-
1
-
-
0026422435
-
Convergent evolution of similar function in two structurally divergent enzymes
-
Kuriyan J, Krishna TSR, Wong L, Guenther B, Pahler A, Williams CHJ, Model P (1991) Convergent evolution of similar function in two structurally divergent enzymes. Nature 352:172–174
-
(1991)
Nature
, vol.352
, pp. 172-174
-
-
Kuriyan, J.1
Krishna, T.S.R.2
Wong, L.3
Guenther, B.4
Pahler, A.5
Williams, C.H.J.6
Model, P.7
-
2
-
-
0000876731
-
Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and mercuric ion reductase - a family of flavoenzyme transhydrogenases
-
Boca Raton, FL
-
Williams CH Jr (1992) Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and mercuric ion reductase - a family of flavoenzyme transhydrogenases. In: M€uller F (ed) Chemistry and biochemistry of flavoen-zymes, vol 3. CRC Press, Boca Raton, FL, pp 121–211
-
(1992)
M€uller F (Ed) Chemistry and Biochemistry of Flavoen-Zymes, Vol 3. CRC Press
, pp. 121-211
-
-
Williams, C.H.1
-
3
-
-
0030887844
-
The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli
-
Arscott LD, Gromer S, Schirmer RH, Becker K, Williams CH Jr (1997) The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli. Proc Natl Acad Sci U S A 94:3621–3626
-
(1997)
Proc Natl Acad Sci U S A
, vol.94
, pp. 3621-3626
-
-
Arscott, L.D.1
Gromer, S.2
Schirmer, R.H.3
Becker, K.4
Williams, C.H.5
-
4
-
-
0033781942
-
Thioredoxin reductase two modes of catalysis have evolved
-
Williams CH, Arscott LD, Muller S, Lennon BW, Ludwig ML, Wang PF, Veine DM, Becker K, Schirmer RH (2000) Thioredoxin reductase two modes of catalysis have evolved. Eur J Biochem 267:6110–6117
-
(2000)
Eur J Biochem
, vol.267
, pp. 6110-6117
-
-
Williams, C.H.1
Arscott, L.D.2
Muller, S.3
Lennon, B.W.4
Ludwig, M.L.5
Wang, P.F.6
Veine, D.M.7
Becker, K.8
Schirmer, R.H.9
-
5
-
-
0242300123
-
Active sites of thioredoxin reductases—Why selenoproteins?
-
Gromer S, Johansson L, Bauer H, Arscott LD, Rauch S, Ballou DP, Williams CH Jr, Schirmer RH, Arnér ESJ (2003) Active sites of thioredoxin reductases—Why selenoproteins? Proc Natl Acad Sci U S A 100:12618–12623
-
(2003)
Proc Natl Acad Sci U S A
, vol.100
, pp. 12618-12623
-
-
Gromer, S.1
Johansson, L.2
Bauer, H.3
Arscott, L.D.4
Rauch, S.5
Ballou, D.P.6
Williams, C.H.7
Schirmer, R.H.8
Arnér, E.S.J.9
-
6
-
-
0032502720
-
Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue
-
Zhong L, Arnér ESJ, Ljung J, Åslund F, Holmgren A (1998) Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue. J Biol Chem 273:8581–8591
-
(1998)
J Biol Chem
, vol.273
, pp. 8581-8591
-
-
Zhong, L.1
Arnér, E.S.J.2
Ljung, J.3
Åslund, F.4
Holmgren, A.5
-
7
-
-
0033775891
-
Physiological functions of thioredoxin and thioredoxin reductase
-
Arner ES, Holmgren A (2000) Physiological functions of thioredoxin and thioredoxin reductase. Eur J Biochem 267:6102–6109
-
(2000)
Eur J Biochem
, vol.267
, pp. 6102-6109
-
-
Arner, E.S.1
Holmgren, A.2
-
8
-
-
0034705133
-
Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence
-
Zhong L, Arnér ESJ, Holmgren A (2000) Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence. Proc Natl Acad Sci U S A 97:5854–5859
-
(2000)
Proc Natl Acad Sci U S A
, vol.97
, pp. 5854-5859
-
-
Zhong, L.1
Arnér, E.S.J.2
Holmgren, A.3
-
9
-
-
0031773474
-
Preparation and assay of mammalian thioredoxin and thioredoxin reductase
-
