PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2669972-1 1989 Thioredoxin contains a single disulfide bond that can be reduced without perturbing significantly the structure of the enzyme. Disulfides 30-39 thioredoxin Homo sapiens 0-11 2669972-3 1989 We have experimentally tested the expected linkage relationship between disulfide bond formation and protein stability for thioredoxin. Disulfides 72-81 thioredoxin Homo sapiens 123-134 2669972-5 1989 Using glutathione as a reference species, we have measured the equilibrium constant for forming the disulfide bond (effective concentration) in thioredoxin as a function of urea concentration. Disulfides 100-109 thioredoxin Homo sapiens 144-155 2669972-7 1989 Comparison of the values obtained for disulfide bond formation in the folded and unfolded states with the free energies for unfolding oxidized and reduced thioredoxin using circular dichroism confirms the expected linkage relationship. Disulfides 38-47 thioredoxin Homo sapiens 155-166 3606128-3 1987 FTR possesses a catalytically active dithiol group localized on the 13 kDa (similar) subunit, that occurs in all species investigated and accepts reducing equivalents from photoreduced ferredoxin and transfers them stoichiometrically to the disulfide form of thioredoxin m. The reduced thioredoxin m, in turn, reduces NADP-malate dehydrogenase, thereby converting it from an inactive (S-S) to an active (SH) form. Disulfides 241-250 thioredoxin Homo sapiens 259-270 2826432-1 1988 Phosphoribulokinase is light-regulated via thioredoxin by reversible oxidation/reduction of sulfhydryl/disulfide groups. Disulfides 103-112 thioredoxin Homo sapiens 43-54 2452651-0 1988 Subunits of human alpha 2-macroglobulin produced by specific reduction of interchain disulfide bonds with thioredoxin. Disulfides 85-94 thioredoxin Homo sapiens 106-117 2452651-1 1988 Disulfide bonds in alpha 2-macroglobulin (alpha 2M) were reduced with the thioredoxin system from Escherichia coli. Disulfides 0-9 thioredoxin Homo sapiens 74-85 3606128-3 1987 FTR possesses a catalytically active dithiol group localized on the 13 kDa (similar) subunit, that occurs in all species investigated and accepts reducing equivalents from photoreduced ferredoxin and transfers them stoichiometrically to the disulfide form of thioredoxin m. The reduced thioredoxin m, in turn, reduces NADP-malate dehydrogenase, thereby converting it from an inactive (S-S) to an active (SH) form. Disulfides 241-250 thioredoxin Homo sapiens 286-297 6438823-0 1984 Structure-function relationships of human factor VIII complex studied by thioredoxin dependent disulfide reduction. Disulfides 95-104 thioredoxin Homo sapiens 73-84 3463991-6 1986 Reduced thioredoxin was optimal for catalyzing disulfide interchange in scrambled RNase, whereas oxidized thioredoxin was required for reactivation of the reduced, denatured species. Disulfides 47-56 thioredoxin Homo sapiens 8-19 3463991-8 1986 Addition of reduced thioredoxin after initiating refolding of reduced denatured RNase with oxidized glutathione effected a rapid reactivation of RNase, suggesting a two-step model for protein refolding in which the monothiol catalyzes the rapid initial formation of protein disulfides and thioredoxin catalyzes the second step of disulfide interchange. Disulfides 274-284 thioredoxin Homo sapiens 20-31 3463991-8 1986 Addition of reduced thioredoxin after initiating refolding of reduced denatured RNase with oxidized glutathione effected a rapid reactivation of RNase, suggesting a two-step model for protein refolding in which the monothiol catalyzes the rapid initial formation of protein disulfides and thioredoxin catalyzes the second step of disulfide interchange. Disulfides 274-283 thioredoxin Homo sapiens 20-31 3884381-1 1985 The insulin disulfide reducing thioredoxin system from E. coli was used to investigate a possible mechanism of degradation for the two somatomedins, insulin-like growth factor I and II (IGF-I and -II). Disulfides 12-21 thioredoxin Homo sapiens 31-42 6438823-2 1984 Limited reduction of disulfide bonds in this complex by NADPH, thioredoxin reductase and thioredoxin leads to partial disaggregation of the multimeric VIII:vWF with concomitant loss of its platelet agglutinating activity in the presence of ristocetin, and with dissociation of factor VIII:C from the complex. Disulfides 21-30 thioredoxin Homo sapiens 63-74 3463991-0 1986 Thioredoxin-catalyzed refolding of disulfide-containing proteins. Disulfides 35-44 thioredoxin Homo sapiens 0-11 3463991-1 1986 Thioredoxin, a known catalyst for reducing protein disulfides, was shown to catalyze efficiently the refolding of pancreatic RNase either from the reduced, denatured form or from the scrambled form containing oxidized but incorrectly paired disulfides. Disulfides 51-61 thioredoxin Homo sapiens 0-11 3463991-1 1986 Thioredoxin, a known catalyst for reducing protein disulfides, was shown to catalyze efficiently the refolding of pancreatic RNase either from the reduced, denatured form or from the scrambled form containing oxidized but incorrectly paired disulfides. Disulfides 241-251 thioredoxin Homo sapiens 0-11 3463991-2 1986 Thioredoxin was 1000-fold more efficient on a molar basis than the model dithiol, dithiothreitol, in reactivating reduced, denatured RNase, suggesting that thioredoxin acts as an efficient catalyst for disulfide interchange. Disulfides 202-211 thioredoxin Homo sapiens 0-11 3463991-2 1986 Thioredoxin was 1000-fold more efficient on a molar basis than the model dithiol, dithiothreitol, in reactivating reduced, denatured RNase, suggesting that thioredoxin acts as an efficient catalyst for disulfide interchange. Disulfides 202-211 thioredoxin Homo sapiens 156-167 3463991-5 1986 Thioredoxin was most effective in reactivating inactive scrambled RNase, which contained mispaired disulfides, showing a t1/2 of 2 hr. Disulfides 99-109 thioredoxin Homo sapiens 0-11 6860677-1 1983 A synthetic model peptide, (formula; see text) which mimics the active-site disulfide loop of thioredoxin has been prepared. Disulfides 76-85 thioredoxin Homo sapiens 94-105 6390091-0 1984 Enzymatic reduction-oxidation of protein disulfides by thioredoxin. Disulfides 41-51 thioredoxin Homo sapiens 55-66 6860677-7 1983 Large structural differences have been established between the thioredoxin active-site model disulfide and its acyclic precursor. Disulfides 93-102 thioredoxin Homo sapiens 63-74 32681182-3 2020 Protein disulfide isomerase (PDI) is a member of the thioredoxin (Trx) superfamily, is capable of catalyzing the formation and heterogeneity of protein disulfide bonds and inhibiting the aggregation of misfolded proteins. Disulfides 8-17 thioredoxin Homo sapiens 53-64 6761143-2 1982 Recycling of the disulfide of thioredoxin subunit to its dithiol form was made by thioredoxin reductase. Disulfides 17-26 thioredoxin Homo sapiens 30-41 6950391-1 1981 Thioredoxin and glutaredoxin may be important in regulating cell metabolism by mediating interchanges between sulfhydryl and disulfide groups. Disulfides 125-134 thioredoxin Homo sapiens 0-11 6950391-8 1981 The HeLa enzyme has low species and substrate specificity and can reduce HeLa PI and PIII, E. coli thioredoxin and glutaredoxin, and the disulfide bond in 5,5"-dithiobis(2-nitrobenzoic acid). Disulfides 137-146 thioredoxin Homo sapiens 99-110 39074-0 1979 Reduction of disulfides by thioredoxin. Disulfides 13-23 thioredoxin Homo sapiens 27-38 12950-0 1976 Enzyme reduction of disulfide bonds by thioredoxin. Disulfides 20-29 thioredoxin Homo sapiens 39-50 12950-2 1976 The NADPH-dependent enzymic reduction of disulfide bonds in human choriogonadotropin and its two subunits, alpha and beta, was examined with thioredoxin and thioredoxin reductase from Escherichia coli. Disulfides 41-50 thioredoxin Homo sapiens 141-152 12950-3 1976 With 12 muM thioredoxin and 0.1 muM thioredoxin reductase at pH 7 all disulfide bonds in the alpha subunit could be reduced in 15 min. Disulfides 70-79 thioredoxin Homo sapiens 12-23 12950-6 1976 The usefulness of thioredoxin reduction of disulfide bonds as a chemical probe of protein structure was shown by the much slower reaction of disulfide bonds in the intact hormone as compared to its two biologically inactive subunits. Disulfides 43-52 thioredoxin Homo sapiens 18-29 12950-6 1976 The usefulness of thioredoxin reduction of disulfide bonds as a chemical probe of protein structure was shown by the much slower reaction of disulfide bonds in the intact hormone as compared to its two biologically inactive subunits. Disulfides 141-150 thioredoxin Homo sapiens 18-29 33136379-7 2020 Importantly, we demonstrate the advantages of our newly developed method for the protection and deprotection of native cysteine with a succinimide group in a peptide fragment derived from thioredoxin-1 (Trx-1) obtained via intein based expression to enable ligation/desulfurization and subsequent disulfide bond formation in a one-pot process. Disulfides 297-306 thioredoxin Homo sapiens 188-201 33136379-7 2020 Importantly, we demonstrate the advantages of our newly developed method for the protection and deprotection of native cysteine with a succinimide group in a peptide fragment derived from thioredoxin-1 (Trx-1) obtained via intein based expression to enable ligation/desulfurization and subsequent disulfide bond formation in a one-pot process. Disulfides 297-306 thioredoxin Homo sapiens 203-208 32376199-5 2020 Their mixture contains a mixed disulfide between insulin B-chain and thioredoxin-Cys73, which limits their activities. Disulfides 31-40 thioredoxin Homo sapiens 69-80 4151431-0 1974 Enzymatic reduction of disulfide bonds in fibrin-ogen by the thioredoxin system. Disulfides 23-32 thioredoxin Homo sapiens 61-72 33652022-3 2021 It has been long recognized from in vitro evidence that Txnip forms a disulfide bridge through cysteine 247 (C247) with reduced thioredoxin to inhibit the anti-oxidative properties of thioredoxin. Disulfides 70-79 thioredoxin Homo sapiens 184-195 33985344-6 2021 Four of the six H1 and H3 HA bonds are cleaved by the vascular thiol isomerases, thioredoxin and protein disulphide isomerase, in recombinant proteins, which correlated with surface exposure of the disulfides in crystal structures. Disulfides 198-208 thioredoxin Homo sapiens 81-92 33756234-0 2021 Synthesis and biological evaluation of disulfides as anticancer agents with thioredoxin inhibition. Disulfides 39-49 thioredoxin Homo sapiens 76-87 33756234-3 2021 Herein, we synthesized 72 disulfides and evaluated theirinhibition for Trx and antitumor activity. Disulfides 26-36 thioredoxin Homo sapiens 71-74 33756234-7 2021 Next, we performed kinetic studies of both two disulfides, 68 had faster inhibition of Trx than 69. Disulfides 47-57 thioredoxin Homo sapiens 87-90 33011677-8 2020 A mechanistic explanation that ADAM17cyto favors the monomeric, active state of Trx-1 is the formation of a disulfide bond between Cys824 at the C-terminal of ADAM17cyto with the Cys73 of Trx-1, which is involved in the dimerization site of Trx-1. Disulfides 108-117 thioredoxin Homo sapiens 80-85 33011677-8 2020 A mechanistic explanation that ADAM17cyto favors the monomeric, active state of Trx-1 is the formation of a disulfide bond between Cys824 at the C-terminal of ADAM17cyto with the Cys73 of Trx-1, which is involved in the dimerization site of Trx-1. Disulfides 108-117 thioredoxin Homo sapiens 188-193 33011677-8 2020 A mechanistic explanation that ADAM17cyto favors the monomeric, active state of Trx-1 is the formation of a disulfide bond between Cys824 at the C-terminal of ADAM17cyto with the Cys73 of Trx-1, which is involved in the dimerization site of Trx-1. Disulfides 108-117 thioredoxin Homo sapiens 188-193 32601209-6 2020 Using the approach, we confirm peroxide- and thioredoxin-related quaternary transitions to take place in cellulo and observe that the relationship between dimer-decamer transitions and intersubunit disulfide bond formation is more complex than previously thought. Disulfides 198-207 thioredoxin Homo sapiens 45-56 32681182-3 2020 Protein disulfide isomerase (PDI) is a member of the thioredoxin (Trx) superfamily, is capable of catalyzing the formation and heterogeneity of protein disulfide bonds and inhibiting the aggregation of misfolded proteins. Disulfides 8-17 thioredoxin Homo sapiens 66-69 31623019-8 2020 Although oxidative stress induces relatively moderate structural changes in thioredoxin, the formation of intramolecular disulfide bridges leads to a considerable conformational rearrangement of the thioredoxin-binding interface on ASK1. Disulfides 121-130 thioredoxin Homo sapiens 199-210 29848267-6 2020 In contrast to the sulfinic and sulfonic acids, the mixed disulfide and the intramolecular disulfide bond are reversible oxidation products that can be reduced in the presence of GSH or thioredoxin. Disulfides 58-67 thioredoxin Homo sapiens 186-197 31124420-5 2020 Thioredoxin and glutathione systems are two main cellular disulfide reductase systems maintaining cellular ROS level. Disulfides 58-67 thioredoxin Homo sapiens 0-11 29848267-6 2020 In contrast to the sulfinic and sulfonic acids, the mixed disulfide and the intramolecular disulfide bond are reversible oxidation products that can be reduced in the presence of GSH or thioredoxin. Disulfides 91-100 thioredoxin Homo sapiens 186-197 31177768-0 2019 Fluorophore-Dependent Cleavage of Disulfide Bond Leading to a Highly Selective Fluorescent Probe of Thioredoxin. Disulfides 34-43 thioredoxin Homo sapiens 100-111 31597700-1 2019 Thioredoxin (Trx) is a redox-responsive protein that modulates the activities of its target proteins mostly by reducing their disulfide bonds. Disulfides 126-135 thioredoxin Homo sapiens 0-11 31597700-1 2019 Thioredoxin (Trx) is a redox-responsive protein that modulates the activities of its target proteins mostly by reducing their disulfide bonds. Disulfides 126-135 thioredoxin Homo sapiens 13-16 31050145-4 2019 The redox couple thioredoxin reductase-thioredoxin (TrxR-Trx) was identified as the responsible for reduction of this disulfide occurring on the cytosolic surface of synaptic vesicles. Disulfides 118-127 thioredoxin Homo sapiens 52-55 31727737-0 2019 The impact of thioredoxin reduction of allosteric disulfide bonds on the therapeutic potential of monoclonal antibodies. Disulfides 50-59 thioredoxin Homo sapiens 14-25 31727737-3 2019 Increased levels of oxidative stress associated with several diseases are counteracted by the activities of various oxidoreductase enzymes, such as thioredoxin (Trx), which also reduces allosteric disulfide bonds in proteins, including mAbs. Disulfides 197-206 thioredoxin Homo sapiens 148-159 31727737-3 2019 Increased levels of oxidative stress associated with several diseases are counteracted by the activities of various oxidoreductase enzymes, such as thioredoxin (Trx), which also reduces allosteric disulfide bonds in proteins, including mAbs. Disulfides 197-206 thioredoxin Homo sapiens 161-164 31727737-5 2019 We found that Trx reduces the interchain disulfide bonds of the mAbs, after which they remain intact but have altered function. Disulfides 41-50 thioredoxin Homo sapiens 14-17 31727737-9 2019 We also confirmed that without alkylation, Trx-reduced interchain disulfide bonds reoxidize, and ADCC activity is restored. Disulfides 66-75 thioredoxin Homo sapiens 43-46 31085544-6 2019 For a diverse set of drug-linker conjugates, we determined that TRX in the presence of TRX-reductase and NADPH generated the cleaved products that are consistent with catalytic disulfide cleavage and linker immolation. Disulfides 177-186 thioredoxin Homo sapiens 64-67 31085544-6 2019 For a diverse set of drug-linker conjugates, we determined that TRX in the presence of TRX-reductase and NADPH generated the cleaved products that are consistent with catalytic disulfide cleavage and linker immolation. Disulfides 177-186 thioredoxin Homo sapiens 87-90 31085544-8 2019 Collectively, these in vitro experiments demonstrate that TRX as well as GRX can catalyze the cleavage of disulfide bonds in both small molecules and linkers of ADCs. Disulfides 106-115 thioredoxin Homo sapiens 58-61 31266802-6 2019 Thioredoxin (Trx) and glutaredoxin (Grx) systems have been implicated as electron donors for the RNR disulfide reduction via the swinging arm. Disulfides 101-110 thioredoxin Homo sapiens 0-11 31266802-6 2019 Thioredoxin (Trx) and glutaredoxin (Grx) systems have been implicated as electron donors for the RNR disulfide reduction via the swinging arm. Disulfides 101-110 thioredoxin Homo sapiens 13-16 31177768-5 2019 In addition, our discovery, i.e., the preference reduction of simple disulfide bonds by Trx over glutathione, also advances the development of disulfide cleavage-based probes, prodrugs, and theranostic agents. Disulfides 69-78 thioredoxin Homo sapiens 88-91 31177768-5 2019 In addition, our discovery, i.e., the preference reduction of simple disulfide bonds by Trx over glutathione, also advances the development of disulfide cleavage-based probes, prodrugs, and theranostic agents. Disulfides 143-152 thioredoxin Homo sapiens 88-91 30718304-9 2019 On the basis of these results, I propose that the DeltacysL mutation causes phosphoadenosine phosphosulfate reductase to consume large amounts of reduced thioredoxin, inducing disulfide stress and activating Spx. Disulfides 176-185 thioredoxin Homo sapiens 154-165 30948772-6 2019 Moreover, PX-12 inhibited the enzymatic activity of Trx1 and the Trx1-dependent disulfide reduction of gp120. Disulfides 80-89 thioredoxin Homo sapiens 65-69 30853337-9 2019 Although the disulfide-bonded form of homocysteine (HSSH) modified PTP1B to form an inactive S-homocysteinylated PTP1B, HcySH-induced increase in the activities of cellular thioredoxin and thioredoxin reductase, components of thioredoxin system, could recover active PTP1B from S-homocysteinylated PTP1B. Disulfides 13-22 thioredoxin Homo sapiens 173-184 30853337-9 2019 Although the disulfide-bonded form of homocysteine (HSSH) modified PTP1B to form an inactive S-homocysteinylated PTP1B, HcySH-induced increase in the activities of cellular thioredoxin and thioredoxin reductase, components of thioredoxin system, could recover active PTP1B from S-homocysteinylated PTP1B. Disulfides 13-22 thioredoxin Homo sapiens 189-200 30853337-9 2019 Although the disulfide-bonded form of homocysteine (HSSH) modified PTP1B to form an inactive S-homocysteinylated PTP1B, HcySH-induced increase in the activities of cellular thioredoxin and thioredoxin reductase, components of thioredoxin system, could recover active PTP1B from S-homocysteinylated PTP1B. Disulfides 13-22 thioredoxin Homo sapiens 189-200 30367780-2 2019 The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction. Disulfides 90-99 thioredoxin Homo sapiens 4-15 30367780-2 2019 The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction. Disulfides 90-99 thioredoxin Homo sapiens 40-51 30367780-2 2019 The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction. Disulfides 90-99 thioredoxin Homo sapiens 53-56 30367780-2 2019 The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction. Disulfides 171-180 thioredoxin Homo sapiens 4-15 30367780-2 2019 The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction. Disulfides 171-180 thioredoxin Homo sapiens 40-51 30367780-2 2019 The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction. Disulfides 171-180 thioredoxin Homo sapiens 53-56 30367780-2 2019 The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction. Disulfides 171-180 thioredoxin Homo sapiens 4-15 30367780-2 2019 The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction. Disulfides 171-180 thioredoxin Homo sapiens 40-51 30367780-2 2019 The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction. Disulfides 171-180 thioredoxin Homo sapiens 53-56 30948772-2 2019 The host thioredoxin-1 (Trx1) efficiently reduces disulfides of gp120 and CD4 in vitro, and recently CD4-dependent HIV-1 entry was shown to be inhibited by anti-Trx1-antibodies, indicating a central role for Trx1. Disulfides 50-60 thioredoxin Homo sapiens 24-28 30948772-2 2019 The host thioredoxin-1 (Trx1) efficiently reduces disulfides of gp120 and CD4 in vitro, and recently CD4-dependent HIV-1 entry was shown to be inhibited by anti-Trx1-antibodies, indicating a central role for Trx1. Disulfides 50-60 thioredoxin Homo sapiens 161-165 30948772-2 2019 The host thioredoxin-1 (Trx1) efficiently reduces disulfides of gp120 and CD4 in vitro, and recently CD4-dependent HIV-1 entry was shown to be inhibited by anti-Trx1-antibodies, indicating a central role for Trx1. Disulfides 50-60 thioredoxin Homo sapiens 161-165 30545068-5 2018 Disulfide can be easily reversed by different enzymatic systems such as the thioredoxin/thioredoxin reductase and the glutaredoxin/glutathione/glutathione reductase systems. Disulfides 0-9 thioredoxin Homo sapiens 76-87 30401714-1 2019 Glutathione (GSH)/GSH reductase (GSR) and thioredoxin/thioredoxin reductase (TXNRD) are two major compensating thiol-dependent antioxidant pathways that maintain protein dithiol/disulfide balance. Disulfides 178-187 thioredoxin Homo sapiens 42-53 30742135-6 2019 Impeding intra-endosomal disulfide reduction by knocking down TRX-1 protects nematodes from infection by Corynebacterium diphtheriae, revealing the importance of this minor pool of endosomal TRX-1. Disulfides 25-34 thioredoxin Homo sapiens 62-67 30742135-6 2019 Impeding intra-endosomal disulfide reduction by knocking down TRX-1 protects nematodes from infection by Corynebacterium diphtheriae, revealing the importance of this minor pool of endosomal TRX-1. Disulfides 25-34 thioredoxin Homo sapiens 191-196 30742135-7 2019 TRX-1 also mediates endosomal disulfide reduction in human cells. Disulfides 30-39 