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1 ynureninyl products as well as betaMet-55 to methionine sulfoxide.
2 elding both the (R) and (S) diastereomers of methionine sulfoxide.
3 non-polar methionine to the more hydrophilic methionine sulfoxide.
4 ected SO band at 1025 cm-1 characteristic of methionine sulfoxide.
5  of one of the peptides had been oxidized to methionine sulfoxide.
6  could not grow, in the presence of H2O2 and methionine sulfoxide.
7  yeast strain could grow on either form of L-methionine sulfoxide.
8 on of surface-exposed methionine residues to methionine sulfoxide.
9 ontaining DmsABC enzymatic complex to reduce methionine sulfoxide.
10 ted four out of nine Met residues of RecA to methionine sulfoxide.
11 by phagocytes oxidize methionine, generating methionine sulfoxide.
12 residues are posttranslationally oxidized to methionine sulfoxide.
13 eferentially targeted, forming predominantly methionine sulfoxide.
14 HypT is activated by methionine oxidation to methionine sulfoxide.
15 e reaction, oxidizing methionine residues to methionine sulfoxide.
16 ic oxidation and reduction of methionine and methionine sulfoxide.
17 thionine and is specific for the S epimer of methionine sulfoxide.
18 rrelated and also correlated positively with methionine sulfoxide.
19 ic oxidation and reduction of methionine and methionine sulfoxide.
20 ndogenous methionines to their corresponding methionine sulfoxides.
21 ated CaMox, which varies from three to eight methionine sulfoxides.
22  multiple methionines to their corresponding methionine sulfoxides.
23 r/MsrA mutant could not grow on a mixture of methionine sulfoxides.
24 olysis of methionine gives rise primarily to methionine sulfoxide (+16 Da mass shift); this can be fu
25             Furthermore, peptides containing methionine sulfoxide, 3-chlorotyrosine, and nonspecific
26 d amino acid profile and increased levels of methionine sulfoxide, an oxidative stress biomarker, in
27 ich both methionine residues are oxidized to methionine sulfoxide and a control peptide consisting of
28 e msrA gene increases free and protein-bound methionine sulfoxide and decreases cell viability.
29 correlated with an increase in the levels of methionine sulfoxide and dityrosine.
30 rew better, had lower free and protein-bound methionine sulfoxide and had a better survival rate unde
31                         Singlet oxygen forms methionine sulfoxide and methionine sulfone.
32 al oxidative protein modifications involving methionine sulfoxide and nitrotyrosine.
33 shed through mass spectrometric detection of methionine sulfoxide and the reactivation of a significa
34               HOCl can oxidize methionine to methionine sulfoxide and tyrosine to chlorotyrosine.
35 amino acid methionine is readily oxidized to methionine sulfoxide, and its reduction is catalyzed by
36  malondialdehyde, protein carbonyls, protein methionine sulfoxide, and oxidized glutathione as well a
37 on of microcystins containing methionine and methionine sulfoxide, and reveals the oxidation state of
38 idants react readily with methionine to form methionine sulfoxide, and surface exposed methionine res
39 xygen species oxidize methionine residues to methionine sulfoxide, and the methionine sulfoxide reduc
40 n spectroscopy reveals the presence of H2O2, methionine sulfoxide, and tryptophan metabolites; i.e.,
41              We show that ortho-tyrosine and methionine sulfoxide are formed in concert with Nepsilon
42 eir corresponding oxidized forms cystine and methionine sulfoxide are presented.
43   This suggests that microcystins containing methionine sulfoxide are primarily postextraction oxidat
44 ver tissue confirms that both methionine and methionine-sulfoxide are significantly more elevated in
45 ereospecific methionine oxidase, producing S-methionine sulfoxide as its product.
46 to its facile oxidation via the formation of methionine sulfoxide, as shown by mass spectrometry.
47 is demonstrated that oxidation of Met-148 to methionine sulfoxide associated quantitatively with loss
48  the effects of oxidative damage by reducing methionine sulfoxide back to methionine and recovering p
49                              MSRs reduce the methionine sulfoxide back to methionine, restoring the a
50  oxidized methionine in proteins by reducing methionine sulfoxide back to methionine.
51 atalyze a thioredoxin-dependent reduction of methionine sulfoxide back to methionine.
