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1 sbF interaction partner, Rv1676, a predicted peroxiredoxin.
2  removal was observed following oxidation of peroxiredoxin.
3 des and regulates the expression of the OhrA peroxiredoxin.
4 tic mechanism of Asp f3, a two-cysteine type peroxiredoxin.
5 roxyperoxide reductase E (AhpE), among other peroxiredoxins.
6 entative of the major class of bacterial BCP peroxiredoxins.
7 ses, catalases, glutathione-peroxidases, and peroxiredoxins.
8 x homeostasis through reducing hyperoxidized peroxiredoxins.
9 xy-eicosatetraenoic acids also over-oxidized peroxiredoxins.
10 mple assay to quantify the hyperoxidation of peroxiredoxins.
11  was associated with increased expression of peroxiredoxin 1 (P<0.05), peroxiredoxin 3 (P<0.01), and
12 igomers and shifts in isoelectric points for peroxiredoxin 1 (Prdx-1), Prdx-3, and Prdx-4 isoforms wi
13              We previously demonstrated that peroxiredoxin 1 (Prdx1), a scavenger of reactive oxygen
14                  Recent studies suggest that Peroxiredoxin 1 (Prdx1), in addition to its known H(2)O(
15       In particular, the antioxidant protein peroxiredoxin 1 (Prx1) exhibited both decreased expressi
16                                              Peroxiredoxin 1 (Prx1) has been found to be elevated in
17                                              Peroxiredoxin 1 (Prx1) is an antioxidant and molecular c
18         In the present study, we showed that peroxiredoxin 1 (Prx1), a member of the peroxiredoxin pr
19 re used to assess the effect of UVB on TOPK, peroxiredoxin 1 (Prx1), and apoptosis in RPMI7951 cells.
20 lar proteins such as heat shock proteins and peroxiredoxin 1 (Prx1).
21 f PUMA induced up-regulation (>1.34-fold) of peroxiredoxin 1 and down-regulation (by 25%) of stathmin
22 enerated from oxidation of Trx1 catalyzed by peroxiredoxin 1 in the presence of H2O2.
23 te-cysteine ligase catalytic subunit, ABCC1, peroxiredoxin 1).
24 ntified GAPDH, vimentin, beta-galactosidase, peroxiredoxin 1, beta-actin, and ubiquitin-conjugating e
25 1s) and the antioxidant enzymes catalase and peroxiredoxin 1, which may influence antioxidant potenti
26                                        Human peroxiredoxins 1 and 2, also known as Prx1 and Prx2, are
27 eroxide dismutase 1), anti-oxidant proteins (peroxiredoxins 1 and 6), and metabolic proteins (e.g., p
28 se-1, and cyclooxygenase-2 oxidize the 2-Cys-peroxiredoxins 1, 2, and 3 to their sulfinic and sulfoni
29 gi apparatus tether, and antioxidant enzymes peroxiredoxins 1-2.
30 been shown to reactivate oxidized 1-cysteine peroxiredoxin (1-Cys Prx, Prx VI, Prdx6, and AOP2).
31 xidases, or by overexpression of catalase or peroxiredoxin-1 (Prx-1).