thioredoxin Homo sapiens 0-5 30341785-4 2019 The enzymes of this class often use a CXXC active-site motif embedded in their thioredoxin-like fold to promote formation, isomerization, and reduction of a disulfide bond in their target proteins. Disulfides 157-166 thioredoxin Homo sapiens 79-90 29410996-2 2018 The thioredoxin system, comprised of NADPH, thioredoxin reductase (TrxR) and thioredoxin (Trx), exerts its activities via a disulfide-dithiol exchange reaction. Disulfides 124-133 thioredoxin Homo sapiens 4-15 30104382-0 2018 Interleukin 4 is inactivated via selective disulfide-bond reduction by extracellular thioredoxin. Disulfides 43-52 thioredoxin Homo sapiens 85-96 30104382-2 2018 Recently, we showed that TRX activates extracellular transglutaminase 2 via reduction of an allosteric disulfide bond. Disulfides 103-112 thioredoxin Homo sapiens 25-28 30104382-5 2018 To test this hypothesis, the C35S mutant of human TRX was shown to form a mixed disulfide bond with recombinant IL-4 but not IL-13. Disulfides 80-89 thioredoxin Homo sapiens 50-53 30104382-7 2018 Mass spectrometry identified the C46-C99 bond of IL-4 as the target of TRX, consistent with the essential role of this disulfide bond in IL-4 activity. Disulfides 119-128 thioredoxin Homo sapiens 71-74 30104382-9 2018 By establishing that IL-4 is posttranslationally regulated by TRX-promoted reduction of a disulfide bond, our findings highlight a novel regulatory mechanism of the type 2 immune response that is specific to IL-4 over IL-13. Disulfides 90-99 thioredoxin Homo sapiens 62-65 29420254-8 2018 This involves an initial sulfenylation of the active site thiol followed by the formation of an intrachain disulfide with a resolving thiol group and completed by the reduction of this disulfide by a thioredoxin-like protein to regenerate the active site thiol. Disulfides 107-116 thioredoxin Homo sapiens 200-211 29420254-8 2018 This involves an initial sulfenylation of the active site thiol followed by the formation of an intrachain disulfide with a resolving thiol group and completed by the reduction of this disulfide by a thioredoxin-like protein to regenerate the active site thiol. Disulfides 185-194 thioredoxin Homo sapiens 200-211 30043021-0 2018 Modulating the GSH/Trx selectivity of a fluorogenic disulfide-based thiol sensor to reveal diminished GSH levels under ER stress. Disulfides 52-61 thioredoxin Homo sapiens 19-22 29305423-9 2018 We conclude that, to the best of our knowledge, the disulfide bond switch in human TG2 represents the first example of a post-translational redox regulatory mechanism that is reversibly and allosterically modulated by two distinct proteins (ERp57 and TRX). Disulfides 52-61 thioredoxin Homo sapiens 251-254 29410996-2 2018 The thioredoxin system, comprised of NADPH, thioredoxin reductase (TrxR) and thioredoxin (Trx), exerts its activities via a disulfide-dithiol exchange reaction. Disulfides 124-133 thioredoxin Homo sapiens 44-55 29410996-2 2018 The thioredoxin system, comprised of NADPH, thioredoxin reductase (TrxR) and thioredoxin (Trx), exerts its activities via a disulfide-dithiol exchange reaction. Disulfides 124-133 thioredoxin Homo sapiens 67-70 29278740-1 2018 Mammalian thioredoxin reductases (TrxRs) are selenocysteine-containing proteins (selenoproteins) that propel a large number of functions through reduction of several substrates including the active site disulfide of thioredoxins (Trxs). Disulfides 203-212 thioredoxin Homo sapiens 216-228 29261301-3 2018 The currently available inhibitors of Trx1 and Grx1 are thiol-reactive electrophiles or disulfides that may suffer from low selectivity because of their thiol reactivity. Disulfides 88-98 thioredoxin Homo sapiens 38-42 28939765-1 2017 Thioredoxin 1 (Trx1) is a 12-kDa oxidoreductase that catalyzes thiol-disulfide exchange reactions to reduce proteins with disulfide bonds. Disulfides 69-78 thioredoxin Homo sapiens 15-19 28917053-1 2018 Thioredoxin reductases are important oxidoreductases that keep the active site disulfide/dithiol motif of thioredoxins reduced using NADPH, thereby supporting many thioredoxin-dependent reductive pathways in cells. Disulfides 79-88 thioredoxin Homo sapiens 0-11 28917053-1 2018 Thioredoxin reductases are important oxidoreductases that keep the active site disulfide/dithiol motif of thioredoxins reduced using NADPH, thereby supporting many thioredoxin-dependent reductive pathways in cells. Disulfides 79-88 thioredoxin Homo sapiens 106-117 28939765-1 2017 Thioredoxin 1 (Trx1) is a 12-kDa oxidoreductase that catalyzes thiol-disulfide exchange reactions to reduce proteins with disulfide bonds. Disulfides 122-131 thioredoxin Homo sapiens 15-19 28375144-5 2017 Crystallographic data for shrimp thioredoxin (LvTrx) obtained under different redox conditions reveal a dimeric arrangement mediated by a disulfide bond through residue Cys73 and other hydrophobic interactions located in the crystallographic interface, as reported for human Trx. Disulfides 138-147 thioredoxin Homo sapiens 33-44 28878015-6 2017 Recombinant Trx1 preferentially binds to monomeric MLKL and blocks MLKL disulfide bond formation and polymerization in vitro Inhibition of MLKL polymer formation requires the reducing activity of Trx1. Disulfides 72-81 thioredoxin Homo sapiens 12-16 28878015-6 2017 Recombinant Trx1 preferentially binds to monomeric MLKL and blocks MLKL disulfide bond formation and polymerization in vitro Inhibition of MLKL polymer formation requires the reducing activity of Trx1. Disulfides 72-81 thioredoxin Homo sapiens 196-200 28411237-3 2017 Thioredoxin (Trx) and glutaredoxin (Grx) are ubiquitous redox proteins, catalyzing thiol-disulfide exchange reactions. Disulfides 89-98 thioredoxin Homo sapiens 0-11 28411237-3 2017 Thioredoxin (Trx) and glutaredoxin (Grx) are ubiquitous redox proteins, catalyzing thiol-disulfide exchange reactions. Disulfides 89-98 thioredoxin Homo sapiens 13-16 29016988-1 2017 Once the ferredoxin/thioredoxin system was established as a mechanism linking light to the post-translational regulation of chloroplast enzymes, I considered that plants might harbor a light-independent mechanism utilizing this same enzyme chemistry based on thiol-disulfide redox transitions. Disulfides 265-274 thioredoxin Homo sapiens 20-31 28551108-3 2017 On the other hand, PbTx-2 activates the reduction of small disulfides such as 5,5"-dithio-bis-(2-nitrobenzoic acid) by thioredoxin reductase. Disulfides 59-69 thioredoxin Homo sapiens 119-130 28262915-0 2017 Glutathione and thioredoxin systems contribute to recombinant monoclonal antibody interchain disulfide bond reduction during bioprocessing. Disulfides 93-102 thioredoxin Homo sapiens 16-27 28375144-5 2017 Crystallographic data for shrimp thioredoxin (LvTrx) obtained under different redox conditions reveal a dimeric arrangement mediated by a disulfide bond through residue Cys73 and other hydrophobic interactions located in the crystallographic interface, as reported for human Trx. Disulfides 138-147 thioredoxin Homo sapiens 48-51 28139457-1 2017 Thioredoxins are ubiquitous enzymes catalyzing reversible disulfide-bond formation to regulate structure and function of many proteins in diverse organisms. Disulfides 58-67 thioredoxin Homo sapiens 0-12 28093500-4 2017 Here, we use a novel assay to demonstrate that the reduction in non-native disulfides requires NADPH as the ultimate electron donor, and a robust cytosolic thioredoxin system, driven by thioredoxin reductase 1 (TrxR1 or TXNRD1). Disulfides 75-85 thioredoxin Homo sapiens 156-167 28044432-8 2017 The oxidation and reduction of redox-active disulfides are mediated by cellular reactive oxygen species and activity of reductases, such as glutaredoxin and thioredoxin. Disulfides 44-54 thioredoxin Homo sapiens 157-168 27404998-7 2017 We also found that geldanamycin strongly synergises with PX-12, an inhibitor of thioredoxin, suggesting that the processes of L chain refolding and interchain disulfide reduction are strictly coupled. Disulfides 159-168 thioredoxin Homo sapiens 80-91 27588831-7 2016 The disulfide bond formation between C32 and C35 within the active site of TRX1 is the main factor responsible for the TRX1 dissociation upon its oxidation as the formation of the second disulfide bond between noncatalytic cysteines C62 and C69 did not have any additional effect. Disulfides 4-13 thioredoxin Homo sapiens 75-79 27588831-7 2016 The disulfide bond formation between C32 and C35 within the active site of TRX1 is the main factor responsible for the TRX1 dissociation upon its oxidation as the formation of the second disulfide bond between noncatalytic cysteines C62 and C69 did not have any additional effect. Disulfides 4-13 thioredoxin Homo sapiens 119-123 27588831-7 2016 The disulfide bond formation between C32 and C35 within the active site of TRX1 is the main factor responsible for the TRX1 dissociation upon its oxidation as the formation of the second disulfide bond between noncatalytic cysteines C62 and C69 did not have any additional effect. Disulfides 187-196 thioredoxin Homo sapiens 75-79 27588831-7 2016 The disulfide bond formation between C32 and C35 within the active site of TRX1 is the main factor responsible for the TRX1 dissociation upon its oxidation as the formation of the second disulfide bond between noncatalytic cysteines C62 and C69 did not have any additional effect. Disulfides 187-196 thioredoxin Homo sapiens 119-123 27588831-9 2016 Furthermore, our data show that the catalytic site of TRX1 interacts with ASK1-TBD region containing cysteine C200 and that the oxidative stress induces intramolecular disulfide bond formation within ASK1-TBD and affects its structure in regions directly involved and/or important for TRX1 binding. Disulfides 168-177 thioredoxin Homo sapiens 54-58 27588831-9 2016 Furthermore, our data show that the catalytic site of TRX1 interacts with ASK1-TBD region containing cysteine C200 and that the oxidative stress induces intramolecular disulfide bond formation within ASK1-TBD and affects its structure in regions directly involved and/or important for TRX1 binding. Disulfides 168-177 thioredoxin Homo sapiens 285-289 26513450-7 2015 This is because disulfide bonds are stable in most blood pools but are efficiently cleaved by cellular thiols, including glutathione (GSH) and thioredoxin (Trx), which are generally found at elevated levels in tumors. Disulfides 16-25 thioredoxin Homo sapiens 143-154 27029462-12 2016 We show that Escherichia coli Trx83 with a truncated Trx fold induces PBMC proliferation, but only in the disulfide-reduced form. Disulfides 106-115 thioredoxin Homo sapiens 30-33 26945066-5 2016 The dimeric disulfide DJ-1 complex was stabilized by auranofin, suggesting that thioredoxin recycles it in cells. Disulfides 12-21 thioredoxin Homo sapiens 80-91 26772871-4 2016 We used a redox sensitive green fluorescent protein (GFP) fused to the N- or C-terminus to show that these regions face the cytosol, and introduction of glycosylation sites along with mixed disulfide formation with thioredoxin-like transmembrane protein (TMX) to demonstrate ER localization of the major loop. Disulfides 190-199 thioredoxin Homo sapiens 215-226 28955804-2 2016 Thioredoxin 1 (Trx1) is an important reducing enzyme that cleaves disulfides in proteins and acts as an S-denitrosylase. Disulfides 66-76 thioredoxin Homo sapiens 0-13 28955804-2 2016 Thioredoxin 1 (Trx1) is an important reducing enzyme that cleaves disulfides in proteins and acts as an S-denitrosylase. Disulfides 66-76 thioredoxin Homo sapiens 15-19 26451472-0 2015 Thioredoxin Cross-Linking by Nitrogen Mustard in Lung Epithelial Cells: Formation of Multimeric Thioredoxin/Thioredoxin Reductase Complexes and Inhibition of Disulfide Reduction. Disulfides 158-167 thioredoxin Homo sapiens 0-11 26451472-1 2015 The thioredoxin (Trx) system, which consists of Trx and thioredoxin reductase (TrxR), is a major cellular disulfide reduction system important in antioxidant defense. Disulfides 106-115 thioredoxin Homo sapiens 4-15 26451472-1 2015 The thioredoxin (Trx) system, which consists of Trx and thioredoxin reductase (TrxR), is a major cellular disulfide reduction system important in antioxidant defense. Disulfides 106-115 thioredoxin Homo sapiens 17-20 26451472-1 2015 The thioredoxin (Trx) system, which consists of Trx and thioredoxin reductase (TrxR), is a major cellular disulfide reduction system important in antioxidant defense. Disulfides 106-115 thioredoxin Homo sapiens 48-51 26451472-11 2015 Inhibition of the Trx system by HN2 can disrupt cellular thiol-disulfide balance, contributing to vesicant-induced lung toxicity. Disulfides 63-72 thioredoxin Homo sapiens 18-21 25911959-2 2016 In vitro, thioredoxin reduces this disulfide and thioredoxin reductase (TrxR) is part of a cytosolic complex facilitating DTA-translocation. Disulfides 35-44 thioredoxin Homo sapiens 10-21 26795153-4 2016 Thiol-disulfide redox regulation is dependent on the conserved redox proteins, glutathione/glutaredoxin (GRX) and thioredoxin (TRX) systems. Disulfides 6-15 thioredoxin Homo sapiens 114-125 26795153-4 2016 Thiol-disulfide redox regulation is dependent on the conserved redox proteins, glutathione/glutaredoxin (GRX) and thioredoxin (TRX) systems. Disulfides 6-15 thioredoxin Homo sapiens 127-130 26453009-5 2015 The non-active disulfide switches the alpha3-helix of TRX, composed of residues Cys62 to Glu70, to a bulging loop and dramatically changes the environment of the TRX residues involved in the interaction with its reductase and other cellular substrates. Disulfides 15-24 thioredoxin Homo sapiens 54-57 26453009-5 2015 The non-active disulfide switches the alpha3-helix of TRX, composed of residues Cys62 to Glu70, to a bulging loop and dramatically changes the environment of the TRX residues involved in the interaction with its reductase and other cellular substrates. Disulfides 15-24 thioredoxin Homo sapiens 162-165 26513450-7 2015 This is because disulfide bonds are stable in most blood pools but are efficiently cleaved by cellular thiols, including glutathione (GSH) and thioredoxin (Trx), which are generally found at elevated levels in tumors. Disulfides 16-25 thioredoxin Homo sapiens 156-159 26417924-2 2015 TrxR catalyzes disulfide reduction in Trx with NADPH as cofactor. Disulfides 15-24 thioredoxin Homo sapiens 0-3 26417924-3 2015 Because Trx is an antioxidant, oxidative stress results in an increase in Trx, which has a reduced disulfide component. Disulfides 99-108 thioredoxin Homo sapiens 8-11 26417924-3 2015 Because Trx is an antioxidant, oxidative stress results in an increase in Trx, which has a reduced disulfide component. Disulfides 99-108 thioredoxin Homo sapiens 74-77 26119781-2 2015 One of its component, Trx, is involved in redox homeostasis and many cellular biological processes through participating in disulfide reduction, S-nitrosylation/S-denitrosylation reactions and protein-protein interactions. Disulfides 124-133 thioredoxin Homo sapiens 22-25 25926547-3 2015 Thioredoxin system not only plays a crucial role as thiol/disulfide redox controller, it is also essential for certain organisms as the only system ensuring the redox homeostasis. Disulfides 58-67 thioredoxin Homo sapiens 0-11 25805991-2 2015 Glutathione-cysteine adducts may be removed from proteins by glutaredoxin, whereas disulfides may be reduced by thioredoxin. Disulfides 83-93 thioredoxin Homo sapiens 112-123 25856548-4 2015 We devise a free-energy calculation scheme, which makes use of the Crooks Gaussian intersection method to estimate the redox potential of thiol/disulfide pairs in 12 proteins belonging to the thioredoxin superfamily, namely, thioredoxins, glutaredoxins, and thiol-disulfide oxidoreductases in disulfide bond formation systems. Disulfides 144-153 thioredoxin Homo sapiens 192-203 25856548-4 2015 We devise a free-energy calculation scheme, which makes use of the Crooks Gaussian intersection method to estimate the redox potential of thiol/disulfide pairs in 12 proteins belonging to the thioredoxin superfamily, namely, thioredoxins, glutaredoxins, and thiol-disulfide oxidoreductases in disulfide bond formation systems. Disulfides 264-273 thioredoxin Homo sapiens 192-203 25874934-1 2015 Thioredoxins are small soluble proteins that contain a redox-active disulfide (CXXC). Disulfides 68-77 thioredoxin Homo sapiens 0-12 25874934-2 2015 These disulfides are tuned to oxidizing or reducing potentials depending on the function of the thioredoxin within the cell. Disulfides 6-16 thioredoxin Homo sapiens 96-107 25877331-4 2015 All the corresponding recombinant proteins form various types of covalent oligomers linked by intermolecular disulfide bonds that are reduced in vitro by the thioredoxin (TRX) and/or glutathione/glutaredoxin (GRX) systems. Disulfides 109-118 thioredoxin Homo sapiens 158-169 25877331-4 2015 All the corresponding recombinant proteins form various types of covalent oligomers linked by intermolecular disulfide bonds that are reduced in vitro by the thioredoxin (TRX) and/or glutathione/glutaredoxin (GRX) systems. Disulfides 109-118 thioredoxin Homo sapiens 171-174 25873657-1 2015 In plants, the presence of thioredoxin (Trx), peroxiredoxin (Prx), and sulfiredoxin (Srx) has been reported as a component of a redox system involved in the control of dithiol-disulfide exchanges of target proteins, which modulate redox signalling during development and stress adaptation. Disulfides 176-185 thioredoxin Homo sapiens 27-38 25873657-1 2015 In plants, the presence of thioredoxin (Trx), peroxiredoxin (Prx), and sulfiredoxin (Srx) has been reported as a component of a redox system involved in the control of dithiol-disulfide exchanges of target proteins, which modulate redox signalling during development and stress adaptation. Disulfides 176-185 thioredoxin Homo sapiens 40-43 25805991-3 2015 Glutaredoxin is homologous to the disulfide-reducing thioredoxin and shares similar binding modes of the protein substrate. Disulfides 34-43 thioredoxin Homo sapiens 53-64 25725525-11 2015 Thioredoxin reduces the disulfide bond more effectively than dithiothreitol, although the specificity mechanism has not been identified. Disulfides 24-33 thioredoxin Homo sapiens 0-11 26461388-6 2014 Here we examine the design requirements for the Peroxiredoxin/Thioredoxin/Thioredoxin-Reductase/Protein-Dithiol System (PTTRDS) to effectively integrate H2O2 signaling and anticipatory blocking of protein dithiols as disulfides, and we compared them to the designs found in cells. Disulfides 217-227 thioredoxin Homo sapiens 62-73 25242227-4 2014 The Thioredoxin Reductase-Thioredoxin system cleaves the interchain disulfide, and its inhibition prevents neurotoxicity, and may provide novel strategies for chemoprophylaxis and therapy. Disulfides 68-77 thioredoxin Homo sapiens 4-15 26064419-7 2015 An increase in total antioxidant activity (82%, p <= 0.01) and thiol-disulfide system response (thioredoxin increasing by 33%, p <= 0.01; glutathione, 30%, p <= 0.01 with stable reductases levels) maintains a balance of peroxidation-antioxidant processes, protecting cellular and subcellular structures from significant oxidative damage. Disulfides 72-81 thioredoxin Homo sapiens 99-110 25231459-2 2014 Trx1 is a key reductase that reduces specific disulfide bonds and other cysteine post-translational modifications. Disulfides 46-55 thioredoxin Homo sapiens 0-4 25231459-6 2014 The wild-type Trx1 contains a conserved C32XXC35 motif, and the C32 thiol initiates the reduction of a target disulfide bond by forming an intermolecular disulfide with one of the oxidized target cysteines, resulting in a transient Trx1-target protein complex. Disulfides 110-119 thioredoxin Homo sapiens 14-18 25231459-6 2014 The wild-type Trx1 contains a conserved C32XXC35 motif, and the C32 thiol initiates the reduction of a target disulfide bond by forming an intermolecular disulfide with one of the oxidized target cysteines, resulting in a transient Trx1-target protein complex. Disulfides 110-119 thioredoxin Homo sapiens 232-236 25231459-6 2014 The wild-type Trx1 contains a conserved C32XXC35 motif, and the C32 thiol initiates the reduction of a target disulfide bond by forming an intermolecular disulfide with one of the oxidized target cysteines, resulting in a transient Trx1-target protein complex. Disulfides 154-163 thioredoxin Homo sapiens 14-18 25231459-6 2014 The wild-type Trx1 contains a conserved C32XXC35 motif, and the C32 thiol initiates the reduction of a target disulfide bond by forming an intermolecular disulfide with one of the oxidized target cysteines, resulting in a transient Trx1-target protein complex. Disulfides 154-163 thioredoxin Homo sapiens 232-236 25231459-7 2014 The reduction is rapidly consummated by the donation of a C35 proton to the target molecule, forming a Trx1 C32-C35 disulfide, and results in the concurrent release of the target protein containing reduced thiols. Disulfides 116-125 thioredoxin Homo sapiens 103-107 24328910-4 2014 RECENT ADVANCES: The thioredoxin (Trx) system, which is predominantly expressed in pulmonary epithelia in the newborn lung, acts as an antioxidant system; however, it is increasingly recognized as a key redox regulator of signal transduction and gene expression via thiol-disulfide exchange reactions. Disulfides 272-281 thioredoxin Homo sapiens 21-32 24328910-4 2014 RECENT ADVANCES: The thioredoxin (Trx) system, which is predominantly expressed in pulmonary epithelia in the newborn lung, acts as an antioxidant system; however, it is increasingly recognized as a key redox regulator of signal transduction and gene expression via thiol-disulfide exchange reactions. Disulfides 272-281 thioredoxin Homo sapiens 34-37 24863694-2 2014 The thioredoxin (Trx) and glutaredoxin (Grx) systems are two central systems