메뉴 건너뛰기




Volumn 3, Issue 11, 2002, Pages 836-847

Formation and transfer of disulphide bonds in living cells

Author keywords

[No Author keywords available]

Indexed keywords

DISULFIDE;

EID: 0036842559     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm954     Document Type: Review
Times cited : (638)

References (128)
  • 2
    • 0034723368 scopus 로고    scopus 로고
    • Redox signaling in chloroplasts: Cleavage of disulfides by an iron-sulfur cluster
    • Dai S., Schwendtmayer C., Schurmann, P., Ramaswamy, S. & Eklund, H. Redox signaling in chloroplasts: Cleavage of disulfides by an iron-sulfur cluster. Science 287, 655-658 (2000).
    • (2000) Science , vol.287 , pp. 655-658
    • Dai, S.1    Schwendtmayer, C.2    Schurmann, P.3    Ramaswamy, S.4    Eklund, H.5
  • 3
    • 0025923587 scopus 로고
    • Regulation of C02 assimilation in oxygenic photosynthesis: The ferredoxin/thioredoxin system, Perspective on its discovery, present status, and future development
    • Buchanan, B. B. Regulation of C02 assimilation in oxygenic photosynthesis: the ferredoxin/thioredoxin system, Perspective on its discovery, present status, and future development. Arch. Biochem. Biophys. 288, 1-9 (1991).
    • (1991) Arch. Biochem. Biophys. , vol.288 , pp. 1-9
    • Buchanan, B.B.1
  • 4
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng, M., F. Åslund, R & Storz, G. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279, 1718-1721 (1998).
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Åslund, F.R.2    Storz, G.3
  • 5
    • 0033524938 scopus 로고    scopus 로고
    • Chaperone activity with a redox switch
    • Jakob, U., Muse, W., Eser, M. & Bardwell, J. C. Chaperone activity with a redox switch. Cell 96, 341-352 (1999).
    • (1999) Cell , vol.96 , pp. 341-352
    • Jakob, U.1    Muse, W.2    Eser, M.3    Bardwell, J.C.4
  • 6
    • 73649177752 scopus 로고
    • Acceleration of reactivation of reduced bovine pancreatic ribobonuclease by a microsomal system from rat liver
    • Gotberger, R. F., Epstein, C. J. & Anfinsen, C. B. Acceleration of reactivation of reduced bovine pancreatic ribobonuclease by a microsomal system from rat liver. J. Biol. Chem. 238, 628-635 (1963).
    • (1963) J. Biol. Chem. , vol.238 , pp. 628-635
    • Gotberger, R.F.1    Epstein, C.J.2    Anfinsen, C.B.3
  • 7
    • 0033210414 scopus 로고    scopus 로고
    • Protein disulfide isomerase: The multifunctional redox chaperone of the endoplasmic reticulum
    • Noiva, R. Protein disulfide isomerase: The multifunctional redox chaperone of the endoplasmic reticulum. Semin. Cell Dev. Biol. 10, 481-493 (1999).
    • (1999) Semin. Cell Dev. Biol. , vol.10 , pp. 481-493
    • Noiva, R.1
  • 8
    • 2442761708 scopus 로고    scopus 로고
    • The protein disulphide-isomerase family: Unravelling a string of folds
    • Ferrari, D. M. & Soling, H. D. The protein disulphide-isomerase family: Unravelling a string of folds. Biochem. J. 339, 1-10 (1999).
    • (1999) Biochem. J. , vol.339 , pp. 1-10
    • Ferrari, D.M.1    Soling, H.D.2
  • 9
    • 0036198797 scopus 로고    scopus 로고
    • Protein disulfide isomerases exploit synergy between catalytic and specific binding domains
    • Freedman, R. B., Klappa, P. & Ruddock, L. W, Protein disulfide isomerases exploit synergy between catalytic and specific binding domains. EMBO Rep. 3.136-140 (2002).
    • (2002) EMBO Rep. , vol.3 , pp. 136-140
    • Freedman, R.B.1    Klappa, P.2    Ruddock, L.W.3
  • 10
    • 0000942752 scopus 로고
    • ed. Pain, R. H. (Oxford Univ. Press, Oxford, UK)
    • Gilbert, H. F. in Mechanisms of Protein Folding (ed. Pain, R. H.) 104-135 (Oxford Univ. Press, Oxford, UK, 1994).
    • (1994) Mechanisms of Protein Folding , pp. 104-135
    • Gilbert, H.F.1
  • 11
    • 0025819371 scopus 로고
    • Redox properties and cross-linking of the dithiol/disulphide active sites of mammalian protein disulphide-isomerase
    • Hawkins, H. C., de Nardi, M. & Freedman, R. B. Redox properties and cross-linking of the dithiol/disulphide active sites of mammalian protein disulphide-isomerase. Biochem. J. 275, 341-348(1991).
