-
1
-
-
34147210988
-
Hydrogen peroxide sensing and signaling
-
Veal, E.A., Day, A.M. and Morgan, B.A. (2007) Hydrogen peroxide sensing and signaling. Mol. Cell 26, 1-14
-
(2007)
Mol. Cell
, vol.26
, pp. 1-14
-
-
Veal, E.A.1
Day, A.M.2
Morgan, B.A.3
-
2
-
-
33748564986
-
Membrane transport of hydrogen peroxide
-
Bienert, G.P., Schjoerring, J.K. and Jahn, T.P. (2006) Membrane transport of hydrogen peroxide. Biochim. Biophys. Acta 1758, 994-1003
-
(2006)
Biochim. Biophys. Acta
, vol.1758
, pp. 994-1003
-
-
Bienert, G.P.1
Schjoerring, J.K.2
Jahn, T.P.3
-
3
-
-
0017406503
-
Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria
-
Cadenas, E., Boveris, A., Ragan, C.I. and Stoppani, A.O. (1977) Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria. Arch. Biochem. Biophys. 180, 248-257
-
(1977)
Arch. Biochem. Biophys.
, vol.180
, pp. 248-257
-
-
Cadenas, E.1
Boveris, A.2
Ragan, C.I.3
Stoppani, A.O.4
-
4
-
-
58249093939
-
How mitochondria produce reactive oxygen species
-
Murphy, M.P. (2009) How mitochondria produce reactive oxygen species. Biochem. J. 417, 1-13
-
(2009)
Biochem. J.
, vol.417
, pp. 1-13
-
-
Murphy, M.P.1
-
5
-
-
33846794822
-
The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology
-
Bedard, K. and Krause, K.H. (2007) The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol. Rev. 87, 245-313
-
(2007)
Physiol. Rev.
, vol.87
, pp. 245-313
-
-
Bedard, K.1
Krause, K.H.2
-
6
-
-
10644262971
-
The Nox family of NAD(P)H oxidases: Host defense and beyond
-
Geiszt, M. and Leto, T.L. (2004) The Nox family of NAD(P)H oxidases: host defense and beyond. J. Biol. Chem. 279, 51715-51718
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 51715-51718
-
-
Geiszt, M.1
Leto, T.L.2
-
7
-
-
77955359156
-
Peroxiredoxin IV protects cells from oxidative stress by removing H2O2 produced during disulphide formation
-
Tavender, T.J. and Bulleid, N.J. (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
-
-
0013897667
-
Peroxisomes (microbodies and related particles)
-
De Duve, C. and Baudhuin, P. (1966) Peroxisomes (microbodies and related particles). Physiol. Rev. 46, 323-357
-
(1966)
Physiol. Rev.
, vol.46
, pp. 323-357
-
-
De Duve, C.1
Baudhuin, P.2
-
9
-
-
0021681841
-
Catalase: An old enzyme with a new role?
-
Percy, M.E. (1984) Catalase: an old enzyme with a new role? Can. J. Biochem. Cell Biol. 62, 1006-1014
-
(1984)
Can. J. Biochem. Cell Biol.
, vol.62
, pp. 1006-1014
-
-
Percy, M.E.1
-
10
-
-
41049100518
-
A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase
-
Beers, Jr, R.F. and Sizer, I.W. (1952) A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J. Biol. Chem. 195, 133-140
-
(1952)
J. Biol. Chem.
, vol.195
, pp. 133-140
-
-
Beers Jr., R.F.1
Sizer, I.W.2
-
11
-
-
0042819604
-
Catalase is regulated by ubiquitination and proteosomal degradation: Role of the c-Abl and Arg tyrosine kinases
-
Cao, C., Leng, Y., Liu, X., Yi, Y., Li, P. and Kufe, D. (2003) Catalase is regulated by ubiquitination and proteosomal degradation: role of the c-Abl and Arg tyrosine kinases. Biochemistry 42, 10348-10353
-
(2003)
Biochemistry
, vol.42
, pp. 10348-10353
-
-
Cao, C.1
Leng, Y.2
Liu, X.3
Yi, Y.4
Li, P.5
Kufe, D.6
-
13
-
-
67349155642
-
The oligomeric conformation of peroxiredoxins links redox state to function
-
Barranco-Medina, S., Lazaro, J.J. and Dietz, K.J. (2009) The oligomeric conformation of peroxiredoxins links redox state to function. FEBS Lett. 583, 1809-1816
-
(2009)
FEBS Lett.
