戻る
「早戻しボタン」を押すと検索画面に戻ります。 [閉じる]

コーパス検索結果 (1語後でソート)

通し番号をクリックするとPubMedの該当ページを表示します
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 tion status of tubulin, HSP90, TGF-beta, and peroxiredoxins.
6 mple assay to quantify the hyperoxidation of peroxiredoxins.
7 roxyperoxide reductase E (AhpE), among other peroxiredoxins.
8 entative of the major class of bacterial BCP peroxiredoxins.
9 ses, catalases, glutathione-peroxidases, and peroxiredoxins.
10 x homeostasis through reducing hyperoxidized peroxiredoxins.
11 xy-eicosatetraenoic acids also over-oxidized peroxiredoxins.
12  was associated with increased expression of peroxiredoxin 1 (P<0.05), peroxiredoxin 3 (P<0.01), and
13 igomers and shifts in isoelectric points for peroxiredoxin 1 (Prdx-1), Prdx-3, and Prdx-4 isoforms wi
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 enerated from oxidation of Trx1 catalyzed by peroxiredoxin 1 in the presence of H2O2.
22 te-cysteine ligase catalytic subunit, ABCC1, peroxiredoxin 1).
23 1s) and the antioxidant enzymes catalase and peroxiredoxin 1, which may influence antioxidant potenti
24                                        Human peroxiredoxins 1 and 2, also known as Prx1 and Prx2, are
25 se-1, and cyclooxygenase-2 oxidize the 2-Cys-peroxiredoxins 1, 2, and 3 to their sulfinic and sulfoni
26 gi apparatus tether, and antioxidant enzymes peroxiredoxins 1-2.
27 xidases, or by overexpression of catalase or peroxiredoxin-1 (Prx-1).
28 /SNO may affect the redox cycle of mammalian peroxiredoxin-1 (Prx1), a representative of the 2-Cys Pr
29 ically interacts with the antioxidant enzyme peroxiredoxin-1 (PRX1), protects it from proteasome-medi
30 (2) (mH(2)O(2)) acting via the redox sensor, peroxiredoxin-1, a thiol peroxidase with high reactivity
31 ation of primary antioxidant systems such as peroxiredoxins-1, heme oxygenase-1, and anti-apoptotic f
32                  Intriguingly, we identified peroxiredoxin 2 (PRDX2) as a novel potential tumor suppr
33                                              Peroxiredoxin 2 (Prx2) is a thiol protein that functions
34 ductase 1 (TrxR1), thioredoxin 1 (Trx1), and peroxiredoxin 2 (Prx2) together with NADPH.
35 nduces CDK5/p25-dependent phosphorylation of peroxiredoxin 2 (Prx2), resulting in inhibition of its p
36 estigated interactions between PTP1B and the peroxiredoxin 2 (Prx2)/thioredoxin 1 (Trx1)/thioredoxin
37 y in vitro; during therapy, disulfide-linked peroxiredoxin 2 dimer did not accumulate in red blood ce
38 tropomyosin alpha4 p=0.0108), antioxidative (peroxiredoxin 2 p=0.0092), and anti-inflammatory effects
39 pical thioredoxin ACHT1 is oxidized by 2-Cys peroxiredoxin (2-Cys Prx) in Arabidopsis plants illumina
40  studies revealed the participation of 2-Cys peroxiredoxin (2-Cys PRX), a thiol-dependent peroxidase,
41      NTRC is an efficient reductant of 2-Cys peroxiredoxins (2-Cys Prxs) and thus is involved in the
42 on of Cys-sulfinic acid derivatives of 2-Cys peroxiredoxins (2-Cys Prxs), has been shown to catalyze
43                                   Many 2-Cys-peroxiredoxins (2-Cys-Prxs) are dual-function proteins,
44 alysis revealed that the antioxidant enzymes peroxiredoxin-2 (Prdx2) and heme oxygenase-1 were upregu
45 lammatory stimuli induce release of oxidized peroxiredoxin-2 (PRDX2), a ubiquitous redox-active intra
46 mitochondria to the cytosol was evidenced by peroxiredoxin-2 (Prx2) oxidation, and Prx3 collapse was
47              For example, S-nitrosylation of peroxiredoxin-2 (Prx2), a peroxidase widely expressed in
48                     Two additional proteins, peroxiredoxin-2 and endophilin-1, are implicated in Abet
49 ased expression of peroxiredoxin 1 (P<0.05), peroxiredoxin 3 (P<0.01), and heme oxygenase-1 (HO-1) (P
50 e (Sod), glutathione peroxidase 4 (Gpx4) and peroxiredoxin 3 (Prdx3) that render them susceptible to
51 merase gamma, mitochondrial topoisomerase I, peroxiredoxin 3 and manganese superoxide dismutase--are
52 re, N-acetylcysteine increased the levels of peroxiredoxin 3 and superoxide dismutase 2 in adipose ti
53                                              Peroxiredoxin-3 (PRDX3) is a mitochondrial antioxidant e
54                 LRRK2 has been shown to bind peroxiredoxin-3 (PRDX3), the most important scavenger of
55  interacts with the mitochondrial peroxidase peroxiredoxin-3 (PRDX3).
