메뉴 건너뛰기




Volumn 279, Issue 13, 2012, Pages 2262-2271

Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals

Author keywords

Disulfide bond; DsbA; DsbB; Ero1; PDI; Prx4

Indexed keywords

CELL SURFACE PROTEIN; OXIDOREDUCTASE; PROTEIN DISULFIDE ISOMERASE; SECRETORY PROTEIN; THIOREDOXIN;

EID: 84862548210     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2012.08593.x     Document Type: Short Survey
Times cited : (71)

References (72)
  • 1
    • 67349189383 scopus 로고
    • The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain
    • Anfinsen CB, Haber E, Sela M & White FH Jr (1961) The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain. Proc Natl Acad Sci USA 47, 1309-1314.
    • (1961) Proc Natl Acad Sci USA , vol.47 , pp. 1309-1314
    • Anfinsen, C.B.1    Haber, E.2    Sela, M.3    White Jr., F.H.4
  • 2
    • 77955957534 scopus 로고    scopus 로고
    • Structural basis of protein disulfide bond generation in the cell
    • Inaba K (2010) Structural basis of protein disulfide bond generation in the cell. Genes Cells 15, 935-943.
    • (2010) Genes Cells , vol.15 , pp. 935-943
    • Inaba, K.1
  • 3
    • 41449116766 scopus 로고    scopus 로고
    • Ero1 and redox homeostasis in the endoplasmic reticulum
    • Sevier CS & Kaiser CA (2008) Ero1 and redox homeostasis in the endoplasmic reticulum. Biochim Biophys Acta 1783, 549-556.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 549-556
    • Sevier, C.S.1    Kaiser, C.A.2
  • 4
    • 50149109183 scopus 로고    scopus 로고
    • Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation
    • Dutton RJ, Boyd D, Berkmen M & Beckwith J (2008) Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation. Proc Natl Acad Sci USA 105, 11933-11938.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 11933-11938
    • Dutton, R.J.1    Boyd, D.2    Berkmen, M.3    Beckwith, J.4
  • 5
    • 0042768090 scopus 로고    scopus 로고
    • Protein disulfide bond formation in prokaryotes
    • Kadokura H, Katzen F & Beckwith J (2003) Protein disulfide bond formation in prokaryotes. Annu Rev Biochem 72, 111-135.
    • (2003) Annu Rev Biochem , vol.72 , pp. 111-135
    • Kadokura, H.1    Katzen, F.2    Beckwith, J.3
  • 6
    • 70449674774 scopus 로고    scopus 로고
    • Disulfide bond formation system in Escherichia coli
    • Inaba K (2009) Disulfide bond formation system in Escherichia coli. J Biochem (Tokyo) 146, 591-597.
    • (2009) J Biochem (Tokyo) , vol.146 , pp. 591-597
    • Inaba, K.1
  • 7
    • 0027373949 scopus 로고
    • Crystal structure of the DsbA protein required for disulphide bond formation in vivo
    • Martin JL, Bardwell JC & Kuriyan J (1993) Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Nature 365, 464-468.
    • (1993) Nature , vol.365 , pp. 464-468
    • Martin, J.L.1    Bardwell, J.C.2    Kuriyan, J.3
  • 8
    • 33750813327 scopus 로고    scopus 로고
    • Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation
    • Inaba K, Murakami S, Suzuki M, Nakagawa A, Yamashita E, Okada K & Ito K (2006) Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation. Cell 127, 789-801.
    • (2006) Cell , vol.127 , pp. 789-801
    • Inaba, K.1    Murakami, S.2    Suzuki, M.3    Nakagawa, A.4    Yamashita, E.5    Okada, K.6    Ito, K.7
  • 9
    • 0032562757 scopus 로고    scopus 로고
    • Reconstitution of a protein disulfide catalytic system
    • Bader M, Muse W, Zander T & Bardwell J (1998) Reconstitution of a protein disulfide catalytic system. J Biol Chem 273, 10302-10307.