Arnér ESJ, Zhong L, Holmgren A (1999) Preparation and assay of mammalian thioredoxin and thioredoxin reductase. Methods Enzymol 300:226–239
-
(1999)
Methods Enzymol
, vol.300
, pp. 226-239
-
-
Arnér, E.S.J.1
Zhong, L.2
Holmgren, A.3
-
10
-
-
0006895581
-
Measurement of thioredoxin and thioredoxin reductase
-
Maines M, Costa L, Reed D, Sassa S, Wiley, New York
-
Arnér ESJ, Holmgren A (2000) Measurement of thioredoxin and thioredoxin reductase. In: Maines M, Costa L, Reed D, Sassa S (eds) Current protocols in toxicology. Wiley, New York, pp 7.4.1–7.4.14
-
(2000)
Current Protocols in Toxicology
, pp. 1-7
-
-
Arnér, E.S.J.1
Holmgren, A.2
-
11
-
-
67349120863
-
Focus on mammalian thioredoxin reductases – important selenoproteins with versatile functions
-
Arnér ESJ (2009) Focus on mammalian thioredoxin reductases – important selenoproteins with versatile functions. Biochim Biophys Acta 1790:495–526
-
(2009)
Biochim Biophys Acta
, vol.1790
, pp. 495-526
-
-
Arnér, E.S.J.1
-
12
-
-
0017653811
-
Bovine thioredoxin system. Purification of thioredoxin reductase from calf liver and thymus and studies of its function in disulfide reduction
-
Holmgren A (1977) Bovine thioredoxin system. Purification of thioredoxin reductase from calf liver and thymus and studies of its function in disulfide reduction. J Biol Chem 252:4600–4606
-
(1977)
J Biol Chem
, vol.252
, pp. 4600-4606
-
-
Holmgren, A.1
-
13
-
-
0018728098
-
Reduction of disulfides by thioredoxin. Exceptional reactivity of insulin and suggested functions of thioredoxin in mechanism of hormone action
-
Holmgren A (1979) Reduction of disulfides by thioredoxin. Exceptional reactivity of insulin and suggested functions of thioredoxin in mechanism of hormone action. J Biol Chem 254:9113–9119
-
(1979)
J Biol Chem
, vol.254
, pp. 9113-9119
-
-
Holmgren, A.1
-
14
-
-
0018723651
-
Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
-
Holmgren A (1979) Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J Biol Chem 254:9627–9632
-
(1979)
J Biol Chem
, vol.254
, pp. 9627-9632
-
-
Holmgren, A.1
-
15
-
-
0036119837
-
Human placenta thioredoxin reductase: Preparation and inhibitor studies
-
Gromer S, Merkle H, Schirmer RH, Becker K (2002) Human placenta thioredoxin reductase: preparation and inhibitor studies. Methods Enzymol 347:382–394
-
(2002)
Methods Enzymol
, vol.347
, pp. 382-394
-
-
Gromer, S.1
Merkle, H.2
Schirmer, R.H.3
Becker, K.4
-
16
-
-
0032493647
-
Human placenta thioredoxin reductase: Isolation of the selenoen-zyme, steady state kinetics, and inhibition by therapeutic gold compounds
-
Gromer S, Arscott LD, Williams CH, Schirmer RH, Becker K (1998) Human placenta thioredoxin reductase: isolation of the selenoen-zyme, steady state kinetics, and inhibition by therapeutic gold compounds. J Biol Chem 273:20096–20101
-
(1998)
J Biol Chem
, vol.273
, pp. 20096-20101
-
-
Gromer, S.1
Arscott, L.D.2
Williams, C.H.3
Schirmer, R.H.4
Becker, K.5
-
17
-
-
0036119737
-
High-throughput 96-well microplate assays for determining specific activities of glutathione peroxidase and thioredoxin reductase
-
Smith AD, Levander OA (2002) High-throughput 96-well microplate assays for determining specific activities of glutathione peroxidase and thioredoxin reductase. Methods Enzymol 347:113–121
-
(2002)
Methods Enzymol
, vol.347
, pp. 113-121
-
-
Smith, A.D.1
Levander, O.A.2
-
18
-
-
0242300123
-
Active sites of thioredoxin reductases: Why selenoproteins?
