-
1
-
-
33749986298
-
Free radicals and antioxidants in normal physiological functions and human disease
-
DOI 10.1016/j.biocel.2006.07.001, PII S1357272506002196
-
Valko M, Leibfritz D, Moncol J, Cronin MT, Mazur M, et al. (2007) Free radicals and antioxidants in normal physiological functions and human disease. Int J Biochem Cell Biol 39: 44-84. (Pubitemid 44566469)
-
(2007)
International Journal of Biochemistry and Cell Biology
, vol.39
, Issue.1
, pp. 44-84
-
-
Valko, M.1
Leibfritz, D.2
Moncol, J.3
Cronin, M.T.D.4
Mazur, M.5
Telser, J.6
-
2
-
-
31044452359
-
Generating disulfides enzymatically: Reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p
-
DOI 10.1073/pnas.0506448103
-
Gross E, Sevier CS, Heldman N, Vitu E, Bentzur M, et al. (2006) Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p. Proc Natl Acad Sci U S A 103: 299-304. (Pubitemid 43122395)
-
(2006)
Proceedings of the National Academy of Sciences of the United States of America
, vol.103
, Issue.2
, pp. 299-304
-
-
Gross, E.1
Sevier, C.S.2
Heldman, N.3
Vitu, E.4
Bentzur, M.5
Kaiser, C.A.6
Thorpe, C.7
Fass, D.8
-
3
-
-
58649096169
-
Reconstitution of human Ero1-Lalpha/protein-disulfide isomerase oxidative folding pathway in vitro. Position-dependent differences in role between the a and a′ domains of protein-disulfide isomerase
-
Wang L, Li SJ, Sidhu A, Zhu L, Liang Y, et al. (2009) Reconstitution of human Ero1-Lalpha/protein-disulfide isomerase oxidative folding pathway in vitro. Position-dependent differences in role between the a and a′ domains of protein-disulfide isomerase. J Biol Chem 284: 199-206.
-
(2009)
J Biol Chem
, vol.284
, pp. 199-206
-
-
Wang, L.1
Li, S.J.2
Sidhu, A.3
Zhu, L.4
Liang, Y.5
-
4
-
-
0242668686
-
Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
-
DOI 10.1126/science.1080405
-
Wood ZA, Poole LB, Karplus PA (2003) Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300: 650-653. (Pubitemid 36520591)
-
(2003)
Science
, vol.300
, Issue.5619
, pp. 650-653
-
-
Wood, Z.A.1
Poole, L.B.2
Karplus, P.A.3
-
5
-
-
64149085448
-
Typical 2-Cys peroxiredoxins-structures, mechanisms and functions
-
Hall A, Karplus PA, Poole LB (2009) Typical 2-Cys peroxiredoxins- structures, mechanisms and functions. FEBS J 276: 2469-2477.
-
(2009)
FEBS J
, vol.276
, pp. 2469-2477
-
-
Hall, A.1
Karplus, P.A.2
Poole, L.B.3
-
6
-
-
41649110016
-
Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells
-
DOI 10.1042/BJ20071428
-
Tavender TJ, Sheppard AM, Bulleid NJ (2008) Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells. Biochem J 411: 191-199. (Pubitemid 351482361)
-
(2008)
Biochemical Journal
, vol.411
, Issue.1
, pp. 191-199
-
-
Tavender, T.J.1
Sheppard, A.M.2
Bulleid, N.J.3
-
7
-
-
77955359156
-
Peroxiredoxin IV protects cells from oxidative stress by removing H2O2 produced during disulphide formation
-
Tavender TJ, Bulleid NJ (2010) Peroxiredoxin IV protects cells from oxidative stress by removing H2O2 produced during disulphide formation. J Cell Sci 123: 2672-2679.
-
(2010)
J Cell Sci
, vol.123
, pp. 2672-2679
-
-
Tavender, T.J.1
Bulleid, N.J.2
-
8
-
-
78650270477
-
Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum
-
Tavender TJ, Springate JJ, Bulleid NJ (2010) Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum. EMBO J 29: 4185-4197.
-
(2010)
EMBO J
, vol.29
, pp. 4185-4197
-
-
Tavender, T.J.1
Springate, J.J.2
Bulleid, N.J.3
-
9
-
-
0031034725
-
Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2
-
DOI 10.1093/emboj/16.3.651
-
Yao Y, Zhou Y, Wang C (1997) Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2. EMBO J 16: 651-658. (Pubitemid 27067793)
-
(1997)
EMBO Journal
, vol.16
, Issue.3
, pp. 651-658
-
-
Yao, Y.1
Zhou, Y.-C.2
Wang, C.-C.3
-
10
-
-
0036198797
-
Protein disulfide isomerases exploit synergy between catalytic and specific binding domains
-
DOI 10.1093/embo-reports/kvf035
-
Freedman RB, Klappa P, Ruddock LW (2002) Protein disulfide isomerases exploit synergy between catalytic and specific binding domains. EMBO Rep 3: 136-140. (Pubitemid 34213490)
-
(2002)
EMBO Reports
, vol.3
, Issue.2
, pp. 136-140
-
-
Freedman, R.B.1
Klappa, P.2
Ruddock, L.W.3
-
11
-
-
78649918283
-
Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin
-
Zito E, Melo EP, Yang Y, Wahlander A, Neubert TA, et al. (2010) Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin. Mol Cell 40: 787-797.