    • (1998) J Biol Chem , vol.273 , pp. 10302-10307
    • Bader, M.1    Muse, W.2    Zander, T.3    Bardwell, J.4
  • 10
    • 0030671552 scopus 로고    scopus 로고
    • Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells
    • Kobayashi T, Kishigami S, Sone M, Inokuchi H, Mogi T & Ito K (1997) Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells. Proc Natl Acad Sci USA 94, 11857-11862.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11857-11862
    • Kobayashi, T.1    Kishigami, S.2    Sone, M.3    Inokuchi, H.4    Mogi, T.5    Ito, K.6
  • 11
    • 31044433084 scopus 로고    scopus 로고
    • Critical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB
    • Inaba K, Takahashi YH, Ito K & Hayashi S (2006) Critical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB. Proc Natl Acad Sci USA 103, 287-292.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 287-292
    • Inaba, K.1    Takahashi, Y.H.2    Ito, K.3    Hayashi, S.4
  • 12
    • 62649151322 scopus 로고    scopus 로고
    • Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB
    • Inaba K, Murakami S, Nakagawa A, Iida H, Kinjo M, Ito K & Suzuki M (2009) Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB. EMBO J 28, 779-791.
    • (2009) EMBO J , vol.28 , pp. 779-791
    • Inaba, K.1    Murakami, S.2    Nakagawa, A.3    Iida, H.4    Kinjo, M.5    Ito, K.6    Suzuki, M.7
  • 14
    • 0033609929 scopus 로고    scopus 로고
    • Functional analysis of paralogous thiol-disulfide oxidoreductases in Bacillus subtilis
    • Bolhuis A, Venema G, Quax WJ, Bron S & van Dijl JM (1999) Functional analysis of paralogous thiol-disulfide oxidoreductases in Bacillus subtilis. J Biol Chem 274, 24531-24538.
    • (1999) J Biol Chem , vol.274 , pp. 24531-24538
    • Bolhuis, A.1    Venema, G.2    Quax, W.J.3    Bron, S.4    Van Dijl, J.M.5
  • 15
    • 0038381449 scopus 로고    scopus 로고
    • Bacillus subtilis ResA is a thiol-disulfide oxidoreductase involved in cytochrome c synthesis
    • Erlendsson LS, Acheson R, Hederstedt L & Le Brun NE (2003) Bacillus subtilis ResA is a thiol-disulfide oxidoreductase involved in cytochrome c synthesis. J Biol Chem 278, 17852-17858.
    • (2003) J Biol Chem , vol.278 , pp. 17852-17858
    • Erlendsson, L.S.1    Acheson, R.2    Hederstedt, L.3    Le Brun, N.E.4
  • 16
    • 65649116921 scopus 로고    scopus 로고
    • Structure and functional properties of Bacillus subtilis endospore biogenesis factor StoA
    • Crow A, Liu Y, Moller MC, Le Brun NE & Hederstedt L (2009) Structure and functional properties of Bacillus subtilis endospore biogenesis factor StoA. J Biol Chem 284, 10056-10066.
    • (2009) J Biol Chem , vol.284 , pp. 10056-10066
    • Crow, A.1    Liu, Y.2    Moller, M.C.3    Le Brun, N.E.4    Hederstedt, L.5
  • 18
    • 13444261412 scopus 로고    scopus 로고
    • Characterization of new DsbB-like thiol-oxidoreductases of Campylobacter jejuni and Helicobacter pylori and classification of the DsbB family based on phylogenomic, structural and functional criteria
    • Raczko AM, Bujnicki JM, Pawlowski M, Godlewska R, Lewandowska M & Jagusztyn-Krynicka EK (2005) Characterization of new DsbB-like thiol-oxidoreductases of Campylobacter jejuni and Helicobacter pylori and classification of the DsbB family based on phylogenomic, structural and functional criteria. Microbiology 151, 219-231.
    • (2005) Microbiology , vol.151 , pp. 219-231
    • Raczko, A.M.1    Bujnicki, J.M.2    Pawlowski, M.3    Godlewska, R.4    Lewandowska, M.5    Jagusztyn-Krynicka, E.K.6
  • 21
    • 30344467827 scopus 로고    scopus 로고
    • Insights on a new PDI-like family: Structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus
    • Pedone E, D'Ambrosio K, De Simone G, Rossi M, Pedone C & Bartolucci S (2006) Insights on a new PDI-like family: structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus. J Mol Biol 356, 155-164.
    • (2006) J Mol Biol , vol.356 , pp. 155-164
    • Pedone, E.1    D'Ambrosio, K.2    De Simone, G.3    Rossi, M.4    Pedone, C.5    Bartolucci, S.6
  • 22
    • 36148946799 scopus 로고    scopus 로고
    • The machinery for oxidative protein folding in thermophiles
    • Pedone M, Limauro D & Bartolucci S (2008) The machinery for oxidative protein folding in thermophiles. Antioxid Redox Signal 10, 157-169.