52 he presence of Sec improves the reduction of methionine sulfoxide by MsrAs.
53               Quantification of the abundant methionine sulfoxide by NMR and MS gave highly comparabl
54 n be repaired via reduction of the resulting methionine sulfoxides by methionine-S-sulfoxide reductas
55  susceptible to oxidation, and the resulting methionine sulfoxides can be reduced back to methionines
56  oxidized proteins and MsrA, which reduces S-methionine sulfoxide, can protect lens cells against oxi
57 s are particularly sensitive to oxidation to methionine sulfoxide derivatives, these oxidations are r
58 sidues in proteins and peptides to (R and S)-methionine sulfoxide diasteriomers.
59 ification of methionine to the corresponding methionine sulfoxide does not predispose CaM to further
60 n was through the oxidation of methionine to methionine sulfoxide, established through mass spectrome
61 ctivate the PM Ca-ATPase results solely from methionine sulfoxide formation and (ii) MsrA can repair
62 idation of protein-bound methionines to form methionine sulfoxides has a broad range of biological ra
63 e roles of MsrB1, -B2 and -B3 which reduce R-methionine sulfoxide have not been established for any m
64              Substitution of methionine with methionine sulfoxide in a medium lacking hydrogen peroxi
65 ctional domains of ADAMTS13 were oxidized to methionine sulfoxide in an HOCl concentration-dependent
66 ine residues of ingested Escherichia coli to methionine sulfoxide in high yield.
67 , except that the myristoylated form reduced methionine sulfoxide in protein much faster than the non
68 e discuss how the oxidation of methionine to methionine sulfoxide in signalling proteins such as ion
69 -Raman Spectroscopy revealed the presence of methionine sulfoxide in the depigmented skin of patients
70 of Bacillus species were readily oxidized to methionine sulfoxide in vitro by t-butyl hydroperoxide (
71 hat MsrA is responsible for the reduction of methionine sulfoxide in vivo as well as in vitro in euka
72                           Repair of selected methionine sulfoxides in CaMox by MsrA results in a part
73                   Oxidation of methionine to methionine sulfoxide is a common form of damage observed
74                   Oxidation of methionine to methionine sulfoxide is a major oxidative stress product
75                           However, no single methionine sulfoxide is completely repaired in all CaM o
76   The oxidation of methionine in proteins to methionine sulfoxide is implicated in aging as well as i
77 lysis by reducing agents such as TCEP, while methionine sulfoxide is refractory to reduction by this
78 gments of CaMox vary by a factor of 2, where methionine sulfoxides located within hydrophobic sequenc
79 osition (x = 7, 9, and 11) of methionine (M)/methionine sulfoxide (M-ox) within the peptide sequences
80 that oxidation of the Met-35 side chain to a methionine sulfoxide (Met-35(ox)) significantly hinders
81 ctase (MsrA; EC ) catalyzes the reduction of methionine sulfoxide (Met-O) in proteins to methionine (
82 lot in association with a functional loss of methionine sulfoxide (Met-S=O) repair in the entire gray
83                       An enzyme that reduces methionine sulfoxide [Met(O)] residues in proteins [pept
84 epair enzyme that catalyzes the reduction of methionine sulfoxide [Met(O)] residues in proteins to me
85 ling, and their reversible oxidation to form methionine sulfoxides [Met(O)] in calmodulin (CaM) and o
86  of critical methionine residues by reducing methionine sulfoxide, Met(O), to methionine.
87                                 We show that methionine sulfoxide, methionine sulfone, N-formylkynure
88                             The reduction of methionine sulfoxide (MetO) is mediated by methionine su
89                          Mammals contain two methionine sulfoxide (MetO) reductases, MsrA and MsrB, t
90                                 Reduction of methionine sulfoxide (MetO) residues in proteins is cata
91  These latter small peptides are enriched in methionine sulfoxides (MetO), suggesting a preferential
92 e oxygen species (ROS) oxidize methionine to methionine sulfoxide (MetSO) and thereby inactivate prot
93 e oxygen species (ROS) oxidize methionine to methionine sulfoxide (MetSO) and thereby inactivate prot
94 ve developed a new technique for quantifying methionine sulfoxide (MetSO) in protein to assess levels
95 the oxidative stress-induced R enantiomer of methionine sulfoxide (MetSO), reducing it to methionine
96                    ROS oxidize methionine to methionine sulfoxide (MetSO), rendering several proteins
97 ies that reduce the S and R stereoisomers of methionine sulfoxide (MetSO), respectively, and together
98 es, which is illustrated in the synthesis of methionine sulfoxide (MSO).