32 /SNO may affect the redox cycle of mammalian peroxiredoxin-1 (Prx1), a representative of the 2-Cys Pr
33 ically interacts with the antioxidant enzyme peroxiredoxin-1 (PRX1), protects it from proteasome-medi
34 ation of primary antioxidant systems such as peroxiredoxins-1, heme oxygenase-1, and anti-apoptotic f
35 pectively), but comparable with TR-dependent peroxiredoxins (16.5 and 2.7x10(4) s(-1) M(-1), respecti
36 ed genes encoding Fe hydrogenase (9.m00419), peroxiredoxin (176.m00112), type A flavoprotein (6.m0046
37                  Intriguingly, we identified peroxiredoxin 2 (PRDX2) as a novel potential tumor suppr
38                                              Peroxiredoxin 2 (Prx2) is a thiol protein that functions
39 nduces CDK5/p25-dependent phosphorylation of peroxiredoxin 2 (Prx2), resulting in inhibition of its p
40 estigated interactions between PTP1B and the peroxiredoxin 2 (Prx2)/thioredoxin 1 (Trx1)/thioredoxin
41 y in vitro; during therapy, disulfide-linked peroxiredoxin 2 dimer did not accumulate in red blood ce
42 tropomyosin alpha4 p=0.0108), antioxidative (peroxiredoxin 2 p=0.0092), and anti-inflammatory effects
43 ansfer flavoprotein were increased, nm23/H1, peroxiredoxin 2, nucleophosmin 1/B23, and inorganic pyro
44 pical thioredoxin ACHT1 is oxidized by 2-Cys peroxiredoxin (2-Cys Prx) in Arabidopsis plants illumina
45               Here, we reveal that the 2-Cys peroxiredoxin (2-Cys Prx) Tpx1 is required for the perox
46      NTRC is an efficient reductant of 2-Cys peroxiredoxins (2-Cys Prxs) and thus is involved in the
47 on of Cys-sulfinic acid derivatives of 2-Cys peroxiredoxins (2-Cys Prxs), has been shown to catalyze
48 alysis revealed that the antioxidant enzymes peroxiredoxin-2 (Prdx2) and heme oxygenase-1 were upregu
49 lammatory stimuli induce release of oxidized peroxiredoxin-2 (PRDX2), a ubiquitous redox-active intra
50              For example, S-nitrosylation of peroxiredoxin-2 (Prx2), a peroxidase widely expressed in
51 ased expression of peroxiredoxin 1 (P<0.05), peroxiredoxin 3 (P<0.01), and heme oxygenase-1 (HO-1) (P
52 e (Sod), glutathione peroxidase 4 (Gpx4) and peroxiredoxin 3 (Prdx3) that render them susceptible to
53                                              Peroxiredoxin 3 (Prx3), a mitochondrial thioredoxin-depe
54 merase gamma, mitochondrial topoisomerase I, peroxiredoxin 3 and manganese superoxide dismutase--are
55                                              Peroxiredoxin-3 (PRDX3) is a mitochondrial antioxidant e
56                 LRRK2 has been shown to bind peroxiredoxin-3 (PRDX3), the most important scavenger of
57  interacts with the mitochondrial peroxidase peroxiredoxin-3 (PRDX3).
58 uctions (P<0.001) in the antioxidant enzymes peroxiredoxin-3 and CuZn-superoxide-dismutase.
59                 The mitochondrial peroxidase peroxiredoxin-3 reduces H(2)O(2) to water using reducing
60 ion of a mitochondria-localized antioxidant (peroxiredoxin-3) was protective against VIDD.
61 unolabeling for markers of oxidative stress (peroxiredoxin-3/5) and for a lipid peroxidation product
62                         Here, we report that peroxiredoxin 4 (PRDX4) is a putative tumor driver.
63     The endoplasmic reticulum (ER)-localized peroxiredoxin 4 (PRDX4) supports disulfide bond formatio
64                                              Peroxiredoxin 4 (Prdx4), an ER-specific antioxidative pe
65 llothionein 3 (Mt3), tetraspanin 2 (Tspan2), peroxiredoxin 4 (Prdx4), stathmin-like 2 (Stmn2), myelin
66                                              Peroxiredoxin 4 (Prx4) has been implicated in a wide var
67                       Blocking either Akt or peroxiredoxin 4 activity with Akt Inhibitor IV or a pero
68 study examined the role of Akt signaling and peroxiredoxin 4 expression in human umbilical cord blood
69 o increased Akt phosphorylation and elevated peroxiredoxin 4 expression in oligodendrocytes.