56  be inversely dependent on the total pool of peroxiredoxin-3 (Prx3).
57 uctions (P<0.001) in the antioxidant enzymes peroxiredoxin-3 and CuZn-superoxide-dismutase.
58                 The mitochondrial peroxidase peroxiredoxin-3 reduces H(2)O(2) to water using reducing
59 ion of a mitochondria-localized antioxidant (peroxiredoxin-3) was protective against VIDD.
60 unolabeling for markers of oxidative stress (peroxiredoxin-3/5) and for a lipid peroxidation product
61                         Here, we report that peroxiredoxin 4 (PRDX4) is a putative tumor driver.
62     The endoplasmic reticulum (ER)-localized peroxiredoxin 4 (PRDX4) supports disulfide bond formatio
63                                              Peroxiredoxin 4 (Prdx4), an ER-specific antioxidative pe
64 llothionein 3 (Mt3), tetraspanin 2 (Tspan2), peroxiredoxin 4 (Prdx4), stathmin-like 2 (Stmn2), myelin
65                                              Peroxiredoxin 4 (Prx4) has been implicated in a wide var
66                       Blocking either Akt or peroxiredoxin 4 activity with Akt Inhibitor IV or a pero
67 study examined the role of Akt signaling and peroxiredoxin 4 expression in human umbilical cord blood
68 o increased Akt phosphorylation and elevated peroxiredoxin 4 expression in oligodendrocytes.
69  cord blood cells converge on Akt to elevate peroxiredoxin 4 levels, and these effects contribute to
70  occlusion increased Akt phosphorylation and peroxiredoxin 4 protein expression while reducing proteo
71 transferase 1A and reductions in mitofusin1, peroxiredoxin 4, and fumarate hydratase.
72 edoxin 4 activity with Akt Inhibitor IV or a peroxiredoxin 4-neutralizing antibody, respectively, neg
73 , we show that the thiol-specific peroxidase peroxiredoxin-4 (Prdx4) directly regulates IL-1beta gene
74 t enzymes, superoxide dismutase 1 (SOD1) and peroxiredoxin-4 (PRDX4) during hyperosmotic stress.
75 s), NAD(P)H quinone oxidoreductase-1 (Nqo1), peroxiredoxin-4 (Prdx4), and serine peptidase inhibitor
76 anganese-containing superoxide dismutase and peroxiredoxin 5 were only upregulated by PgLPS1690.