, vol.583
, pp. 1809-1816
-
-
Barranco-Medina, S.1
Lazaro, J.J.2
Dietz, K.J.3
-
14
-
-
0242668688
-
Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation
-
Woo, H.A., Chae, H.Z., Hwang, S.C., Yang, K.S., Kang, S.W., Kim, K. and Rhee, S.G. (2003) Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation. Science 300, 653-656
-
(2003)
Science
, vol.300
, pp. 653-656
-
-
Woo, H.A.1
Chae, H.Z.2
Hwang, S.C.3
Yang, K.S.4
Kang, S.W.5
Kim, K.6
Rhee, S.G.7
-
15
-
-
79959481888
-
Protein folding and modification in the mammalian endoplasmic reticulum
-
Braakman, I. and Bulleid, N.J. (2011) Protein folding and modification in the mammalian endoplasmic reticulum. Annu. Rev. Biochem. 80, 71-99
-
(2011)
Annu. Rev. Biochem.
, vol.80
, pp. 71-99
-
-
Braakman, I.1
Bulleid, N.J.2
-
16
-
-
0031939209
-
Protein disulfide isomerase
-
Gilbert, H.F. (1998) Protein disulfide isomerase. Methods Enzymol. 290, 26-50
-
(1998)
Methods Enzymol.
, vol.290
, pp. 26-50
-
-
Gilbert, H.F.1
-
18
-
-
71549132149
-
Protein disulfide isomerase: A critical evaluation of its function in disulfide bond formation
-
Hatahet, F. and Ruddock, L.W. (2009) Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation. Antioxid. Redox Signal. 11, 2807-2850
-
(2009)
Antioxid. Redox Signal.
, vol.11
, pp. 2807-2850
-
-
Hatahet, F.1
Ruddock, L.W.2
-
19
-
-
79955878526
-
Reexamination of the role of interplay between glutathione and protein disulfide isomerase
-
Lappi, A.K. and Ruddock, L.W. (2011) Reexamination of the role of interplay between glutathione and protein disulfide isomerase. J. Mol. Biol. 409, 238-249
-
(2011)
J. Mol. Biol.
, vol.409
, pp. 238-249
-
-
Lappi, A.K.1
Ruddock, L.W.2
-
20
-
-
0036862532
-
The FAD- and O2-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum
-
Tu, B.P. and Weissman, J.S. (2002) The FAD- and O2-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum. Mol. Cell 10, 983-994
-
(2002)
Mol. Cell
, vol.10
, pp. 983-994
-
-
Tu, B.P.1
Weissman, J.S.2
-
21
-
-
0031609760
-
The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
-
Frand, A.R. and Kaiser, C.A. (1998) The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol. Cell 1, 161-170
-
(1998)
Mol. Cell
, vol.1
, pp. 161-170
-
-
Frand, A.R.1
Kaiser, C.A.2
-
22
-
-
0031610364
-
Ero1p: A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum
-
Pollard, M.G., Travers, K.J. and Weissman, J.S. (1998) Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol. Cell 1, 171-182
-
(1998)
Mol. Cell
, vol.1
, pp. 171-182
-
-
Pollard, M.G.1
Travers, K.J.2
Weissman, J.S.3
-
23
-
-
84868574593
-
Disulfide bond formation in the mammalian endoplasmic reticulum
-
Bulleid, N.J. (2012) Disulfide bond formation in the mammalian endoplasmic reticulum. Cold Spring Harb. Perspect. Biol. 4, 81-92
-
(2012)
Cold Spring Harb. Perspect. Biol.
