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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
10 xidase, ascorbate peroxidase, and methionine sulfoxide reductase 2) are slightly up-regulated.
11 KII inhibition, overexpression of methionine sulfoxide reductase A (an enzyme that reduces oxidized C
12                                   Methionine sulfoxide reductase A (MsrA) catalyzes the reduction of
13                The enzyme peptide methionine sulfoxide reductase A (MSRA) catalyzes the repair of oxi
14                                   Methionine sulfoxide reductase A (MsrA) is an antioxidant repair en
15                                   Methionine sulfoxide reductase A (MsrA) is an enzyme involved in re
16                                   Methionine sulfoxide reductase A (MsrA) maintains the function of m
17                                   Methionine sulfoxide reductase A (MsrA) repairs oxidized methionine
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
21 in (NT domain) is fused to tandem methionine sulfoxide reductase A and B domains (MsrA/B).
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
24                                   Methionine sulfoxide reductase A is an essential enzyme in the anti
25                                   Methionine sulfoxide reductase A is an essential enzyme in the anti
26                     Lipidation of methionine sulfoxide reductase A occurs in the mouse, in transfecte
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
35 ylated and nonmyristoylated mouse methionine sulfoxide reductase A.
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
38 epaired in the human epidermis by methionine sulfoxide reductases A and B, respectively.
39                            MSRAs (methionine sulfoxide reductases A) are enzymes that reverse the eff
40 activation of HypT depends on the methionine sulfoxide reductases A/B.
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
46 reduced pyridine nucleotide-dependent biotin sulfoxide reductase activity.
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
49                           Peptide methionine sulfoxide reductases are conserved enzymes that reduce o
50                                   Methionine sulfoxide reductases are conserved enzymes that reduce o
51                                   Methionine sulfoxide reductases are key enzymes that repair oxidati
52                                   Methionine-sulfoxide reductases are unique, in that their ability t
53 hionine sulfoxide reductase A and methionine sulfoxide reductase B activities in mouse liver is descr
54 f inactivated GroEL by the enzyme methionine sulfoxide reductase B/A (MsrB/A).
55 onjunction with Mical proteins, methionine-R-sulfoxide reductase B1 (MsrB1) regulates mammalian actin
56        We further expressed mouse methionine sulfoxide reductase B1 (MsrB1), a selenoenzyme that cata
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-
59               Rhodobacter sphaeroides biotin sulfoxide reductase (BSOR) contains the bis(molybdopteri
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
63 of bis-molybdopterin enzymes of the dimethyl sulfoxide reductase (DMSOR) family.
64 ed with those of previously studied dimethyl sulfoxide reductase (DMSOr) models.
65 tic intermediate in the reaction of dimethyl sulfoxide reductase (DMSOR) with (CH(3))(3)NO has been p
66                                     Dimethyl sulfoxide reductase (DMSOR), trimethylamine-N-oxide redu
67 cofactor in Rhodobacter sphaeroides dimethyl sulfoxide reductase (DMSOR).
68  plastidial thiol peroxidases and methionine sulfoxide reductases employing a single cysteine residue
69                                   Methionine sulfoxide reductase enzymes MsrA and MsrB have complemen
70 f recombinant Rhodobacter sphaeroides biotin sulfoxide reductase expressed in Escherichia coli.
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
74 olybdenum containing enzymes of the dimethyl sulfoxide reductase family.
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
79  are fused to form a bifunctional methionine sulfoxide reductase (i.e., MsrBA) enzyme.
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
82 haracteristic supports a role for methionine sulfoxide reductase in redox signaling.
83  repair of oxidized calmodulin by methionine sulfoxide reductase induces comparable changes in alpha-
84      However, the identity of all methionine sulfoxide reductases involved, their cellular locations
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
87                                       Biotin sulfoxide reductase is not reduced by biotin or the nonp
88             The results indicate that biotin sulfoxide reductase is thermodynamically tuned to cataly
89 cepted, primarily from studies on methionine sulfoxide reductase (Msr) A, that the biological reducin
90                               The methionine sulfoxide reductase (MSR) enzyme converts MetSO back to
91                                   Methionine sulfoxide reductase (MSR) enzyme converts MetSO back to
92                       The role of methionine sulfoxide reductase (Msr), a methionine repair enzyme, i
93 phaS are excellent substrates for methionine sulfoxide reductase (Msr), thereby providing an efficien
94 de can be repaired back to Met by methionine sulfoxide reductase (Msr).