70  cord blood cells converge on Akt to elevate peroxiredoxin 4 levels, and these effects contribute to
71  occlusion increased Akt phosphorylation and peroxiredoxin 4 protein expression while reducing proteo
72 edoxin 4 activity with Akt Inhibitor IV or a peroxiredoxin 4-neutralizing antibody, respectively, neg
73 t enzymes, superoxide dismutase 1 (SOD1) and peroxiredoxin-4 (PRDX4) during hyperosmotic stress.
74 s), NAD(P)H quinone oxidoreductase-1 (Nqo1), peroxiredoxin-4 (Prdx4), and serine peptidase inhibitor
75 anganese-containing superoxide dismutase and peroxiredoxin 5 were only upregulated by PgLPS1690.
76 e E1, PYGB, Pgm2), and antioxidant proteins (peroxiredoxin 5, ferritin heavy chain 1) following rapam
77 f four proteins (macrophage capping protein, peroxiredoxin 5, heterogeneous nuclear ribonucleoprotein
78 ther by crystallography or NMR for the human peroxiredoxin 5, their affinities were for the first tim
79      Herein we show that the transduction of Peroxiredoxin 6 (PRDX6) attenuates TNF-alpha- and glutam
80                                              Peroxiredoxin 6 (Prdx6) is a "moonlighting" protein with
81                                              Peroxiredoxin 6 (PRDX6) is a key regulator of cellular r
82                       The antioxidant enzyme peroxiredoxin 6 (Prdx6) is a key regulator of the cellul
83                                              Peroxiredoxin 6 (Prdx6) is essential for activation of N
84 o show that following opioid administration, peroxiredoxin 6 (PRDX6) is recruited to the opioid recep
85 holipase A2 (PLA2)activity of phosphorylated peroxiredoxin 6 (Prdx6) is required for activation of NA
86 how that opioid receptor activation recruits peroxiredoxin 6 (PRDX6) to the receptor-Galphai complex
87                                              Peroxiredoxin 6 (Prdx6), a bifunctional enzyme with glut
88                                              Peroxiredoxin 6 (Prdx6), a bifunctional protein with pho
89                                We identified peroxiredoxin 6 (Prdx6), a host factor that contributes
90 tathione peroxidase 2 and 3 (GPx2 and GPx3), peroxiredoxin 6 (Prdx6), and sulfyhydryl oxidase Q6 (Qsc
91             The phospholipase A2 activity of peroxiredoxin 6 modulates NADPH oxidase 2 activation via
92 or of PRDX6 and suggest that co-targeting of peroxiredoxin 6 or modulating miR-371-3p expression toge
93                           We identify PRDX6 (peroxiredoxin 6) as a key target of miR-371-3p in establ
94 d and confirmed that Saitohin interacts with peroxiredoxin 6, a unique member of that family that is
95 27, cathepsin D, triose-phosphate isomerase, peroxiredoxin 6, and electron transfer flavoprotein were
96 cs analysis, we found that uterine levels of peroxiredoxin-6 (PRDX6), a unique antioxidant, are signi
97 transporter (EAAT-2), apo-J (Clusterin), and peroxiredoxin-6) are selectively expressed in astrocytes
98        One Zap1 target gene encodes the Tsa1 peroxiredoxin, a protein with both peroxidase and protei
99                                          The peroxiredoxins, a family of peroxidases initially descri
100 roxidase and glutathione peroxidase, and the peroxiredoxin abundance were increased for ROS scavengin
101 soluble antioxidative systems, in particular peroxiredoxins, accumulate at higher levels in M chlorop
102 one and thioredoxin oxidation and suppressed peroxiredoxin activity in vitro.
103 this residue was not absolutely required for peroxiredoxin activity.
104                   We have confirmed that the peroxiredoxin Ahp1 is such a substrate in S. cerevisiae
105 tributions of the sole catalase KatE and the peroxiredoxin AhpC produced by these strains in defense
106                                The bacterial peroxiredoxin AhpC, a cysteine-dependent peroxidase, can
107 rains is restored by a mutant (ahpC*) of the peroxiredoxin AhpC, converting it to a disulfide reducta
108 tress includes the flavoprotein AhpF and the peroxiredoxin AhpC.