    • (1991) Biochem. J. , vol.275 , pp. 341-348
    • Hawkins, H.C.1    De Nardi, M.2    Freedman, R.B.3
  • 12
    • 0027293791 scopus 로고
    • Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin
    • Lundstrom, J. & Holmgren, A. Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin. Biochemistry 32, 6649-6655(1993).
    • (1993) Biochemistry , vol.32 , pp. 6649-6655
    • Lundstrom, J.1    Holmgren, A.2
  • 13
    • 0031609760 scopus 로고    scopus 로고
    • The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
    • Frand, A. R. & Kaiser, C. A. The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum, Mol. Cell 1 161-170 (1998).
    • (1998) Mol. Cell , vol.1 , pp. 161-170
    • Frand, A.R.1    Kaiser, C.A.2
  • 14
    • 0031610364 scopus 로고    scopus 로고
    • Ero1p: A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum
    • Pollard, M. G., Travers, K. J. & Weissman, J. S. Ero1p: A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol. Cell 1, 171-182 (1998).
    • (1998) Mol. Cell , vol.1 , pp. 171-182
    • Pollard, M.G.1    Travers, K.J.2    Weissman, J.S.3
  • 15
    • 0033213605 scopus 로고    scopus 로고
    • Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum
    • Frand, A. R. & Kaiser, C. A. Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol. Cell 4, 469-477 (1999). This paper presents the first evidence for the direct flow of oxidizing equivalents from Ero1 to substrate proteins by PDI.
    • (1999) Mol. Cell , vol.4 , pp. 469-477
    • Frand, A.R.1    Kaiser, C.A.2
  • 16
    • 0034711439 scopus 로고    scopus 로고
    • Biochemical basis of oxidative protein folding in the endoplasmic reticulum
    • Tu, B. P., Ho-Schleyer, S. C., Travers, K. J. & Weissman, J.S. Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science 290, 1571-1574 (2000). This paper shows that oxidative protein folding in yeast is dependent on FAD levels and provides evidence that Ero1 binds FAD. The reconstitution of the eukaryotic ER pathway for protein disulphide-bond formation in vitro using FAD, Ero1 and PDI is also described.
    • (2000) Science , vol.290 , pp. 1571-1574
    • Tu, B.P.1    Ho-Schleyer, S.C.2    Travers, K.J.3    Weissman, J.S.4
  • 17
    • 0034494605 scopus 로고    scopus 로고
    • Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum
    • Frand, A. R. & Kaiser, C. A. Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum. Mol. Biol. Cell 11, 2833-2843 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2833-2843
    • Frand, A.R.1    Kaiser, C.A.2
  • 18
    • 0034681340 scopus 로고    scopus 로고
    • ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
    • Cabibbo, A. et al. ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum. J. Biol. Chem. 275, 4827-4833 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 4827-4833
    • Cabibbo, A.1
  • 19
    • 0034604675 scopus 로고    scopus 로고
    • Endoplasmic reticulum oxidoreductin 1-Lβ (ERO1-Lβ), a human gene induced in the course of the unfolded protein response
    • Pagani, M. et al. Endoplasmic reticulum oxidoreductin 1-Lβ (ERO1-Lβ), a human gene induced in the course of the unfolded protein response. J. Biol. Chem. 275, 23685-23692 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 23685-23692
    • Pagani, M.1
  • 20
    • 0035834372 scopus 로고    scopus 로고
    • The C-terminal domain of yeast Ero 1p mediates membrane localization and is essential for function
    • Pagani, M., Pilati, S., Bertoli, G., Valsasina, B. & Sitia, R. The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function. FEBS Lett. 508, 117-120 (2001).
    • (2001) FEBS Lett. , vol.508 , pp. 117-120
    • Pagani, M.1    Pilati, S.2    Bertoli, G.3    Valsasina, B.4    Sitia, R.5
  • 21
    • 0035890070 scopus 로고    scopus 로고
    • Manipulation of oxidative protein folding and PDI redox state in mammalian cells
    • Mezghrani, A. et al. Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO J. 20, 6288-6296 (2001). This article reports that mammalian Ero1 selectively oxidizes PDI, which, in turn, catalyses the formation of disulphide bonds in immunoglobulin subunits. The interesting observation that exogenous expression of active-site mutants of Ero1-Lα limits substrate protein oxidation is also presented.
    • (2001) EMBO J. , vol.20 , pp. 6288-6296
    • Mezghrani, A.1
  • 22
    • 0034282738 scopus 로고    scopus 로고
    • The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lα
    • Benham, A. M. et al. The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lα. EMBO J. 19, 4493-4502 (2000).