upholding the sulfhydryl homeostasis by reducing disulfides and mixed disulfides within the cell and thereby protecting against oxidative stress. Disulfides 147-157 thioredoxin Homo sapiens 4-15 25220457-3 2014 Here, we show that the thioredoxin reductase-thioredoxin protein disulfide-reducing system is present on synaptic vesicles and that it is functional and responsible for the reduction of the interchain disulfide of botulinum neurotoxin serotypes A, C, and E. Specific inhibitors of thioredoxin reductase or thioredoxin prevent intoxication of cultured neurons in a dose-dependent manner and are also very effective inhibitors of the paralysis of the neuromuscular junction. Disulfides 65-74 thioredoxin Homo sapiens 23-34 25220457-3 2014 Here, we show that the thioredoxin reductase-thioredoxin protein disulfide-reducing system is present on synaptic vesicles and that it is functional and responsible for the reduction of the interchain disulfide of botulinum neurotoxin serotypes A, C, and E. Specific inhibitors of thioredoxin reductase or thioredoxin prevent intoxication of cultured neurons in a dose-dependent manner and are also very effective inhibitors of the paralysis of the neuromuscular junction. Disulfides 65-74 thioredoxin Homo sapiens 45-56 25220457-3 2014 Here, we show that the thioredoxin reductase-thioredoxin protein disulfide-reducing system is present on synaptic vesicles and that it is functional and responsible for the reduction of the interchain disulfide of botulinum neurotoxin serotypes A, C, and E. Specific inhibitors of thioredoxin reductase or thioredoxin prevent intoxication of cultured neurons in a dose-dependent manner and are also very effective inhibitors of the paralysis of the neuromuscular junction. Disulfides 201-210 thioredoxin Homo sapiens 23-34 25220457-3 2014 Here, we show that the thioredoxin reductase-thioredoxin protein disulfide-reducing system is present on synaptic vesicles and that it is functional and responsible for the reduction of the interchain disulfide of botulinum neurotoxin serotypes A, C, and E. Specific inhibitors of thioredoxin reductase or thioredoxin prevent intoxication of cultured neurons in a dose-dependent manner and are also very effective inhibitors of the paralysis of the neuromuscular junction. Disulfides 201-210 thioredoxin Homo sapiens 45-56 24863694-2 2014 The thioredoxin (Trx) and glutaredoxin (Grx) systems are two central systems upholding the sulfhydryl homeostasis by reducing disulfides and mixed disulfides within the cell and thereby protecting against oxidative stress. Disulfides 126-136 thioredoxin Homo sapiens 4-15 24863694-2 2014 The thioredoxin (Trx) and glutaredoxin (Grx) systems are two central systems upholding the sulfhydryl homeostasis by reducing disulfides and mixed disulfides within the cell and thereby protecting against oxidative stress. Disulfides 126-136 thioredoxin Homo sapiens 17-20 24863694-2 2014 The thioredoxin (Trx) and glutaredoxin (Grx) systems are two central systems upholding the sulfhydryl homeostasis by reducing disulfides and mixed disulfides within the cell and thereby protecting against oxidative stress. Disulfides 147-157 thioredoxin Homo sapiens 17-20 24483600-1 2014 SIGNIFICANCE: The thioredoxin (Trx) superfamily proteins, including protein disulfide isomerases (PDI) and Dsb protein family, are major players in oxidative protein folding, which involves native disulfide bond formation. Disulfides 76-85 thioredoxin Homo sapiens 18-29 24483600-1 2014 SIGNIFICANCE: The thioredoxin (Trx) superfamily proteins, including protein disulfide isomerases (PDI) and Dsb protein family, are major players in oxidative protein folding, which involves native disulfide bond formation. Disulfides 76-85 thioredoxin Homo sapiens 31-34 24483600-6 2014 CRITICAL ISSUES: Electron transfer pathways of the oxidative protein folding show conserved Trx-like thiol-disulfide chemistry. Disulfides 107-116 thioredoxin Homo sapiens 92-95 24778250-3 2014 Moreover, the l-cystine reduction with TRP14 was in contrast to that of Trx1 fully maintained in the presence of a protein disulfide substrate of Trx1 such as insulin, suggesting that TRP14 is a more dedicated l-cystine reductase compared with Trx1. Disulfides 123-132 thioredoxin Homo sapiens 146-150 24846539-6 2014 Significantly, the disulfides were reduced by thioredoxin, suggesting that autolysis of HtrA1 in vivo is linked to the endogenous redox balance and that the N-terminal domain acts as a redox-sensing switch. Disulfides 19-29 thioredoxin Homo sapiens 46-57 24700462-6 2014 The disulfide has a standard redox potential of -261 mV and is efficiently reduced by the protein reductant, thioredoxin, with a rate constant of 16,180 m(-1) s(-1). Disulfides 4-13 thioredoxin Homo sapiens 109-120 24778250-3 2014 Moreover, the l-cystine reduction with TRP14 was in contrast to that of Trx1 fully maintained in the presence of a protein disulfide substrate of Trx1 such as insulin, suggesting that TRP14 is a more dedicated l-cystine reductase compared with Trx1. Disulfides 123-132 thioredoxin Homo sapiens 146-150 24374250-0 2014 Activity assays of mammalian thioredoxin and thioredoxin reductase: fluorescent disulfide substrates, mechanisms, and use with tissue samples. Disulfides 80-89 thioredoxin Homo sapiens 29-40 24374250-2 2014 Human cytosolic Trx1 has Cys32 and Cys35 as the active site and three additional cysteine residues (Cys62, Cys69, and Cys73), which by oxidation generates inactive Cys62 to Cys69 two-disulfide Trx. Disulfides 183-192 thioredoxin Homo sapiens 16-20 24374250-2 2014 Human cytosolic Trx1 has Cys32 and Cys35 as the active site and three additional cysteine residues (Cys62, Cys69, and Cys73), which by oxidation generates inactive Cys62 to Cys69 two-disulfide Trx. Disulfides 183-192 thioredoxin Homo sapiens 16-19 24462249-0 2014 Radically different thioredoxin domain arrangement of ERp46, an efficient disulfide bond introducer of the mammalian PDI family. Disulfides 74-83 thioredoxin Homo sapiens 20-31 24591711-3 2014 In the reduced state, thioredoxins control the structure and function of proteins by reducing disulfide bridges in the redox active site of a protein. Disulfides 94-103 thioredoxin Homo sapiens 22-34 24103200-8 2014 In a purified system, ABX shortened the initial lag phase during the reduction of insulin disulfide by Trx system. Disulfides 90-99 thioredoxin Homo sapiens 103-106 24422500-9 2014 This experimental observation most likely means that the selenolate is the nucleophile initially attacking the disulfide bond of Trx because a complex resulted only when Cys was present in the second position of the dyad. Disulfides 111-120 thioredoxin Homo sapiens 129-132 24506865-6 2014 Thioredoxin1 (Trx1), an important reducing enzyme that cleaves disulfides in proteins, prevents AMPK oxidation, serving as an essential cofactor for AMPK activation. Disulfides 63-73 thioredoxin Homo sapiens 0-12 24506865-6 2014 Thioredoxin1 (Trx1), an important reducing enzyme that cleaves disulfides in proteins, prevents AMPK oxidation, serving as an essential cofactor for AMPK activation. Disulfides 63-73 thioredoxin Homo sapiens 14-18 24409188-2 2014 Thioredoxin1 (Trx1) and Thioredoxin2 (Trx2), mainly located in the cytoplasm and mitochondria, respectively, are ubiquitously expressed in variety of cells and control cellular reactive oxygen species by reducing the disulfides into thiol groups. Disulfides 217-227 thioredoxin Homo sapiens 14-18 24409188-3 2014 Thioredoxin interacting protein (Txnip/thioredoxin binding protein-2/vitamin D3 upregulated protein) directly binds to Trx1 and Trx2 (Trx) and inhibit the reducing activity of Trx through their disulfide exchange. Disulfides 194-203 thioredoxin Homo sapiens 0-11 24409188-3 2014 Thioredoxin interacting protein (Txnip/thioredoxin binding protein-2/vitamin D3 upregulated protein) directly binds to Trx1 and Trx2 (Trx) and inhibit the reducing activity of Trx through their disulfide exchange. Disulfides 194-203 thioredoxin Homo sapiens 119-123 24136556-0 2014 Identification of thioredoxin target disulfides using isotope-coded affinity tags. Disulfides 37-47 thioredoxin Homo sapiens 18-29 23899494-1 2014 The thioredoxin (Trx) system, which is composed of NADPH, thioredoxin reductase (TrxR), and thioredoxin, is a key antioxidant system in defense against oxidative stress through its disulfide reductase activity regulating protein dithiol/disulfide balance. Disulfides 181-190 thioredoxin Homo sapiens 4-15 23899494-1 2014 The thioredoxin (Trx) system, which is composed of NADPH, thioredoxin reductase (TrxR), and thioredoxin, is a key antioxidant system in defense against oxidative stress through its disulfide reductase activity regulating protein dithiol/disulfide balance. Disulfides 181-190 thioredoxin Homo sapiens 17-20 24324475-4 2013 Indeed, 4 out of 11 enzymes of the cycle were shown to have a low activity in the dark and to be activated in the light through thioredoxin-dependent reduction of regulatory disulfide bonds. Disulfides 174-183 thioredoxin Homo sapiens 128-139 24391652-3 2013 Through a dithiol-disulfide exchange reaction, the reduced form of thioredoxin preferentially interacts with the oxidized forms of targets, which are immediately released after this reaction is complete. Disulfides 18-27 thioredoxin Homo sapiens 67-78 24391652-7 2013 These results explain the reason for selective association of thioredoxin with oxidized targets for reduction, whereas immediate dissociation from a reduced target when the dithiol-disulfide exchange reaction is complete. Disulfides 181-190 thioredoxin Homo sapiens 62-73 24142694-5 2013 The disulfide bond has a standard redox potential of -301 mV and is stoichiometrically reduced by the inflammatory mediator, thioredoxin, with a rate constant of 350 m(-1) s(-1). Disulfides 4-13 thioredoxin Homo sapiens 125-136 24062305-10 2013 In conclusion, reversible oxidation of the non-active site disulfide of Trx1 is suggested to play an important role in redox regulation and cell signaling via temporal inhibition of its protein-disulfide reductase activity for the transmission of oxidative signals under oxidative stress. Disulfides 59-68 thioredoxin Homo sapiens 72-76 24062305-3 2013 A two-disulfide form of Trx1, containing an active site disulfide between Cys-32 and Cys-35 and a non-active site disulfide between Cys-62 and Cys-69, is inactive either as a disulfide reductase or as a substrate for Trx reductase. Disulfides 6-15 thioredoxin Homo sapiens 24-28 24062305-3 2013 A two-disulfide form of Trx1, containing an active site disulfide between Cys-32 and Cys-35 and a non-active site disulfide between Cys-62 and Cys-69, is inactive either as a disulfide reductase or as a substrate for Trx reductase. Disulfides 6-15 thioredoxin Homo sapiens 24-27 24062305-3 2013 A two-disulfide form of Trx1, containing an active site disulfide between Cys-32 and Cys-35 and a non-active site disulfide between Cys-62 and Cys-69, is inactive either as a disulfide reductase or as a substrate for Trx reductase. Disulfides 56-65 thioredoxin Homo sapiens 24-28 24062305-3 2013 A two-disulfide form of Trx1, containing an active site disulfide between Cys-32 and Cys-35 and a non-active site disulfide between Cys-62 and Cys-69, is inactive either as a disulfide reductase or as a substrate for Trx reductase. Disulfides 56-65 thioredoxin Homo sapiens 24-27 23356510-2 2013 New understanding of thiol-disulfide systems have occurred during the past decade as a consequence of the discoveries that thiol and disulfide systems are maintained in kinetically controlled steady states displaced from thermodynamic equilibrium, that a widely distributed family of NADPH oxidases produces oxidants that function in cell signaling and that a family of peroxiredoxins utilize thioredoxin as a reductant to complement the well-studied glutathione antioxidant system for peroxide elimination and redox regulation. Disulfides 27-36 thioredoxin Homo sapiens 393-404 23403036-2 2013 Thioredoxin is an important regulator of cellular redox homeostasis, which catalyzes the reduction of disulfide bonds. Disulfides 102-111 thioredoxin Homo sapiens 0-11 23414292-1 2013 Thioredoxin protects cells against oxidative damage by reducing disulfide bonds in improperly oxidized proteins. Disulfides 64-73 thioredoxin Homo sapiens 0-11 23428047-0 2013 Single-molecule studies of disulfide bond reduction pathways used by human thioredoxin. Disulfides 27-36 thioredoxin Homo sapiens 75-86 23428047-1 2013 Disulfide bond reduction pathways used by human thioredoxin (hTrx) are studied at the single molecule level using a recombinant protein (I27SS)8. Disulfides 0-9 thioredoxin Homo sapiens 48-59 23428047-1 2013 Disulfide bond reduction pathways used by human thioredoxin (hTrx) are studied at the single molecule level using a recombinant protein (I27SS)8. Disulfides 0-9 thioredoxin Homo sapiens 61-65 23428047-5 2013 Earlier FC-AFM studies observed one disulfide reduction pathway used by hTrx and suggested an additional electron tunneling mechanism. Disulfides 36-45 thioredoxin Homo sapiens 72-76 23428047-7 2013 By analyzing the data using exponential fits and dwell time histograms two disulfide reduction pathways used by hTrx are resolved. Disulfides 75-84 thioredoxin Homo sapiens 112-116 23571504-2 2013 We demonstrated recently that hBD-1 shows activity against enteric commensals and Candida species only after its disulfide bonds have been reduced by thioredoxin (TRX) or a reducing environment. Disulfides 113-122 thioredoxin Homo sapiens 150-161 24040747-0 2013 Unequivocal determination of site-specific protein disulfide bond reduction potentials by top-down FTICR MS: characterization of the N- and C-terminal redox-active sites in human thioredoxin 1. Disulfides 51-60 thioredoxin Homo sapiens 179-192 23244515-7 2013 Central to redox signaling processes are the glutathione and thioredoxin systems controlling H(2)O(2) levels and, hence, the thiol/disulfide balance. Disulfides 131-140 thioredoxin Homo sapiens 61-72 23521534-5 2013 PDI catalyzes an isomerization of disulfide bridges within the thioredoxin motif C600XXC603 of the MPD and results in a drastic structural change between an active open state and an inactive closed conformation. Disulfides 34-43 thioredoxin Homo sapiens 63-74 23516120-11 2013 Targets of Trx, such as phosphoribulokinase, glyceraldehyde-3-phosphate dehydrogenase, transketolase, and sedoheptulose-1,7-bisphosphatase have at least one regulatory disulfide bridge which supports the conclusion that the identified proteins undergo reversible thiol oxidation. Disulfides 168-177 thioredoxin Homo sapiens 11-14 23356510-2 2013 New understanding of thiol-disulfide systems have occurred during the past decade as a consequence of the discoveries that thiol and disulfide systems are maintained in kinetically controlled steady states displaced from thermodynamic equilibrium, that a widely distributed family of NADPH oxidases produces oxidants that function in cell signaling and that a family of peroxiredoxins utilize thioredoxin as a reductant to complement the well-studied glutathione antioxidant system for peroxide elimination and redox regulation. Disulfides 133-142 thioredoxin Homo sapiens 393-404 22702224-4 2013 RECENT ADVANCES: Human cytosolic/nuclear Trx1 in the disulfide form can be nitrosylated at Cys73 and transnitrosylate target proteins, including caspase 3. Disulfides 53-62 thioredoxin Homo sapiens 41-45 23327656-0 2013 Selective inhibition of extracellular thioredoxin by asymmetric disulfides. Disulfides 64-74 thioredoxin Homo sapiens 38-49 23327656-2 2013 Only few extracellular targets of Trx-mediated thiol-disulfide exchange are known. Disulfides 53-62 thioredoxin Homo sapiens 34-37 23327656-3 2013 For example, Trx activates extracellular transglutaminase 2 (TG2) via reduction of an intramolecular disulfide bond. Disulfides 101-110 thioredoxin Homo sapiens 13-16 23327656-5 2013 Starting from a clinical-stage asymmetric disulfide lead, we have identified analogs with >100-fold specificity for Trx. Disulfides 42-51 thioredoxin Homo sapiens 119-122 23223577-5 2013 The association is dependent on hTrx1-Cys-73 that bridges TF-Cys-209 via a disulfide bond. Disulfides 75-84 thioredoxin Homo sapiens 32-37 23178719-4 2013 By using specific inhibitors of the various cytosolic protein disulfides reducing systems, we show here that the NADPH-thioredoxin reductase-thioredoxin redox system is the main responsible for this disulfide reduction. Disulfides 62-72 thioredoxin Homo sapiens 119-130 23178719-4 2013 By using specific inhibitors of the various cytosolic protein disulfides reducing systems, we show here that the NADPH-thioredoxin reductase-thioredoxin redox system is the main responsible for this disulfide reduction. Disulfides 62-72 thioredoxin Homo sapiens 141-152 23178719-4 2013 By using specific inhibitors of the various cytosolic protein disulfides reducing systems, we show here that the NADPH-thioredoxin reductase-thioredoxin redox system is the main responsible for this disulfide reduction. Disulfides 62-71 thioredoxin Homo sapiens 119-130 23178719-4 2013 By using specific inhibitors of the various cytosolic protein disulfides reducing systems, we show here that the NADPH-thioredoxin reductase-thioredoxin redox system is the main responsible for this disulfide reduction. Disulfides 62-71 thioredoxin Homo sapiens 141-152 22704541-2 2012 We present evidence that disulfide bonds in FXI are reduced to free thiols by oxidoreductases thioredoxin-1 (TRX-1) and protein disulfide isomerase (PDI). Disulfides 25-34 thioredoxin Homo sapiens 94-107 25206370-2 2013 Based on peptide aptamers, the present study inserted ABAD-DP into the disulfide bond of human thioredoxin (TRX) using molecular cloning technique to construct a fusion gene that can express the TRX1-ABAD-DP-TRX2 aptamer. Disulfides 71-80 thioredoxin Homo sapiens 95-106 25206370-2 2013 Based on peptide aptamers, the present study inserted ABAD-DP into the disulfide bond of human thioredoxin (TRX) using molecular cloning technique to construct a fusion gene that can express the TRX1-ABAD-DP-TRX2 aptamer. Disulfides 71-80 thioredoxin Homo sapiens 108-111 25206370-2 2013 Based on peptide aptamers, the present study inserted ABAD-DP into the disulfide bond of human thioredoxin (TRX) using molecular cloning technique to construct a fusion gene that can express the TRX1-ABAD-DP-TRX2 aptamer. Disulfides 71-80 thioredoxin Homo sapiens 195-199 22920903-4 2013 Disulfide forming/ isomerizing enzymes like thioredoxin (Trx), protein disulfide isomerase (PDI), which are chaperone proteins, are implicated into transnitrosation reactions, which are the transfer of NO from one cysteine residue to another one. Disulfides 0-9 thioredoxin Homo sapiens 44-55 22920903-4 2013 Disulfide forming/ isomerizing enzymes like thioredoxin (Trx), protein disulfide isomerase (PDI), which are chaperone proteins, are implicated into transnitrosation reactions, which are the transfer of NO from one cysteine residue to another one. Disulfides 0-9 thioredoxin Homo sapiens 57-60 23010496-3 2012 Human Trx1 contains the active-site cysteines, Cys32 and Cys35, and three additional structural cysteines, Cys62, Cys69, and Cys73, that regulate Trx1 structure and activity via a second disulfide formation, S-glutathionylation or S-nitrosylation. Disulfides 187-196 thioredoxin Homo sapiens 6-10 23010496-3 2012 Human Trx1 contains the active-site cysteines, Cys32 and Cys35, and three additional structural cysteines, Cys62, Cys69, and Cys73, that regulate Trx1 structure and activity via a second disulfide formation, S-glutathionylation or S-nitrosylation. Disulfides 187-196 thioredoxin Homo sapiens 146-150 22977247-10 2012 Monitoring the redox state of Trx1 shows that cell death occurs when Trx1 is oxidized, followed by general protein oxidation catalyzed by the disulfide form of thioredoxin. Disulfides 142-151 thioredoxin Homo sapiens 30-34 22977247-10 2012 Monitoring the redox state of Trx1 shows that cell death occurs when Trx1 is oxidized, followed by general protein oxidation catalyzed by the disulfide form of thioredoxin. Disulfides 142-151 thioredoxin Homo sapiens 160-171 22833674-1 2012 NADPH-dependent thioredoxin reductases (NTRs) contain a flavin cofactor and a disulfide as redox-active groups. Disulfides 78-87 thioredoxin Homo sapiens 16-27 22704541-2 2012 We present evidence that disulfide bonds in FXI are reduced to free thiols by oxidoreductases thioredoxin-1 (TRX-1) and protein disulfide isomerase (PDI). Disulfides 25-34 thioredoxin Homo sapiens 109-114 22704541-3 2012 We identified that Cys362-Cys482 and Cys118-Cys147 disulfide bonds are reduced by TRX-1. Disulfides 51-60 thioredoxin Homo sapiens 82-87 22760822-0 2012 Mutagenic analysis in a pure molecular system shows that thioredoxin-interacting protein residue Cys247 is necessary and sufficient for a mixed disulfide formation with thioredoxin. Disulfides 144-153 thioredoxin Homo sapiens 57-68 22760822-11 2012 A mutant with all but one cysteine changed to serine (Cys 247) also showed an enhanced capacity to form complexes with TRX demonstrating, in a pure molecular system, that this particular cysteine is likely responsible for the disulfide bridge between TRX-interacting protein and TRX. Disulfides 226-235 thioredoxin Homo sapiens 119-122 22760822-11 2012 A mutant with all but one cysteine changed to serine (Cys 247) also showed an enhanced capacity to form complexes with TRX demonstrating, in a pure molecular system, that this particular cysteine is likely responsible for the disulfide bridge between TRX-interacting protein and TRX. Disulfides 226-235 thioredoxin Homo sapiens 251-254 22760822-11 2012 A mutant with all but one cysteine changed to serine (Cys 247) also showed an enhanced