reductases MsrA and MsrB, which red
85 erations of RecA activity were suppressed by methionine sulfoxide reductases MsrA and MsrB.
86                                      Peptide methionine sulfoxide reductase (MsrA) repairs oxidative
87                                      Peptide methionine sulfoxide reductase (MsrA) reverses oxidative
88          We have investigated the ability of methionine sulfoxide reductase (MsrA) to maintain optima
89                         A gene homologous to methionine sulfoxide reductase (msrA) was identified as
90                            The yeast peptide-methionine sulfoxide reductase (MsrA) was overexpressed
91                       We report that peptide methionine sulfoxide reductase (MsrA), a repair enzyme,
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
96 ly matches that of only one protein, peptide methionine sulfoxide reductase (MsrA).
97 ations are readily repaired by the action of methionine sulfoxide reductase (MsrA).
98                                      Peptide methionine sulfoxide reductase (MsrA; EC ) catalyzes the
99                                      Peptide methionine sulfoxide reductase (MsrA; EC ) reverses the
100                                      Peptide methionine sulfoxide reductase (MsrA; EC 1.8.4.6) is a u
101                                      Peptide methionine sulfoxide reductases (MsrA) from many differe
102           Moreover, we show that periplasmic methionine sulfoxide reductase (MsrP) is part of the Cpx
103 the E. coli periplasmic molybdenum-dependent methionine sulfoxide reductase (MsrP).
104                                              Methionine sulfoxide reductases (MSRs) are key enzymes i
105                                              Methionine sulfoxide reductases (Msrs) are oxidoreductas
106 s damage is reversible through the action of methionine sulfoxide reductases (MSRs), which play key r
107 ically oxidized, and subsequently reduced by methionine sulfoxide reductases (Msrs).
108 n is catalyzed by a family of enzymes called methionine sulfoxide reductases (MSRs).
109 oxidized methionine residues is catalyzed by methionine sulfoxide reductases (Msrs).
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
112                       In contrast, CshA- and methionine sulfoxide reductase-negative (MsrA-) strains
113                                      Peptide methionine sulfoxide reductase (PMSR) is a ubiquitous en
114 ild-type plants and a mutant lacking peptide methionine sulfoxide reductase (pmsr2-1) showed increase
115                         The highly conserved methionine sulfoxide reductases protect proteins from ox
116 sporadically evolved Sec-containing forms of methionine sulfoxide reductases reflect catalytic advant
117                     Reversing oxidation with methionine sulfoxide reductase restored HDL's ability to
118 rx2) and the intracellular and extracellular methionine sulfoxide reductases (SpMsrAB1 and SpMsrAB2,
119                  MsrPQ is a newly identified methionine sulfoxide reductase system found in bacteria,
120              MtsZ is a molybdenum-containing methionine sulfoxide reductase that supports virulence i
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
123                                              Methionine sulfoxide reductase, which reduces methionine
124                           Most cells contain methionine sulfoxide reductases, which catalyze a thiore
125              Reduction back to methionine by methionine sulfoxide reductases would allow the antioxid

 
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