    • (2000) EMBO J. , vol.19 , pp. 4493-4502
    • Benham, A.M.1
  • 23
    • 0034790475 scopus 로고    scopus 로고
    • A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation
    • Sevier, C. S., Cuozzo, J. W., Vala, A., Åslund, F & Kaiser, C. A. A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation. Nature Cell Biol. 3, 874-882 (2001). This paper presents evidence for a second, Erol -independent oxidation pathway in yeast ER that uses the small ER oxidase Erv2 and PDI. This and reference 24 show that Erv2 is a flavoenzyme that uses the oxidizing potential of molecular oxygen to drive the formation of disulphide bonds.
    • (2001) Nature Cell Biol. , vol.3 , pp. 874-882
    • Sevier, C.S.1    Cuozzo, J.W.2    Vala, A.3    Åslund, F.4    Kaiser, C.A.5
  • 24
    • 0035968186 scopus 로고    scopus 로고
    • Yeast ERV2p is the first microsomal FAD-linked sulfhydryl oxidase of the Erv1p/Alrp protein family
    • Gerber, J., Muhlenhoff, U., Hofhaus, G., Liff, R. & Lisowsky, T. Yeast ERV2p is the first microsomal FAD-linked sulfhydryl oxidase of the Erv1p/Alrp protein family.. J. Biol. Chem. 276, 23485-23491 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 23485-23491
    • Gerber, J.1    Muhlenhoff, U.2    Hofhaus, G.3    Liff, R.4    Lisowsky, T.5
  • 25
    • 0036142325 scopus 로고    scopus 로고
    • A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p
    • Gross, E., Sevier, C. S., Vala, A., Kaiser, C, A. & Fass, D. A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Nature Struct. Biol. 9, 61-67 (2002).This paper presents the structural analysis of yeast Erv2. Structural and biochemical analysis indicates that Erv2 might use an internal thiol-transfer relay between two pairs of cysteines to facilitate the transfer of disulphide bonds to substrate proteins.
    • (2002) Nature Struct. Biol. , vol.9 , pp. 61-67
    • Gross, E.1    Sevier, C.S.2    Vala, A.3    Kaiser, C.A.4    Fass, D.5
  • 26
    • 0029828860 scopus 로고    scopus 로고
    • A sulfhydryl oxidase from chicken egg white
    • Hoober, K. L., Joneja, B., White, H. B. & Thorpe, C. A sulfhydryl oxidase from chicken egg white. J. Biol. Chem. 271, 30510-30516 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 30510-30516
    • Hoober, K.L.1    Joneja, B.2    White, H.B.3    Thorpe, C.4
  • 27
    • 0033527552 scopus 로고    scopus 로고
    • Homology between egg white sulfhydryl oxidase and quiescin Q6 defines a new class of flavin-linked sulfhydryl oxidases
    • Hoober, K. L., Glynn, N.M., Burnside, J., Coppock, D. L. & Thorpe, C. Homology between egg white sulfhydryl oxidase and quiescin Q6 defines a new class of flavin-linked sulfhydryl oxidases. J. Biol. Chem. 274, 31759-31762 (1999). This article shows that the flavin-dependent sulfhydryl oxidase from chicken egg white is homologous to the human protein quiescin Q6, thereby identifying a new family of cellular oxidases. See references 26, 28 and 29 for the biochemical characterization of the avian sulfhydryl oxidase.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31759-31762
    • Hoober, K.L.1    Glynn, N.M.2    Burnside, J.3    Coppock, D.L.4    Thorpe, C.5
  • 28
    • 0033529555 scopus 로고    scopus 로고
    • Sulfhydryl oxidase from egg white. A facile catalyst for disulfide bond formation in proteins and peptides
    • Hoober, K. L., Sheasley, S. L., Gilbert, H. F. &Thorpe, C, Sulfhydryl oxidase from egg white. A facile catalyst for disulfide bond formation in proteins and peptides. J. Biol. Chem. 274, 22147-22150(1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 22147-22150
    • Hoober, K.L.1    Sheasley, S.L.2    Gilbert, H.F.3    Thorpe, C.4
  • 29
    • 0033537679 scopus 로고    scopus 로고
    • Egg white sulfhydryl oxidase: Kinetic mechanism of the catalysis of disulfide bond formation
    • Hoober, K, L. & Thorpe, C. Egg white sulfhydryl oxidase: Kinetic mechanism of the catalysis of disulfide bond formation. Biochemistry 38, 3211-3217 (1999).