109  disulfide center of the antioxidant protein peroxiredoxin (AhpC) to detoxify ROS such as hydrogen pe
110 d catalase, H. pylori depends on a family of peroxiredoxins (alkylhydroperoxide reductase, bacteriofe
111 that mass spectrometry shows contained 2-Cys peroxiredoxin also formed and precedes the appearance of
112 ne, a residue that occurs in place of Pro in peroxiredoxins, also led to the formation of the cluster
113 arrying 2 functional elements, an N-terminal peroxiredoxin and a C-terminal chitinase domain.
114 ing the thioredoxin peroxidase activity of a peroxiredoxin and increasing the hydrogen peroxide resis
115  two proteins with antioxidative properties (peroxiredoxin and superoxide dismutase), and three prote
116 chanism is similar to that of atypical 2-Cys peroxiredoxin and that selenocysteine allows SelS to sus
117 and structural features of the mitochondrial peroxiredoxin and thioredoxin of P. falciparum.
118 in reveals a fold typical of the 2-Cys class peroxiredoxins and a dimeric form with an intermolecular
119 were identified, including ATPase, clathrin, peroxiredoxins and enolase, which may provide clues to t
120 h wild-type and mutant strains deficient for peroxiredoxins and glutathione peroxidases were equally
121  H2O2 is under sophisticated fine control of peroxiredoxins and glutathione peroxidases with their ba
122 d that Sesn2 physically interacts with 2-Cys peroxiredoxins and Nrf2 albeit under different reductive
123 ting from nonlinearity of H2O2 scavenging by peroxiredoxins and our study reveals that this regulator
124 s, including cysteine-dependent peroxidases (peroxiredoxins) and proteases, only relatively few pK(a)
125 y on select proteins, including thioredoxin, peroxiredoxins, and other validated redox active protein
126                                              Peroxiredoxins are a diverse and ubiquitous family of hi
127 d out in this list, as the related cytosolic peroxiredoxins are known to form disulfides in the prese
128                                Typical 2-Cys peroxiredoxins are required to remove hydrogen peroxide
129                                              Peroxiredoxins are ubiquitous proteins that catalyze the
130 ain the phenotypic differences, and identify peroxiredoxin as an important component of virulence in
131                        Here we show that the peroxiredoxin Asp f3 of Aspergillus fumigatus inactivate
132 ctrometry, we recently reclassified one such peroxiredoxin, bacterioferritin comigratory protein (BCP
133                                        2-Cys peroxiredoxins belonging to the Prx1 subfamily are Cys-b
134 ssion of an antioxidative enzyme, 2-Cysteine peroxiredoxin (BxPrx), was elevated in B. xylophilus fol
135 ces cerevisiae Altogether, the processing of peroxiredoxins by Imp2 or Oct1 likely represents systems
136 the selective benefits endowed to eukaryotic peroxiredoxins by their reversible hyperoxidation.
137                            Hyperoxidation of peroxiredoxins can only occur efficiently in the presenc
138                   The absence of Tsa1, a key peroxiredoxin, caused increased rates of mutations, chro
139 demonstrate a clear physiological role for a peroxiredoxin chaperone and reveal a novel and unexpecte
140                                          The peroxiredoxin clearly preferred PfTrx2 to PfTrx1 as a re
141 ongs to the atypical 2-cysteine subfamily of peroxiredoxins, commonly referred to as bacterioferritin
142                 AhpC, the peroxide-reducing (peroxiredoxin) component of this alkyl hydroperoxidase s
143                          We also explore how peroxiredoxins contribute to YROs.
144                               In these 2-Cys peroxiredoxins, decamer formation is important for the c
145                                              Peroxiredoxin-dependent mechanisms may modulate the rece
146                The functional versatility of peroxiredoxins depends on progressive oxidation of key c
147       This is the first report of 2-cysteine peroxiredoxins efficiently utilizing reducing equivalent
148            Deletion of TSA1, which encodes a peroxiredoxin, exacerbated iron toxicity in Deltaccc1 ce
149                                      Prx1, a peroxiredoxin family member, was shown to be frequently
150  a thioredoxin fold similar to that of other peroxiredoxin family members.