capacity to form complexes with TRX demonstrating, in a pure molecular system, that this particular cysteine is likely responsible for the disulfide bridge between TRX-interacting protein and TRX. Disulfides 226-235 thioredoxin Homo sapiens 251-254 22700979-5 2012 For the disulfide bond in cVIMP-Cys we determined the reduction potential to -200 mV, and showed it to be a good substrate of thioredoxin. Disulfides 8-17 thioredoxin Homo sapiens 126-137 22362842-6 2012 In addition, we investigated the significance of the electrochemical proton gradient in reducing the gamma subunit by the reduced form of thioredoxin in chloroplasts, providing strong insights into the molecular mechanisms underlying the formation and reduction of the disulfide bond on the gamma subunit in vivo. Disulfides 269-278 thioredoxin Homo sapiens 138-149 21453190-6 2011 The dramatic progress in redox proteomics techniques has enabled the identification of an increasing number of proteins, including peroxiredoxin 1, whose disulfide bond formation and nitrosylation status are regulated by Trx1. Disulfides 154-163 thioredoxin Homo sapiens 221-225 22053845-1 2012 SIGNIFICANCE: In photosynthetic organisms, besides the well-established disulfide/dithiol exchange reactions specifically controlled by thioredoxins (TRXs), protein S-glutathionylation is emerging as an alternative redox modification occurring under stress conditions. Disulfides 72-81 thioredoxin Homo sapiens 136-148 22053845-2 2012 This modification, consisting of the formation of a mixed disulfide between glutathione and a protein cysteine residue, can not only protect specific cysteines from irreversible oxidation but also modulate protein activities and appears to be specifically controlled by small disulfide oxidoreductases of the TRX superfamily named glutaredoxins (GRXs). Disulfides 58-67 thioredoxin Homo sapiens 309-312 22230366-4 2012 Here, it was demonstrated that PDI and Trx1 have similar gp120 disulfide targets as determined by labeling after reduction, but with some pattern differences, including overall stronger labeling with Trx1 than with PDI. Disulfides 63-72 thioredoxin Homo sapiens 39-43 22248238-1 2012 INTRODUCTION: Nowadays the "redox hypothesis" is based on the fact that thiol/disulfide couples such as glutathione (GSH/GSSG), cysteine (Cys/CySS) and thioredoxin ((Trx-(SH)2/Trx-SS)) are functionally organized in redox circuits controlled by glutathione pools, thioredoxins and other control nodes, and they are not in equilibrium relative to each other. Disulfides 78-87 thioredoxin Homo sapiens 152-163 22248238-1 2012 INTRODUCTION: Nowadays the "redox hypothesis" is based on the fact that thiol/disulfide couples such as glutathione (GSH/GSSG), cysteine (Cys/CySS) and thioredoxin ((Trx-(SH)2/Trx-SS)) are functionally organized in redox circuits controlled by glutathione pools, thioredoxins and other control nodes, and they are not in equilibrium relative to each other. Disulfides 78-87 thioredoxin Homo sapiens 166-169 22248238-1 2012 INTRODUCTION: Nowadays the "redox hypothesis" is based on the fact that thiol/disulfide couples such as glutathione (GSH/GSSG), cysteine (Cys/CySS) and thioredoxin ((Trx-(SH)2/Trx-SS)) are functionally organized in redox circuits controlled by glutathione pools, thioredoxins and other control nodes, and they are not in equilibrium relative to each other. Disulfides 78-87 thioredoxin Homo sapiens 176-179 22230366-0 2012 Thioredoxin-1 and protein disulfide isomerase catalyze the reduction of similar disulfides in HIV gp120. Disulfides 80-90 thioredoxin Homo sapiens 0-13 22230366-3 2012 Previous studies indicate that protein disulfide isomerase (PDI), thioredoxin-1 (Trx1), and glutaredoxin-1 (Grx1) catalyze gp120 reduction, but their specific disulfide targets are not known. Disulfides 39-48 thioredoxin Homo sapiens 81-85 20929858-5 2010 The reduction of the catalytic disulfide of the atypical 2-Cys Prx5 is limited to the Trx system. Disulfides 31-40 thioredoxin Homo sapiens 86-89 21704743-3 2011 With a disulfide bond formed between the two catalytic cysteines, Trx1 is not only inactive as a denitrosylase, but it may also be nitrosylated at Cys73 and serve as a transnitrosylating agent. Disulfides 7-16 thioredoxin Homo sapiens 66-70 20955713-1 2011 Thioredoxin 1 (Trx1) is a small molecule with reactive cysteines that reduces proteins with disulfide bonds through a thiol disulfide exchange reaction. Disulfides 92-101 thioredoxin Homo sapiens 0-13 20955713-1 2011 Thioredoxin 1 (Trx1) is a small molecule with reactive cysteines that reduces proteins with disulfide bonds through a thiol disulfide exchange reaction. Disulfides 92-101 thioredoxin Homo sapiens 15-19 21910912-6 2011 TRX activity was assayed by the insulin disulfide-reducing assay. Disulfides 40-49 thioredoxin Homo sapiens 0-3 21755988-0 2011 Heme-dependent activation of neuronal nitric oxide synthase by cytosol is due to an Hsp70-dependent, thioredoxin-mediated thiol-disulfide interchange in the heme/substrate binding cleft. Disulfides 128-137 thioredoxin Homo sapiens 101-112 21755988-6 2011 Previous work has shown that apo-nNOS can be activated by thiol-disulfide exchange, and we show substantial activation with a small molecule dithiol modeled on the active motifs of thioredoxin and protein disulfide isomerase. Disulfides 64-73 thioredoxin Homo sapiens 181-192 21594273-2 2011 Mechanisms associated with cysteine oxidation to form sulfenic acid and disulfides (i.e., cystine and glutathione adducts), and their reversibility through thioredoxin-dependent mechanisms, are broadly appreciated as important regulatory mechanisms that control the function of a range of different proteins. Disulfides 72-82 thioredoxin Homo sapiens 156-167 20177947-3 2011 The redox-sensing cysteine residues and the disulfide bond formed between these cysteine residues serve as redox-sensing molecular switches; these switches sense cellular oxidizing factors such as oxygen, reactive oxygen species, and cellular reducing factors such as thioredoxin (Trx), glutathione (GSH), and their family molecules. Disulfides 44-53 thioredoxin Homo sapiens 268-279 20177947-3 2011 The redox-sensing cysteine residues and the disulfide bond formed between these cysteine residues serve as redox-sensing molecular switches; these switches sense cellular oxidizing factors such as oxygen, reactive oxygen species, and cellular reducing factors such as thioredoxin (Trx), glutathione (GSH), and their family molecules. Disulfides 44-53 thioredoxin Homo sapiens 281-284 21521879-4 2011 Oxidized CRMP2 then formed a transient disulfide-linked complex with TRX, which stimulated CRMP2 phosphorylation by glycogen synthase kinase-3, leading to growth cone collapse. Disulfides 39-48 thioredoxin Homo sapiens 69-72 20943653-0 2010 Disulfide bond that constrains the HIV-1 gp120 V3 domain is cleaved by thioredoxin. Disulfides 0-9 thioredoxin Homo sapiens 71-82 20943653-2 2010 The disulfide bonds in both proteins are cleaved at the cell surface by the small redox protein, thioredoxin. Disulfides 4-13 thioredoxin Homo sapiens 97-108 20943653-3 2010 The target gp120 disulfide and its mechanism of cleavage were determined using a thioredoxin kinetic trapping mutant and mass spectrometry. Disulfides 17-26 thioredoxin Homo sapiens 81-92 20943653-5 2010 The Cys(32) sulfur ion of thioredoxin attacks the Cys(296) sulfur ion of the gp120 V3 domain Cys(296)-Cys(331) disulfide bond, cleaving the bond. Disulfides 111-120 thioredoxin Homo sapiens 26-37 22645650-4 2011 These labile disulfide bonds are common, with several classes of proteins being identified and around 30 membrane proteins regularly identified under different reducing conditions including using enzymes such as thioredoxin. Disulfides 13-22 thioredoxin Homo sapiens 212-223 21812504-6 2011 The overall cellular redox state is regulated by three systems that modulate cellular redox status by counteracting free radicals and ROS, or by reversing the formation of disulfides; two of these are dependent on glutathione and the third on thioredoxin. Disulfides 172-182 thioredoxin Homo sapiens 243-254 21036950-8 2011 This study is the first in vitro observation indicating that glutaredoxin and thioredoxin in human liver are active in reducing the mixed disulfide formed between xenobiotics and glutathione. Disulfides 138-147 thioredoxin Homo sapiens 78-89 20121341-6 2010 A steady-state flux analysis predicted an unequal distribution of the intracellular anti-oxidative burden between thioredoxin-dependent and glutathione-dependent antioxidant pathways, with the former contributing the majority of the cellular antioxidant defense due to peroxiredoxins and protein disulfides. Disulfides 296-306 thioredoxin Homo sapiens 114-125 21076498-3 2010 Covalent binding of these molecules slightly decreases the disulfide-reducing activity of recombinant TRX1, when compared with the effect of strong thioalkylating agents such as N-ethylmaleimide. Disulfides 59-68 thioredoxin Homo sapiens 102-106 20660346-5 2010 Here we used an optimized mass spectrometric method to demonstrate that Trx1 is itself nitrosylated by S-nitrosoglutathione at Cys(73) only after the formation of a Cys(32)-Cys(35) disulfide bond upon which the disulfide reductase and denitrosylase activities of Trx1 are attenuated. Disulfides 181-190 thioredoxin Homo sapiens 72-76 20550946-6 2010 Protein disulfide isomerase (PDI) is a member of the thioredoxin (TX) superfamily and is believed to accelerate the folding of disulfide-bonded proteins by catalyzing the disulfide interchange reaction, which is the rate-limiting step during protein folding in the luminal space of the endoplasmic reticulum (ER). Disulfides 8-17 thioredoxin Homo sapiens 53-64 23350160-2 2010 Several systems are able to control the activity, stability, and correct folding of enzymes through dithiol/disulfide isomerization reactions including the enzyme protein disulfide-isomerase, the glutathione-dependent glutaredoxin system, and the thioredoxin systems. Disulfides 108-117 thioredoxin Homo sapiens 247-258 20435060-3 2010 The anti-oxidative effect of Trx 1 is mediated by the dithiol-disulfide exchange in the active site. Disulfides 62-71 thioredoxin Homo sapiens 29-34 20696932-4 2010 Our results suggest that, during the redox reaction, Cys43 in a luminal loop of human VKOR forms a transient disulfide bond with a thioredoxin (Trx)-like protein located in the lumen of the endoplasmic reticulum (ER). Disulfides 109-118 thioredoxin Homo sapiens 144-147 20696932-5 2010 We screened for redox partners of VKOR among the large number of mammalian Trx-like ER proteins by testing a panel of these candidates for their ability to form this specific disulfide bond with human VKOR. Disulfides 175-184 thioredoxin Homo sapiens 75-78 20550946-6 2010 Protein disulfide isomerase (PDI) is a member of the thioredoxin (TX) superfamily and is believed to accelerate the folding of disulfide-bonded proteins by catalyzing the disulfide interchange reaction, which is the rate-limiting step during protein folding in the luminal space of the endoplasmic reticulum (ER). Disulfides 8-17 thioredoxin Homo sapiens 66-68 20550946-6 2010 Protein disulfide isomerase (PDI) is a member of the thioredoxin (TX) superfamily and is believed to accelerate the folding of disulfide-bonded proteins by catalyzing the disulfide interchange reaction, which is the rate-limiting step during protein folding in the luminal space of the endoplasmic reticulum (ER). Disulfides 127-136 thioredoxin Homo sapiens 53-64 19958171-6 2010 Oxidized protein repair systems, thioredoxin/thioredoxin reductase or glutaredoxin/glutathione/glutathione reductase that catalytically reduce disulfide bridges or sulfenic acids, and methionine sulfoxide reductase that reverses methionine sulfoxide back to methionine within proteins, are present in the mitochondrial matrix. Disulfides 143-152 thioredoxin Homo sapiens 33-44 20550946-6 2010 Protein disulfide isomerase (PDI) is a member of the thioredoxin (TX) superfamily and is believed to accelerate the folding of disulfide-bonded proteins by catalyzing the disulfide interchange reaction, which is the rate-limiting step during protein folding in the luminal space of the endoplasmic reticulum (ER). Disulfides 127-136 thioredoxin Homo sapiens 66-68 20609916-5 2010 The active site of Trx contains two cysteine residues that undergo reversible oxidation to form a disulfide bond with each other, so that the conformation of Trx is changed by intracellular redox conditions. Disulfides 98-107 thioredoxin Homo sapiens 19-22 20382731-6 2010 To date, single-molecule force spectroscopy has been applied to gain insight into the reduction of disulfide bonds by different enzymes of the thioredoxin family. Disulfides 99-108 thioredoxin Homo sapiens 143-154 20306235-16 2010 Recent evidence suggests selenoprotein W and the six other small thioredoxin-like mammalian selenoproteins may serve to transduce hydrogen peroxide signals into regulatory disulfide bonds in specific target proteins. Disulfides 172-181 thioredoxin Homo sapiens 65-76 20473443-1 2010 Thiol-disulfide exchange reactions between thiol-disulfide oxidoreductases (e.g. thioredoxin or Trx) and client proteins can obtain a rate several orders faster than those between chemical reagents (e.g. dithiothreitol) and client proteins. Disulfides 6-15 thioredoxin Homo sapiens 81-92 20473443-1 2010 Thiol-disulfide exchange reactions between thiol-disulfide oxidoreductases (e.g. thioredoxin or Trx) and client proteins can obtain a rate several orders faster than those between chemical reagents (e.g. dithiothreitol) and client proteins. Disulfides 6-15 thioredoxin Homo sapiens 96-99 20056998-1 2010 In the endoplasmic reticulum (ER), a number of thioredoxin (Trx) superfamily proteins are present to enable correct disulfide bond formation of secretory and membrane proteins via Trx-like domains. Disulfides 116-125 thioredoxin Homo sapiens 47-58 20056998-1 2010 In the endoplasmic reticulum (ER), a number of thioredoxin (Trx) superfamily proteins are present to enable correct disulfide bond formation of secretory and membrane proteins via Trx-like domains. Disulfides 116-125 thioredoxin Homo sapiens 60-63 20056998-1 2010 In the endoplasmic reticulum (ER), a number of thioredoxin (Trx) superfamily proteins are present to enable correct disulfide bond formation of secretory and membrane proteins via Trx-like domains. Disulfides 116-125 thioredoxin Homo sapiens 180-183 20384132-0 2010 [Effects of redox state of disulfide bonds on the intrinsic fluorescence and denaturation of Trx-fused gibberellin-induced cysteine-rich protein from Gymnadnia conopsea]. Disulfides 27-36 thioredoxin Homo sapiens 93-96 20609916-5 2010 The active site of Trx contains two cysteine residues that undergo reversible oxidation to form a disulfide bond with each other, so that the conformation of Trx is changed by intracellular redox conditions. Disulfides 98-107 thioredoxin Homo sapiens 158-161 19597482-1 2009 Thioredoxins (Trxs) are oxidoreductase enzymes, present in all organisms, that catalyze the reduction of disulfide bonds in proteins. Disulfides 105-114 thioredoxin Homo sapiens 0-12 19703554-12 2009 In contrast, the oxidation of Trx1, Trx2, and Prx3 was reversible by disulfide reductants. Disulfides 69-78 thioredoxin Homo sapiens 30-34 19570911-5 2009 First, in H(2)O(2)-treated cells, Trx1 reduces the various disulfide bonds generated between cysteines of ASK1 by a rapid and transient action. Disulfides 59-68 thioredoxin Homo sapiens 34-38 19878651-3 2009 IL-4 disulfides were in vitro reduced by thioredoxin 1 (Trx1) and protein disulfide isomerase (PDI). Disulfides 5-15 thioredoxin Homo sapiens 41-54 19878651-3 2009 IL-4 disulfides were in vitro reduced by thioredoxin 1 (Trx1) and protein disulfide isomerase (PDI). Disulfides 5-15 thioredoxin Homo sapiens 56-60 19878651-4 2009 Reduction of IL-4 disulfides by the cell surface of HeLa cells was inhibited by auranofin, an inhibitor of thioredoxin reductase that is an electron donor to both Trx1 and PDI. Disulfides 18-28 thioredoxin Homo sapiens 163-167 19878651-5 2009 Both Trx1 and PDI have been shown to be located at the cell surface and our data suggests that these enzymes are involved in catalyzing reduction of IL-4 disulfides. Disulfides 154-164 thioredoxin Homo sapiens 5-9 19908864-3 2009 FTR reduces an intramolecular disulfide bridge of Trx, and Trx reduction involves a transient cross-link with FTR. Disulfides 30-39 thioredoxin Homo sapiens 50-53 19675666-0 2009 How thioredoxin dissociates its mixed disulfide. Disulfides 38-47 thioredoxin Homo sapiens 4-15 19675666-1 2009 The dissociation mechanism of the thioredoxin (Trx) mixed disulfide complexes is unknown and has been debated for more than twenty years. Disulfides 58-67 thioredoxin Homo sapiens 34-45 19675666-1 2009 The dissociation mechanism of the thioredoxin (Trx) mixed disulfide complexes is unknown and has been debated for more than twenty years. Disulfides 58-67 thioredoxin Homo sapiens 47-50 19675666-5 2009 With theoretical reactivity analysis, molecular dynamics simulations, and biochemical complex formation experiments with Cys-mutants, Trx mixed disulfide dissociation was studied. Disulfides 144-153 thioredoxin Homo sapiens 134-137 19675666-9 2009 This multidisciplinary approach provides fresh insights into a universal thiol/disulfide exchange reaction mechanism that results in reduced substrate and oxidized Trx. Disulfides 79-88 thioredoxin Homo sapiens 164-167 19597482-2 2009 By applying a calibrated force to a substrate disulfide, the chemical mechanisms of Trx catalysis can be examined in detail at the single-molecule level. Disulfides 46-55 thioredoxin Homo sapiens 84-87 19364476-3 2009 Mammalian thioredoxin reductases are selenium-containing flavoprotein oxidoreductases, dependent upon a selenocysteine residue for reduction of the active site disulfide in thioredoxins. Disulfides 160-169 thioredoxin Homo sapiens 10-21 19170525-2 2009 The TRX redox mechanism is based on reversible oxidation of two cysteine thiol groups to a disulfide, accompanied by the transfer of two protons. Disulfides 91-100 thioredoxin Homo sapiens 4-7 19385090-3 2009 In addition to its anti-oxidative effect by dithiol-disulfide exchange in its active site, Trx 1 has anti-apoptotic and anti-inflammatory effects. Disulfides 52-61 thioredoxin Homo sapiens 91-96 19181668-1 2009 The ubiquitous thioredoxin fold proteins catalyze oxidation, reduction, or disulfide exchange reactions depending on their redox properties. Disulfides 75-84 thioredoxin Homo sapiens 15-26 23045011-2 2009 Examination of thiol/disulfide redox changes in thioredoxin (Trx) family members including Trx1 in cytoplasm and nucleus and Trx2 in mitochondria should aid in the understanding of compartmentalized redox signaling mechanisms. Disulfides 21-30 thioredoxin Homo sapiens 48-59 23045011-2 2009 Examination of thiol/disulfide redox changes in thioredoxin (Trx) family members including Trx1 in cytoplasm and nucleus and Trx2 in mitochondria should aid in the understanding of compartmentalized redox signaling mechanisms. Disulfides 21-30 thioredoxin Homo sapiens 61-64 18552403-6 2008 We propose thus a four-step disulfide cascade mechanism involving the transient glutathionylation of Cys(4) to convert this atypical thioredoxin h back to its active reduced form. Disulfides 28-37 thioredoxin Homo sapiens 133-144 18692066-1 2008 Proteins of the thioredoxin (Trx) superfamily catalyze disulfide-bond formation, reduction and isomerization in substrate proteins both in prokaryotic and in eukaryotic cells. Disulfides 55-64 thioredoxin Homo sapiens 16-27 18692066-1 2008 Proteins of the thioredoxin (Trx) superfamily catalyze disulfide-bond formation, reduction and isomerization in substrate proteins both in prokaryotic and in eukaryotic cells. Disulfides 55-64 thioredoxin Homo sapiens 29-32 19216714-1 2008 Among the key antioxidant enzymes, thioredoxin and glutaredoxin systems play an important role in cell defense against oxidative stress and maintenance of redox homeostasis owing to the regulation of thiol-disulfide exchange. Disulfides 206-215 thioredoxin Homo sapiens 35-46 19216714-2 2008 The thioredoxin isoforms Trx1 (cytoplasmic form) and Trx2 (mitochondrial form) can reduce inter- and intramolecular disulfide bonds in proteins, in particular, in oxidized peroxiredoxins, which disrupt organic hydroperoxides, H2O2, and peroxynitrite. Disulfides 116-125 thioredoxin Homo sapiens 4-15 19216714-2 2008 The thioredoxin isoforms Trx1 (cytoplasmic form) and Trx2 (mitochondrial form) can reduce inter- and intramolecular disulfide bonds in proteins, in particular, in oxidized peroxiredoxins, which disrupt organic hydroperoxides, H2O2, and peroxynitrite. Disulfides 116-125 thioredoxin Homo sapiens 25-29 18624400-4 2008 This review examines the usefulness of a disulfide proteome technique for the analysis of thioredoxin-dependent redox regulation as well as for use in allergen studies. Disulfides 41-50 thioredoxin Homo sapiens 90-101 18544525-2 2008 The active site of reduced Trx comprises Cys(32)-Gly-Pro-Cys(35) thiols that catalyze target disulfide reduction, generating a disulfide. Disulfides 93-102 thioredoxin Homo sapiens 27-30 18544525-2 2008 The active site of reduced Trx comprises Cys(32)-Gly-Pro-Cys(35) thiols that catalyze target disulfide reduction, generating a disulfide. Disulfides 127-136 thioredoxin Homo sapiens 27-30 18544525-3 2008 Human Trx1 has also three structural Cys residues in positions 62, 69, and 73 that upon diamide oxidation induce a second Cys(62)-Cys(69) disulfide as well as dimers and multimers. Disulfides 138-147 thioredoxin Homo sapiens 6-10 18544525-7 2008 Starting from fully reduced human Trx, both Cys(69) and Cys(73) were