    • (1999) Biochemistry , vol.38 , pp. 3211-3217
    • Hoober, K.L.1    Thorpe, C.2
  • 30
    • 0036224573 scopus 로고    scopus 로고
    • Oxidative protein folding in bacteria
    • Collet, J. F. & Bardwell, J. C. Oxidative protein folding in bacteria. Mol. Microbiol. 44, 1-8 (2002). This paper and reference 31 provide the most recent reviews focused on the bacterial disulphide-bond formation and isomerization pathways. See the references in these reviews for a more detailed discussion of the history of the identification of the bacterial enzymes for disulphide-bond formation.
    • (2002) Mol. Microbiol. , vol.44 , pp. 1-8
    • Collet, J.F.1    Bardwell, J.C.2
  • 31
    • 0034770083 scopus 로고    scopus 로고
    • Roles of thiol-redox pathways in bacteria
    • Ritz, D. & Beckwith, J. Roles of thiol-redox pathways in bacteria. Annu. Rev. Microbiol. 55, 21-48 (2001).
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 21-48
    • Ritz, D.1    Beckwith, J.2
  • 32
    • 0034115404 scopus 로고    scopus 로고
    • Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli
    • Fabianek, R. A., Hennecke, H. & Thöny-Meyer, L. Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli. FEMS Microbiol. Rev. 24, 303-316 (2000).
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 303-316
    • Fabianek, R.A.1    Hennecke, H.2    Thöny-Meyer, L.3
  • 33
    • 0032720032 scopus 로고    scopus 로고
    • Electron avenue: Pathways of disulfide bond formation and isomerization
    • Debarbieux, L. & Beckwith, J. Electron avenue: Pathways of disulfide bond formation and isomerization. Cell 99, 117-119 (1999).
    • (1999) Cell , vol.99 , pp. 117-119
    • Debarbieux, L.1    Beckwith, J.2
  • 34
    • 0028971218 scopus 로고
    • Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA
    • Guilhot, C., Jander, G., Martin, N. L. & Beckwith, J. Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA. Proc. Natl. Acad. Sci. USA 92, 9895-9899 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9895-9899
    • Guilhot, C.1    Jander, G.2    Martin, N.L.3    Beckwith, J.4
  • 35
    • 0028948780 scopus 로고
    • Redox states of DsbA in the periplasm of Escherichia coli
    • Kishigami, S., Akiyama, Y. & Ito, K. Redox states of DsbA in the periplasm of Escherichia coli. FEBS Lett. 364, 55-58(1995).
    • (1995) FEBS Lett. , vol.364 , pp. 55-58
    • Kishigami, S.1    Akiyama, Y.2    Ito, K.3
  • 36
    • 0028979629 scopus 로고
    • Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli
    • Missiakas, D., Schwager, F. & Raina, S. Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. EMBO J. 14, 3415-3424 (1995),
    • (1995) EMBO J. , vol.14 , pp. 3415-3424
    • Missiakas, D.1    Schwager, F.2    Raina, S.3
  • 37
    • 0030668672 scopus 로고    scopus 로고
    • Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin
    • Rietsch,A., Bessette, P, Georgiou, G. & Beckwith, J. Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. J. Bacteriol. 179, 6602-6608 (1997).
    • (1997) J. Bacteriol. , vol.179 , pp. 6602-6608
    • Rietsch, A.1    Bessette, P.2    Georgiou, G.3    Beckwith, J.4
  • 38
    • 0034703766 scopus 로고    scopus 로고
    • Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade
    • Katzen, F. & Beckwith, J. Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade. Cell 103, 769-779 (2000). This article probes the mechanism of the thiol-disulphide oxidoreductase DsbD and provides an elegant example of the intra-protein transfer of disulphide bonds that seems be important in the function of several proteins involved in cellular protein oxidation and reduction.
    • (2000) Cell , vol.103 , pp. 769-779
    • Katzen, F.1    Beckwith, J.2
  • 39
    • 0035793545 scopus 로고    scopus 로고
    • DsbD-catalyzed transport of electrons across the membrane of Escherichia coli
    • Krupp, R., Chan, C. & Missiakas, D. DsbD-catalyzed transport of electrons across the membrane of Escherichia coli. J. Biol. Chem. 276, 3696-3701 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 3696-3701
    • Krupp, R.1    Chan, C.2    Missiakas, D.3
  • 40
    • 0037178798 scopus 로고    scopus 로고
    • Reconstitution of a disulfide isomerization system
    • Collet, J. F., Riemer, J., Bader, M. W. & Bardwell, J. C. Reconstitution of a disulfide isomerization system. J. Biol. Chem. 277, 26886-26892 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 26886-26892
    • Collet, J.F.1    Riemer, J.2    Bader, M.W.3    Bardwell, J.C.4
  • 41
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell, J. C., McGovern, K. & Beckwith, J. Identification of a protein required for disulfide bond formation in vivo. Cell 67, 581-589 (1991). This paper reports the initial identification of DsbA, providing the first evidence that the formation of protein disulphide bonds in bacteria is a catalysed process.