    • (2008) Antioxid Redox Signal , vol.10 , pp. 157-169
    • Pedone, M.1    Limauro, D.2    Bartolucci, S.3
  • 23
    • 0031816805 scopus 로고    scopus 로고
    • A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units
    • Ren B, Tibbelin G, de Pascale D, Rossi M, Bartolucci S & Ladenstein R (1998) A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units. Nat Struct Biol 5, 602-611.
    • (1998) Nat Struct Biol , vol.5 , pp. 602-611
    • Ren, B.1    Tibbelin, G.2    De Pascale, D.3    Rossi, M.4    Bartolucci, S.5    Ladenstein, R.6
  • 24
    • 77956334107 scopus 로고    scopus 로고
    • Molecular mechanisms regulating oxidative activity of the Ero1 family in the endoplasmic reticulum
    • Tavender TJ & Bulleid NJ (2010) Molecular mechanisms regulating oxidative activity of the Ero1 family in the endoplasmic reticulum. Antioxid Redox Signal 13, 1177-1187.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 1177-1187
    • Tavender, T.J.1    Bulleid, N.J.2
  • 25
    • 0031609760 scopus 로고    scopus 로고
    • The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
    • Frand AR & Kaiser CA (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
  • 26
    • 0031610364 scopus 로고    scopus 로고
    • Ero1p: A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum
    • Pollard MG, Travers KJ & Weissman JS (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
  • 27
    • 2542475140 scopus 로고    scopus 로고
    • Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell
    • Gross E, Kastner DB, Kaiser CA & Fass D (2004) Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell. Cell 117, 601-610.
    • (2004) Cell , vol.117 , pp. 601-610
    • Gross, E.1    Kastner, D.B.2    Kaiser, C.A.3    Fass, D.4
  • 28
    • 31044452359 scopus 로고    scopus 로고
    • Generating disulfides enzymatically: Reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p
    • Gross E, Sevier CS, Heldman N, Vitu E, Bentzur M, Kaiser CA, Thorpe C & Fass D (2006) Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p. Proc Natl Acad Sci USA 103, 299-304.
    • (2006) Proc Natl Acad Sci USA , 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
  • 29
    • 34147126077 scopus 로고    scopus 로고
    • Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1
    • Sevier CS, Qu H, Heldman N, Gross E, Fass D & Kaiser CA (2007) Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1. Cell 129, 333-344.
    • (2007) Cell , vol.129 , pp. 333-344
    • Sevier, C.S.1    Qu, H.2    Heldman, N.3    Gross, E.4    Fass, D.5    Kaiser, C.A.6
  • 30
  • 31
    • 0034790475 scopus 로고    scopus 로고
    • A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation
    • Sevier CS, Cuozzo JW, Vala A, Aslund F & Kaiser CA (2001) A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation. Nat Cell Biol 3, 874-882.
    • (2001) Nat Cell Biol , vol.3 , pp. 874-882
    • Sevier, C.S.1    Cuozzo, J.W.2    Vala, A.3    Aslund, F.4    Kaiser, C.A.5
  • 32
    • 41449101717 scopus 로고    scopus 로고
    • The Erv family of sulfhydryl oxidases
    • Fass D (2008) The Erv family of sulfhydryl oxidases. Biochim Biophys Acta 1783, 557-566.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 557-566
    • Fass, D.1
  • 33
    • 30344444015 scopus 로고    scopus 로고
    • The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites
    • erratum appears in Cell 2006; 124:1085-1088
    • Tian G, Xiang S, Noiva R, Lennarz WJ & Schindelin H (2006) The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites [erratum appears in Cell 2006; 124:1085-1088]. Cell 124, 61-73.
    • (2006) Cell , vol.124 , pp. 61-73
    • Tian, G.1    Xiang, S.2    Noiva, R.3    Lennarz, W.J.4    Schindelin, H.5
  • 34
    • 57749102824 scopus 로고    scopus 로고
    • The catalytic activity of protein-disulfide isomerase requires a conformationally flexible molecule
    • Tian G, Kober FX, Lewandrowski U, Sickmann A, Lennarz WJ & Schindelin H (2008) The catalytic activity of protein-disulfide isomerase requires a conformationally flexible molecule. J Biol Chem 283, 33630-33640.