95  the reducing requirement for the methionine sulfoxide reductases (Msr), we have shown that thioredox
96 e sulfoxide (MetO) is mediated by methionine sulfoxide reductases (Msr).
97 nal changes through the action of methionine sulfoxide reductases (Msr).
98                Here we used yeast methionine sulfoxide reductases MsrA and MsrB to address this hypot
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
103                           Peptide methionine sulfoxide reductase (MsrA) repairs oxidative damage to m
104                           Peptide methionine sulfoxide reductase (MsrA) reverses oxidative damage to
105  have investigated the ability of methionine sulfoxide reductase (MsrA) to maintain optimal calmoduli
106              A gene homologous to methionine sulfoxide reductase (msrA) was identified as the predict
107                 The yeast peptide-methionine sulfoxide reductase (MsrA) was overexpressed in a Saccha
108            We report that peptide methionine sulfoxide reductase (MsrA), a repair enzyme, contributes
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
114 that of only one protein, peptide methionine sulfoxide reductase (MsrA).
115 readily repaired by the action of methionine sulfoxide reductase (MsrA).
116                           Peptide methionine sulfoxide reductase (MsrA; EC ) catalyzes the reduction
117                           Peptide methionine sulfoxide reductase (MsrA; EC ) reverses the inactivatio
118                           Peptide methionine sulfoxide reductase (MsrA; EC 1.8.4.6) is a ubiquitous p
119                           Peptide methionine sulfoxide reductases (MsrA) from many different organism
120 S) elements, one of which was a methionine-R-sulfoxide reductase (MsrB) homolog from Metridium senile
121 -sulfoxide reductase (MsrA) and methionine-R-sulfoxide reductase (MsrB).
122 -sulfoxide reductase (MsrA) and methionine-R-sulfoxide reductase (MsrB).
123 -sulfoxide reductase (MsrA) and methionine-R-sulfoxide reductase (MsrB).
124                                   Methionine sulfoxide reductases (Msrs) are oxidoreductases that cat
125  reversible through the action of methionine sulfoxide reductases (MSRs), which play key roles in lif
126 thionine residues is catalyzed by methionine sulfoxide reductases (Msrs).
127 zed by a family of enzymes called methionine sulfoxide reductases (MSRs).
128  a model, we show that of the two methionine sulfoxide reductases (MXR1, MXR2), deletion of mitochond
129            In contrast, CshA- and methionine sulfoxide reductase-negative (MsrA-) strains neither adh
130 he ycbX- and yiiM-dependent pathways, biotin sulfoxide reductase plays also a role in the detoxificat
131                       The enzyme peptide Met sulfoxide reductase (PMSR) catalyzes the reduction of Me
132                           Peptide methionine sulfoxide reductase (PMSR) is a ubiquitous enzyme that r
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
136 icroM for reduced methyl viologen and biotin sulfoxide reductase, respectively.
137          Reversing oxidation with methionine sulfoxide reductase restored HDL's ability to activate L
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
140       MsrPQ is a newly identified methionine sulfoxide reductase system found in bacteria, which appe
141 n-Benson-Bassham, dinitrogenase and dimethyl sulfoxide reductase systems, were probed in strains grow
142        (2-Ad = 2-adamantyl, DMSOR = dimethyl sulfoxide reductase, TMAOR = trimethylamine N-oxide redu
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
146                                       Biotin sulfoxide reductase was also capable of reducing nicotin
147 (MsrA)-dependent reduction, but methionine-R-sulfoxide reductases were not involved in this process,
148                                   Methionine sulfoxide reductase, which reduces methionine sulfoxide
149                Most cells contain methionine sulfoxide reductases, which catalyze a thioredoxin-depen
150   Reduction back to methionine by methionine sulfoxide reductases would allow the antioxidant system

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