, vol.4
, pp. 81-92
-
-
Bulleid, N.J.1
-
24
-
-
77949716997
-
ERO1-β, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis
-
Zito, E., Chin, K.-T., Blais, J., Harding, H.P. and Ron, D. (2010) ERO1-β, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis. J. Cell Biol. 188, 821-832
-
(2010)
J. Cell Biol.
, vol.188
, pp. 821-832
-
-
Zito, E.1
Chin, K.-T.2
Blais, J.3
Harding, H.P.4
Ron, D.5
-
25
-
-
31044452359
-
Generating disulfides enzymatically: Reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p
-
Gross, E., Sevier, C.S., Heldman, N., Vitu, E., Bentzur, M., Kaiser, C.A., Thorpe, C. and Fass, D. (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
-
(2006)
Proc. Natl. Acad. Sci. U.S.A.
, vol.103
, 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
-
26
-
-
56549083161
-
A novel disulphide switch mechanism in Ero1α balances ER oxidation in human cells
-
Appenzeller-Herzog, C., Riemer, J., Christensen, B., Sørensen, E.S. and Ellgaard, L. (2008) A novel disulphide switch mechanism in Ero1α balances ER oxidation in human cells. EMBO J. 27, 2977-2987
-
(2008)
EMBO J.
, vol.27
, pp. 2977-2987
-
-
Appenzeller-Herzog, C.1
Riemer, J.2
Christensen, B.3
Sørensen, E.S.4
Ellgaard, L.5
-
27
-
-
56549124032
-
Low reduction potential of Ero1α regulatory disulphides ensures tight control of substrate oxidation
-
Baker, K.M., Chakravarthi, S., Langton, K.P., Sheppard, A.M., Lu, H. and Bulleid, N.J. (2008) Low reduction potential of Ero1α regulatory disulphides ensures tight control of substrate oxidation. EMBO J. 27, 2988-2997
-
(2008)
EMBO J.
, vol.27
, pp. 2988-2997
-
-
Baker, K.M.1
Chakravarthi, S.2
Langton, K.P.3
Sheppard, A.M.4
Lu, H.5
Bulleid, N.J.6
-
28
-
-
78650270477
-
Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum
-
Tavender, T.J., Springate, J.J. and Bulleid, N.J. (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
-
29
-
-
78649918283
-
Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin
-
Zito, E., Melo, E.P., Yang, Y., Wahlander, A., Neubert, T.A. and Ron, D. (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
Ron, D.6
-
30
-
-
79551689187
-
Two endoplasmic reticulum PDI peroxidases increase the efficiency of the use of peroxide during disulfide bond formation
-
Nguyen, V.D., Saaranen, M.J., Karala, A.-R., Lappi, A.-K., Wang, L., Raykhel, I.B., Alanen, H.I., Salo, K.E.H., Wang, C.-c. and Ruddock, L.W. (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
Raykhel, I.B.6
Alanen, H.I.7
Salo, K.E.H.8
Wang, C.-C.9
Ruddock, L.W.10
-
31
-
-
34347204504
-
Generating disulfides in multicellular organisms: Emerging roles for a new flavoprotein family
-
Thorpe, C. and Coppock, D.L. (2007) Generating disulfides in multicellular organisms: emerging roles for a new flavoprotein family. J. Biol. Chem. 282, 13929-13933
-
(2007)