    • (2008) J Biol Chem , vol.283 , pp. 33630-33640
    • Tian, G.1    Kober, F.X.2    Lewandrowski, U.3    Sickmann, A.4    Lennarz, W.J.5    Schindelin, H.6
  • 36
    • 77953313165 scopus 로고    scopus 로고
    • Oxidative activity of yeast Ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulum
    • Vitu E, Kim S, Sevier CS, Lutzky O, Heldman N, Bentzur M, Unger T, Yona M, Kaiser CA & Fass D (2010) Oxidative activity of yeast Ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulum. J Biol Chem 285, 18155-18165.
    • (2010) J Biol Chem , vol.285 , pp. 18155-18165
    • Vitu, E.1    Kim, S.2    Sevier, C.S.3    Lutzky, O.4    Heldman, N.5    Bentzur, M.6    Unger, T.7    Yona, M.8    Kaiser, C.A.9    Fass, D.10
  • 37
    • 24744471839 scopus 로고    scopus 로고
    • Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities
    • Kimura T, Hosoda Y, Sato Y, Kitamura Y, Ikeda T, Horibe T & Kikuchi M (2005) Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities. J Biol Chem 280, 31438-31441.
    • (2005) J Biol Chem , vol.280 , pp. 31438-31441
    • Kimura, T.1    Hosoda, Y.2    Sato, Y.3    Kitamura, Y.4    Ikeda, T.5    Horibe, T.6    Kikuchi, M.7
  • 38
    • 84857570189 scopus 로고    scopus 로고
    • Structure, mechanism and evolution of Ero1 family enzymes
    • Araki K & Inaba K (2012) Structure, mechanism and evolution of Ero1 family enzymes. Antioxid Redox Signal 16, 790-799.
    • (2012) Antioxid Redox Signal , vol.16 , pp. 790-799
    • Araki, K.1    Inaba, K.2
  • 40
    • 77949716997 scopus 로고    scopus 로고
    • Ero1-beta, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis
    • Zito E, Chin K-T, Blais H & Ron D (2010) Ero1-beta, 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, H.3    Ron, D.4
  • 41
    • 56549124032 scopus 로고    scopus 로고
    • Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation
    • Baker KM, Chakravarthi S, Langton KP, Sheppard AM, Lu H & Bulleid NJ (2008) Low reduction potential of Ero1alpha 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
  • 42
    • 56549083161 scopus 로고    scopus 로고
    • A novel disulphide switch mechanism in Ero1alpha balances ER oxidation in human cells
    • Appenzeller-Herzog C, Riemer J, Christensen B, Sorensen ES & Ellgaard L (2008) A novel disulphide switch mechanism in Ero1alpha 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    Sorensen, E.S.4    Ellgaard, L.5
  • 43
    • 79251539550 scopus 로고    scopus 로고
    • The endoplasmic reticulum sulfhydryl oxidase Ero1beta drives efficient oxidative protein folding with loose regulation
    • Wang L, Zhu L & Wang CC (2010) The endoplasmic reticulum sulfhydryl oxidase Ero1beta drives efficient oxidative protein folding with loose regulation. Biochem J 434, 113-121.
    • (2010) Biochem J , vol.434 , pp. 113-121
    • Wang, L.1    Zhu, L.2    Wang, C.C.3
  • 44
    • 77957773053 scopus 로고    scopus 로고
    • Crystal structures of human Ero1alpha reveal the mechanisms of regulated and targeted oxidation of PDI
    • Inaba K, Masui S, Iida H, Vavassori S, Sitia R & Suzuki M (2010) Crystal structures of human Ero1alpha reveal the mechanisms of regulated and targeted oxidation of PDI. EMBO J 29, 3330-3343.
    • (2010) EMBO J , vol.29 , pp. 3330-3343
    • Inaba, K.1    Masui, S.2    Iida, H.3    Vavassori, S.4    Sitia, R.5    Suzuki, M.6
  • 46
    • 79955527426 scopus 로고    scopus 로고
    • Molecular bases of cyclic and specific disulfide interchange between human ERO1alpha protein and protein-disulfide isomerase (PDI)
    • Masui S, Vavassori S, Fagioli C, Sitia R & Inaba K (2011) Molecular bases of cyclic and specific disulfide interchange between human ERO1alpha protein and protein-disulfide isomerase (PDI). J Biol Chem 286, 16261-16271.