-
(2010)
Mol Cell
, vol.40
, pp. 787-797
-
-
Zito, E.1
Melo, E.P.2
Yang, Y.3
Wahlander, A.4
Neubert, T.A.5
-
12
-
-
84867395326
-
Endoplasmic reticulum thiol oxidase deficiency leads to ascorbic acid depletion and noncanonical scurvy in mice
-
Zito E, Hansen HG, Yeo GS, Fujii J, Ron D (2012) Endoplasmic reticulum thiol oxidase deficiency leads to ascorbic acid depletion and noncanonical scurvy in mice. Mol Cell 48: 39-51.
-
(2012)
Mol Cell
, vol.48
, pp. 39-51
-
-
Zito, E.1
Hansen, H.G.2
Yeo, G.S.3
Fujii, J.4
Ron, D.5
-
13
-
-
0026062381
-
Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: Dependence of the rate on the composition of the redox buffer
-
Lyles MM, Gilbert HF (1991) Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer. Biochemistry 30: 613-619.
-
(1991)
Biochemistry
, vol.30
, pp. 613-619
-
-
Lyles, M.M.1
Gilbert, H.F.2
-
14
-
-
84055178426
-
Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4
-
Wang X, Wang L, Wang X, Sun F, Wang CC (2012) Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4. Biochem J 441: 113-118.
-
(2012)
Biochem J
, vol.441
, pp. 113-118
-
-
Wang, X.1
Wang, L.2
Wang, X.3
Sun, F.4
Wang, C.C.5
-
16
-
-
0025331418
-
Protein disulfide-isomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity
-
Lundstrom J, Holmgren A (1990) Protein disulfide-isomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity. J Biol Chem 265: 9114-9120.
-
(1990)
J Biol Chem
, vol.265
, pp. 9114-9120
-
-
Lundstrom, J.1
Holmgren, A.2
-
17
-
-
84862907646
-
Human protein-disulfide isomerase is a redox-regulated chaperone activated by oxidation of domain a′
-
Wang C, Yu J, Huo L, Wang L, Feng W, et al. (2012) Human protein-disulfide isomerase is a redox-regulated chaperone activated by oxidation of domain a′. J Biol Chem 287: 1139-1149.
-
(2012)
J Biol Chem
, vol.287
, pp. 1139-1149
-
-
Wang, C.1
Yu, J.2
Huo, L.3
Wang, L.4
Feng, W.5
-
18
-
-
33750002010
-
Redox Regulation Facilitates Optimal Peptide Selection by MHC Class I during Antigen Processing
-
DOI 10.1016/j.cell.2006.08.041, PII S0092867406012190
-
Park B, Lee S, Kim E, Cho K, Riddell SR, et al. (2006) Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing. Cell 127: 369-382. (Pubitemid 44572373)
-
(2006)
Cell
, vol.127
, Issue.2
, pp. 369-382
-
-
Park, B.1
Lee, S.2
Kim, E.3
Cho, K.4
Riddell, S.R.5
Cho, S.6
Ahn, K.7
-
19
-
-
77957806157
-
Disulphide production by Ero1alpha-PDI relay is rapid and effectively regulated
-
Appenzeller-Herzog C, Riemer J, Zito E, Chin KT, Ron D, et al. (2010) Disulphide production by Ero1alpha-PDI relay is rapid and effectively regulated. EMBO J 29: 3318-3329.
-
(2010)
EMBO J
, vol.29
, pp. 3318-3329
-
-
Appenzeller-Herzog, C.1
Riemer, J.2
Zito, E.3
Chin, K.T.4
Ron, D.5
-
20
-
-
84861662334
-
Vitamin K epoxide reductase contributes to protein disulfide formation and redox homeostasis within the endoplasmic reticulum
-
Rutkevich LA, Williams DB (2012) Vitamin K epoxide reductase contributes to protein disulfide formation and redox homeostasis within the endoplasmic reticulum. Mol Biol Cell 23: 2017-2027.
-
(2012)
Mol Biol Cell
, vol.23
, pp. 2017-2027
-
-
Rutkevich, L.A.1
Williams, D.B.2
-
21
-
-
84857602613
-
Peroxides and peroxidases in the endoplasmic reticulum: Integrating redox homeostasis and oxidative folding
-
Kakihana T, Nagata K, Sitia R (2012) Peroxides and peroxidases in the endoplasmic reticulum: integrating redox homeostasis and oxidative folding. Antioxid Redox Signal 16: 763-771.