99 nd conversion of some methionine residues to methionine sulfoxide (MSOX) residues.
100 tified the major metabolite, 3-nitrotyrosine-methionine-sulfoxide (NSO)-MENK, using liquid chromatogr
101 mmunosuppressive activity than their reduced methionine sulfoxide peptide forms 4 and 6, respectively
102 loped a sensitive method of quantitating the methionine sulfoxide present at position 213 (MetSO213)
103 r Met(146) in wheat germ calmodulin (CaM) to methionine sulfoxide prevents the CaM-dependent activati
104  commentary shows that both diastereomers of methionine sulfoxide (R and S) can be repaired in the hu
105 rves as an excellent model for protein-bound methionine sulfoxide recognition and repair.
106 these genes are fused to form a bifunctional methionine sulfoxide reductase (i.e., MsrBA) enzyme.
107 enerally accepted, primarily from studies on methionine sulfoxide reductase (Msr) A, that the biologi
108                                          The methionine sulfoxide reductase (MSR) enzyme converts Met
109                                              Methionine sulfoxide reductase (MSR) enzyme converts Met
110 presses antioxidant enzymes, among which are methionine sulfoxide reductase (Msr) enzymes, which are
111                                  The role of methionine sulfoxide reductase (Msr), a methionine repai
112  Met5 of alphaS are excellent substrates for methionine sulfoxide reductase (Msr), thereby providing
113 Met sulfoxide can be repaired back to Met by methionine sulfoxide reductase (Msr).
114                                      Peptide methionine sulfoxide reductase (MsrA) repairs oxidative
115                                      Peptide methionine sulfoxide reductase (MsrA) reverses oxidative
116          We have investigated the ability of methionine sulfoxide reductase (MsrA) to maintain optima
117                         A gene homologous to methionine sulfoxide reductase (msrA) was identified as
118                            The yeast peptide-methionine sulfoxide reductase (MsrA) was overexpressed
119 ty with the carboxyl terminus of the peptide-methionine sulfoxide reductase (MsrA), a repair enzyme,
120                       We report that peptide methionine sulfoxide reductase (MsrA), a repair enzyme,
121 ted by an unrelated protein known as peptide methionine sulfoxide reductase (MsrA), an antioxidant re
122 an mutants in cytochrome c peroxidase (ccp), methionine sulfoxide reductase (msrA), or the metal-bind
123  oxidized alpha/beta-type SASP with peptidyl methionine sulfoxide reductase (MsrA), which can reduce
124 ly matches that of only one protein, peptide methionine sulfoxide reductase (MsrA).
125 ations are readily repaired by the action of methionine sulfoxide reductase (MsrA).
126                                      Peptide methionine sulfoxide reductase (MsrA; EC ) catalyzes the
127                                      Peptide methionine sulfoxide reductase (MsrA; EC ) reverses the
128                                      Peptide methionine sulfoxide reductase (MsrA; EC 1.8.4.6) is a u
129           Moreover, we show that periplasmic methionine sulfoxide reductase (MsrP) is part of the Cpx
130 the E. coli periplasmic molybdenum-dependent methionine sulfoxide reductase (MsrP).