-
Gromer S, Johansson L, Bauer H, Arscott LD, Rauch S, Ballou DP, Williams CH Jr, Schirmer RH, Arner ES (2003) Active sites of thioredoxin reductases: why selenoproteins? Proc Natl Acad Sci U S A 100:12618–12623
-
(2003)
Proc Natl Acad Sci U S A
, vol.100
, pp. 12618-12623
-
-
Gromer, S.1
Johansson, L.2
Bauer, H.3
Arscott, L.D.4
Rauch, S.5
Ballou, D.P.6
Williams, C.H.7
Schirmer, R.H.8
Arner, E.S.9
-
19
-
-
84900498924
-
Thioredoxin-related protein of 14 kDa is an efficient L-cystine reductase and S-denitrosylase
-
Pader I, Sengupta R, Cebula M, Xu J, Lund-berg JO, Holmgren A, Johansson K, Arner ES (2014) Thioredoxin-related protein of 14 kDa is an efficient L-cystine reductase and S-denitrosylase. Proc Natl Acad Sci U S A 111:6964–6969
-
(2014)
Proc Natl Acad Sci U S A
, vol.111
, pp. 6964-6969
-
-
Pader, I.1
Sengupta, R.2
Cebula, M.3
Xu, J.4
Lund-Berg, J.O.5
Holmgren, A.6
Johansson, K.7
Arner, E.S.8
-
20
-
-
84892924777
-
Activity assays of mammalian thioredoxin and thioredoxin reductase: Fluorescent disulfide substrates, mechanisms, and use with tissue samples
-
Montano SJ, Lu J, Gustafsson TN, Holmgren A (2014) Activity assays of mammalian thioredoxin and thioredoxin reductase: fluorescent disulfide substrates, mechanisms, and use with tissue samples. Anal Biochem 449:139–146
-
(2014)
Anal Biochem
, vol.449
, pp. 139-146
-
-
Montano, S.J.1
Lu, J.2
Gustafsson, T.N.3
Holmgren, A.4
-
21
-
-
84990020613
-
A fast response and red emission probe for mammalian thioredoxin reductase
-
Ma H, Zhang J, Zhang Z, Liu Y, Fang J (2016) A fast response and red emission probe for mammalian thioredoxin reductase. Chem Commun (Camb) 52:12060–12063
-
(2016)
Chem Commun (Camb)
, vol.52
, pp. 12060-12063
-
-
Ma, H.1
Zhang, J.2
Zhang, Z.3
Liu, Y.4
Fang, J.5
-
22
-
-
84957580289
-
A small molecule probe reveals declined mitochondrial thioredoxin reductase activity in a Parkinson’s disease model
-
Liu Y, Ma H, Zhang L, Cui Y, Liu X, Fang J (2016) A small molecule probe reveals declined mitochondrial thioredoxin reductase activity in a Parkinson’s disease model. Chem Commun (Camb) 52:2296–2299
-
(2016)
Chem Commun (Camb)
, vol.52
, pp. 2296-2299
-
-
Liu, Y.1
Ma, H.2
Zhang, L.3
Cui, Y.4
Liu, X.5
Fang, J.6
-
23
-
-
84921523909
-
Selective selenol fluorescent probes: Design, synthesis, structural determinants, and biological applications
-
Zhang B, Ge C, Yao J, Liu Y, Xie H, Fang J (2015) Selective selenol fluorescent probes: design, synthesis, structural determinants, and biological applications. J Am Chem Soc 137:757–769
-
(2015)
J am Chem Soc
, vol.137
, pp. 757-769
-
-
Zhang, B.1
Ge, C.2
Yao, J.3
Liu, Y.4
Xie, H.5
Fang, J.6
-
24
-
-
84892164605
-
Highly selective off-on fluorescent probe for imaging thioredoxin reductase in living cells
-
Zhang L, Duan D, Liu Y, Ge C, Cui X, Sun J, Fang J (2014) Highly selective off-on fluorescent probe for imaging thioredoxin reductase in living cells. J Am Chem Soc 136:226–233
-
(2014)
J am Chem Soc
, vol.136
, pp. 226-233
-
-
Zhang, L.1
Duan, D.2
Liu, Y.3
Ge, C.4
Cui, X.5
Sun, J.6
Fang, J.7
-
25
-
-
79951682393
-
Substrate and inhibitor specificities differ between human cytosolic and mitochondrial thioredoxin reductases: Implications for development of specific inhibitors
-
Rackham O, Shearwood AM, Thyer R, McNamara E, Davies SM, Callus BA, Miranda-Vizuete A, Berners-Price SJ, Cheng Q, Arnér ES, Filipovska A (2011) Substrate and inhibitor specificities differ between human cytosolic and mitochondrial thioredoxin reductases: implications for development of specific inhibitors. Free Radic Biol Med 50:689–699
-
(2011)
Free Radic Biol Med
, vol.50