77 e E1, PYGB, Pgm2), and antioxidant proteins (peroxiredoxin 5, ferritin heavy chain 1) following rapam
78 f four proteins (macrophage capping protein, peroxiredoxin 5, heterogeneous nuclear ribonucleoprotein
79 ther by crystallography or NMR for the human peroxiredoxin 5, their affinities were for the first tim
80 ynthase, sperm equatorial segment protein 1, peroxiredoxin-5, secretoglobin family 1D and glucose-6-p
81 Sperm of bulls was related to seminal plasma peroxiredoxin-5, spermadhesin-1 and the spermadhesin-1 x
82      Herein we show that the transduction of Peroxiredoxin 6 (PRDX6) attenuates TNF-alpha- and glutam
83                                              Peroxiredoxin 6 (PRDX6) is a key regulator of cellular r
84                       The antioxidant enzyme peroxiredoxin 6 (Prdx6) is a key regulator of the cellul
85                                              Peroxiredoxin 6 (Prdx6) is essential for activation of N
86 o show that following opioid administration, peroxiredoxin 6 (PRDX6) is recruited to the opioid recep
87 holipase A2 (PLA2)activity of phosphorylated peroxiredoxin 6 (Prdx6) is required for activation of NA
88 how that opioid receptor activation recruits peroxiredoxin 6 (PRDX6) to the receptor-Galphai complex
89                                              Peroxiredoxin 6 (Prdx6), a bifunctional enzyme with glut
90                                              Peroxiredoxin 6 (Prdx6), a bifunctional protein with pho
91                                We identified peroxiredoxin 6 (Prdx6), a host factor that contributes
92 opioid, and D2 dopamine receptors stimulates peroxiredoxin 6 (PRDX6)-mediated production of reactive
93             The phospholipase A2 activity of peroxiredoxin 6 modulates NADPH oxidase 2 activation via
94 or of PRDX6 and suggest that co-targeting of peroxiredoxin 6 or modulating miR-371-3p expression toge
95                           We identify PRDX6 (peroxiredoxin 6) as a key target of miR-371-3p in establ
96 cs analysis, we found that uterine levels of peroxiredoxin-6 (PRDX6), a unique antioxidant, are signi
97 r BQ-123, or ROS scavenging after SDRT using peroxiredoxin-6 overexpression or the SOD mimetic tempol
98 transporter (EAAT-2), apo-J (Clusterin), and peroxiredoxin-6) are selectively expressed in astrocytes
99        One Zap1 target gene encodes the Tsa1 peroxiredoxin, a protein with both peroxidase and protei
100                                          The peroxiredoxins, a family of peroxidases initially descri
101 roxidase and glutathione peroxidase, and the peroxiredoxin abundance were increased for ROS scavengin
102 s and their changes are closely connected to peroxiredoxin activity and function but so far have been
103 one and thioredoxin oxidation and suppressed peroxiredoxin activity in vitro.
104 this residue was not absolutely required for peroxiredoxin activity.
105 mes such as thioredoxins (Trx1 and Trx2) and peroxiredoxin Ahp1 in a Grh1-dependent manner.
106                   We have confirmed that the peroxiredoxin Ahp1 is such a substrate in S. cerevisiae
107 tributions of the sole catalase KatE and the peroxiredoxin AhpC produced by these strains in defense
108                                The bacterial peroxiredoxin AhpC, a cysteine-dependent peroxidase, can
109 rains is restored by a mutant (ahpC*) of the peroxiredoxin AhpC, converting it to a disulfide reducta
110 tress includes the flavoprotein AhpF and the peroxiredoxin AhpC.
111  disulfide center of the antioxidant protein peroxiredoxin (AhpC) to detoxify ROS such as hydrogen pe
112                             The one-cysteine peroxiredoxin alkyl hydroperoxide reductase E from Mycob
113 that mass spectrometry shows contained 2-Cys peroxiredoxin also formed and precedes the appearance of
114 ne, a residue that occurs in place of Pro in peroxiredoxins, also led to the formation of the cluster
115 acks with a putative antioxidant OsmC family peroxiredoxin, an indicator of oxidative stress derived
116 arrying 2 functional elements, an N-terminal peroxiredoxin and a C-terminal chitinase domain.
117 ing the thioredoxin peroxidase activity of a peroxiredoxin and increasing the hydrogen peroxide resis
118  two proteins with antioxidative properties (peroxiredoxin and superoxide dismutase), and three prote
119 chanism is similar to that of atypical 2-Cys peroxiredoxin and that selenocysteine allows SelS to sus
120 and structural features of the mitochondrial peroxiredoxin and thioredoxin of P. falciparum.