131                                      Peptide methionine sulfoxide reductase (PMSR) is a ubiquitous en
132 ild-type plants and a mutant lacking peptide methionine sulfoxide reductase (pmsr2-1) showed increase
133 hesin (one UGA) of Mycoplasma pneumoniae and methionine sulfoxide reductase (two UGAs) of Mycoplasma
134 thione peroxidase, ascorbate peroxidase, and methionine sulfoxide reductase 2) are slightly up-regula
135 cardial CaMKII inhibition, overexpression of methionine sulfoxide reductase A (an enzyme that reduces
136                           The enzyme peptide methionine sulfoxide reductase A (MSRA) catalyzes the re
137                                              Methionine sulfoxide reductase A (MsrA) catalyzes the re
138 o lower laying rate, egg mass, expression of methionine sulfoxide reductase A (MSRA) gene, and antiox
139                                              Methionine sulfoxide reductase A (MsrA) is an antioxidan
140                                              Methionine sulfoxide reductase A (MsrA) is an enzyme inv
141                                              Methionine sulfoxide reductase A (MsrA) maintains the fu
142 quitously expressed methionine repair enzyme methionine sulfoxide reductase A (MsrA) on the metabolic
143                                              Methionine sulfoxide reductase A (MsrA) repairs oxidized
144  that a mutant form of M. genitalium lacking methionine sulfoxide reductase A (MsrA), an antioxidant
145              CaMKII oxidation is reversed by methionine sulfoxide reductase A (MsrA), and MsrA-/- mic
146                         Here, we report that methionine sulfoxide reductase A (MSRA), which can reduc
147 n that can be reversed through the action of methionine sulfoxide reductase A (MsrA), which is implic
148 n-like domain (NT domain) is fused to tandem methionine sulfoxide reductase A and B domains (MsrA/B).
149 r, we demonstrate almost absent catalase and methionine sulfoxide reductase A and B protein expressio
150 horesis (CE) method for the determination of methionine sulfoxide reductase A and methionine sulfoxid
151                                              Methionine sulfoxide reductase A is an essential enzyme
152                                              Methionine sulfoxide reductase A is an essential enzyme
153                                Lipidation of methionine sulfoxide reductase A occurs in the mouse, in
154 have unraveled the redox relay mechanisms of methionine sulfoxide reductase A of the pathogen Coryneb
155 quinone reductase, glutathione reductase and methionine sulfoxide reductase A proteins were significa
156 xpressions of only glutathione reductase and methionine sulfoxide reductase A proteins were significa
157 ecies signaling by targeting the antioxidant methionine sulfoxide reductase A to modulate liposarcoma
158 TARD3 as an in vivo binding partner of MSRA (methionine sulfoxide reductase A), an enzyme that reduce
159 dium-restricted transgenic overexpression of methionine sulfoxide reductase A, an enzyme that reduces
160 dants superoxide dismutase (SOD2), catalase, methionine sulfoxide reductase A, and the 20S proteasome
161 ysine residues of diverse targets, including methionine sulfoxide reductase A, myosin light chain kin
162  whereas over-expression of a repair enzyme, methionine sulfoxide reductase A, rendered them resistan
163  of myristoylated and nonmyristoylated mouse methionine sulfoxide reductase A.
164 ained by uniform selenium deficiency because methionine sulfoxide reductase activities were similar i
165                Besides, higher expression of methionine sulfoxide reductase and cysteine peroxiredoxi
166 tion of methionine sulfoxide reductase A and methionine sulfoxide reductase B activities in mouse liv
167 o binding MSRA, STARD3 binds all three MSRB (methionine sulfoxide reductase B), enzymes that reduce m
168  fraction of inactivated GroEL by the enzyme methionine sulfoxide reductase B/A (MsrB/A).
169                   We further expressed mouse methionine sulfoxide reductase B1 (MsrB1), a selenoenzym
170 lly, we found that a cytosolic pool of human methionine sulfoxide reductase B2 (MsrB2) is strongly re
171                The enzymatic activity of the methionine sulfoxide reductase DmsABC helps Salmonella m
172                                              Methionine sulfoxide reductase enzymes MsrA and MsrB hav
173 liquid-like droplets in a manner reversed by methionine sulfoxide reductase enzymes.
174 ossesses significant homology to the peptide methionine sulfoxide reductase family of enzymes, specif
175                                      Here, a methionine sulfoxide reductase gene (AdMsrB1) was identi
176 s of apoA-I and oxidized apoA-I treated with methionine sulfoxide reductase implicate oxidation of sp