    • (2011) J Biol Chem , vol.286 , pp. 16261-16271
    • Masui, S.1    Vavassori, S.2    Fagioli, C.3    Sitia, R.4    Inaba, K.5
  • 47
    • 58649096169 scopus 로고    scopus 로고
    • Reconstitution of human Ero1-Lalpha? protein-disulfide isomerase oxidative folding pathway in vitro. Position-dependent differences in role between the a and á domains of protein-disulfide isomerase
    • Wang L, Li SJ, Sidhu A, Zhu L, Liang Y, Freedman RB & Wang CC (2009) Reconstitution of human Ero1-Lalpha ? protein-disulfide isomerase oxidative folding pathway in vitro. Position-dependent differences in role between the a and á 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    Freedman, R.B.6    Wang, C.C.7
  • 48
  • 49
    • 78649918283 scopus 로고    scopus 로고
    • Oxidative protein folding by an endoplasmic reticulum localized peroxiredoxin
    • Zito E, Melo EP, Yang Y, Wahlander A, Neubert TA & 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
  • 50
    • 78650270477 scopus 로고    scopus 로고
    • 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
  • 52
    • 82755171868 scopus 로고    scopus 로고
    • Crystal structure of reduced and oxidized peroxiredoxin IV reveals a stable oxidized decamer and a non disulfide-bonded intermediate in the catalytic cycle
    • Cao Z, Tavender TJ, Roszak AW, Cogdell RJ & Bulleid NJ (2011) Crystal structure of reduced and oxidized peroxiredoxin IV 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
  • 53
    • 84055178426 scopus 로고    scopus 로고
    • Structural insights into peroxidase activity and inactivation of human peroxiredoxin 4
    • Wang XF, Wang L, Wang XF, Sun F & Wang CC (2012) Structural insights into peroxidase activity and inactivation of human peroxiredoxin 4. Biochem J 441, 113-118.
    • (2012) Biochem J , vol.441 , pp. 113-118
    • Wang, X.F.1    Wang, L.2    Wang, X.F.3    Sun, F.4    Wang, C.C.5
  • 55
    • 79953218059 scopus 로고    scopus 로고
    • 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 MA, Usubalieva A, Hallgren KW & Berkner KL (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
  • 56
    • 77957007036 scopus 로고    scopus 로고
    • Vitamin K epoxide reductase prefers ER membraneanchored thioredoxin-like redox partners
    • Schulman S, Wang B, Li W & Rapoport TA (2010) Vitamin K epoxide reductase prefers ER membraneanchored thioredoxin-like redox partners. Proc Natl Acad Sci USA 107, 15027-15032.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 15027-15032
    • Schulman, S.1    Wang, B.2    Li, W.3    Rapoport, T.A.4
  • 57
    • 79955393313 scopus 로고    scopus 로고
    • Human vitamin K 2,3-epoxide reductase complex subunit 1-like 1 (VKORC1L1) mediates vitamin K-dependent intracellular antioxidant function
    • Westhofen P, Watzka M, Marinova M, Hass M, Kirfel G, Muller J, Bevans CG, Muller CR & Oldenburg J (2011) Human vitamin K 2,3-epoxide reductase complex subunit 1-like 1 (VKORC1L1) mediates vitamin K-dependent intracellular antioxidant function. J Biol Chem 286, 15085-15094.
    • (2011) J Biol Chem , vol.286 , pp. 15085-15094
    • Westhofen, P.1    Watzka, M.2    Marinova, M.3    Hass, M.4    Kirfel, G.5    Muller, J.6    Bevans, C.G.7    Muller, C.R.8    Oldenburg, J.9
  • 58
    • 77956313447 scopus 로고    scopus 로고
    • Oxidative protein folding and the quiescin-sulfhydryl oxidase family of flavoproteins
    • Kodali VK & Thorpe C (2010) Oxidative protein folding and the quiescin-sulfhydryl oxidase family of flavoproteins. Antioxid Redox Signal 13, 1217-1230.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 1217-1230
    • Kodali, V.K.1    Thorpe, C.2
  • 59
    • 42449098493 scopus 로고    scopus 로고
    • Human quiescin-sulfhydryl oxidase, QSOX1: Probing internal redox steps by mutagenesis
    • Heckler EJ, Alon A, Fass D & Thorpe C (2008) Human quiescin-sulfhydryl oxidase, QSOX1: probing internal redox steps by mutagenesis. Biochemistry 47, 4955-4963.
    • (2008) Biochemistry , vol.47 , pp. 4955-4963
    • Heckler, E.J.1    Alon, A.2    Fass, D.3    Thorpe, C.4
  • 60
    • 34250787527 scopus 로고    scopus 로고
    • Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1
    • Chakravarthi S, Jessop CE, Willer M, Stirling CJ & Bulleid NJ (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
  • 61
    • 0032807338 scopus 로고    scopus 로고
    • ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin
    • Oliver JD, Roderick HL, Llewellyn DH & High S (1999) ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin. Mol Biol Cell 10, 2573-2582.