151 typhimurium AhpC is a founding member of the peroxiredoxin family, a ubiquitous group of cysteine-bas
152 osis Tpx is a member of the atypical two-Cys peroxiredoxin family.
153 obacter pylori contains three members of the peroxiredoxin family: AhpC (alkyl hydroperoxide reductas
154    Those studies, however, have not examined peroxiredoxin for a potential dual functionality as both
155 ved the crystal structure of a typical 2-Cys peroxiredoxin from Leishmania in the dimeric (pH 8.5) an
156   Thiol peroxidases (Tpxs) are dimeric 2-Cys peroxiredoxins from bacteria that preferentially reduce
157 to those obtained for two typical 2-cysteine peroxiredoxins from Saccharomyces cerevisiae (5.4 and 6.
158 atalase (encoded by hktE) and a bifunctional peroxiredoxin-glutaredoxin (encoded by pdgX) in resistan
159 on these data, we conclude that catalase and peroxiredoxin-glutaredoxin are determinants of bacterial
160               These include catalase (HktE), peroxiredoxin/glutaredoxin (PgdX), and a ferritin-like p
161 circadian oscillations in the redox state of peroxiredoxin have been described as an additional non-t
162                   Cytosolic eukaryotic 2-Cys-peroxiredoxins have been widely reported to act as dual-
163         Using red blood cells, we found that peroxiredoxins, highly conserved antioxidant proteins, u
164 and contribute to osteoarthritis and suggest peroxiredoxin hyperoxidation as a potential mechanism.
165                                              Peroxiredoxin hyperoxidation was associated with inhibit
166                                              Peroxiredoxin hyperoxidation was observedin situin human
167 pecifically, our experiments have identified peroxiredoxin I (Prx I) as one of these up-regulated pro
168 stimulation, the expression and oxidation of peroxiredoxin II (PrdxII), a critical antioxidant enzyme
169        By proteomics analysis, we found that peroxiredoxin II (PrxII), a member of a family of peroxi
170                            Overexpression of peroxiredoxin in Rahman rendered the transgenic trophozo
171 have been due to the absence of catalase and peroxiredoxin in the purified Hb.
172 perones, Hsp33 in bacteria and typical 2-Cys peroxiredoxins in eukaryotes.
173 ism to stabilize the decameric form of 2-Cys peroxiredoxins in Leishmania mitochondria.
174  the structure and function of typical 2-Cys peroxiredoxins in response to oxidative stress.
175             Thus, AhpC and potentially other peroxiredoxins in this widespread family can elaborate a
176 the expression of Prx III, the mitochondrial peroxiredoxin, in human cardiac fibroblasts.
177 l, Day et al. reveal a surprising benefit of peroxiredoxin inactivation at high H(2)O(2), showing tha
178 ans Srx1 was also found to be required for a peroxiredoxin-independent function in promoting fungicid
179                    Mutagenesis of S. mansoni peroxiredoxins indicated that glutathione dependence and
180 igand, whereas catalase and a membrane-bound peroxiredoxin inhibited ligand-dependent signaling.
181 support the subdivision of the BCP family of peroxiredoxins into two classes based on their catalytic
182 tive cysteine, the resolving cysteine of BCP peroxiredoxins is not conserved across all members of th
183                     Together with 2-cysteine peroxiredoxin, it forms a two-component peroxide-detoxif
184 ein folding, which led to the discovery that peroxiredoxin IV (PRDX4) catalyzes a parallel oxidation
185                                              Peroxiredoxin IV (PRDX4) stood out in this list, as the
186  produced can be metabolized by ER-localized peroxiredoxin IV (PrxIV).