nitrosylated, and the active site formed a disulfide; the nitrosylated Trx was not a substrate for TrxR but regained activity after a lag phase consistent with autoactivation. Disulfides 112-121 thioredoxin Homo sapiens 34-37 18544525-7 2008 Starting from fully reduced human Trx, both Cys(69) and Cys(73) were nitrosylated, and the active site formed a disulfide; the nitrosylated Trx was not a substrate for TrxR but regained activity after a lag phase consistent with autoactivation. Disulfides 112-121 thioredoxin Homo sapiens 140-143 18557934-7 2008 The corresponding peptides, purified after cleavage from thioredoxin, were properly folded and contained the expected four-disulfide bridges without the need of any renaturation or oxidation steps. Disulfides 123-132 thioredoxin Homo sapiens 57-68 18452709-4 2008 We further identified MsrB2- or MsrB3-Trx complexes formed through intermolecular disulfide bonds involving catalytic residue of Trx. Disulfides 82-91 thioredoxin Homo sapiens 38-41 18452709-4 2008 We further identified MsrB2- or MsrB3-Trx complexes formed through intermolecular disulfide bonds involving catalytic residue of Trx. Disulfides 82-91 thioredoxin Homo sapiens 129-132 18479973-5 2008 Interestingly, LvTRX contains aside of the canonical active site CXXC disulfide motif, one Cys (C73) residue in the interface of a putative dimer previously reported for human TRX. Disulfides 70-79 thioredoxin Homo sapiens 17-20 18537713-1 2008 An intermolecular disulfide bond serves as a thioredoxin-dependent redox-sensing switch for the regulation of the enzymatic activity of 3-mercaptopyruvate sulfurtransferase (MST, EC.2.8.1.2). Disulfides 18-27 thioredoxin Homo sapiens 45-56 18555775-1 2008 Thioredoxin 1 (Trx1) facilitates the reduction of signaling molecules and transcription factors by cysteine thiol-disulfide exchange, thereby regulating cell growth and death. Disulfides 114-123 thioredoxin Homo sapiens 0-13 18555775-1 2008 Thioredoxin 1 (Trx1) facilitates the reduction of signaling molecules and transcription factors by cysteine thiol-disulfide exchange, thereby regulating cell growth and death. Disulfides 114-123 thioredoxin Homo sapiens 15-19 18555775-4 2008 Both Cys-274/Cys-276 in DnaJb5 and Cys-667/Cys-669 in HDAC4 are oxidized and form intramolecular disulfide bonds in response to reactive oxygen species (ROS)-generating hypertrophic stimuli, such as phenylephrine, whereas they are reduced by Trx1. Disulfides 97-106 thioredoxin Homo sapiens 242-246 18537713-2 2008 A cysteine residue on the surface of each subunit was oxidized to form an intersubunit disulfide bond so as to decrease MST activity, and thioredoxin-specific conversion of a dimer to a monomer increased MST activity. Disulfides 87-96 thioredoxin Homo sapiens 138-149 18643017-0 2008 Two-pathway four-state kinetic model of thioredoxin-catalyzed reduction of single forced disulfide bonds. Disulfides 89-98 thioredoxin Homo sapiens 40-51 18321861-6 2008 Mass spectra analysis demonstrated binding of 2.5 mol of Hg(2+) and 5 mol of MeHg(+)/mol of Trx1 with the very strong Hg(2+) complexes involving active site and structural disulfides. Disulfides 172-182 thioredoxin Homo sapiens 92-96 18035847-1 2008 Mammalian thioredoxin reductase (TR) catalyzes the reduction of the redox-active disulfide bond of thioredoxin (Trx) and is similar in structure and mechanism to glutathione reductase except for a C-terminal 16-amino acid extension containing a rare vicinal selenylsulfide bond. Disulfides 81-90 thioredoxin Homo sapiens 10-21 18035847-1 2008 Mammalian thioredoxin reductase (TR) catalyzes the reduction of the redox-active disulfide bond of thioredoxin (Trx) and is similar in structure and mechanism to glutathione reductase except for a C-terminal 16-amino acid extension containing a rare vicinal selenylsulfide bond. Disulfides 81-90 thioredoxin Homo sapiens 112-115 18643017-1 2008 Recent single-molecule experiments found that the thioredoxin-catalyzed reduction of individual disulfide bonds placed under a stretching mechanical force has distinct characteristics: the reduction rate of human thioredoxin monotonically decreases with the force, while the rate of E. coli thioredoxin first decreases and then increases as the force goes beyond a certain threshold. Disulfides 96-105 thioredoxin Homo sapiens 50-61 18643017-1 2008 Recent single-molecule experiments found that the thioredoxin-catalyzed reduction of individual disulfide bonds placed under a stretching mechanical force has distinct characteristics: the reduction rate of human thioredoxin monotonically decreases with the force, while the rate of E. coli thioredoxin first decreases and then increases as the force goes beyond a certain threshold. Disulfides 96-105 thioredoxin Homo sapiens 213-224 18643017-1 2008 Recent single-molecule experiments found that the thioredoxin-catalyzed reduction of individual disulfide bonds placed under a stretching mechanical force has distinct characteristics: the reduction rate of human thioredoxin monotonically decreases with the force, while the rate of E. coli thioredoxin first decreases and then increases as the force goes beyond a certain threshold. Disulfides 96-105 thioredoxin Homo sapiens 213-224 18331844-3 2008 The active site dithiol/disulfide of thioredoxin fold proteins is CXXC where variations of the residues inside the disulfide ring are known to increase the redox potential like in protein disulfide isomerases. Disulfides 24-33 thioredoxin Homo sapiens 37-48 18331844-2 2008 Oxidoreductases of the thioredoxin fold superfamily catalyze steps in oxidative protein folding via protein-protein interactions and covalent catalysis to act as chaperones and isomerases of disulfides to generate a native fold. Disulfides 191-201 thioredoxin Homo sapiens 23-34 18331844-3 2008 The active site dithiol/disulfide of thioredoxin fold proteins is CXXC where variations of the residues inside the disulfide ring are known to increase the redox potential like in protein disulfide isomerases. Disulfides 115-124 thioredoxin Homo sapiens 37-48 18331844-4 2008 In the catalytic mechanism thioredoxin fold proteins bind to target proteins through conserved backbone-backbone hydrogen bonds and induce conformational changes of the target disulfide followed by nucleophilic attack by the N-terminally located low pK(a) Cys residue. Disulfides 176-185 thioredoxin Homo sapiens 27-38 18349143-1 2008 Thioredoxins (Trxs) are ubiquitous small proteins with a redox-active disulfide bridge. Disulfides 70-79 thioredoxin Homo sapiens 0-12 18322016-6 2008 Based on our data, we propose a model for thioredoxin f-mediated activation of PRK and GAPDH by two mechanisms: directly through reduction of disulfide bonds within these enzymes and indirectly by mediating the breakdown of the complex in response to changes in light intensity. Disulfides 142-151 thioredoxin Homo sapiens 42-53 18164270-4 2008 Increased H2O2 triggers peroxiredoxin overoxidation to a sulphinic acid; however during apoptosis peroxiredoxin 3 was captured as a disulfide, suggesting impairment of the thioredoxin system responsible for maintaining peroxiredoxin 3 in its reduced form. Disulfides 132-141 thioredoxin Homo sapiens 172-183 17641688-6 2007 Fourth, mixed disulfide complexes, apparent intermediates in the electron transfer process, are detected between DsbDbeta and thioredoxin molecules on each side of the membrane. Disulfides 14-23 thioredoxin Homo sapiens 126-137 18237164-0 2008 Mechanism of thioredoxin-catalyzed disulfide reduction. Disulfides 35-44 thioredoxin Homo sapiens 13-24 17956189-2 2008 A large number of thiol-disulfide oxidoreductases, belonging to the thioredoxin superfamily, catalyze protein disulfide bond formation in all living cells, from bacteria to humans. Disulfides 24-33 thioredoxin Homo sapiens 68-79 17716625-1 2007 Thioredoxin-1 (Trx) becomes inactive when cysteine-73 forms a mixed disulfide with glutathione. Disulfides 68-77 thioredoxin Homo sapiens 0-13 17716625-1 2007 Thioredoxin-1 (Trx) becomes inactive when cysteine-73 forms a mixed disulfide with glutathione. Disulfides 68-77 thioredoxin Homo sapiens 15-18 17673175-7 2007 All these tested Trx-independent MsrB enzymes lack an additional cysteine (resolving cysteine) that is capable of forming a disulfide bond on the enzyme during the catalytic reaction. Disulfides 124-133 thioredoxin Homo sapiens 17-20 17546662-1 2007 Glutaredoxins (Grxs) are glutathione-dependent oxidoreductases that belong to the thioredoxin superfamily catalyzing thiol-disulfide exchange reactions via active site cysteine residues. Disulfides 123-132 thioredoxin Homo sapiens 82-93 18575274-1 2008 Thioredoxin (TRX) is a small multifunctional protein with a redox-active dithiol/disulfide in the conserved active site. Disulfides 81-90 thioredoxin Homo sapiens 0-11 18575274-1 2008 Thioredoxin (TRX) is a small multifunctional protein with a redox-active dithiol/disulfide in the conserved active site. Disulfides 81-90 thioredoxin Homo sapiens 13-16 17727880-0 2007 Design of disulfide-linked thioredoxin dimers and multimers through analysis of crystal contacts. Disulfides 10-19 thioredoxin Homo sapiens 27-38 17675287-4 2007 It is surprising that nearly all of our thioredoxin mutants had increased activity in disulfide isomerization in vitro and in vivo. Disulfides 86-95 thioredoxin Homo sapiens 40-51 17627468-1 2007 Human thioredoxin-1 (hTrx) exhibits a disulfide reducing activity and was originally identified as a soluble cytokine-like factor secreted from cells of a human T-cell leukemia virus type I (HTLV-I)-transformed cell line. Disulfides 38-47 thioredoxin Homo sapiens 21-25 17661444-1 2007 High-molecular weight thioredoxin reductases (TRs) catalyze the reduction of the redox-active disulfide bond of thioredoxin, but an important difference in the TR family is the sequence of the C-terminal redox-active tetrapeptide that interacts directly with thioredoxin, especially the presence or absence of a selenocysteine (Sec) residue in this tetrapeptide. Disulfides 94-103 thioredoxin Homo sapiens 22-33 17661444-1 2007 High-molecular weight thioredoxin reductases (TRs) catalyze the reduction of the redox-active disulfide bond of thioredoxin, but an important difference in the TR family is the sequence of the C-terminal redox-active tetrapeptide that interacts directly with thioredoxin, especially the presence or absence of a selenocysteine (Sec) residue in this tetrapeptide. Disulfides 94-103 thioredoxin Homo sapiens 112-123 17661444-1 2007 High-molecular weight thioredoxin reductases (TRs) catalyze the reduction of the redox-active disulfide bond of thioredoxin, but an important difference in the TR family is the sequence of the C-terminal redox-active tetrapeptide that interacts directly with thioredoxin, especially the presence or absence of a selenocysteine (Sec) residue in this tetrapeptide. Disulfides 94-103 thioredoxin Homo sapiens 112-123 17555594-9 2007 TRX activity was assayed by the insulin disulfide reducing assay. Disulfides 40-49 thioredoxin Homo sapiens 0-3 17557078-4 2007 Using a mechanism-based kinetic trapping technique to identify disulfide exchange interactions on the intact surface of living lymphocytes, we found that Trx1 catalytically interacts with a single principal target protein. Disulfides 63-72 thioredoxin Homo sapiens 154-158 17575238-5 2007 Thioredoxin activity was assayed by the insulin disulfide-reducing assay. Disulfides 48-57 thioredoxin Homo sapiens 0-11 17503775-7 2007 By analogy to thioredoxin, Rdx proteins can use catalytic cysteine (or Sec) to form transient mixed disulfides with substrate proteins. Disulfides 100-110 thioredoxin Homo sapiens 14-25 17444035-4 2007 The research in thioltransferase (TTase) and thioredoxin (Trx) system show TTase can specifically dithiolate protein-S-S-glutathione and restore protein free SH groups for proper enzymatic or protein functions; Trx system can dithiolate protein disulfides and thus is an extremely important regulator for redox homeostasis in the cells. Disulfides 245-255 thioredoxin Homo sapiens 45-56 17444035-4 2007 The research in thioltransferase (TTase) and thioredoxin (Trx) system show TTase can specifically dithiolate protein-S-S-glutathione and restore protein free SH groups for proper enzymatic or protein functions; Trx system can dithiolate protein disulfides and thus is an extremely important regulator for redox homeostasis in the cells. Disulfides 245-255 thioredoxin Homo sapiens 58-61 17444035-4 2007 The research in thioltransferase (TTase) and thioredoxin (Trx) system show TTase can specifically dithiolate protein-S-S-glutathione and restore protein free SH groups for proper enzymatic or protein functions; Trx system can dithiolate protein disulfides and thus is an extremely important regulator for redox homeostasis in the cells. Disulfides 245-255 thioredoxin Homo sapiens 211-214 16893552-5 2006 We have determined by X-ray crystallography the structure of AtErv1, an ERV/ALR enzyme that contains a Cys-X4-Cys shuttle disulfide and oxidizes thioredoxin in vitro, and compared it to ScErv2, which has a Cys-X-Cys shuttle and does not oxidize thioredoxin at an appreciable rate. Disulfides 122-131 thioredoxin Homo sapiens 145-156 17154358-9 2007 In contrast, for thioredoxin a bonding of As that depended on the concentration of the disulfide-reducing agent tris(2-carboxyethyl) phosphine was demonstrated. Disulfides 87-96 thioredoxin Homo sapiens 17-28 17034341-4 2006 The thioredoxin system also makes a significant contribution to the redox environment by reducing inter- and intrachain protein disulfide bonds as well as maintaining the activity of important antioxidant enzymes such as peroxiredoxins and methionine sulfoxide reductases. Disulfides 128-137 thioredoxin Homo sapiens 4-15 16893552-9 2006 We found that the AtErv1 shuttle disulfide region could indeed confer thioredoxin oxidase activity on the ScErv2 core. Disulfides 33-42 thioredoxin Homo sapiens 70-81 16507315-5 2006 We evaluated one such candidate, thioredoxin, a PDI family member reported to reduce a labile disulfide bond in CD4. Disulfides 94-103 thioredoxin Homo sapiens 33-44 16766796-5 2006 We explored the mechanism of the Txnip-thioredoxin interaction and present evidence that Txnip and thioredoxin form a stable disulfide-linked complex. Disulfides 125-134 thioredoxin Homo sapiens 39-50 16766796-5 2006 We explored the mechanism of the Txnip-thioredoxin interaction and present evidence that Txnip and thioredoxin form a stable disulfide-linked complex. Disulfides 125-134 thioredoxin Homo sapiens 99-110 16766796-6 2006 We identified two Txnip cysteines that are important for thioredoxin binding and showed that this interaction is consistent with a disulfide exchange reaction between oxidized Txnip and reduced thioredoxin. Disulfides 131-140 thioredoxin Homo sapiens 57-68 16766796-6 2006 We identified two Txnip cysteines that are important for thioredoxin binding and showed that this interaction is consistent with a disulfide exchange reaction between oxidized Txnip and reduced thioredoxin. Disulfides 131-140 thioredoxin Homo sapiens 194-205 17089213-3 2006 The most studied redox system in photosynthetic organisms is the thioredoxin (TRX) system, involved in the regulation of a growing number of target proteins via thiol/disulfide exchanges. Disulfides 167-176 thioredoxin Homo sapiens 65-76 17089213-3 2006 The most studied redox system in photosynthetic organisms is the thioredoxin (TRX) system, involved in the regulation of a growing number of target proteins via thiol/disulfide exchanges. Disulfides 167-176 thioredoxin Homo sapiens 78-81 16507315-6 2006 We found that the ability of thioredoxin to reduce the disulfide bond in CD4 is enhanced in the presence of HIV-1 Env gp120 and that thioredoxin also reduces disulfide bonds in gp120 directly in the absence of CD4. Disulfides 158-167 thioredoxin Homo sapiens 133-144 16507315-6 2006 We found that the ability of thioredoxin to reduce the disulfide bond in CD4 is enhanced in the presence of HIV-1 Env gp120 and that thioredoxin also reduces disulfide bonds in gp120 directly in the absence of CD4. Disulfides 55-64 thioredoxin Homo sapiens 29-40 16586531-1 2006 Thioredoxin superfamily members share a considerable degree of structural similarity, with a conserved CX(i)X(j)C motif at the active site, where C stand for two cysteines that alternate between a reduced thiol and oxidized disulfide states, and X(i)and X(j) are two amino acids different in each family member. Disulfides 224-233 thioredoxin Homo sapiens 0-11 16098567-4 2006 Interestingly, the proteins that are responsible for maintenance of the reduced state belong to the same superfamily as those responsible for the formation of disulfide bridges: all are members of the thioredoxin superfamily. Disulfides 159-168 thioredoxin Homo sapiens 201-212 16586531-3 2006 Thioredoxin, for example, promotes the reduction of disulfide bonds, while DsbA promotes their oxidation in prokaryotic cells. Disulfides 52-61 thioredoxin Homo sapiens 0-11 16618105-1 2006 Thioredoxin reductase and thioredoxin constitute the cellular thioredoxin system, which provides reducing equivalents to numerous intracellular target disulfides. Disulfides 151-161 thioredoxin Homo sapiens 26-37 16481328-7 2006 The corresponding reaction with reduced Escherichia coli Trx was also negligible, but MGd was a better substrate (kcat/Km of 2.23 x 10(5) M(-1) s(-1)) for TrxR from E. coli and a strong inhibitor of Trx-dependent protein disulfide reduction. Disulfides 221-230 thioredoxin Homo sapiens 155-158 16618105-1 2006 Thioredoxin reductase and thioredoxin constitute the cellular thioredoxin system, which provides reducing equivalents to numerous intracellular target disulfides. Disulfides 151-161 thioredoxin Homo sapiens 62-73 16343416-0 2006 Disulfide between Cys392 and Cys438 of human serum albumin is redox-active, which is responsible for the thioredoxin-supported lipid peroxidase activity. Disulfides 0-9 thioredoxin Homo sapiens 105-116 16421453-4 2006 The cysteine residues in this motif form a redox-active disulfide necessary for thioredoxin activity. Disulfides 56-65 thioredoxin Homo sapiens 80-91 16231315-9 2006 TRP-1 has a thioredoxin activity, which was detected using the insulin disulfide reduction assay. Disulfides 71-80 thioredoxin Homo sapiens 12-23 16343416-3 2006 In this paper, we identified the redox-active disulfide, which can be specifically reduced by Trx, responsible for the Trx-dependent lipid peroxidase activity. Disulfides 46-55 thioredoxin Homo sapiens 94-97 16343416-3 2006 In this paper, we identified the redox-active disulfide, which can be specifically reduced by Trx, responsible for the Trx-dependent lipid peroxidase activity. Disulfides 46-55 thioredoxin Homo sapiens 119-122 16343416-7 2006 Taken together, these results suggested that HSA has a capability to reduce lipid hydroperoxide with the use of Trx as an in vivo electron donor, and that the redox-active disulfide between Cys392 and Cys438 acts as a primary site of the catalysis for the Trx-linked lipid peroxidase activity. Disulfides 172-181 thioredoxin Homo sapiens 256-259 16356134-1 2005 Thioredoxin (Trx) is a redox-active protein that has been shown to regulate various cellular processes due to its thiol-disulfide exchange reaction. Disulfides 120-129 thioredoxin Homo sapiens 0-11 16356134-1 2005 Thioredoxin (Trx) is a redox-active protein that has been shown to regulate various cellular processes due to its thiol-disulfide exchange reaction. Disulfides 120-129 thioredoxin Homo sapiens 13-16 15651042-6 2005 By means of DFT (B3LYP, lacv3p**) calculations, we could show that the formation of such a triad is essential to support the proton transfer from selenol to a histidine to stabilise a selenolate anion, which is able to interact with the disulfide of thioredoxin and catalyses the reductive disulfide opening. Disulfides 237-246 thioredoxin Homo sapiens 250-261 16307478-6 2005 For the catalytic cycle of TPx1, we conclude that oxidation of the peroxidatic Cys50 by the oxidising substrate is followed by the formation of an intermolecular disulfide bond between Cys50 and Cys170" of the second subunit, which is then attacked by an external electron donor such as thioredoxin or plasmoredoxin. Disulfides 162-171 thioredoxin Homo sapiens 287-298 16217027-5 2005 Once activated, the C-terminal redox center reduces a disulfide bond within thioredoxin. Disulfides 54-63 thioredoxin Homo sapiens 76-87 15521073-1 2005 Thioredoxin reductase (TrxR) is a selenoprotein that catalyzes the reduction of the active site disulfide of thioredoxin (Trx), which regulates the redox status of the cells. Disulfides 96-105 thioredoxin Homo sapiens 109-120 15521073-1 2005 Thioredoxin reductase (TrxR) is a selenoprotein that catalyzes the reduction of the active site disulfide of thioredoxin (Trx), which regulates the redox status of the cells. Disulfides 96-105 thioredoxin Homo sapiens 23-26 15806300-1 2005 Thioredoxin (TRX), which is a stress-inducible protein with redox-active disulfide structures, has various biological activities by regulating DNA binding of transcription factors in cells. Disulfides 73-82 thioredoxin Homo sapiens 0-11 15806300-1 2005 Thioredoxin (TRX), which is a stress-inducible protein with redox-active disulfide structures, has various biological activities by regulating DNA binding of transcription factors in cells. Disulfides 73-82 thioredoxin Homo sapiens 13-16 15651042-6 2005 By means of DFT (B3LYP, lacv3p**) calculations, we could show that the formation of such a triad is essential to support the proton transfer from selenol to a histidine to stabilise a selenolate anion, which is able to interact with the disulfide of thioredoxin and catalyses the reductive disulfide opening. Disulfides 