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.1    McGovern, K.2    Beckwith, J.3
  • 42
    • 0028850389 scopus 로고
    • Human protein disulfide isomerase functionally complements a dsbA mutation and enhances the yield of pectate lyase C in Escherichia coli
    • Humphreys, D. P., Weir, N., Mountain, A. & Lund, P. A. Human protein disulfide isomerase functionally complements a dsbA mutation and enhances the yield of pectate lyase C in Escherichia coli. J. Biol. Chem. 270, 28210-28215(1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 28210-28215
    • Humphreys, D.P.1    Weir, N.2    Mountain, A.3    Lund, P.A.4
  • 43
    • 0027475212 scopus 로고
    • A pathway for disulfide bond formation in vivo
    • Bardwell, J. C. et al. A pathway for disulfide bond formation in vivo. Proc. NatlAcad. Sci. USA 90, 1038-1042 (1993).
    • (1993) Proc. NatlAcad. Sci. USA , vol.90 , pp. 1038-1042
    • Bardwell, J.C.1
  • 44
    • 0028154918 scopus 로고
    • Two cysteines in each pedplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation
    • Jander, G., Martin, N. L. & Beckwith, J. Two cysteines in each pedplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation. EMBO J. 13, 5121-5127 (1994).
    • (1994) EMBO J. , vol.13 , pp. 5121-5127
    • Jander, G.1    Martin, N.L.2    Beckwith, J.3
  • 45
    • 0030072669 scopus 로고    scopus 로고
    • Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coli
    • Kishigami, S. & lto, K. Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coli. Genes Cells 1, 201-208 (1996).
    • (1996) Genes Cells , vol.1 , pp. 201-208
    • Kishigami, S.1    Ito, K.2
  • 46
    • 0034718489 scopus 로고    scopus 로고
    • Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli
    • Kadokura, H., Bader, M., Tian, H., Bardwell, J. C. & Beckwith, J. Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli. Proc. Natl. Acad. Sci. USA 97, 10884-10889 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10884-10889
    • Kadokura, H.1    Bader, M.2    Tian, H.3    Bardwell, J.C.4    Beckwith, J.5
  • 47
    • 0033230589 scopus 로고    scopus 로고
    • Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli
    • Stewart, E. J., Katzen, F. & Beckwith, J. Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli. EMBO J. 18, 5963-5971 (1999).
    • (1999) EMBO J. , vol.18 , pp. 5963-5971
    • Stewart, E.J.1    Katzen, F.2    Beckwith, J.3
  • 48
    • 0034011364 scopus 로고    scopus 로고
    • Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm
    • Chung, J., Chen, T. & Missiakas, D. Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm. Mol. Microbiol. 35, 1099-1109 (2000).
    • (2000) Mol. Microbiol. , vol.35 , pp. 1099-1109
    • Chung, J.1    Chen, T.2    Missiakas, D.3
  • 49
    • 0034099457 scopus 로고    scopus 로고
    • Escherichia coli DipZ: Anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function
    • Gordon, E. H., Page, M. D., Willis, A. C. & Ferguson, S. J. Escherichia coli DipZ: Anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function. Mol. Microbiol. 35, t360-1374 (2000).
    • (2000) Mol. Microbiol. , vol.35 , pp. 1360-1374
    • Gordon, E.H.1    Page, M.D.2    Willis, A.C.3    Ferguson, S.J.4
  • 50
    • 0035859924 scopus 로고    scopus 로고
    • DsbC activation by the N-terminal domain of DsbD
    • Goldstone, D. et al. DsbC activation by the N-terminal domain of DsbD. Proc. NatlAcad. Sci. USA 98, 9551-9556 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9551-9556
    • Goldstone, D.1
  • 51
    • 0037093512 scopus 로고    scopus 로고
    • Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA
    • Kadokura, H. & Beckwith, J. Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA. EMBO J. 21, 2354-2363 (2002). This study shows the direct flow of electrons between the two pairs of cysteines in DsbB, and between the cysteines in DsbB and DsbA. See also references 34 and 35 for the original observations of a direct interaction between DsbA and DsbB, and the recent references 84 and 85, which report the redox potentials for the DsbB cysteine pairs.