J. Biol. Chem.
, vol.282
, pp. 13929-13933
-
-
Thorpe, C.1
Coppock, D.L.2
-
32
-
-
84861662334
-
Vitamin K epoxide reductase contributes to protein disulfide formation and redox homeostasis within the endoplasmic reticulum
-
Rutkevich, L.A. and Williams, D.B. (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
-
33
-
-
84865123844
-
The dynamic disulphide relay of quiescin sulphydryl oxidase
-
Alon, A., Grossman, I., Gat, Y., Kodali, V.K., DiMaio, F., Mehlman, T., Haran, G., Baker, D., Thorpe, C. and Fass, D. (2012) The dynamic disulphide relay of quiescin sulphydryl oxidase. Nature 488, 414-418
-
(2012)
Nature
, vol.488
, pp. 414-418
-
-
Alon, A.1
Grossman, I.2
Gat, Y.3
Kodali, V.K.4
Dimaio, F.5
Mehlman, T.6
Haran, G.7
Baker, D.8
Thorpe, C.9
Fass, D.10
-
34
-
-
84861362218
-
Protein substrate discrimination in the quiescin sulfhydryl oxidase (QSOX) family
-
Codding, J.A., Israel, B.A. and Thorpe, C. (2012) Protein substrate discrimination in the quiescin sulfhydryl oxidase (QSOX) family. Biochemistry 51, 4226-4235
-
(2012)
Biochemistry
, vol.51
, pp. 4226-4235
-
-
Codding, J.A.1
Israel, B.A.2
Thorpe, C.3
-
35
-
-
56249094492
-
Oxidative protein folding in vitro: A study of the cooperation between quiescin-sulfhydryl oxidase and protein disulfide isomerase
-
Rancy, P.C. and Thorpe, C. (2008) Oxidative protein folding in vitro: a study of the cooperation between quiescin-sulfhydryl oxidase and protein disulfide isomerase. Biochemistry 47, 12047-12056
-
(2008)
Biochemistry
, vol.47
, pp. 12047-12056
-
-
Rancy, P.C.1
Thorpe, C.2
-
36
-
-
34250787527
-
Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1
-
Chakravarthi, S., Jessop, C.E., Willer, M., Stirling, C.J. and Bulleid, N.J. (2007) Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1. Biochem. J. 404, 403-411
-
(2007)
Biochem. J.
, vol.404
, pp. 403-411
-
-
Chakravarthi, S.1
Jessop, C.E.2
Willer, M.3
Stirling, C.J.4
Bulleid, N.J.5
-
37
-
-
79953218059
-
Novel insight into the mechanism of the vitamin K oxidoreductase (VKOR): Electron relay through Cys43 and Cys51 reduces VKOR to allow vitamin K reduction and facilitation of vitamin K-dependent protein carboxylation
-
Rishavy, M.A., Usubalieva, A., Hallgren, K.W. and Berkner, K.L. (2011) Novel insight into the mechanism of the vitamin K oxidoreductase (VKOR): electron relay through Cys43 and Cys51 reduces VKOR to allow vitamin K reduction and facilitation of vitamin K-dependent protein carboxylation. J. Biol. Chem. 286, 7267-7278
-
(2011)
J. Biol. Chem.
, vol.286
, pp. 7267-7278
-
-
Rishavy, M.A.1
Usubalieva, A.2
Hallgren, K.W.3
Berkner, K.L.4
-
38
-
-
34047258016
-
Disulfide-dependent protein folding is linked to operation of the vitamin K cycle in the endoplasmic reticulum: A protein disulfide isomerase-VKORC1 redox enzyme complex appears to be responsible for vitamin K1 2,3-epoxide reduction
-
Wajih, N., Hutson, S.M. and Wallin, R. (2007) Disulfide-dependent protein folding is linked to operation of the vitamin K cycle in the endoplasmic reticulum: a protein disulfide isomerase-VKORC1 redox enzyme complex appears to be responsible for vitamin K1 2,3-epoxide reduction. J. Biol. Chem. 282, 2626-2635
-
(2007)
J. Biol. Chem.
, vol.282
, pp. 2626-2635
-
-
Wajih, N.1
Hutson, S.M.2
Wallin, R.3
-
39
-
-
77957007036
-
Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners
-
Schulman, S., Wang, B., Li, W. and Rapoport, T.A. (2010) Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners. Proc. Natl. Acad. Sci. U.S.A. 107, 15027-15032
-
(2010)
Proc. Natl. Acad. Sci. U.S.A.