-
(2012)
Antioxid Redox Signal
, vol.16
, pp. 763-771
-
-
Kakihana, T.1
Nagata, K.2
Sitia, R.3
-
22
-
-
0034711439
-
Biochemical basis of oxidative protein folding in the endoplasmic reticulum
-
Tu BP, Ho-Schleyer SC, Travers KJ, Weissman JS (2000) Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science 290: 1571-1574.
-
(2000)
Science
, vol.290
, pp. 1571-1574
-
-
Tu, B.P.1
Ho-Schleyer, S.C.2
Travers, K.J.3
Weissman, J.S.4
-
23
-
-
79551689187
-
Two endoplasmic reticulum PDI peroxidases increase the efficiency of the use of peroxide during disulfide bond formation
-
Nguyen VD, Saaranen MJ, Karala AR, Lappi AK, Wang L, et al. (2011) Two endoplasmic reticulum PDI peroxidases increase the efficiency of the use of peroxide during disulfide bond formation. J Mol Biol 406: 503-515.
-
(2011)
J Mol Biol
, vol.406
, pp. 503-515
-
-
Nguyen, V.D.1
Saaranen, M.J.2
Karala, A.R.3
Lappi, A.K.4
Wang, L.5
-
24
-
-
84887465759
-
Glutathione peroxidase 7 utilizes hydrogen peroxide generated by ero1alpha to promote oxidative protein folding
-
Wang L, Zhang L, Niu Y, Sitia R, Wang CC (2014) Glutathione peroxidase 7 utilizes hydrogen peroxide generated by ero1alpha to promote oxidative protein folding. Antioxid Redox Signal 20: 545-556.
-
(2014)
Antioxid Redox Signal
, vol.20
, pp. 545-556
-
-
Wang, L.1
Zhang, L.2
Niu, Y.3
Sitia, R.4
Wang, C.C.5
-
25
-
-
84882771697
-
Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding
-
Sato Y, Kojima R, Okumura M, Hagiwara M, Masui S, et al. (2013) Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding. Sci Rep 3: 2456.
-
(2013)
Sci Rep
, vol.3
, pp. 2456
-
-
Sato, Y.1
Kojima, R.2
Okumura, M.3
Hagiwara, M.4
Masui, S.5
-
26
-
-
0026632893
-
Folding in vitro of bovine pancreatic trypsin inhibitor in the presence of proteins of the endoplasmic reticulum
-
Zapun A, Creighton TE, Rowling PJ, Freedman RB (1992) Folding in vitro of bovine pancreatic trypsin inhibitor in the presence of proteins of the endoplasmic reticulum. Proteins 14: 10-15.
-
(1992)
Proteins
, vol.14
, pp. 10-15
-
-
Zapun, A.1
Creighton, T.E.2
Rowling, P.J.3
Freedman, R.B.4
-
27
-
-
33745315287
-
S-Nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration
-
DOI 10.1038/nature04782, PII NATURE04782
-
Uehara T, Nakamura T, Yao D, Shi ZQ, Gu Z, et al. (2006) S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration. Nature 441: 513-517. (Pubitemid 44050153)
-
(2006)
Nature
, vol.441
, Issue.7092
, pp. 513-517
-
-
Uehara, T.1
Nakamura, T.2
Yao, D.3
Shi, Z.-Q.4
Gu, Z.5
Ma, Y.6
Masliah, E.7
Nomura, Y.8
Lipton, S.A.9
-
28
-
-
66049156169
-
Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS
-
Karch CM, Prudencio M, Winkler DD, Hart PJ, Borchelt DR (2009) Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS. Proc Natl Acad Sci U S A 106: 7774-7779.
-
(2009)
Proc Natl Acad Sci U S A
, vol.106
, pp. 7774-7779
-
-
Karch, C.M.1
Prudencio, M.2
Winkler, D.D.3
Hart, P.J.4
Borchelt, D.R.5
-
29
-
-
84857997227
-
Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking
-
Cohen TJ, Hwang AW, Unger T, Trojanowski JQ, Lee VM (2012) Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking. EMBO J 31: 1241-1252.
-
(2012)
EMBO J
, vol.31
, pp. 1241-1252
-
-
Cohen, T.J.1
Hwang, A.W.2
Unger, T.3
Trojanowski, J.Q.4
Lee, V.M.5
-
30
-
-
84865559539
-
Overexpression of the rhodanese PspE, a single cysteine-containing protein, restores disulphide bond formation to an Escherichia coli strain lacking DsbA
-
Chng SS, Dutton RJ, Denoncin K, Vertommen D, Collet JF, et al. (2012) Overexpression of the rhodanese PspE, a single cysteine-containing protein, restores disulphide bond formation to an Escherichia coli strain lacking DsbA. Mol Microbiol 85: 996-1006.
-
(2012)
Mol Microbiol
, vol.85
, pp. 996-1006
-
-
Chng, S.S.1
Dutton, R.J.2
Denoncin, K.3
Vertommen, D.4
Collet, J.F.5
|