290-299 thioredoxin Homo sapiens 250-261 15650396-4 2005 Thioredoxin (TRX), a key redox molecule, plays crucial roles as an antioxidant and a catalyst in protein disulfide/dithiol exchange. Disulfides 105-114 thioredoxin Homo sapiens 0-11 15680231-3 2005 The mechanism includes three steps with (1) formation of a sulfenic acid intermediate with a concomitant release of 1 mol of methionine per mol of enzyme; (2) formation of an intramonomeric disulfide Msr bond followed by; (3) reduction of the oxidized Msr by thioredoxin (Trx). Disulfides 190-199 thioredoxin Homo sapiens 259-270 15680231-3 2005 The mechanism includes three steps with (1) formation of a sulfenic acid intermediate with a concomitant release of 1 mol of methionine per mol of enzyme; (2) formation of an intramonomeric disulfide Msr bond followed by; (3) reduction of the oxidized Msr by thioredoxin (Trx). Disulfides 190-199 thioredoxin Homo sapiens 272-275 15650396-4 2005 Thioredoxin (TRX), a key redox molecule, plays crucial roles as an antioxidant and a catalyst in protein disulfide/dithiol exchange. Disulfides 105-114 thioredoxin Homo sapiens 13-16 15180957-8 2004 A circuitry model incorporating cysteine as a redox node, along with Trx1 and GSH, reveals how selective interactions between the different thiol/disulfide couples and reactive protein thiols could differentially regulate metabolic functions. Disulfides 146-155 thioredoxin Homo sapiens 69-73 15282410-2 2004 The glutathione (GSH) and thioredoxin (TRX) systems have overlapping functions in thiol/disulfide redox control in both the cytoplasm and the nucleus, and it is unclear whether these are redundant or have unique functions in control of Nrf-2-dependent signaling. Disulfides 88-97 thioredoxin Homo sapiens 26-37 15282410-2 2004 The glutathione (GSH) and thioredoxin (TRX) systems have overlapping functions in thiol/disulfide redox control in both the cytoplasm and the nucleus, and it is unclear whether these are redundant or have unique functions in control of Nrf-2-dependent signaling. Disulfides 88-97 thioredoxin Homo sapiens 39-42 15313215-6 2004 Molecular docking and site-specific mutation studies show that the binding of Trx-1 to PTEN occurs through a disulfide bond between the active site Cys(32) of Trx-1 and Cys(212) of the C2 domain of PTEN leading to steric interference by bound Trx-1 of the catalytic site of PTEN and of the C2 lipid membrane-binding domain. Disulfides 109-118 thioredoxin Homo sapiens 78-83 15313215-6 2004 Molecular docking and site-specific mutation studies show that the binding of Trx-1 to PTEN occurs through a disulfide bond between the active site Cys(32) of Trx-1 and Cys(212) of the C2 domain of PTEN leading to steric interference by bound Trx-1 of the catalytic site of PTEN and of the C2 lipid membrane-binding domain. Disulfides 109-118 thioredoxin Homo sapiens 159-164 15313215-6 2004 Molecular docking and site-specific mutation studies show that the binding of Trx-1 to PTEN occurs through a disulfide bond between the active site Cys(32) of Trx-1 and Cys(212) of the C2 domain of PTEN leading to steric interference by bound Trx-1 of the catalytic site of PTEN and of the C2 lipid membrane-binding domain. Disulfides 109-118 thioredoxin Homo sapiens 159-164 15341729-4 2004 The redox potential of this disulfide bond is -251.6 mV, comparing well to that of disulfides in other thioredoxin-like proteins. Disulfides 28-37 thioredoxin Homo sapiens 103-114 15341729-4 2004 The redox potential of this disulfide bond is -251.6 mV, comparing well to that of disulfides in other thioredoxin-like proteins. Disulfides 83-93 thioredoxin Homo sapiens 103-114 15193566-1 2004 The thioredoxin and glutathione systems play a central role in thiol-disulfide redox homeostasis in many organisms by providing electrons to essential enzymes, and defence against oxidative stress. Disulfides 69-78 thioredoxin Homo sapiens 4-15 15118998-1 2004 Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses. Disulfides 186-195 thioredoxin Homo sapiens 49-60 15118998-1 2004 Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses. Disulfides 186-195 thioredoxin Homo sapiens 79-90 15118998-1 2004 Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses. Disulfides 186-195 thioredoxin Homo sapiens 23-26 15118998-1 2004 Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses. Disulfides 186-195 thioredoxin Homo sapiens 92-95 14976238-7 2004 The redox midpoint potential of the peroxiredoxin Q catalytic disulfide is -325 mV at pH 7.0, explaining why the wild-type protein is reduced by thioredoxin but not by glutaredoxin. Disulfides 62-71 thioredoxin Homo sapiens 145-156 14871470-0 2004 TMX, a human transmembrane oxidoreductase of the thioredoxin family: the possible role in disulfide-linked protein folding in the endoplasmic reticulum. Disulfides 90-99 thioredoxin Homo sapiens 49-60 14975452-2 2004 Herein we report that peroxynitrite-induced disulfides in porcine brain tubulin are repaired by the thioredoxin reductase system composed of rat liver thioredoxin reductase, human or Escherichia coli thioredoxin, and NADPH. Disulfides 44-54 thioredoxin Homo sapiens 100-111 14975452-2 2004 Herein we report that peroxynitrite-induced disulfides in porcine brain tubulin are repaired by the thioredoxin reductase system composed of rat liver thioredoxin reductase, human or Escherichia coli thioredoxin, and NADPH. Disulfides 44-54 thioredoxin Homo sapiens 151-162 14975452-3 2004 Disulfide bonds between the alpha-tubulin and the beta-tubulin subunits were repaired by thioredoxin reductase as determined by Western blot under nonreducing conditions. Disulfides 0-9 thioredoxin Homo sapiens 89-100 14975452-9 2004 Thiol-disulfide exchange between tubulin and thioredoxin was detected by Western blot, thereby providing further support for our observations that optimal repair of tubulin disulfides required thioredoxin. Disulfides 6-15 thioredoxin Homo sapiens 45-56 14975452-9 2004 Thiol-disulfide exchange between tubulin and thioredoxin was detected by Western blot, thereby providing further support for our observations that optimal repair of tubulin disulfides required thioredoxin. Disulfides 6-15 thioredoxin Homo sapiens 193-204 14975452-9 2004 Thiol-disulfide exchange between tubulin and thioredoxin was detected by Western blot, thereby providing further support for our observations that optimal repair of tubulin disulfides required thioredoxin. Disulfides 173-183 thioredoxin Homo sapiens 45-56 14975452-9 2004 Thiol-disulfide exchange between tubulin and thioredoxin was detected by Western blot, thereby providing further support for our observations that optimal repair of tubulin disulfides required thioredoxin. Disulfides 173-183 thioredoxin Homo sapiens 193-204 16328790-1 2004 The role of the ferredoxin:thioredoxin system in the reversible light activation of chloroplast enzymes by thiol-disulfide interchange with thioredoxins is now well established. Disulfides 113-122 thioredoxin Homo sapiens 27-38 16328790-5 2004 Thioredoxins in turn reduce regulatory disulfides of various target enzymes. Disulfides 39-49 thioredoxin Homo sapiens 0-12 16328791-1 2004 Thioredoxin-mediated light regulation in plant chloroplasts involves a unique class of disulfide reductases that catalyze disulfide reduction in two one-electron steps using a [2Fe-2S] ferredoxin as the electron donor and an active site comprising a [4Fe-4S] cluster and a redox-active disulfide. Disulfides 87-96 thioredoxin Homo sapiens 0-11 16328791-1 2004 Thioredoxin-mediated light regulation in plant chloroplasts involves a unique class of disulfide reductases that catalyze disulfide reduction in two one-electron steps using a [2Fe-2S] ferredoxin as the electron donor and an active site comprising a [4Fe-4S] cluster and a redox-active disulfide. Disulfides 122-131 thioredoxin Homo sapiens 0-11 16328790-4 2004 The unique 4Fe-4S cluster enzyme ferredoxin:thioredoxin reductase (FTR) uses photosynthetically reduced ferredoxin as an electron donor to reduce the disulfide bridge of different thioredoxin isoforms. Disulfides 150-159 thioredoxin Homo sapiens 44-55 16328790-4 2004 The unique 4Fe-4S cluster enzyme ferredoxin:thioredoxin reductase (FTR) uses photosynthetically reduced ferredoxin as an electron donor to reduce the disulfide bridge of different thioredoxin isoforms. Disulfides 150-159 thioredoxin Homo sapiens 180-191 12939134-8 2003 These intramolecular disulfides can then be rapidly and effectively rereduced by thioredoxin/thioredoxin reductase but not glutathione. Disulfides 21-31 thioredoxin Homo sapiens 81-92 12816947-1 2003 Thioredoxin (Trx1) is a redox-active protein containing two active site cysteines (Cys-32 and Cys-35) that cycle between the dithiol and disulfide forms as Trx1 reduces target proteins. Disulfides 137-146 thioredoxin Homo sapiens 0-11 12816947-1 2003 Thioredoxin (Trx1) is a redox-active protein containing two active site cysteines (Cys-32 and Cys-35) that cycle between the dithiol and disulfide forms as Trx1 reduces target proteins. Disulfides 137-146 thioredoxin Homo sapiens 13-17 12816947-1 2003 Thioredoxin (Trx1) is a redox-active protein containing two active site cysteines (Cys-32 and Cys-35) that cycle between the dithiol and disulfide forms as Trx1 reduces target proteins. Disulfides 137-146 thioredoxin Homo sapiens 156-160 12816947-3 2003 Using the redox Western blot technique and matrix assisted laser desorption ionization time-of-flight mass spectrometry mass spectrometry, we determined the midpoint potential (E0) of the Trx1 active site (-230 mV) and identified a second redox-active dithiol/disulfide (Cys-62 and Cys-69) in an alpha helix proximal to the active site, which formed under oxidizing conditions. Disulfides 260-269 thioredoxin Homo sapiens 188-192 12816947-7 2003 Taken together these results suggest that the Cys-62-Cys-69 disulfide could provide a means to transiently inhibit Trx1 activity under conditions of redox signaling or oxidative stress, allowing more time for the sensing and transmission of oxidative signals. Disulfides 60-69 thioredoxin Homo sapiens 115-119 12626117-6 2003 A fine-tuning redox-dependent regulatory loop inhibits the activation of the kinase via reduction of protein disulfide groups, possibly involving the thioredoxin complex. Disulfides 109-118 thioredoxin Homo sapiens 150-161 12553798-1 2003 Ferredoxin:thioredoxin reductase (FTR) catalyzes the reduction of the disulfide in thioredoxin in two one-electron steps using an active site comprising a [4Fe-4S] in close proximity to a redox active disulfide. Disulfides 70-79 thioredoxin Homo sapiens 11-22 12553798-1 2003 Ferredoxin:thioredoxin reductase (FTR) catalyzes the reduction of the disulfide in thioredoxin in two one-electron steps using an active site comprising a [4Fe-4S] in close proximity to a redox active disulfide. Disulfides 70-79 thioredoxin Homo sapiens 83-94 12553798-1 2003 Ferredoxin:thioredoxin reductase (FTR) catalyzes the reduction of the disulfide in thioredoxin in two one-electron steps using an active site comprising a [4Fe-4S] in close proximity to a redox active disulfide. Disulfides 201-210 thioredoxin Homo sapiens 11-22 12553798-1 2003 Ferredoxin:thioredoxin reductase (FTR) catalyzes the reduction of the disulfide in thioredoxin in two one-electron steps using an active site comprising a [4Fe-4S] in close proximity to a redox active disulfide. Disulfides 201-210 thioredoxin Homo sapiens 83-94 12362327-3 2002 Thioredoxin, a ubiquitous 12 kDa protein with a catalytically active disulfide active site (Cys-Gly-Pro-Cys), plays a central role in controlling the redox status of disulfide bonds in proteins that regulate a range of processes. Disulfides 69-78 thioredoxin Homo sapiens 0-11 12677197-1 2002 Thioredoxin (Trx) is a small multifunctional protein with a redox active dithiol/disulfide in the active-site sequence Cys-Gly-Pro-Cys. Disulfides 81-90 thioredoxin Homo sapiens 0-11 12677197-1 2002 Thioredoxin (Trx) is a small multifunctional protein with a redox active dithiol/disulfide in the active-site sequence Cys-Gly-Pro-Cys. Disulfides 81-90 thioredoxin Homo sapiens 13-16 12145281-7 2002 Dithiothreitol could reduce either the sulfenic acid or the disulfide, but the disulfide was a preferred substrate for thioredoxin, a natural electron donor. Disulfides 79-88 thioredoxin Homo sapiens 119-130 12213606-1 2002 Thioredoxins are small molecular weight disulfide oxidoreductases specialized in the reduction of disulfide bonds on other proteins. Disulfides 40-49 thioredoxin Homo sapiens 0-12 12362327-3 2002 Thioredoxin, a ubiquitous 12 kDa protein with a catalytically active disulfide active site (Cys-Gly-Pro-Cys), plays a central role in controlling the redox status of disulfide bonds in proteins that regulate a range of processes. Disulfides 166-175 thioredoxin Homo sapiens 0-11 12362327-7 2002 In so doing, the usefulness of applying this method for both in vitro and in vivo analyses is discussed for thioredoxin and other disulfide proteins, especially those occurring in plants. Disulfides 130-139 thioredoxin Homo sapiens 108-119 12119401-7 2002 These data suggest that the intracellular glutathione/glutathione disulfide ratio, an indicator of the redox state of the cell, can regulate Trx functions reversibly through thiol-disulfide exchange reactions. Disulfides 66-75 thioredoxin Homo sapiens 141-144 12089508-5 2002 The redox state of the thiols (disulfide versus dithiol) appeared to be regulated by thioredoxin, which is secreted by CD4(+) T cells. Disulfides 31-40 thioredoxin Homo sapiens 85-96 12004064-2 2002 In prokaryotes, the catalytic pathway responsible for disulfide isomerization involves thioredoxin, thioredoxin reductase, and the DsbC, DsbG, and DsbD proteins. Disulfides 54-63 thioredoxin Homo sapiens 87-98 12070343-5 2002 This rate is orders of magnitude faster than the reaction of dithiol Trx with insulin disulfides. Disulfides 86-96 thioredoxin Homo sapiens 69-72 12089063-2 2002 Apoptotic stimuli such as tumor necrosis factor (TNF) and reactive oxygen species (ROS) activate ASK1 in part by oxidizing Trx (forming intramolecular disulfide between C32 and C35) to release Trx from ASK1. Disulfides 151-160 thioredoxin Homo sapiens 123-126 12070343-6 2002 Ebselen competed with disulfide substrates for reduction by Trx and, therefore, acted as an inhibitor of protein disulfide reduction by the Trx system. Disulfides 22-31 thioredoxin Homo sapiens 140-143 12070343-6 2002 Ebselen competed with disulfide substrates for reduction by Trx and, therefore, acted as an inhibitor of protein disulfide reduction by the Trx system. Disulfides 113-122 thioredoxin Homo sapiens 60-63 12070343-6 2002 Ebselen competed with disulfide substrates for reduction by Trx and, therefore, acted as an inhibitor of protein disulfide reduction by the Trx system. Disulfides 113-122 thioredoxin Homo sapiens 140-143 12070343-6 2002 Ebselen competed with disulfide substrates for reduction by Trx and, therefore, acted as an inhibitor of protein disulfide reduction by the Trx system. Disulfides 22-31 thioredoxin Homo sapiens 60-63 12169016-2 2002 In oxidized thioredoxin, the two cysteines form a disulfide bond that is targeted by the enzyme thioredoxin reductase. Disulfides 50-59 thioredoxin Homo sapiens 12-23 12169016-4 2002 Thioredoxins participate in dithiol/disulfide exchange reactions with a large range of cellular substrates. Disulfides 36-45 thioredoxin Homo sapiens 0-12 12189047-3 2002 Thioredoxin (TRX), a small protein with redox-active dithiol/disulfide in the active site, is induced by a variety of oxidative stresses and secreted from the cells. Disulfides 61-70 thioredoxin Homo sapiens 0-11 11785944-4 2002 The disulfide forms of other cellular proteins rose in parallel with thioredoxin oxidation. Disulfides 4-13 thioredoxin Homo sapiens 69-80 16228530-1 2002 Chloroplast NADP-dependent malate dehydrogenase (NADP-MDH, EC 1.1.1.82) is inactive in the dark and activated in the light via a reduction of specific disulfides by thiol-disulfide interchange with thioredoxin, reduced by the photosynthetic electron transfer. Disulfides 151-161 thioredoxin Homo sapiens 198-209 12189047-3 2002 Thioredoxin (TRX), a small protein with redox-active dithiol/disulfide in the active site, is induced by a variety of oxidative stresses and secreted from the cells. Disulfides 61-70 thioredoxin Homo sapiens 13-16 11764282-1 2001 An important constituent of the cellular antioxidant buffering system that controls the redox state of proteins is thioredoxin (TRX), a 13 kDa protein that catalyzes thiol-disulfide exchange reactions, regulates activation of transcription factors, and possesses several other biologic functions similar to cytokines. Disulfides 172-181 thioredoxin Homo sapiens 115-126 11705765-10 2001 Inhibition of disulfide bond formation by thioredoxin or thioredoxin reductase significantly decreased xanthine/xanthine oxidase-induced activation of renal 5"-ND. Disulfides 14-23 thioredoxin Homo sapiens 42-53 11705765-10 2001 Inhibition of disulfide bond formation by thioredoxin or thioredoxin reductase significantly decreased xanthine/xanthine oxidase-induced activation of renal 5"-ND. Disulfides 14-23 thioredoxin Homo sapiens 57-68 11764282-1 2001 An important constituent of the cellular antioxidant buffering system that controls the redox state of proteins is thioredoxin (TRX), a 13 kDa protein that catalyzes thiol-disulfide exchange reactions, regulates activation of transcription factors, and possesses several other biologic functions similar to cytokines. Disulfides 172-181 thioredoxin Homo sapiens 128-131 11259642-7 2001 These observations, together with the biochemical probing and molecular modeling of the TGR structure, suggest a mechanism whereby the C-terminal selenotetrapeptide serves a role of a protein-linked GSSG and shuttles electrons from the disulfide center within the TR domain to either the glutaredoxin domain or Trx. Disulfides 236-245 thioredoxin Homo sapiens 311-314 11481439-7 2001 A model of the complex of TrxR with Trx suggests that electron transfer from NADPH to the disulfide of the substrate is possible without large conformational changes. Disulfides 90-99 thioredoxin Homo sapiens 26-29 11481439-8 2001 The C-terminal extension typical of mammalian TrxRs has two functions: (i) it extends the electron transport chain from the catalytic disulfide to the enzyme surface, where it can react with Trx, and (ii) it prevents the enzyme from acting as a GR by blocking the redox-active disulfide. Disulfides 134-143 thioredoxin Homo sapiens 46-49 11481439-8 2001 The C-terminal extension typical of mammalian TrxRs has two functions: (i) it extends the electron transport chain from the catalytic disulfide to the enzyme surface, where it can react with Trx, and (ii) it prevents the enzyme from acting as a GR by blocking the redox-active disulfide. Disulfides 277-286 thioredoxin Homo sapiens 46-49 11152479-5 2001 Using recombinant proteins expressed in Escherichia coli, we demonstrated the activity of the Trx domain of TMX to cleave the interchain disulfide bridges in insulin in vitro. Disulfides 137-146 thioredoxin Homo sapiens 94-97 10982790-1 2000 Human thioredoxin (Trx) catalyzes intracellular disulfide reductions but has also co-cytokine activity with interleukins after leaderless secretion. Disulfides 48-57 thioredoxin Homo sapiens 6-17 11778846-1 2001 Thioredoxin (TRX) is a small ubiquitous and multifunctional protein having a redox-active dithiol/disulfide within the conserved active site sequence -Cys-Gly-Pro-Cys-. Disulfides 98-107 thioredoxin Homo sapiens 0-11 11778846-1 2001 Thioredoxin (TRX) is a small ubiquitous and multifunctional protein having a redox-active dithiol/disulfide within the conserved active site sequence -Cys-Gly-Pro-Cys-. Disulfides 98-107 thioredoxin Homo sapiens 13-16 10982790-1 2000 Human thioredoxin (Trx) catalyzes intracellular disulfide reductions but has also co-cytokine activity with interleukins after leaderless secretion. Disulfides 48-57 thioredoxin Homo sapiens 19-22 11012661-2 2000 Thioredoxins, with a dithiol/disulfide active site (CGPC) are the major cellular protein disulfide reductases; they therefore also serve as electron donors for enzymes such as ribonucleotide reductases, thioredoxin peroxidases (peroxiredoxins) and methionine sulfoxide reductases. Disulfides 29-38 thioredoxin Homo sapiens 203-214 11005828-5 2000 (ii) A disulfide bond in the LHCII kinase, rather than in its substrate, may be a target component regulated by thioredoxin. Disulfides 7-16 thioredoxin Homo sapiens 112-123 11005828-9 2000 (iv) Upon high-light illumination of leaves, the target disulfide bond becomes exposed and thus is made available for reduction by thioredoxin, resulting in a stable inactivation of LHCII kinase. Disulfides 56-65 thioredoxin Homo sapiens 131-142 10942760-5 2000 This motif comprises the active site in enzymes involved in disulfide exchange reactions, including protein-disulfide isomerase (EC ) and thioredoxin. Disulfides 60-69 thioredoxin Homo sapiens 138-149 10801830-1 2000 The chloroplastic NADP-malate dehydrogenase is activated by reduction of its N- and C-terminal disulfides by reduced thioredoxin. Disulfides 95-105 thioredoxin Homo sapiens 117-128 10751410-6 2000 The disulfide formed by PrxV is reduced by thioredoxin but not by glutaredoxin or glutathione. Disulfides 4-13 thioredoxin Homo sapiens 43-54 10987366-0 2000 The thioredoxin boxes of thyroglobulin: possible implications for intermolecular disulfide bond formation in the follicle lumen. Disulfides 81-90 thioredoxin Homo sapiens 4-15 10649999-1 2000 Light generates reducing equivalents in chloroplasts that are used not only for carbon reduction, but also for the regulation of the activity of chloroplast enzymes by reduction of