121 in reveals a fold typical of the 2-Cys class peroxiredoxins and a dimeric form with an intermolecular
122 were identified, including ATPase, clathrin, peroxiredoxins and enolase, which may provide clues to t
123 h wild-type and mutant strains deficient for peroxiredoxins and glutathione peroxidases were equally
124  H2O2 is under sophisticated fine control of peroxiredoxins and glutathione peroxidases with their ba
125 d that Sesn2 physically interacts with 2-Cys peroxiredoxins and Nrf2 albeit under different reductive
126 ting from nonlinearity of H2O2 scavenging by peroxiredoxins and our study reveals that this regulator
127 s, including cysteine-dependent peroxidases (peroxiredoxins) and proteases, only relatively few pK(a)
128 y on select proteins, including thioredoxin, peroxiredoxins, and other validated redox active protein
129                                              Peroxiredoxins are a diverse and ubiquitous family of hi
130                                              Peroxiredoxins are central to cellular redox homeostasis
131                                              Peroxiredoxins are H(2)O(2) scavenging enzymes that also
132 d out in this list, as the related cytosolic peroxiredoxins are known to form disulfides in the prese
133                                Typical 2-Cys peroxiredoxins are known to switch between different oli
134                                Typical 2-Cys peroxiredoxins are required to remove hydrogen peroxide
135                                              Peroxiredoxins are ubiquitous proteins that catalyze the
136 ain the phenotypic differences, and identify peroxiredoxin as an important component of virulence in
137 including the redox proteins thioredoxin and peroxiredoxin, as well as the growth factor receptors IG
138                        Here we show that the peroxiredoxin Asp f3 of Aspergillus fumigatus inactivate
139 ctrometry, we recently reclassified one such peroxiredoxin, bacterioferritin comigratory protein (BCP
140 to use this insight to improve the design of peroxiredoxin-based redox biosensors.
141                                        2-Cys peroxiredoxins belonging to the Prx1 subfamily are Cys-b
142 ssion of an antioxidative enzyme, 2-Cysteine peroxiredoxin (BxPrx), was elevated in B. xylophilus fol
143 ces cerevisiae Altogether, the processing of peroxiredoxins by Imp2 or Oct1 likely represents systems
144 the selective benefits endowed to eukaryotic peroxiredoxins by their reversible hyperoxidation.
145                            Hyperoxidation of peroxiredoxins can only occur efficiently in the presenc
146 demonstrate a clear physiological role for a peroxiredoxin chaperone and reveal a novel and unexpecte
147 i containing the disaggregase Hsp104 and the peroxiredoxin chaperone Tsa1.
148                                          The peroxiredoxin clearly preferred PfTrx2 to PfTrx1 as a re
149 ongs to the atypical 2-cysteine subfamily of peroxiredoxins, commonly referred to as bacterioferritin
150                 AhpC, the peroxide-reducing (peroxiredoxin) component of this alkyl hydroperoxidase s
151                          We also explore how peroxiredoxins contribute to YROs.
152                               In these 2-Cys peroxiredoxins, decamer formation is important for the c
153                                              Peroxiredoxin-dependent mechanisms may modulate the rece
154 multiple aging-related conduits, including a peroxiredoxin-dependent response to H(2)O(2).
155                The functional versatility of peroxiredoxins depends on progressive oxidation of key c
156            Deletion of TSA1, which encodes a peroxiredoxin, exacerbated iron toxicity in Deltaccc1 ce
157                                      Prx1, a peroxiredoxin family member, was shown to be frequently
158 typhimurium AhpC is a founding member of the peroxiredoxin family, a ubiquitous group of cysteine-bas
159 osis Tpx is a member of the atypical two-Cys peroxiredoxin family.
160  fatty acids (FA) desaturases do not require peroxiredoxins for their activity, nor does FAD4 require
161 ved the crystal structure of a typical 2-Cys peroxiredoxin from Leishmania in the dimeric (pH 8.5) an
162   Thiol peroxidases (Tpxs) are dimeric 2-Cys peroxiredoxins from bacteria that preferentially reduce
163 to those obtained for two typical 2-cysteine peroxiredoxins from Saccharomyces cerevisiae (5.4 and 6.