187 r mitochondria, leading to the protection of peroxiredoxin IV from hyperoxidation.
188                 Our results demonstrate that peroxiredoxin IV recycling in the endoplasmic reticulum
189 quence similarity 213, member A (FAM213A), a peroxiredoxin-like antioxidative protein, was repressed
190 spectrometry reveal that DJ-1 is an atypical peroxiredoxin-like peroxidase that scavenges H(2)O(2) th
191 hysiological function of DJ-1 as an atypical peroxiredoxin-like peroxidase.
192  peroxidase, the parasites rely primarily on peroxiredoxin-linked systems for protection.
193            The sulfinic or sulfonic forms of peroxiredoxin lose their peroxidase activity, which allo
194    These results show that the mitochondrial peroxiredoxin of P. falciparum occurs in both dimeric an
195 or that represses expression of an inducible peroxiredoxin, OhrA.
196 riod determination by CK1 and GSK3, and have peroxiredoxin over-oxidation cycles.
197 2 is mediated by an evolutionarily conserved peroxiredoxin-p38/MAPK signaling cascade.
198 atalysis occurs via an atypical two-cysteine peroxiredoxin pathway.
199 oresistant cancer cells suggested that human peroxiredoxin plays an important role in eliminating the
200 ire GUR-3 and a conserved antioxidant enzyme peroxiredoxin PRDX-2.
201 he mitohormetic pathway is propagated by the peroxiredoxin PRDX-2.
202                                          The peroxiredoxin (Prdx) family of antioxidant enzymes uses
203 roxidase activity of the antioxidant protein peroxiredoxin (Prdx-1) in breast cancer cells.
204 regulation of ROS/RNS is largely attended by peroxiredoxins (Prdxs) and their main reductants, thiore
205                                              Peroxiredoxins (Prdxs) are small H(2)O(2) scavenging pro
206 rtile, and the deficiency or inactivation of Peroxiredoxins (PRDXs) is associated with human male inf
207 , peroxynitrite, and organic hydroperoxides, peroxiredoxins (Prdxs) represent a major potential prote
208 that peroxiredoxin 1 (Prx1), a member of the peroxiredoxin protein family, acts as a key mediator in
209 ediated by the membrane protein GDE2 and the peroxiredoxin protein Prdx1 that promotes neurogenesis.
210 n the oxidation state of a broadly conserved peroxiredoxin protein.
211                     We identify oxidation of peroxiredoxin proteins as a transcription-independent rh
212 e we show that oxidation-reduction cycles of peroxiredoxin proteins constitute a universal marker for
213 TXNRD1) and sulfiredoxin (SRXN1), suggesting peroxiredoxin proteins had been oxidized during monoHAA
214          Genes encoding two novel 2-cysteine peroxiredoxin proteins were identified in the expressed
215 t discovery of oxidation-reduction cycles of peroxiredoxin proteins, which persist even in the absenc
216 ing, e.g., over-oxidation cycles of abundant peroxiredoxin proteins.
217         PREX is a database of currently 3516 peroxiredoxin (Prx or PRDX) protein sequences unambiguou
218                             Although this Tp peroxiredoxin (Prx) closely resembles AhpC-like Prxs, Tp
219 PC-mutation-positive colorectal cancer.2-Cys peroxiredoxin (Prx) enzymes are highly expressed in most
220                              Mammalian 2-Cys peroxiredoxin (Prx) enzymes are overexpressed in most ca
221  parasite Leishmania infantum, mitochondrial peroxiredoxin (Prx) exerts intrinsic ATP-independent cha
222                                          The peroxiredoxin (PRX) family of antioxidant enzymes helps
223 iscovery that the redox regulatory proteins, peroxiredoxin (Prx) I and Prx II are specific targets of
224 fects on apoptotic signaling of depletion of peroxiredoxin (Prx) III, a mitochondrion-specific H(2)O(
225            Srx preferentially interacts with Peroxiredoxin (Prx) IV relative to other Prxs due to its
226 ivity in vitro Remarkably, the processing of peroxiredoxin (Prx) proteins by Oct1 appears to be an ev
227 efenses by making changes to the thioredoxin-peroxiredoxin (Prx) system.