regulatory disulfides via the ferredoxin:thioredoxin reductase (FTR) system. Disulfides 192-202 thioredoxin Homo sapiens 222-233 15012197-1 2000 Thioredoxins, the ubiquitous small proteins with a redox active disulfide bridge, are important regulatory elements in plant metabolism. Disulfides 64-73 thioredoxin Homo sapiens 0-12 10847613-11 2000 These data suggest that the relative participation of the thioltransferase (glutaredoxin) and thioredoxin systems in overall cellular disulfide reduction is cell line specific. Disulfides 134-143 thioredoxin Homo sapiens 94-105 10196131-6 1999 Two surface-exposed and thioredoxin-accessible disulfide bonds are present, one in the N-terminal extension and the other in the C-terminal extension. Disulfides 47-56 thioredoxin Homo sapiens 24-35 10800594-4 2000 Thioredoxin of mediated thiol-disulfide exchange interconverts eukaryotic PRKs between reduced (active) and oxidized (inactive) forms. Disulfides 30-39 thioredoxin Homo sapiens 0-11 10397171-1 1999 Thioredoxin (TRX) has disulfide reducing activity and is reported to be involved in various cellular functions including the promotion of cell growth and apoptosis. Disulfides 22-31 thioredoxin Homo sapiens 0-11 10397171-1 1999 Thioredoxin (TRX) has disulfide reducing activity and is reported to be involved in various cellular functions including the promotion of cell growth and apoptosis. Disulfides 22-31 thioredoxin Homo sapiens 13-16 10610776-5 1999 Moreover, a novel intramolecular disulfide bond replaces the canonical one found in the thioredoxin family. Disulfides 33-42 thioredoxin Homo sapiens 88-99 10766297-0 1999 Parallel syntheses of disulfide inhibitors of the thioredoxin redox system as potential antitumor agents. Disulfides 22-31 thioredoxin Homo sapiens 50-61 10766297-1 1999 We have reported previously that unsymmetrical disulfide inhibitors of the human thioredoxin/thioredoxin reductase redox system (hTrx/TR) possess antitumor activity. Disulfides 47-56 thioredoxin Homo sapiens 81-92 10766297-1 1999 We have reported previously that unsymmetrical disulfide inhibitors of the human thioredoxin/thioredoxin reductase redox system (hTrx/TR) possess antitumor activity. Disulfides 47-56 thioredoxin Homo sapiens 93-104 10766297-8 1999 The most potent inhibitors of the Trx system contained two heteroatoms ortho to the disulfide moiety in an aromatic functionality. Disulfides 84-93 thioredoxin Homo sapiens 34-37 10766297-11 1999 Bis-disulfides showed patterns of activity which depended on chain length, with optimum activity observed when the disulfide units were separated by 3.9 A, a similar distance to that separating the thioredoxin active site cysteine residues. Disulfides 4-13 thioredoxin Homo sapiens 198-209 10463612-1 1999 Thioredoxin (Trx) is a small redox-active protein that provides reducing equivalents for key cysteine residues of proteins through thiol-disulfide exchange, such as the transcription factor nuclear factor-kappaB (NF-kappaB). Disulfides 137-146 thioredoxin Homo sapiens 0-11 10463612-1 1999 Thioredoxin (Trx) is a small redox-active protein that provides reducing equivalents for key cysteine residues of proteins through thiol-disulfide exchange, such as the transcription factor nuclear factor-kappaB (NF-kappaB). Disulfides 137-146 thioredoxin Homo sapiens 13-16 10428967-5 1999 Thioredoxin was able to reduce oxidized RsrA, suggesting that sigma(R), RsrA and the thioredoxin system comprise a novel feedback homeostasis loop that senses and responds to changes in the intracellular thiol-disulfide redox balance. Disulfides 210-219 thioredoxin Homo sapiens 0-11 10428967-5 1999 Thioredoxin was able to reduce oxidized RsrA, suggesting that sigma(R), RsrA and the thioredoxin system comprise a novel feedback homeostasis loop that senses and responds to changes in the intracellular thiol-disulfide redox balance. Disulfides 210-219 thioredoxin Homo sapiens 85-96 10369668-1 1999 The thiol/disulfide oxidoreductase DsbA is the strongest oxidant of the thioredoxin superfamily and is required for efficient disulfide bond formation in the periplasm of Escherichia coli. Disulfides 10-19 thioredoxin Homo sapiens 72-83 9886847-1 1999 Human thioredoxin (hTrx) is a cellular redox-active protein that catalyzes dithiol/disulfide exchange reactions, thus controlling multiple biological functions, including cell growth-promoting activity. Disulfides 83-92 thioredoxin Homo sapiens 6-17 10383197-12 1999 Structural comparison of the PDI b domain with thioredoxin and PDI a reveals several features important for thiol-disulfide exchange activity. Disulfides 114-123 thioredoxin Homo sapiens 47-58 10066758-4 1999 Several proteins involved in disulfide exchange reactions contain the sequence Cys-X-X-Cys in their active sites, including thioredoxin and protein-disulfide isomerase. Disulfides 29-38 thioredoxin Homo sapiens 124-135 9886847-1 1999 Human thioredoxin (hTrx) is a cellular redox-active protein that catalyzes dithiol/disulfide exchange reactions, thus controlling multiple biological functions, including cell growth-promoting activity. Disulfides 83-92 thioredoxin Homo sapiens 19-23 9668102-4 1998 The thioredoxin domain of TRP32 has thioredoxin-like reducing activity, which can reduce the interchain disulfide bridges of insulin in vitro. Disulfides 104-113 thioredoxin Homo sapiens 4-15 10210188-1 1999 In addition to the Cys-Xaa-Xaa-Cys motif at position 30-33, DsbA, the essential catalyst for disulfide bond formation in the bacterial periplasm shares with other oxidoreductases of the thioredoxin family a cis-proline in proximity of the active site residues. Disulfides 93-102 thioredoxin Homo sapiens 186-197 9668102-4 1998 The thioredoxin domain of TRP32 has thioredoxin-like reducing activity, which can reduce the interchain disulfide bridges of insulin in vitro. Disulfides 104-113 thioredoxin Homo sapiens 36-47 9585516-2 1998 One of the sites predicted by the Dezymer computer program to introduce a tetrahedral tetrathiolate iron center included the intrinsic Cys32-Cys35 disulfide of wild-type thioredoxin and two additional mutants, Trp28Cys and Ile75Cys, thereby converting a disulfide into a metal-based redox center. Disulfides 147-156 thioredoxin Homo sapiens 170-181 9585516-2 1998 One of the sites predicted by the Dezymer computer program to introduce a tetrahedral tetrathiolate iron center included the intrinsic Cys32-Cys35 disulfide of wild-type thioredoxin and two additional mutants, Trp28Cys and Ile75Cys, thereby converting a disulfide into a metal-based redox center. Disulfides 254-263 thioredoxin Homo sapiens 170-181 9605422-5 1998 The disulfides caused reversible thioalkylation of hTrx at the redox catalytic site as shown by the fact that there was no thioalkylation of a mutant hTrx where both the catalytic site Cys32 and Cys35 residues were replaced by Ser. Disulfides 4-14 thioredoxin Homo sapiens 51-55 9679540-7 1998 A class of disulfide inhibitors of thioredoxin has been identified. Disulfides 11-20 thioredoxin Homo sapiens 35-46 9605422-9 1998 The disulfides inhibited the hTrx-dependent proliferation of MCF-7 breast cancer cells with IC50 values for III-2 and IV-2 of 0.2 and 1.2 microM, respectively. Disulfides 4-14 thioredoxin Homo sapiens 29-33 9605422-10 1998 The results show that although the catalytic sites of TR and hTrx are reversibly inhibited by the 2-imidazolyl disulfides, it is the irreversible thioalkylation of Cys73 of hTrx by the disulfides that most probably accounts for the inhibition of thioredoxin-dependent cell growth by the disulfides. Disulfides 111-121 thioredoxin Homo sapiens 61-65 9605422-10 1998 The results show that although the catalytic sites of TR and hTrx are reversibly inhibited by the 2-imidazolyl disulfides, it is the irreversible thioalkylation of Cys73 of hTrx by the disulfides that most probably accounts for the inhibition of thioredoxin-dependent cell growth by the disulfides. Disulfides 185-195 thioredoxin Homo sapiens 61-65 9605422-10 1998 The results show that although the catalytic sites of TR and hTrx are reversibly inhibited by the 2-imidazolyl disulfides, it is the irreversible thioalkylation of Cys73 of hTrx by the disulfides that most probably accounts for the inhibition of thioredoxin-dependent cell growth by the disulfides. Disulfides 185-195 thioredoxin Homo sapiens 173-177 9605422-6 1998 In addition, the disulfides caused a slower irreversible inactivation of hTrx as a substrate for reduction by TR, with half-lives for III-2 of 30 min, for IV-2 of 4 hr, and for IX-2 (t-butyl 2-mercaptoimidazolyl disulfide) of 24 hr. Disulfides 17-27 thioredoxin Homo sapiens 73-77 9605422-7 1998 This irreversible inactivation of hTrx occurred at concentrations of the disulfides an order of magnitude below those that inhibited TR, and involved the Cys73 of hTrx, which is outside the conserved redox catalytic site, as shown by the resistance to inactivation of a mutant hTrx where Cys73 was replaced by Ser. Disulfides 73-83 thioredoxin Homo sapiens 34-38 9605422-8 1998 Electrophoretic and mass spectral analyses of the products of the reaction between the disulfides and hTrx show that modification of 1-3 Cys residues of the protein occurred in a concentration-dependent fashion. Disulfides 87-97 thioredoxin Homo sapiens 102-106 9521781-0 1998 Role of the [Fe4S4] cluster in mediating disulfide reduction in spinach ferredoxin:thioredoxin reductase. Disulfides 41-50 thioredoxin Homo sapiens 83-94 9521781-1 1998 Thioredoxin reduction in plant chloroplasts is catalyzed by a unique class of disulfide reductases which use a one-electron donor, [Fe2S2]2+,+ ferredoxin, and has an active site involving a disulfide in close proximity to a [Fe4S4]2+ cluster. Disulfides 78-87 thioredoxin Homo sapiens 0-11 9521781-2 1998 In this study, spinach ferredoxin:thioredoxin reductase (FTR) reduced with stoichiometric amounts of reduced benzyl viologen or frozen under turnover conditions in the presence of thioredoxin is shown to exhibit a slowly relaxing S = 1/2 resonance (g = 2.11, 2.00, 1.98) identical to that of a modified form of the enzyme in which one of the cysteines of the active-site disulfide is alkylated with N-ethylmaleimide (NEM-FTR). Disulfides 371-380 thioredoxin Homo sapiens 34-45 9521781-2 1998 In this study, spinach ferredoxin:thioredoxin reductase (FTR) reduced with stoichiometric amounts of reduced benzyl viologen or frozen under turnover conditions in the presence of thioredoxin is shown to exhibit a slowly relaxing S = 1/2 resonance (g = 2.11, 2.00, 1.98) identical to that of a modified form of the enzyme in which one of the cysteines of the active-site disulfide is alkylated with N-ethylmaleimide (NEM-FTR). Disulfides 371-380 thioredoxin Homo sapiens 180-191 9521781-8 1998 The catalytic mechanism involves novel S-based cluster chemistry to facilitate electron transfer to the active-site disulfide resulting in covalent attachment of the electron-transfer cysteine and generation of the free interchange cysteine that is required for the thiol-disulfide interchange reaction with thioredoxin. Disulfides 116-125 thioredoxin Homo sapiens 308-319 9521781-8 1998 The catalytic mechanism involves novel S-based cluster chemistry to facilitate electron transfer to the active-site disulfide resulting in covalent attachment of the electron-transfer cysteine and generation of the free interchange cysteine that is required for the thiol-disulfide interchange reaction with thioredoxin. Disulfides 272-281 thioredoxin Homo sapiens 308-319 9950104-1 1998 Thioredoxin (TRX) is known to contain an active site with a redox-active disulfide and has various biological activities. Disulfides 73-82 thioredoxin Homo sapiens 0-11 9950104-1 1998 Thioredoxin (TRX) is known to contain an active site with a redox-active disulfide and has various biological activities. Disulfides 73-82 thioredoxin Homo sapiens 13-16 9407079-1 1997 A catalyst of disulfide formation and isomerization during protein folding, protein-disulfide isomerase (PDI) has two catalytic sites housed in two domains homologous to thioredoxin, one near the N terminus and the other near the C terminus. Disulfides 14-23 thioredoxin Homo sapiens 170-181 9407079-2 1997 The thioredoxin domains, by themselves, can catalyze disulfide formation, but they are unable to catalyze disulfide isomerizations (Darby, N. J. and Creighton, T. E. (1995) Biochemistry 34, 11725-11735). Disulfides 53-62 thioredoxin Homo sapiens 4-15 9315320-6 1997 Glutaredoxin (Grx) which catalyzes GSH-dependent disulfide reduction also via a redox-active disulfide and Trx are both efficient electron donors to the human plasma glutathione peroxidase providing a mechanism by which human plasma glutathione peroxidase may reduce hydroperoxides in an environment almost free from glutathione. Disulfides 49-58 thioredoxin Homo sapiens 107-110 9344598-1 1997 Thioredoxin (Trx) is an intracellular multifunctional 12-kDa protein with a reduction/oxidation (redox) active disulfide constitutively expressed by most cells of the human body. Disulfides 111-120 thioredoxin Homo sapiens 0-11 9344598-1 1997 Thioredoxin (Trx) is an intracellular multifunctional 12-kDa protein with a reduction/oxidation (redox) active disulfide constitutively expressed by most cells of the human body. Disulfides 111-120 thioredoxin Homo sapiens 13-16 9369469-4 1997 A recent crystal structure determination of human thioredoxin revealed an inactive dimeric form of the protein covalently linked through a disulfide bond involving Cys 73 from each monomer [Weichsel et al. Disulfides 139-148 thioredoxin Homo sapiens 50-61 9119370-5 1997 Since the bacterially expressed protein of nucleoredoxin showed oxidoreductase activity of the insulin disulfide bonds with kinetics similar to that of thioredoxin, it may be a redox regulator of the nuclear proteins, such as transcription factors. Disulfides 103-112 thioredoxin Homo sapiens 152-163 9430198-0 1997 Human IgG is substrate for the thioredoxin system: differential cleavage pattern of interchain disulfide bridges in IgG subclasses. Disulfides 95-104 thioredoxin Homo sapiens 31-42 9430198-2 1997 wt protein with two redox-active cysteine residues, together with thioredoxin reductase and NADPH, may reduce protein disulfides and thereby act as a molecular probe of their structure and reactivity. Disulfides 118-128 thioredoxin Homo sapiens 66-77 9430198-3 1997 Interchain and intrachain disulfides are structural elements in all immunoglobulins and therefore potential substrates for the reduced thioredoxin, Trx(SH)2. Disulfides 26-36 thioredoxin Homo sapiens 135-146 9430198-3 1997 Interchain and intrachain disulfides are structural elements in all immunoglobulins and therefore potential substrates for the reduced thioredoxin, Trx(SH)2. Disulfides 26-36 thioredoxin Homo sapiens 148-156 9430198-4 1997 It was investigated whether such disulfides are cleaved in human polyclonal IgG and IgG subclass myeloma proteins by both the human and the Escherichia coli thioredoxin systems. Disulfides 33-43 thioredoxin Homo sapiens 157-168 9430198-6 1997 Human IgG was a substrate for both prokaryotic and eukaryotic Trx(SH)2, which directly reduced IgG disulfides in a time and dose-dependent manner. Disulfides 99-109 thioredoxin Homo sapiens 62-70 9430198-12 1997 The structural and functional importance of interchain disulfides in immunoglobulins suggests physiological implications of the thioredoxin system. Disulfides 55-65 thioredoxin Homo sapiens 128-139 9143692-4 1997 TRX is a small multifunctional protein that has a redox-active disulfide/dithiol within the conserved active site sequence: Cys-Gly-Pro-Cys. Disulfides 63-72 thioredoxin Homo sapiens 0-3 8986137-6 1996 We have recently shown by X-ray crystallography that Trx forms a dimer that is stabilized by an intermolecular Cys73-Cys73 disulfide bond. Disulfides 123-132 thioredoxin Homo sapiens 53-56 9406241-0 1997 Redox active disulfides: the thioredoxin system as a drug target. Disulfides 13-23 thioredoxin Homo sapiens 29-40 9406241-3 1997 We originally determined the disulfides to be weak reversible inhibitors of thioredoxin reductase. Disulfides 29-39 thioredoxin Homo sapiens 76-87 8931546-1 1996 Proteins with the thioredoxin fold have widely differing stabilities of the disulfide bond that can be formed between the two cysteines at their active site sequence motif Cys1-Xaa2-Yaa3-Cys4. Disulfides 76-85 thioredoxin Homo sapiens 18-29 8968078-1 1996 Thioredoxin (TRX), a disulfide-reducing intracellular protein, functions as a cellular defense mechanism against oxidative stress. Disulfides 21-30 thioredoxin Homo sapiens 0-11 8968078-1 1996 Thioredoxin (TRX), a disulfide-reducing intracellular protein, functions as a cellular defense mechanism against oxidative stress. Disulfides 21-30 thioredoxin Homo sapiens 13-16 8931546-3 1996 A consistent relationship between disulfide bond stability and Cys1 thiol pKa value is found here for DsbA, thioredoxin, and the N-terminal thioredoxin-like domain of protein disulfide isomerase (PDI a), which has a very low thiol pKa value of 4.5. Disulfides 34-43 thioredoxin Homo sapiens 108-119 8931546-3 1996 A consistent relationship between disulfide bond stability and Cys1 thiol pKa value is found here for DsbA, thioredoxin, and the N-terminal thioredoxin-like domain of protein disulfide isomerase (PDI a), which has a very low thiol pKa value of 4.5. Disulfides 34-43 thioredoxin Homo sapiens 140-151 8759006-1 1996 Adult T cell leukemia-derived factor (ADF) is a human thioredoxin (Trx) and is a disulfide reducing protein with various biological functions. Disulfides 81-90 thioredoxin Homo sapiens 38-41 8964512-1 1996 Thioredoxin (TRX) is an ubiquitous and relatively conserved oxidoreductant enzyme which is involved in a multitude of redox reactions through the formation of reversible disulfide bonds. Disulfides 170-179 thioredoxin Homo sapiens 0-11 8964512-1 1996 Thioredoxin (TRX) is an ubiquitous and relatively conserved oxidoreductant enzyme which is involved in a multitude of redox reactions through the formation of reversible disulfide bonds. Disulfides 170-179 thioredoxin Homo sapiens 13-16 8784198-1 1996 Thioredoxin reduction in chloroplasts is catalyzed by a unique class of disulfide reductases which use a [2Fe-2S]2+/+ ferredoxin as the electron donor and contain an Fe-S cluster as the sole prosthetic group in addition to the active-site disulfide. Disulfides 72-81 thioredoxin Homo sapiens 0-11 8756708-2 1996 Two of the domains, a and a", which are homologous to thioredoxin and active in catalysis of disulfide bond formation, have been identified and characterized previously. Disulfides 93-102 thioredoxin Homo sapiens 54-65 8914835-0 1996 S-glutathiolated hepatocyte proteins and insulin disulfides as substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase, and glutathione. Disulfides 49-59 thioredoxin Homo sapiens 105-116 8914835-19 1996 Thus, protein disulfide isomerase and thioredoxin are more effective than glutaredoxin as reductants of insulin protein disulfides. Disulfides 120-130 thioredoxin Homo sapiens 38-49 8914835-23 1996 A glutathione binding site at the dithiol region of glutaredoxin may be of primary importance for its function in protein dethiolation, while a different specific peptide binding site in thioredoxin may be more suited to certain protein disulfide structures. Disulfides 237-246 thioredoxin Homo sapiens 187-198 8810647-3 1996 Because S-nitrosylation of vicinal thiols promotes disulfide formation, we determined whether exposure to NO results in modulation of the catalytic activity of NO synthase and whether disulfide reduction catalyzed by thioredoxin/thioredoxin reductase (T/TR) and/or by glutaredoxin restores the catalytic activity of NO synthase in pulmonary artery endothelial cells (PAEC). Disulfides 184-193 thioredoxin Homo sapiens 217-228 8810647-12 1996 Thioredoxin-regulated reversal of NO-induced modulation of NO synthase protein suggests that an oxidative conformational change in vicinal thiols, resulting in the formation of intramolecular or intermolecular disulfides or both, is involved. Disulfides 210-220 thioredoxin Homo sapiens 0-11 8759006-1 1996 Adult T cell leukemia-derived factor (ADF) is a human thioredoxin (Trx) and is a disulfide reducing protein with various biological functions. Disulfides 81-90 thioredoxin Homo sapiens 54-65 8759006-1 1996 Adult T cell leukemia-derived factor (ADF) is a human thioredoxin (Trx) and is a disulfide reducing protein with various biological functions. Disulfides 81-90 thioredoxin Homo sapiens 67-70 8664271-0 1996 A stable mixed disulfide between thioredoxin reductase and its substrate, thioredoxin: preparation and characterization. Disulfides 15-24 thioredoxin Homo sapiens 33-44 8626570-0 1996 NK-lysin, a disulfide-containing effector peptide of T-lymphocytes, is reduced and inactivated by human thioredoxin reductase. Disulfides 12-21 thioredoxin Homo sapiens 104-115 8626570-7 1996 NK-lysin is the first identified macromolecular disulfide substrate for human thioredoxin reductase apart from human thioredoxin. Disulfides 48-57 thioredoxin Homo sapiens 78-89 8805557-1 1996 BACKGROUND: Human thioredoxin reduces the disulfide bonds of numerous proteins in vitro, and can activate transcription factors such as NFkB in vivo. Disulfides 42-51 thioredoxin Homo sapiens 18-29 8805557-4 1996 Surprisingly, thioredoxin is dimeric in all four structures; the dimer is linked through a disulfide bond between Cys73 of each monomer, except in Cys73-->Ser where a hydrogen bond occurs. Disulfides 91-100 thioredoxin Homo sapiens 14-25 8805557-9 1996 This nucleophilicity, in tum, is thought to be necessary for the role of thioredoxin in disulfide-bond reduction. Disulfides 88-97 thioredoxin Homo sapiens 73-84 8631927-9 1996 Thus, two independent