    • (2002) EMBO J. , vol.21 , pp. 2354-2363
    • Kadokura, H.1    Beckwith, J.2
  • 52
    • 0030851338 scopus 로고    scopus 로고
    • The genome of Molluscum contagiosum virus: Analysis and comparison with other poxviruses
    • Senkevich, T. G., Koonin, E. V., Bugert, J. J., Darai, G. & Moss, B. The genome of Molluscum contagiosum virus: Analysis and comparison with other poxviruses. Virology 233, 19-42 (1997).
    • (1997) Virology , vol.233 , pp. 19-42
    • Senkevich, T.G.1    Koonin, E.V.2    Bugert, J.J.3    Darai, G.4    Moss, B.5
  • 53
    • 0037076339 scopus 로고    scopus 로고
    • Complete pathway for protein disulfide bond formation encoded by poxviruses
    • Senkevich, T. G., White, C. L., Koonin, E. V. & Moss, B. Complete pathway for protein disulfide bond formation encoded by poxviruses. Proc. Natl. Acad. Sci. USA 99, 6667-6672 (2002). This paper shows that three cytoplasmic thiol-disulphide oxidoreductases (E10R, A2.SL and G4L) encoded by vaccinia virus cooperate in a cytosolic pathway for the formation of disulphide bonds in virion proteins. See also references 52, 70, 71 and 110 .
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6667-6672
    • Senkevich, T.G.1    White, C.L.2    Koonin, E.V.3    Moss, B.4
  • 54
    • 0029165589 scopus 로고
    • Thioredoxin - A fold for all reasons
    • Martin, J. L. Thioredoxin - A fold for all reasons. Structure 3, 245-250 (1995).
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 55
    • 0034048647 scopus 로고    scopus 로고
    • Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli
    • McCarthy, A. A. et al. Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli. Nature Struct. Biol. 7, 196-199 (2000).
    • (2000) Nature Struct. Biol. , vol.7 , pp. 196-199
    • McCarthy, A.A.1
  • 56
    • 0037018912 scopus 로고    scopus 로고
    • Thiol-disulfide exchange in an immunoglobulin-like fold: Structure of the N-terminal domain of DsbD
    • Goulding, C .W. et al.Thiol-disulfide exchange in an immunoglobulin-like fold: Structure of the N-terminal domain of DsbD. Biochemistry 41, 6920-6927 (2002).
    • (2002) Biochemistry , vol.41 , pp. 6920-6927
    • Goulding, C.W.1
  • 57
    • 0027373949 scopus 로고
    • Crystal structure of the DsbA protein required for disulphide bond formation in vivo
    • Martin, J. L., Bardwell, J. C. & Kuriyan, J. Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Nature 365, 464-468 (1993).
    • (1993) Nature , vol.365 , pp. 464-468
    • Martin, J.L.1    Bardwell, J.C.2    Kuriyan, J.3
  • 58
    • 0035972295 scopus 로고    scopus 로고
    • Functional differences in yeast protein disulfide isomerases
    • NØrgaard, R et al. Functional differences in yeast protein disulfide isomerases. J. Cell Biol. 152, 553-562 (2001). This study addresses the functional differences between yeast PDI and the four yeast PDI homologues, and illustrates some of the difficulties in sorting out the overlapping functions of the PDI homologues.
    • (2001) J. Cell Biol. , vol.152 , pp. 553-562
    • NØrgaard, R.1
  • 59
    • 0037083869 scopus 로고    scopus 로고
    • ERp 44, a novel endoplasmic reticulum folding assistant of the thioredoxin family
    • Anelli, T. et al. ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family. EMBO J. 21, 835844(2002).
    • (2002) EMBO J. , vol.21 , pp. 835844
    • Anelli, T.1
  • 60
    • 0036671471 scopus 로고    scopus 로고
    • Cytochrome c maturation: A complex pathway for a simple task?
    • Thöny-Meyer, L. Cytochrome c maturation: A complex pathway for a simple task? Biochem. Soc. Trans Trar)s. 30, 633-638(2002).
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 633-638
    • Thöny-Meyer, L.1
  • 61
    • 0036682611 scopus 로고    scopus 로고
    • Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD
    • Katzen, F., Deshmukh, M., Daldal, F & Beckwith, J. Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD. EMBO J. 21. 3960-3969 (2002).
    • (2002) EMBO J. , vol.21 , pp. 3960-3969
    • Katzen, F.1    Deshmukh, M.2    Daldal, F.3    Beckwith, J.4
  • 62
    • 0030787850 scopus 로고    scopus 로고
    • In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC
    • Joly, J. C.& Swartz, J. R. In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC. Biochemistry 36, 10067-10072 (1997).