228 terioferritin comigratory protein (BCP) is a peroxiredoxin (Prx) that catalyzes the reduction of H(2)
229 tive site cysteine of the antioxidant enzyme peroxiredoxin (Prx) to the sulfinic acid form, Prx-SO(2)
230 estingly, ACHT1 oxidation is driven by 2-Cys peroxiredoxin (Prx), which in turn eliminates peroxides.
231 zymes and reduced formation of hyperoxidized peroxiredoxin (Prx)2.
232 This reaction is unique to the typical 2-Cys peroxiredoxins (Prx) and plays a role in peroxide-mediat
233                                              Peroxiredoxins (PRX) are a family of antioxidant enzymes
234                             Eukaryotic 2-Cys peroxiredoxins (Prx) are abundant antioxidant enzymes wh
235                                              Peroxiredoxins (PRX) are critical intracellular antioxid
236                                              Peroxiredoxins (Prx) are efficient thiol-dependent perox
237                          Evidence implicates peroxiredoxins (Prx) as providing the main enzymatic act
238 air the inactivated forms of typical two-Cys peroxiredoxins (Prx) implicated in hydrogen peroxide-med
239                                              Peroxiredoxins (Prx) make up a family of enzymes that re
240 of the active site cysteine in typical 2-Cys peroxiredoxins (Prx) to sulfinic acid during oxidative s
241                                              Peroxiredoxins (Prx), a family of peroxidases that reduc
242 e proteins, including thioredoxins (Trx) and peroxiredoxins (Prx), with putative copper-binding ligan
243 st Oct1 could cleave the human mitochondrial peroxiredoxin Prx3 when expressed in Saccharomyces cerev
244 ed to oxidative stress resistance, including peroxiredoxin PrxA, in response to hydrogen peroxide.
245                      The mitochondrial 2-Cys peroxiredoxin PrxIII serves as a thioredoxin-dependent p
246                                              Peroxiredoxins (Prxs or Prdxs) are a large protein super
247 nt peroxidases, including 2-cysteine (2-Cys) peroxiredoxins (PRXs) and thylakoid ascorbate peroxidase
248                                              Peroxiredoxins (Prxs) are a family of peroxidases that r
249                                              Peroxiredoxins (Prxs) are a ubiquitously expressed famil
250                                              Peroxiredoxins (Prxs) are highly conserved proteins foun
251                                              Peroxiredoxins (Prxs) are important peroxidases associat
252 O2H) residues, the sulfinic forms of certain peroxiredoxins (Prxs) are selectively reduced by sulfire
253                                Typical 2-Cys peroxiredoxins (Prxs) are ubiquitous peroxidases that ar
254                                              Peroxiredoxins (Prxs) are vital regulators of intracellu
255             Inactivation of eukaryotic 2-Cys peroxiredoxins (Prxs) by hyperoxidation has been propose
256 ether with thioredoxin reductase 1 (TR1) and peroxiredoxins (Prxs) comprises a key redox regulatory s
257                                              Peroxiredoxins (Prxs) detoxify peroxides and modulate H2
258                                Typical 2-Cys peroxiredoxins (Prxs) have an important role in regulati
259                                              Peroxiredoxins (Prxs) make up a ubiquitous class (propos
260                                Typical 2-Cys peroxiredoxins (Prxs) react rapidly with H2O2 to form a
261 therefore the family of antioxidant enzymes, peroxiredoxins (Prxs) represent a target for antimalaria
262                 Cysteine residues of certain peroxiredoxins (Prxs) undergo reversible oxidation to su
263               NTRC efficiently reduces 2-Cys peroxiredoxins (Prxs), thus having antioxidant function,
264 ed to react fast toward reactive thiols from peroxiredoxins (Prxs).