164 atalase (encoded by hktE) and a bifunctional peroxiredoxin-glutaredoxin (encoded by pdgX) in resistan
165 on these data, we conclude that catalase and peroxiredoxin-glutaredoxin are determinants of bacterial
166               These include catalase (HktE), peroxiredoxin/glutaredoxin (PgdX), and a ferritin-like p
167 porins and H(2) O(2) is removed by catalase, peroxiredoxin, glutathione peroxidase-like enzymes and a
168 circadian oscillations in the redox state of peroxiredoxin have been described as an additional non-t
169                   Cytosolic eukaryotic 2-Cys-peroxiredoxins have been widely reported to act as dual-
170         Using red blood cells, we found that peroxiredoxins, highly conserved antioxidant proteins, u
171 and contribute to osteoarthritis and suggest peroxiredoxin hyperoxidation as a potential mechanism.
172                                              Peroxiredoxin hyperoxidation was associated with inhibit
173                                              Peroxiredoxin hyperoxidation was observedin situin human
174 stimulation, the expression and oxidation of peroxiredoxin II (PrdxII), a critical antioxidant enzyme
175 have been due to the absence of catalase and peroxiredoxin in the purified Hb.
176 perones, Hsp33 in bacteria and typical 2-Cys peroxiredoxins in eukaryotes.
177 ism to stabilize the decameric form of 2-Cys peroxiredoxins in Leishmania mitochondria.
178  the structure and function of typical 2-Cys peroxiredoxins in response to oxidative stress.
179             Thus, AhpC and potentially other peroxiredoxins in this widespread family can elaborate a
180 the expression of Prx III, the mitochondrial peroxiredoxin, in human cardiac fibroblasts.
181 tive oxygen species, oxidizing mitochondrial peroxiredoxin, inactivating AKT/mTOR/p70S6K signaling, a
182 l, Day et al. reveal a surprising benefit of peroxiredoxin inactivation at high H(2)O(2), showing tha
183 ans Srx1 was also found to be required for a peroxiredoxin-independent function in promoting fungicid
184 support the subdivision of the BCP family of peroxiredoxins into two classes based on their catalytic
185 tive cysteine, the resolving cysteine of BCP peroxiredoxins is not conserved across all members of th
186 the use of the approach to compare different peroxiredoxin isoforms and to identify mutations and sma
187                     Together with 2-cysteine peroxiredoxin, it forms a two-component peroxide-detoxif
188 ein folding, which led to the discovery that peroxiredoxin IV (PRDX4) catalyzes a parallel oxidation
189                                              Peroxiredoxin IV (PRDX4) stood out in this list, as the
190  produced can be metabolized by ER-localized peroxiredoxin IV (PrxIV).
191 r mitochondria, leading to the protection of peroxiredoxin IV from hyperoxidation.
192                 Our results demonstrate that peroxiredoxin IV recycling in the endoplasmic reticulum
193 quence similarity 213, member A (FAM213A), a peroxiredoxin-like antioxidative protein, was repressed
194 spectrometry reveal that DJ-1 is an atypical peroxiredoxin-like peroxidase that scavenges H(2)O(2) th
195 hysiological function of DJ-1 as an atypical peroxiredoxin-like peroxidase.
196  peroxidase, the parasites rely primarily on peroxiredoxin-linked systems for protection.
197            The sulfinic or sulfonic forms of peroxiredoxin lose their peroxidase activity, which allo
198    These results show that the mitochondrial peroxiredoxin of P. falciparum occurs in both dimeric an
199 or that represses expression of an inducible peroxiredoxin, OhrA.
200 riod determination by CK1 and GSK3, and have peroxiredoxin over-oxidation cycles.
201 2 is mediated by an evolutionarily conserved peroxiredoxin-p38/MAPK signaling cascade.
202 atalysis occurs via an atypical two-cysteine peroxiredoxin pathway.
203 he mitohormetic pathway is propagated by the peroxiredoxin PRDX-2.
204 ire GUR-3 and a conserved antioxidant enzyme peroxiredoxin PRDX-2.
205                                          The peroxiredoxin (Prdx) family of antioxidant enzymes uses
206 glucose-6-phosphate dehydrogenase (G6PD) and peroxiredoxin (PRDX).