177      This characteristic supports a role for methionine sulfoxide reductase in redox signaling.
178 ding or the repair of oxidized calmodulin by methionine sulfoxide reductase induces comparable change
179 e pK(a) of the active site cysteine of mouse methionine sulfoxide reductase is 7.2 even in the absenc
180 of oxidized methionine residues performed by methionine sulfoxide reductase is important for the gast
181 versible and is regulated by the cytoplasmic methionine sulfoxide reductase Mxr1 (MsrA) and a previou
182                     Reversing oxidation with methionine sulfoxide reductase restored HDL's ability to
183                  MsrPQ is a newly identified methionine sulfoxide reductase system found in bacteria,
184              MtsZ is a molybdenum-containing methionine sulfoxide reductase that supports virulence i
185 ine in proteins involving the enzyme peptide methionine sulfoxide reductase type A (MSRA) is postulat
186 m Escherichia coli and the electron acceptor methionine sulfoxide reductase, also from E. coli, stron
187                                              Methionine sulfoxide reductase, which reduces methionine
188                       In contrast, CshA- and methionine sulfoxide reductase-negative (MsrA-) strains
189 ould be reversed by treating the enzyme with methionine sulfoxide reductase.
190  and the oxidized protein was incubated with methionine sulfoxide reductase.
191 ribonucleotide reductase, peroxiredoxin, and methionine sulfoxide reductase.
192 s, in particular alkenal reductase PTGR1 and methionine sulfoxide reductase.
193  it is reversed by coexpression with peptide methionine sulfoxide reductase.
194 ion mediated by a ubiquitous enzyme, peptide methionine sulfoxide reductase.
195 BC transporter solute-binding protein, and a methionine sulfoxide reductase.
196 nt study on the reducing requirement for the methionine sulfoxide reductases (Msr), we have shown tha
197 f methionine sulfoxide (MetO) is mediated by methionine sulfoxide reductases (Msr).
198 ein functional changes through the action of methionine sulfoxide reductases (Msr).
199                                      Peptide methionine sulfoxide reductases (MsrA) from many differe
200                                              Methionine sulfoxide reductases (MSRs) are key enzymes i
201                                              Methionine sulfoxide reductases (Msrs) are oxidoreductas
202 s damage is reversible through the action of methionine sulfoxide reductases (MSRs), which play key r
203 n is catalyzed by a family of enzymes called methionine sulfoxide reductases (MSRs).
204 oxidized methionine residues is catalyzed by methionine sulfoxide reductases (Msrs).
205 ically oxidized, and subsequently reduced by methionine sulfoxide reductases (Msrs).
206 revisiae as a model, we show that of the two methionine sulfoxide reductases (MXR1, MXR2), deletion o
207 rx2) and the intracellular and extracellular methionine sulfoxide reductases (SpMsrAB1 and SpMsrAB2,
208  (MetO) residues in proteins is catalyzed by methionine sulfoxide reductases A (MSRA) and B (MSRB), w
209                In normal healthy human skin, methionine sulfoxide reductases A and B specifically red
210 S) can be repaired in the human epidermis by methionine sulfoxide reductases A and B, respectively.
211                                       MSRAs (methionine sulfoxide reductases A) are enzymes that reve
212          Inactivation of HypT depends on the methionine sulfoxide reductases A/B.
213                                              Methionine sulfoxide reductases are conserved enzymes th
214                                      Peptide methionine sulfoxide reductases are conserved enzymes th
215                                              Methionine sulfoxide reductases are key enzymes that rep
216 ne residues to methionine sulfoxide, and the methionine sulfoxide reductases catalyze their reduction
217 activity of plastidial thiol peroxidases and methionine sulfoxide reductases employing a single cyste
218 a proof of principle, fluorogenic probes for methionine sulfoxide reductases have been developed.
219                 However, the identity of all methionine sulfoxide reductases involved, their cellular
220            Deletion or mutation in conserved methionine sulfoxide reductases leads to aging and sever
221                           Here we used yeast methionine sulfoxide reductases MsrA and MsrB to address
222 teins or repair oxidized residues, including methionine sulfoxide reductases MsrA and MsrB, which red
223 erations of RecA activity were suppressed by methionine sulfoxide reductases MsrA and MsrB.
224                         The highly conserved methionine sulfoxide reductases protect proteins from ox
225 sporadically evolved Sec-containing forms of methionine sulfoxide reductases reflect catalytic advant
226              Reduction back to methionine by methionine sulfoxide reductases would allow the antioxid
227                           Most cells contain methionine sulfoxide reductases, which catalyze a thiore
228 so observed that are catalyzed by endogenous methionine sulfoxide reductases.