, pp. 689-699
-
-
Rackham, O.1
Shearwood, A.M.2
Thyer, R.3
McNamara, E.4
Davies, S.M.5
Callus, B.A.6
Miranda-Vizuete, A.7
Berners-Price, S.J.8
Cheng, Q.9
Arnér, E.S.10
Filipovska, A.11
-
26
-
-
84959322213
-
Details in the catalytic mechanism of mammalian thioredoxin reductase 1 revealed using point mutations and juglone-coupled enzyme activities
-
Xu J, Cheng Q, Arner ES (2016) Details in the catalytic mechanism of mammalian thioredoxin reductase 1 revealed using point mutations and juglone-coupled enzyme activities. Free Radic Biol Med 94:110–120
-
(2016)
Free Radic Biol Med
, vol.94
, pp. 110-120
-
-
Xu, J.1
Cheng, Q.2
Arner, E.S.3
-
27
-
-
0035865881
-
2- and 3-substituted 1,4-naphthoquinone derivatives as subversive substrates of trypanothione reductase and lipoamide dehydrogenase from Trypanosoma cruzi: Synthesis and correlation between redox cycling activities and in vitro cytotoxicity
-
Salmon-Chemin L, Buisine E, Yardley V, Kohler S, Debreu MA, Landry V, Sergheraert C, Croft SL, Krauth-Siegel RL, Davioud-Charvet E (2001) 2- and 3-substituted 1,4-naphthoquinone derivatives as subversive substrates of trypanothione reductase and lipoamide dehydrogenase from Trypanosoma cruzi: synthesis and correlation between redox cycling activities and in vitro cytotoxicity. J Med Chem 44:548–565
-
(2001)
J Med Chem
, vol.44
, pp. 548-565
-
-
Salmon-Chemin, L.1
Buisine, E.2
Yardley, V.3
Kohler, S.4
Debreu, M.A.5
Landry, V.6
Sergheraert, C.7
Croft, S.L.8
Krauth-Siegel, R.L.9
Davioud-Charvet, E.10
-
28
-
-
44849125526
-
Cell death by SecTRAPs: Thioredoxin reductase as a prooxidant killer of cells
-
Anestal K, Prast-Nielsen S, Cenas N, Arner ES (2008) Cell death by SecTRAPs: thioredoxin reductase as a prooxidant killer of cells. PLoS One 3:e1846
-
(2008)
Plos One
, vol.3
-
-
Anestal, K.1
Prast-Nielsen, S.2
Cenas, N.3
Arner, E.S.4
-
29
-
-
1642535437
-
Interactions of quinones with thioredoxin reductase: A challenge to the antioxidant role of the mammalian selenoprotein
-
Cenas N, Nivinskas H, Anusevicius Z, Sarlaus-kas J, Lederer F, Arner ES (2004) Interactions of quinones with thioredoxin reductase: a challenge to the antioxidant role of the mammalian selenoprotein. J Biol Chem 279:2583–2592
-
(2004)
J Biol Chem
, vol.279
, pp. 2583-2592
-
-
Cenas, N.1
Nivinskas, H.2
Anusevicius, Z.3
Sarlaus-Kas, J.4
Lederer, F.5
Arner, E.S.6
-
30
-
-
84893484616
-
Why is mammalian thioredoxin reductase 1 so dependent upon the use of selenium?
-
Lothrop AP, Snider GW, Ruggles EL, Hondal RJ (2014) Why is mammalian thioredoxin reductase 1 so dependent upon the use of selenium? Biochemistry 53:554–565
-
(2014)
Biochemistry
, vol.53
, pp. 554-565
-
-
Lothrop, A.P.1
Snider, G.W.2
Ruggles, E.L.3
Hondal, R.J.4
-
31
-
-
84976615559
-
Thioredoxin reductase 1 suppresses adipocyte differentiation and insulin responsiveness
-
Peng X, Gimenez-Cassina A, Petrus P, Conrad M, Ryden M, Arner ES (2016) Thioredoxin reductase 1 suppresses adipocyte differentiation and insulin responsiveness. Sci Rep 6:28080
-
(2016)
Sci Rep
, vol.6
-
-
Peng, X.1
Gimenez-Cassina, A.2
Petrus, P.3
Conrad, M.4
Ryden, M.5
Arner, E.S.6
-
32
-
-
0027443868
-
Mutagenesis of structural half-cystine residues in human thioredoxin and effects on the regulation of activity by seleno-diglutathione
-
Ren X, Bjornstedt M, Shen B, Ericson ML, Holmgren A (1993) Mutagenesis of structural half-cystine residues in human thioredoxin and effects on the regulation of activity by seleno-diglutathione. Biochemistry 32:9701–9708
-
(1993)
Biochemistry
, vol.32
, pp. 9701-9708
-
-
Ren, X.1
Bjornstedt, M.2
Shen, B.3
Ericson, M.L.4
Holmgren, A.5
|