207 roxidase activity of the antioxidant protein peroxiredoxin (Prdx-1) in breast cancer cells.
208 regulation of ROS/RNS is largely attended by peroxiredoxins (Prdxs) and their main reductants, thiore
209                                              Peroxiredoxins (Prdxs) are small H(2)O(2) scavenging pro
210 rtile, and the deficiency or inactivation of Peroxiredoxins (PRDXs) is associated with human male inf
211 , peroxynitrite, and organic hydroperoxides, peroxiredoxins (Prdxs) represent a major potential prote
212 that peroxiredoxin 1 (Prx1), a member of the peroxiredoxin protein family, acts as a key mediator in
213 ediated by the membrane protein GDE2 and the peroxiredoxin protein Prdx1 that promotes neurogenesis.
214 n the oxidation state of a broadly conserved peroxiredoxin protein.
215                     We identify oxidation of peroxiredoxin proteins as a transcription-independent rh
216 e we show that oxidation-reduction cycles of peroxiredoxin proteins constitute a universal marker for
217 TXNRD1) and sulfiredoxin (SRXN1), suggesting peroxiredoxin proteins had been oxidized during monoHAA
218 t discovery of oxidation-reduction cycles of peroxiredoxin proteins, which persist even in the absenc
219 ing, e.g., over-oxidation cycles of abundant peroxiredoxin proteins.
220         PREX is a database of currently 3516 peroxiredoxin (Prx or PRDX) protein sequences unambiguou
221                             Although this Tp peroxiredoxin (Prx) closely resembles AhpC-like Prxs, Tp
222 PC-mutation-positive colorectal cancer.2-Cys peroxiredoxin (Prx) enzymes are highly expressed in most
223                              Mammalian 2-Cys peroxiredoxin (Prx) enzymes are overexpressed in most ca
224  parasite Leishmania infantum, mitochondrial peroxiredoxin (Prx) exerts intrinsic ATP-independent cha
225                                          The peroxiredoxin (PRX) family of antioxidant enzymes helps
226 iscovery that the redox regulatory proteins, peroxiredoxin (Prx) I and Prx II are specific targets of
227            Srx preferentially interacts with Peroxiredoxin (Prx) IV relative to other Prxs due to its
228 ivity in vitro Remarkably, the processing of peroxiredoxin (Prx) proteins by Oct1 appears to be an ev
229 efenses by making changes to the thioredoxin-peroxiredoxin (Prx) system.
230 terioferritin comigratory protein (BCP) is a peroxiredoxin (Prx) that catalyzes the reduction of H(2)
231 tive site cysteine of the antioxidant enzyme peroxiredoxin (Prx) to the sulfinic acid form, Prx-SO(2)
232 estingly, ACHT1 oxidation is driven by 2-Cys peroxiredoxin (Prx), which in turn eliminates peroxides.
233 zymes and reduced formation of hyperoxidized peroxiredoxin (Prx)2.
234 This reaction is unique to the typical 2-Cys peroxiredoxins (Prx) and plays a role in peroxide-mediat
235                                              Peroxiredoxins (PRX) are a family of antioxidant enzymes
236                             Eukaryotic 2-Cys peroxiredoxins (Prx) are abundant antioxidant enzymes wh
237                                              Peroxiredoxins (PRX) are critical intracellular antioxid
238                                              Peroxiredoxins (Prx) are efficient thiol-dependent perox
239                          Evidence implicates peroxiredoxins (Prx) as providing the main enzymatic act
240                                              Peroxiredoxins (Prx) make up a family of enzymes that re
241 of the active site cysteine in typical 2-Cys peroxiredoxins (Prx) to sulfinic acid during oxidative s
242                                              Peroxiredoxins (Prx), a family of peroxidases that reduc
243  to study the interactions between H(2)S and peroxiredoxins (Prx).
244 st Oct1 could cleave the human mitochondrial peroxiredoxin Prx3 when expressed in Saccharomyces cerev
245 ed to oxidative stress resistance, including peroxiredoxin PrxA, in response to hydrogen peroxide.