    • (1997) Biochemistry , vol.36 , pp. 10067-10072
    • Joly, J.C.1    Swartz, J.R.2
  • 63
    • 0034714289 scopus 로고    scopus 로고
    • Disulfide bonds are generated by quinone reduction
    • Bader, M. W., Xie, T., Yu, C. A. & Bardwell, J. C. Disulfide bonds are generated by quinone reduction. J. Biol. Chem. 275, 26082-26088(2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 26082-26088
    • Bader, M.W.1    Xie, T.2    Yu, C.A.3    Bardwell, J.C.4
  • 64
    • 0035794534 scopus 로고    scopus 로고
    • Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA
    • Bader, M. W. et al. Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA. EMBOJ. 20, 1555-1562 (2001), This article proposes that the lack of cross-talk between the bacterial oxidation and isomerization pathways is a result of the dimerization of the DsbC isomerase/reductase enzyme. The dimerization of DsbC is suggested to insulate the active sites from recognition by DsbB, preventing misoxidation of DsbC by DsbB.
    • (2001) EMBO J. , vol.20 , pp. 1555-1562
    • Bader, M.W.1
  • 65
    • 0018561484 scopus 로고
    • Studies on the nature and regulation of the cellular thio:disulphide potential
    • Ziegler, D. M., Duffel, M,W. & Poulsen, L. L. Studies on the nature and regulation of the cellular thio:disulphide potential. Ciba Found. Symp. 72, 191-204 (1979),
    • (1979) Ciba Found. Symp. , vol.72 , pp. 191-204
    • Ziegler, D.M.1    Duffel, M.W.2    Poulsen, L.L.3
  • 66
    • 0026547487 scopus 로고
    • Stimulation of the dithiol-dependent reductases in the vitamin K cycle by the thioredoxin system. Strong synergistic effects with protein disulphide-isomerase
    • Soute, B. A., Groenen-van Dooren,M.M., Holmgren,A., Lundstrom, J. & Vermeer, C. Stimulation of the dithiol-dependent reductases in the vitamin K cycle by the thioredoxin system. Strong synergistic effects with protein disulphide-isomerase. Biochem. J. 281, 255-259 (1992).
    • (1992) Biochem. J. , vol.281 , pp. 255-259
    • Soute, B.A.1    Groenen-van Dooren, M.M.2    Holmgren, A.3    Lundstrom, J.4    Vermeer, C.5
  • 67
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang, C., Sinskey, A. J. & Lodish, H. F. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257, 1495-1502 (1992).
    • (1992) Science , vol.257 , pp. 1495-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 68
    • 0027171355 scopus 로고
    • On the biosynthesis of bovine pancreatic trypsin inhibitor (BPTI). Structure, processing, folding and disulphide bond formation of the precursor in vitro and in microsomes
    • Creighton, T.E. et al. On the biosynthesis of bovine pancreatic trypsin inhibitor (BPTI). Structure, processing, folding and disulphide bond formation of the precursor in vitro and in microsomes. J. Mol. Biol. 232, 1176-1196(1993).
    • (1993) J. Mol. Biol. , vol.232 , pp. 1176-1196
    • Creighton, T.E.1
  • 69
    • 0033601739 scopus 로고    scopus 로고
    • An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins
    • Locker, J. K. & Griffiths, G. An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins. J. Cell Biol. 144, 267-279 (1999).
    • (1999) J. Cell Biol. , vol.144 , pp. 267-279
    • Locker, J.K.1    Griffiths, G.2
  • 70
    • 0034710899 scopus 로고    scopus 로고
    • A viral member of the ERVI/ALR protein family participates in a cytoplasmic pathway of disulfide bond formation
    • Senkevich, T. G., White, C. L., Koonin, E. V & Moss, B. A viral member of the ERVI/ALR protein family participates in a cytoplasmic pathway of disulfide bond formation. Proc. Natl. Acad. Sci. USA 97, 12068-12073 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12068-12073
    • Senkevich, T.G.1    White, C.L.2    Koonin, E.V.3    Moss, B.4
  • 71
    • 0036140130 scopus 로고    scopus 로고
    • Vaccinia virus G 4L glutaredoxin is an essential intermediate of a cytoplasmic disulfide bond pathway required for virion assembly
    • White, C. L., Senkevich, T. G. & Moss, B. Vaccinia virus G4L glutaredoxin is an essential intermediate of a cytoplasmic disulfide bond pathway required for virion assembly. J. Virol. 76, 467-472(2002).
    • (2002) J. Virol. , vol.76 , pp. 467-472
    • White, C.L.1    Senkevich, T.G.2    Moss, B.3
  • 72
    • 0033163758 scopus 로고    scopus 로고
    • Competition between glutathione and protein thiols for disulphide bond formation
    • Cuozzo, J. W,& Kaiser, C. A. Competition between glutathione and protein thiols for disulphide bond formation. Nature Cell Biol. 1, 130-135 (1999), This study shows that glutathione is not the predominant source of oxidizing equivalents for the formation of disulphide bonds in proteins in the ER. Instead, it indicates that cellular glutathione might function as a net reductant of the ER, and might protect the ER against transient hyperoxidizing conditions.