, vol.107
, pp. 15027-15032
-
-
Schulman, S.1
Wang, B.2
Li, W.3
Rapoport, T.A.4
-
40
-
-
41649110016
-
Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells
-
Tavender, T.J., Sheppard, A.M. and Bulleid, N.J. (2008) Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells. Biochem. J. 411, 191-199
-
(2008)
Biochem. J.
, vol.411
, pp. 191-199
-
-
Tavender, T.J.1
Sheppard, A.M.2
Bulleid, N.J.3
-
41
-
-
82755171868
-
Crystal structure of reduced and of oxidized peroxiredoxin IV enzyme reveals a stable oxidized decamer and a non-disulfide-bonded intermediate in the catalytic cycle
-
Cao, Z., Tavender, T.J., Roszak, A.W., Cogdell, R.J. and Bulleid, N.J. (2011) Crystal structure of reduced and of oxidized peroxiredoxin IV enzyme reveals a stable oxidized decamer and a non-disulfide-bonded intermediate in the catalytic cycle. J. Biol. Chem. 286, 42257-42266
-
(2011)
J. Biol. Chem.
, vol.286
, pp. 42257-42266
-
-
Cao, Z.1
Tavender, T.J.2
Roszak, A.W.3
Cogdell, R.J.4
Bulleid, N.J.5
-
42
-
-
57049161455
-
Cysteine pKa values for the bacterial peroxiredoxin AhpC
-
Nelson, K.J., Parsonage, D., Hall, A., Karplus, P.A. and Poole, L.B. (2008) Cysteine pKa values for the bacterial peroxiredoxin AhpC. Biochemistry 47, 12860-12868
-
(2008)
Biochemistry
, vol.47
, pp. 12860-12868
-
-
Nelson, K.J.1
Parsonage, D.2
Hall, A.3
Karplus, P.A.4
Poole, L.B.5
-
43
-
-
64149085448
-
Typical 2-Cys peroxiredoxins: Structures, mechanisms and functions
-
Hall, A., Karplus, P.A. and Poole, L.B. (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
-
44
-
-
0346726109
-
How enzymes work: Analysis by modern rate theory and computer simulations
-
Garcia-Viloca, M., Gao, J., Karplus, M. and Truhlar, D.G. (2004) How enzymes work: analysis by modern rate theory and computer simulations. Science 303, 186-195
-
(2004)
Science
, vol.303
, pp. 186-195
-
-
Garcia-Viloca, M.1
Gao, J.2
Karplus, M.3
Truhlar, D.G.4
-
45
-
-
77956171017
-
Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization
-
Hall, A., Parsonage, D., Poole, L.B. and Karplus, P.A. (2010) Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization. J. Mol. Biol. 402, 194-209
-
(2010)
J. Mol. Biol.
, vol.402
, pp. 194-209
-
-
Hall, A.1
Parsonage, D.2
Poole, L.B.3
Karplus, P.A.4
-
46
-
-
42249088093
-
Reconciling the chemistry and biology of reactive oxygen species
-
Winterbourn, C.C. (2008) Reconciling the chemistry and biology of reactive oxygen species. Nat. Chem. Biol. 4, 278-286
-
(2008)
Nat. Chem. Biol.
, vol.4
, pp. 278-286
-
-
Winterbourn, C.C.1
-
47
-
-
77953725586
-
Oxidative protein folding in the endoplasmic reticulum: Tight links to the mitochondria-associated membrane (MAM)
-
Simmen, T., Lynes, E.M., Gesson, K. and Thomas, G. (2010) Oxidative protein folding in the endoplasmic reticulum: tight links to the mitochondria-associated membrane (MAM). Biochim. Biophys. Acta 1798, 1465-1473
-
(2010)
Biochim. Biophys. Acta
, vol.1798
, pp. 1465-1473
-
-
Simmen, T.1
Lynes, E.M.2
Gesson, K.3
Thomas, G.4
|