265 ing age-related oxidation of H2O2-scavenging peroxiredoxins (Prxs).
266                In many bacteria, a dedicated peroxiredoxin reductase, alkyl hydroperoxide reductase s
267    Our results present in vivo evidence of a peroxiredoxin regulating DE-cadherin-mediated adhesion.
268   The crystal structure of the mitochondrial peroxiredoxin reveals a fold typical of the 2-Cys class
269 lose structural similarity to atypical 2-Cys peroxiredoxin(s) (Prx).
270             These observations may represent peroxiredoxin sensing and transducing the oxidant signal
271                                        Human peroxiredoxins serve dual roles as anti-oxidants and reg
272    Because of its evolutionary conservation, peroxiredoxin signaling might underlie a general princip
273 genases and cyclooxygenases may affect 2-Cys peroxiredoxin signaling, analogous to NADPH oxidases in
274 modulate the oligomeric transitions of 2-Cys peroxiredoxins such as redox state, post-translational m
275 provided further support for the thioredoxin/peroxiredoxin system as the major contributor to mitocho
276  H2O2 detoxification through the thioredoxin/peroxiredoxin system.
277 dent manner predominantly by the thioredoxin/peroxiredoxin system.
278 1-Cys peroxiredoxin (TgTrx-Px2), and a 2-Cys peroxiredoxin (TgTrx-Px1) and immunofluorescent studies
279 T. gondii express thioredoxin (TgTrx), 1-Cys peroxiredoxin (TgTrx-Px2), and a 2-Cys peroxiredoxin (Tg
280          Yeast Prx1 is a mitochondrial 1-Cys peroxiredoxin that catalyzes the reduction of endogenous
281 ydroperoxide reductase subunit C (AhpC) is a peroxiredoxin that detoxifies peroxides.
282 P) of Escherichia coli, as an atypical 2-Cys peroxiredoxin that functions through the formation of an
283 es belonging to the class of 1-Cys and 2-Cys peroxiredoxins that play crucial roles in maintaining re
284                               For all of the peroxiredoxins, the catalytic cysteine, referred to as t
285                                              Peroxiredoxins, the enzymes that catalyze the reduction
286 xpressions of those genes encoding catalase, peroxiredoxin, thioredoxin and glutathione were highly i
287 indicate that at high tissue H2O2 levels the peroxiredoxin-thioredoxin antioxidant chain becomes over
288 ivity of the endoplasmic reticulum-localized peroxiredoxin to hyperoxidation compared with either the
289 d that mutation of the TxxC active site in a peroxiredoxin to the CxxC form could lead to coordinatio
290 ctional gain that allows mitochondrial 2-Cys peroxiredoxins to act as molecular chaperones when formi
291 king one, at 1.4 A, one of the best resolved peroxiredoxins to date.
292                   The ability of schistosome peroxiredoxins to use alternative electron donors, and t
293 nhibitor-like allergen (Tri a 39), and 1-cys-peroxiredoxin (Tri a 32), produced the maximal area unde
294 y enhances the expression of the thioredoxin/peroxiredoxin (Trx/Prx) system with the greatest effect
295 fungal meningoencephalitis and regulation of peroxiredoxins, Tsa1 and Tsa3, and thioredoxins, Trx1 an
296  regulon) and only one antioxidant gene, the peroxiredoxin TSA2.
297 creased expression of the antioxidant enzyme peroxiredoxin-V, and a non-significant trend towards dec
298 man trophozoites expressing higher levels of peroxiredoxin was associated with higher levels of intes
299  relative abundance of serpins Z1C and 1-Cys peroxiredoxin was increased at e[CO2].
300 the highly abundant eukaryotic typical 2-Cys peroxiredoxin, whose oxidative stress-induced sulfinic a

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