    • (1999) Mol Biol Cell , vol.10 , pp. 2573-2582
    • Oliver, J.D.1    Roderick, H.L.2    Llewellyn, D.H.3    High, S.4
  • 62
    • 59049105293 scopus 로고    scopus 로고
    • Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin
    • Jessop CE, Tavender TJ, Watkins RH, Chambers JE & Bulleid NJ (2009) Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin. J Biol Chem 284, 2194-2202.
    • (2009) J Biol Chem , vol.284 , pp. 2194-2202
    • Jessop, C.E.1    Tavender, T.J.2    Watkins, R.H.3    Chambers, J.E.4    Bulleid, N.J.5
  • 64
    • 70849101711 scopus 로고    scopus 로고
    • Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins
    • Jessop CE, Watkins RH, Simmons JJ, Tasab M & Bulleid NJ (2009) Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins. J Cell Sci 122, 4287-4295.
    • (2009) J Cell Sci , vol.122 , pp. 4287-4295
    • Jessop, C.E.1    Watkins, R.H.2    Simmons, J.J.3    Tasab, M.4    Bulleid, N.J.5
  • 65
    • 77956684691 scopus 로고    scopus 로고
    • Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteins
    • Rutkevich LA, Cohen-Doyle MF, Brockmeier U & Williams DB (2009) Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteins. Mol Biol Cell 21, 3093-3105.
    • (2009) Mol Biol Cell , vol.21 , pp. 3093-3105
    • Rutkevich, L.A.1    Cohen-Doyle, M.F.2    Brockmeier, U.3    Williams, D.B.4
  • 66
    • 0036911213 scopus 로고    scopus 로고
    • A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins
    • Meunier L, Usherwood YK, Chung KT & Hendershot LM (2002) A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol Biol Cell 13, 4456-4469.
    • (2002) Mol Biol Cell , vol.13 , pp. 4456-4469
    • Meunier, L.1    Usherwood, Y.K.2    Chung, K.T.3    Hendershot, L.M.4
  • 67
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai B, Ye Y & Rapoport TA (2002) Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat Rev Mol Cell Biol 3, 246-255.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 246-255
    • Tsai, B.1    Ye, Y.2    Rapoport, T.A.3
  • 69
    • 48249117110 scopus 로고    scopus 로고
    • ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER
    • Ushioda R, Hoseki J, Araki K, Jansen G, Thomas DY & Nagata K (2008) ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER. Science 321, 569-572.
    • (2008) Science , vol.321 , pp. 569-572
    • Ushioda, R.1    Hoseki, J.2    Araki, K.3    Jansen, G.4    Thomas, D.Y.5    Nagata, K.6
  • 70
    • 27644436010 scopus 로고    scopus 로고
    • Mixed-disulfide folding intermediates between thyroglobulin and endoplasmic reticulum resident oxidoreductases ERp57 and protein disulfide isomerase
    • Di Jeso B, Park YN, Ulianich L, Treglia AS, Urbanas ML, High S & Arvan P (2005) Mixed-disulfide folding intermediates between thyroglobulin and endoplasmic reticulum resident oxidoreductases ERp57 and protein disulfide isomerase. Mol Cell Biol 25, 9793-9805.
    • (2005) Mol Cell Biol , vol.25 , pp. 9793-9805
    • Di Jeso, B.1    Park, Y.N.2    Ulianich, L.3    Treglia, A.S.4    Urbanas, M.L.5    High, S.6    Arvan, P.7
  • 71
    • 0344443678 scopus 로고    scopus 로고
    • EndoPDI, a novel protein-disulfide isomerase-like protein that is preferentially expressed in endothelial cells acts as a stress survival factor
    • Sullivan DC, Huminiecki L, Moore JW, Boyle JJ, Poulsom R, Creamer D, Barker J & Bicknell R (2003) EndoPDI, a novel protein-disulfide isomerase-like protein that is preferentially expressed in endothelial cells acts as a stress survival factor. J Biol Chem 278, 47079-47088.
    • (2003) J Biol Chem , vol.278 , pp. 47079-47088
    • Sullivan, D.C.1    Huminiecki, L.2    Moore, J.W.3    Boyle, J.J.4    Poulsom, R.5    Creamer, D.6    Barker, J.7    Bicknell, R.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.