246                      The mitochondrial 2-Cys peroxiredoxin PrxIII serves as a thioredoxin-dependent p
247                                              Peroxiredoxins (Prxs or Prdxs) are a large protein super
248  reduces hyperoxidized 2-cysteine-containing peroxiredoxins (Prxs) and protects cells against oxidati
249 nt peroxidases, including 2-cysteine (2-Cys) peroxiredoxins (PRXs) and thylakoid ascorbate peroxidase
250                                              Peroxiredoxins (Prxs) are a ubiquitously expressed famil
251                                              Peroxiredoxins (Prxs) are crucially involved in maintain
252                                              Peroxiredoxins (Prxs) are highly conserved proteins foun
253                                              Peroxiredoxins (Prxs) are important peroxidases associat
254 O2H) residues, the sulfinic forms of certain peroxiredoxins (Prxs) are selectively reduced by sulfire
255 st group, glutathione peroxidases (GPxs) and peroxiredoxins (Prxs) are the most widespread and abunda
256                                Typical 2-Cys peroxiredoxins (Prxs) are ubiquitous peroxidases that ar
257                                              Peroxiredoxins (Prxs) are vital regulators of intracellu
258 ether with thioredoxin reductase 1 (TR1) and peroxiredoxins (Prxs) comprises a key redox regulatory s
259                                              Peroxiredoxins (Prxs) detoxify peroxides and modulate H2
260                                Typical 2-Cys peroxiredoxins (Prxs) have an important role in regulati
261                                        2-Cys peroxiredoxins (Prxs) rapidly reduce H(2)O(2), thereby a
262                                Typical 2-Cys peroxiredoxins (Prxs) react rapidly with H2O2 to form a
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 4) and a thylakoid-associated redox protein, PEROXIREDOXIN Q (PRXQ), to produce wild-type levels of 1
267 e polarization to monitor dynamic changes in peroxiredoxin quaternary structure inside the crowded en
268                In many bacteria, a dedicated peroxiredoxin reductase, alkyl hydroperoxide reductase s
269    Our results present in vivo evidence of a peroxiredoxin regulating DE-cadherin-mediated adhesion.
270   The crystal structure of the mitochondrial peroxiredoxin reveals a fold typical of the 2-Cys class
271 lose structural similarity to atypical 2-Cys peroxiredoxin(s) (Prx).
272             These observations may represent peroxiredoxin sensing and transducing the oxidant signal
273                                        Human peroxiredoxins serve dual roles as anti-oxidants and reg
274    Because of its evolutionary conservation, peroxiredoxin signaling might underlie a general princip
275 genases and cyclooxygenases may affect 2-Cys peroxiredoxin signaling, analogous to NADPH oxidases in
276 modulate the oligomeric transitions of 2-Cys peroxiredoxins such as redox state, post-translational m
277 provided further support for the thioredoxin/peroxiredoxin system as the major contributor to mitocho
278  H2O2 detoxification through the thioredoxin/peroxiredoxin system.
279 dent manner predominantly by the thioredoxin/peroxiredoxin system.
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                               For all of the peroxiredoxins, the catalytic cysteine, referred to as t
284 xpressions of those genes encoding catalase, peroxiredoxin, thioredoxin and glutathione were highly i
285 indicate that at high tissue H2O2 levels the peroxiredoxin-thioredoxin antioxidant chain becomes over
286     This detoxification pathway utilizes the peroxiredoxin/thioredoxin antioxidant system, as selecti
287 ignificant upregulation of components of the peroxiredoxin/thioredoxin pathway and processes involved
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 nhibitor-like allergen (Tri a 39), and 1-cys-peroxiredoxin (Tri a 32), produced the maximal area unde
293 y enhances the expression of the thioredoxin/peroxiredoxin (Trx/Prx) system with the greatest effect
294                In yeast, the major cytosolic peroxiredoxin, Tsa1 is required for both promoting resis
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 ity, nor does FAD4 require other chloroplast peroxiredoxins under standard growth conditions.
298 creased expression of the antioxidant enzyme peroxiredoxin-V, and a non-significant trend towards dec
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

 
Page Top