229 he action of stereospecific enzymes known as methionine sulfoxide reductases.
230                                              Methionine-sulfoxide reductases are unique, in that thei
231                        Comparable extents of methionine sulfoxide reduction are also observed that ar
232                            Cd-MsrB catalyzes methionine sulfoxide reduction involving three redox-act
233                Alternatively, MsrA catalyzes methionine sulfoxide reduction linked to the mycothiol/m
234 rved SelR enzyme family, define a pathway of methionine sulfoxide reduction, reveal a case of converg
235                      Disruption of bacterial methionine sulfoxide repair systems rendered E. coli mor
236 metry to investigate the extent and rates of methionine sulfoxide repair within CaMox.
237 sulfoxide reductase (MsrA), which can reduce methionine sulfoxide residues back to methionine, restor
238 4.6) is a ubiquitous protein that can reduce methionine sulfoxide residues in proteins as well as in
239 fense against oxidative stresses by reducing methionine sulfoxide residues in proteins back to methio
240  MsrA and MsrB in E. coli are able to reduce methionine sulfoxide residues in proteins to methionines
241                     Oxidative damage, mainly methionine sulfoxide residues, was also increased: 2.5 v
242  and to conversion of methionine residues to methionine sulfoxide residues.
243  were modified to cysteine sulfenic acid and methionine sulfoxide, respectively.
244 24) thiolate, which directly interacted with methionine sulfoxide, resulting in methionine and a Cys(
245 oxide reductases A and B specifically reduce methionine sulfoxides (S) and (R), respectively, back to
246  activity and the reduction activity of free methionine sulfoxide(s) were stereoselective toward the
247                Raman bands characteristic of methionine sulfoxide show that extensive methionine oxid
248 usly unrecognized part that accommodates the methionine sulfoxide side chain via interaction with His
249 ous substitution by glutamine, mimicking the methionine sulfoxide state, increased the viability of E
250 ge into methionine, N-glycyl-methionine, and methionine sulfoxide suggests that a prominent solvent e
251 )H incorporation into the gamma-methylene of methionine sulfoxide that is absent for N-glycyl-methion
252                                          For methionine sulfoxide the inflection point energy is 2.8
253 nonoxidized), and with increasing numbers of methionine sulfoxides the kinetics of fibrillation becam
254  When this methionine residue is oxidized to methionine sulfoxide, the inactivation is disrupted, and
255 tein repair each targeting a diastereomer of methionine sulfoxide, their deletion resulted in differe
256 ble to oxidation with a 25-75% loss, forming methionine sulfoxide through a two-electron oxidation pa
257 with methionine residues in proteins to form methionine sulfoxide, thus scavenging the reactive speci
258 eductase A (MsrA) catalyzes the reduction of methionine sulfoxide to methionine and is specific for t
259 ethionine sulfoxide reductase, which reduces methionine sulfoxide to methionine in a thioredoxin-depe
260 Taken together, MSRB3-catalyzed reduction of methionine sulfoxides to methionine is essential for hea
261 so capable of reducing nicotinamide N-oxide, methionine sulfoxide, trimethylamine-N-oxide, and dimeth
262                           However, much more methionine sulfoxide was generated by peroxide treatment
263 rmore, high levels of free and protein-bound methionine sulfoxide were detected in extracts of msrA m
264  metformin therapy, arginine-derived AGE and methionine sulfoxide were lower than in patients not rec
265 -Glu-cys, gamma-Glu-met-gly, methionine, and methionine sulfoxide were not transported by Seo1p.
266  markers of oxidative stress such as urinary methionine sulfoxide were observed in Hhip (+/-) but not
267  of a variety of other substrates, including methionine sulfoxide, with decreased efficiencies, sugge
268 sulfoxide formation and (ii) MsrA can repair methionine sulfoxides within cytosolic proteins.
269 air by MsrA, there remains a distribution of methionine sulfoxides within functionally reactivated Ca
270                       The rates of repair of methionine sulfoxides within individual tryptic fragment
271 dary structure, suggesting that MsrA repairs methionine sulfoxides within unfolded sequences until na
272 e report the synthesis of amphiphilic poly(l-methionine sulfoxide)(x)-b-poly(dehydroalanine)(y), dibl

 
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