approaches identify Cys-55 of PRK in the intermolecular disulfide pairing with Trx. Disulfides 78-87 thioredoxin Homo sapiens 101-104 8671648-1 1996 Thioredoxin (Trx), a ubiquitous protein intimately involved in redox and protein disulfide reductions, has been shown to be released from cells and to have cytokine-like activities. Disulfides 81-90 thioredoxin Homo sapiens 0-11 8671648-1 1996 Thioredoxin (Trx), a ubiquitous protein intimately involved in redox and protein disulfide reductions, has been shown to be released from cells and to have cytokine-like activities. Disulfides 81-90 thioredoxin Homo sapiens 13-16 8631927-0 1996 The molecular pathway for the regulation of phosphoribulokinase by thioredoxin f. Phosphoribulokinase (PRK) is one of several plant enzymes that is regulated by thiol-disulfide exchange as mediated by thioredoxin, which contains spatially vicinal, redox-active cysteinyl residues. Disulfides 167-176 thioredoxin Homo sapiens 67-78 8631927-0 1996 The molecular pathway for the regulation of phosphoribulokinase by thioredoxin f. Phosphoribulokinase (PRK) is one of several plant enzymes that is regulated by thiol-disulfide exchange as mediated by thioredoxin, which contains spatially vicinal, redox-active cysteinyl residues. Disulfides 167-176 thioredoxin Homo sapiens 201-212 8631927-3 1996 268, 18411-18414), our laboratory identified Cys-46 of thioredoxin f (Trx), as opposed to the other candidate Cys-49, as the primary nucleophile that attacks the disulfide of target proteins. Disulfides 162-171 thioredoxin Homo sapiens 55-68 8631927-3 1996 268, 18411-18414), our laboratory identified Cys-46 of thioredoxin f (Trx), as opposed to the other candidate Cys-49, as the primary nucleophile that attacks the disulfide of target proteins. Disulfides 162-171 thioredoxin Homo sapiens 70-73 8631927-4 1996 The goal of the present study was to identify which of the two redox-active cysteinyl residues of PRK (Cys-16 or Cys-55) is paired with Cys-46 of Trx in the interprotein disulfide intermediate of the overall oxidation-reduction pathway. Disulfides 170-179 thioredoxin Homo sapiens 146-149 9816187-1 1996 Thioredoxin (TRX) is a widely distributed Mr 13,000 protein with a redox-active dithiol/disulfide in the active site. Disulfides 88-97 thioredoxin Homo sapiens 0-11 9816187-1 1996 Thioredoxin (TRX) is a widely distributed Mr 13,000 protein with a redox-active dithiol/disulfide in the active site. Disulfides 88-97 thioredoxin Homo sapiens 13-16 8543831-2 1996 Thioredoxin is one of the major redox-regulatory molecules which because of its dithiol/disulfide exchange activity determines the oxidation state of protein thiols. Disulfides 88-97 thioredoxin Homo sapiens 0-11 7547690-8 1995 Furthermore, MP6 medium showed Trx activity with NADPH and Trx reductase using an insulin disulfide reduction assay. Disulfides 90-99 thioredoxin Homo sapiens 59-62 8555200-1 1996 The pH dependence of the 13C chemical shifts of the side-chain carboxyl carbons of all Asp and Glu residues in the reduced and oxidized states of human thioredoxin and in a mixed disulfide complex of human thioredoxin with a target peptide from the transcription factor NF kappa B has been investigated by multidimensional triple-resonance NMR spectroscopy. Disulfides 179-188 thioredoxin Homo sapiens 206-217 7577807-1 1995 Adult T cell leukemia-derived factor (ADF), which is identical to a disulfide reducing enzyme human thioredoxin (TRX), is produced and released by activated or virus-infected lymphocytes. Disulfides 68-77 thioredoxin Homo sapiens 38-41 7577807-1 1995 Adult T cell leukemia-derived factor (ADF), which is identical to a disulfide reducing enzyme human thioredoxin (TRX), is produced and released by activated or virus-infected lymphocytes. Disulfides 68-77 thioredoxin Homo sapiens 100-111 7577807-1 1995 Adult T cell leukemia-derived factor (ADF), which is identical to a disulfide reducing enzyme human thioredoxin (TRX), is produced and released by activated or virus-infected lymphocytes. Disulfides 68-77 thioredoxin Homo sapiens 113-116 7876079-2 1995 Human thioredoxin reductase is a dimeric enzyme that catalyzes reduction of the disulfide in oxidized thioredoxin by a mechanism involving transfer of electrons from NADPH via FAD to a redox-active disulfide. Disulfides 80-89 thioredoxin Homo sapiens 6-17 7788289-0 1995 Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide. Disulfides 109-118 thioredoxin Homo sapiens 0-11 7788289-1 1995 The recent high-resolution solution structures of human and Escherichia coli thioredoxin in their oxidized and reduced states support a catalytic model of protein disulfide reduction involving binding of a target protein and nucleophilic attack by the active-site Cys32 thiolate to form a transition state mixed disulfide. Disulfides 163-172 thioredoxin Homo sapiens 77-88 7788289-1 1995 The recent high-resolution solution structures of human and Escherichia coli thioredoxin in their oxidized and reduced states support a catalytic model of protein disulfide reduction involving binding of a target protein and nucleophilic attack by the active-site Cys32 thiolate to form a transition state mixed disulfide. Disulfides 312-321 thioredoxin Homo sapiens 77-88 7788295-0 1995 Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B. Disulfides 51-60 thioredoxin Homo sapiens 28-39 7788295-3 1995 Using multidimensional heteronuclear-edited and hetero-nuclear-filtered NMR spectroscopy, we have solved the solution structure of a complex of human thioredoxin and a 13-residue peptide extending from residues 56-68 of p50, representing a kinetically stable mixed disulfide intermediate along the reaction pathway. Disulfides 265-274 thioredoxin Homo sapiens 150-161 7788295-6 1995 CONCLUSIONS: In addition to the intermolecular disulfide bridge between Cys32 of human thioredoxin and Cys62 of the peptide, the complex is stabilized by numerous hydrogen-bonding, electrostatic and hydrophobic interactions which involve residues 57-65 of the NF kappa B peptide and confer substrate specificity. Disulfides 47-56 thioredoxin Homo sapiens 87-98 7788295-7 1995 These structural features permit one to suggest the specificity requirements for human thioredoxin-catalyzed disulfide bond reduction of proteins. Disulfides 109-118 thioredoxin Homo sapiens 87-98 7876079-2 1995 Human thioredoxin reductase is a dimeric enzyme that catalyzes reduction of the disulfide in oxidized thioredoxin by a mechanism involving transfer of electrons from NADPH via FAD to a redox-active disulfide. Disulfides 198-207 thioredoxin Homo sapiens 6-17 7876079-2 1995 Human thioredoxin reductase is a dimeric enzyme that catalyzes reduction of the disulfide in oxidized thioredoxin by a mechanism involving transfer of electrons from NADPH via FAD to a redox-active disulfide. Disulfides 198-207 thioredoxin Homo sapiens 102-113 7876079-11 1995 The inactivation of the disulfide reducing activity of thioredoxin reductase and thioredoxin with a concomitant large increase of the NADPH oxidase activity producing reactive oxygen intermediates may mediate effects of DNCB on cells in vivo. Disulfides 24-33 thioredoxin Homo sapiens 55-66 7876079-11 1995 The inactivation of the disulfide reducing activity of thioredoxin reductase and thioredoxin with a concomitant large increase of the NADPH oxidase activity producing reactive oxygen intermediates may mediate effects of DNCB on cells in vivo. Disulfides 24-33 thioredoxin Homo sapiens 81-92 7876079-2 1995 Human thioredoxin reductase is a dimeric enzyme that catalyzes reduction of the disulfide in oxidized thioredoxin by a mechanism involving transfer of electrons from NADPH via FAD to a redox-active disulfide. Disulfides 80-89 thioredoxin Homo sapiens 102-113 7979362-2 1994 Thioredoxins undergo reversible redox change through a disulfide group (S-S-->2 SH). Disulfides 55-64 thioredoxin Homo sapiens 0-12 7476356-0 1995 Measurement of equilibrium midpoint potentials of thiol/disulfide regulatory groups on thioredoxin-activated chloroplast enzymes. Disulfides 56-65 thioredoxin Homo sapiens 87-98 7983029-2 1994 The wild-type protein contains two redox active thiol/disulfide sites near the N and C terminus that are homologous to the redox center of thioredoxin. Disulfides 54-63 thioredoxin Homo sapiens 139-150 7834639-1 1995 Thioredoxin (TRX), a disulfide-reducing intracellular dithiol enzyme, is synthesized by both normal liver cells and the hepatocarcinoma cell line HepG2. Disulfides 21-30 thioredoxin Homo sapiens 0-11 7834639-1 1995 Thioredoxin (TRX), a disulfide-reducing intracellular dithiol enzyme, is synthesized by both normal liver cells and the hepatocarcinoma cell line HepG2. Disulfides 21-30 thioredoxin Homo sapiens 13-16 1510657-3 1992 Furthermore, recombinant ADF/human thioredoxin was found to have protein-refolding activity for scrambled (mispaired disulfide-containing) RNase A. Disulfides 117-126 thioredoxin Homo sapiens 25-28 7929311-4 1994 Thioredoxin, in conjunction with thioredoxin reductase and NADPH, allows direct measurements of the rate and extent of disulfide bond reduction. Disulfides 119-128 thioredoxin Homo sapiens 0-11 7929311-4 1994 Thioredoxin, in conjunction with thioredoxin reductase and NADPH, allows direct measurements of the rate and extent of disulfide bond reduction. Disulfides 119-128 thioredoxin Homo sapiens 33-44 7929311-6 1994 Moreover, those disulfide bonds that were resistant to reduction by thioredoxin in the presence of Ca2+, but were readily reduced in the absence of the metal ion, were located in the N-terminal EGF-like module and in the Gla module, whereas disulfide bonds in the C-terminal EGF-like module appeared to be equally accessible whether Ca2+ was present or not. Disulfides 16-25 thioredoxin Homo sapiens 68-79 7929311-6 1994 Moreover, those disulfide bonds that were resistant to reduction by thioredoxin in the presence of Ca2+, but were readily reduced in the absence of the metal ion, were located in the N-terminal EGF-like module and in the Gla module, whereas disulfide bonds in the C-terminal EGF-like module appeared to be equally accessible whether Ca2+ was present or not. Disulfides 241-250 thioredoxin Homo sapiens 68-79 8395501-0 1993 Direct identification of the primary nucleophile of thioredoxin f. Thioredoxin, by virtue of the proximal active-site sulfhydryls (Trp-Cys-Gly-Pro-Cys), catalyzes thiol-disulfide exchange with specific target enzymes. Disulfides 169-178 thioredoxin Homo sapiens 52-63 8395501-0 1993 Direct identification of the primary nucleophile of thioredoxin f. Thioredoxin, by virtue of the proximal active-site sulfhydryls (Trp-Cys-Gly-Pro-Cys), catalyzes thiol-disulfide exchange with specific target enzymes. Disulfides 169-178 thioredoxin Homo sapiens 67-78 8395501-6 1993 Therefore, in the normal thioredoxin-catalyzed reduction pathway, Cys-46 is the nucleophile required to attack the disulfide of the substrate and Cys-49 serves to cleave the mixed disulfide intermediate, thus allowing for the release of oxidized thioredoxin and the reduced target enzyme. Disulfides 115-124 thioredoxin Homo sapiens 25-36 8344427-4 1993 Thioredoxin, which has higher reducing activity of protein disulfides than PDI, catalyzed the reduction with lower efficiency. Disulfides 59-69 thioredoxin Homo sapiens 0-11 8338847-2 1993 Thereby, as is known from comparing the three-dimensional (3D) structures of thioredoxin and glutaredoxin in the reduced and oxidized state, reduction of the disulfide bond is accompanied by minimal perturbation of the backbone folding of the active sites. Disulfides 158-167 thioredoxin Homo sapiens 77-88 8338847-3 1993 In order to estimate the sequence-dependent intrinsic free energy of formation of the active-site disulfide loops in oxidoreductases, synthetic fragments corresponding to the sequences 31-38, 10-17, 134-141, and 34-41 of thioredoxin, glutaredoxin, thioredoxin reductase, and protein disulfide isomerase (PDI), respectively, were analyzed for their tendency to form 14-membered rings. Disulfides 98-107 thioredoxin Homo sapiens 221-232 1332947-1 1992 Thioredoxin, despite its function as an intracellular disulfide reducing enzyme and its lack of a signal sequence, has been found to play some roles extracellularly. Disulfides 54-63 thioredoxin Homo sapiens 0-11 7893813-4 1994 The tetrapeptides found in the redox site of thioredoxin were optimized to conformers in which the two sulfur atoms were in van der Waals contact, so that a disulfide bond may be formed during the function. Disulfides 157-166 thioredoxin Homo sapiens 45-56 8395501-6 1993 Therefore, in the normal thioredoxin-catalyzed reduction pathway, Cys-46 is the nucleophile required to attack the disulfide of the substrate and Cys-49 serves to cleave the mixed disulfide intermediate, thus allowing for the release of oxidized thioredoxin and the reduced target enzyme. Disulfides 180-189 thioredoxin Homo sapiens 25-36 1510657-3 1992 Furthermore, recombinant ADF/human thioredoxin was found to have protein-refolding activity for scrambled (mispaired disulfide-containing) RNase A. Disulfides 117-126 thioredoxin Homo sapiens 35-46 1932345-1 1991 Thioredoxin, a disulfide-containing protein having a highly conservative structure, is present in all types of organisms that are phylogenetically distant from one another. Disulfides 15-24 thioredoxin Homo sapiens 0-11 1318718-4 1992 The reaction of PQQ with reduced thioredoxin brings about the oxidation of two thiol groups of the oxireductase, whereas the enzyme phosphoribulose kinase is inactivated at 25 degrees C. The oxidized disulfide bond of phosphoribulose kinase is reduced by dithiothreitol and the enzyme recovers catalytic activity. Disulfides 200-209 thioredoxin Homo sapiens 33-44 1329444-5 1992 On the other hand, thioredoxin contains a redox active disulfide and has a reducing activity in the presence of thioredoxin reductase and NADPH. Disulfides 55-64 thioredoxin Homo sapiens 19-30 1778302-2 1991 This assay reflects the recently recognized ability of thioredoxin to catalyze disulfide bond formation in proteins. Disulfides 79-88 thioredoxin Homo sapiens 55-66 2188973-3 1990 Protein disulfide-isomerase contains two redox-active disulfides/molecule which were reduced by NADPH and calf thioredoxin reductase (Km approximately 35 microM). Disulfides 54-64 thioredoxin Homo sapiens 111-122 2172979-4 1990 cDNA cloning of ADF demonstrated high homology with the prokaryotic disulfide reducing enzyme thioredoxin. Disulfides 68-77 thioredoxin Homo sapiens 16-19 2172979-4 1990 cDNA cloning of ADF demonstrated high homology with the prokaryotic disulfide reducing enzyme thioredoxin. Disulfides 68-77 thioredoxin Homo sapiens 94-105 2188973-4 1990 The isomerase was a poor substrate for NADPH and Escherichia coli thioredoxin reductase, but the addition of E. coli thioredoxin resulted in rapid reduction of two disulfides/molecule. Disulfides 164-174 thioredoxin Homo sapiens 66-77 2188973-4 1990 The isomerase was a poor substrate for NADPH and Escherichia coli thioredoxin reductase, but the addition of E. coli thioredoxin resulted in rapid reduction of two disulfides/molecule. Disulfides 164-174 thioredoxin Homo sapiens 117-128 2188973-6 1990 Fluorescence measurements demonstrated that thioredoxin--(SH)2 reduced the disulfides of the isomerase and allowed the kinetics of the reaction to be followed; the reaction was also catalyzed by calf thioredoxin reductase. Disulfides 75-85 thioredoxin Homo sapiens 200-211 2188973-7 1990 Equilibrium measurements showed that the apparent redox potential of the active site disulfide/dithiols of the thioredoxin domains of protein disulfide-isomerase was about 30 mV higher than the disulfide/dithiol of E. coli thioredoxin. Disulfides 85-94 thioredoxin Homo sapiens 111-122 2188973-7 1990 Equilibrium measurements showed that the apparent redox potential of the active site disulfide/dithiols of the thioredoxin domains of protein disulfide-isomerase was about 30 mV higher than the disulfide/dithiol of E. coli thioredoxin. Disulfides 85-94 thioredoxin Homo sapiens 223-234 2188973-7 1990 Equilibrium measurements showed that the apparent redox potential of the active site disulfide/dithiols of the thioredoxin domains of protein disulfide-isomerase was about 30 mV higher than the disulfide/dithiol of E. coli thioredoxin. Disulfides 142-151 thioredoxin Homo sapiens 111-122 2188973-7 1990 Equilibrium measurements showed that the apparent redox potential of the active site disulfide/dithiols of the thioredoxin domains of protein disulfide-isomerase was about 30 mV higher than the disulfide/dithiol of E. coli thioredoxin. Disulfides 142-151 thioredoxin Homo sapiens 223-234 34455077-3 2021 The thioredoxin system, comprised of TrxR Trx and NADPH, exerts its activities via a disulfide-dithiol exchange reaction. Disulfides 85-94 thioredoxin Homo sapiens 4-15 2162313-3 1990 Thioredoxin reductase (TR) is a widely distributed flavoenzyme that provides reduced thioredoxin, a dithiol hydrogen donor for protein disulfide reduction and for the reduction of ribonucleotides to deoxyribonucleotides, the first unique step of DNA synthesis. Disulfides 135-144 thioredoxin Homo sapiens 85-96 25880503-8 2015 While thioredoxin and glutaredoxin primarily act as antioxidants by reducing protein disulfides and mixed disulfide, another member of the superfamily, protein disulfide isomerase (PDI), can act as an oxidant by forming intrachain disulfide bonds that contribute to proper protein folding. Disulfides 85-95 thioredoxin Homo sapiens 6-17 25880503-8 2015 While thioredoxin and glutaredoxin primarily act as antioxidants by reducing protein disulfides and mixed disulfide, another member of the superfamily, protein disulfide isomerase (PDI), can act as an oxidant by forming intrachain disulfide bonds that contribute to proper protein folding. Disulfides 85-94 thioredoxin Homo sapiens 6-17 25880503-8 2015 While thioredoxin and glutaredoxin primarily act as antioxidants by reducing protein disulfides and mixed disulfide, another member of the superfamily, protein disulfide isomerase (PDI), can act as an oxidant by forming intrachain disulfide bonds that contribute to proper protein folding. Disulfides 106-115 thioredoxin Homo sapiens 6-17 34455077-3 2021 The thioredoxin system, comprised of TrxR Trx and NADPH, exerts its activities via a disulfide-dithiol exchange reaction. Disulfides 85-94 thioredoxin Homo sapiens 42-45 34575960-11 2021 TRX can remove NO-like glutathione and break down the disulfide bridge. Disulfides 54-63 thioredoxin Homo sapiens 0-3 35340291-5 2022 Specialized chaperones with thioredoxin (Trx) domains catalyze the redox functions necessary for breaking incorrect and forming correct disulfide bonds in proteins. Disulfides 136-145 thioredoxin Homo sapiens 28-39 35340291-5 2022 Specialized chaperones with thioredoxin (Trx) domains catalyze the redox functions necessary for breaking incorrect and forming correct disulfide bonds in proteins. Disulfides 136-145 thioredoxin Homo sapiens 41-44 35340291-8 2022 Activity based crosslinkers that rely on the nucleophilic cysteines on Trx domains and the disulfide bond forming cysteines on clients provide an easily scalable method to trap and identify the substrates of Trx-domain containing chaperones. Disulfides 91-100 thioredoxin Homo sapiens 208-211 35340291-9 2022 The cell permeable crosslinker divinyl sulfone (DVSF) is active only in the presence of nucleophilic cysteines in proteins and, therefore, traps Trx domains with their substrates, as they form mixed disulfide bonds during the course of their catalytic activity. Disulfides 199-208 thioredoxin Homo sapiens 145-148 34061528-0 2021 Selective, Modular Probes for Thioredoxins Enabled by Rational Tuning of a Unique Disulfide Structure Motif. Disulfides 82-91 thioredoxin Homo sapiens 30-42 34061528-8 2021 This design process delivered the first disulfide probes with excellent stability to monothiols yet high selectivity for the key redox-active protein effector, thioredoxin. Disulfides 40-49 thioredoxin Homo sapiens 160-171 34061528-9 2021 We anticipate that further applications of these novel disulfide triggers will deliver unique probes targeting cellular thioredoxins. Disulfides 55-64 thioredoxin Homo sapiens 120-132 35179864-3 2022 Intracellular antioxidant proteins, such as thioredoxin 1 (Trx1) and peroxiredoxin 1 (Prx1), could regulate redox homeostasis through thiol-disulfide exchange. Disulfides 140-149 thioredoxin Homo sapiens 44-57 35179864-3 2022 Intracellular antioxidant proteins, such as thioredoxin 1 (Trx1) and peroxiredoxin 1 (Prx1), could regulate redox homeostasis through thiol-disulfide exchange. Disulfides 140-149 thioredoxin Homo sapiens 59-63 35204825-9 2022 Redox sensitivity of p53 functions is supported by (i) thioredoxin-dependent reduction of p53 disulfides, (ii) inhibition of the thioredoxin-dependent deoxyribonucleotide synthesis by p53 binding to RRM2B and (iii) changed intracellular distribution of p53 through its oxidation by CHCHD4 in the mitochondrial intermembrane space. Disulfides 94-104 thioredoxin Homo sapiens 55-66 35204259-5 2022 Here we investigated whether Fast-TRFS, a disulfide-containing fluorescent probe utilized in analysis of mammalian thioredoxin reductase, could be used to detect cellular disulfide reducibility in bacteria. Disulfides 171-180 thioredoxin Homo sapiens 115-126 35204259-9 2022 The Trx system was shown to be the predominant disulfide reductase for fast disulfide reduction rather than the Grx system. Disulfides 76-85 thioredoxin Homo sapiens 4-7 35204259-11 2022 It also indicated that cellular disulfide reduction could be classified into fast and slow reaction, which are predominantly catalyzed by E. coli Trx and Grx system, respectively. Disulfides 32-41 thioredoxin Homo sapiens 146-149