    • (1999) Nature Cell Biol. , vol.1 , pp. 130-135
    • Cuozzo, J.W.1    Kaiser, C.A.2
  • 73
    • 0032566485 scopus 로고    scopus 로고
    • Chromatographic determination of flavin derivatives in baker's yeast
    • Gliszczynska, A. & Koziolowa, A. Chromatographic determination of flavin derivatives in baker's yeast. J. Chromatogr. A 822, 59-66 (1998).
    • (1998) J. Chromatogr. A , vol.822 , pp. 59-66
    • Gliszczynska, A.1    Koziolowa, A.2
  • 74
    • 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. et al. 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).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11857-11862
    • Kobayashi, T.1
  • 75
    • 0033597878 scopus 로고    scopus 로고
    • Oxidative protein folding is driven by the electron transport system
    • Bader, M., Muse, W., Ballou, D. R, Gassner, C. & Bardwell, J. C. Oxidative protein folding is driven by the electron transport system. Cell 98, 217-227 (1999). This paper, along with references 63 and 74, shows that the bacterial periplasmic disulphide-bond formation pathway derives oxidizing equivalents from the cellular electron-transport system.
    • (1999) Cell , vol.98 , pp. 217-227
    • Bader, M.1    Muse, W.2    Ballou, D.R.3    Gassner, C.4    Bardwell, J.C.5
  • 76
    • 0032562757 scopus 로고    scopus 로고
    • Reconstitution of a protein disulfide catalytic system
    • Bader, M., Muse, W., Zander, T. & Bardwell, J. Reconstitution of a protein disulfide catalytic system. J. Biol. Chem. 273, 10392-10397 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 10392-10397
    • Bader, M.1    Muse, W.2    Zander, T.3    Bardwell, J.4
  • 77
    • 0000519682 scopus 로고
    • Reduction potential of glutathione
    • Rost, J. & Rapoport, S. Reduction potential of glutathione. Nature 201, 185-187 (1964).
    • (1964) Nature , vol.201 , pp. 185-187
    • Rost, J.1    Rapoport, S.2
  • 78
    • 33847087446 scopus 로고
    • Rate constants and equilibrium constants for thiol-disulfide interchange reactions involving oxidized glutathione
    • Szajewski, R, R & Whitesides, G. M. Rate constants and equilibrium constants for thiol-disulfide interchange reactions involving oxidized glutathione, J. Am. Chem. Soc. 102, 2011-2025 (1980).
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 2011-2025
    • Szajewski, R.R.1    Whitesides, G.M.2
  • 79
    • 0025914427 scopus 로고
    • Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin
    • Krause, G., Lundstrom, J., Barea, J. L., Pueyo de la Cuesta, C. & Holmgren, A. Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin. J. Biol. Chem. 266, 9494 -9500 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 9494-9500
    • Krause, G.1    Lundstrom, J.2    Barea, J.L.3    Pueyo de la Cuesta, C.4    Holmgren, A.5
  • 80
    • 0028949156 scopus 로고
    • Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli
    • Zapun, A., Missiakas, D., Raina, S. & Creighton, T. E. Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. Biochemistry 34, 5075-5089 (1995).
    • (1995) Biochemistry , vol.34 , pp. 5075-5089
    • Zapun, A.1    Missiakas, D.2    Raina, S.3    Creighton, T.E.4
  • 81
    • 0027481123 scopus 로고
    • Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli
    • Wunderlich, M. & Glockshuber, R. Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli. Protein Sci. 2, 717-726 (1993).
    • (1993) Protein Sci. , vol.2 , pp. 717-726
    • Wunderlich, M.1    Glockshuber, R.2
  • 82
    • 0027254133 scopus 로고
    • The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo
    • Zapun, A., Bardwell, J. C. & Creighton, T. E. The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. Biochemistry 32, 5083-5092 (1993).
    • (1993) Biochemistry , vol.32 , pp. 5083-5092
    • Zapun, A.1    Bardwell, J.C.2    Creighton, T.E.3
  • 84
    • 0037013828 scopus 로고    scopus 로고
    • Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade
    • Inaba, K. & Ito, K, Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade. EMBOJ. 21, 2646-2654 (2002).
    • (2002) EMBO J. , vol.21 , pp. 2646-2654
    • Inaba, K.1    Ito, K.2
  • 85
    • 0037031882 scopus 로고    scopus 로고
    • DsbB catalyzes disulfide bond formation de novo
    • Regeimbal, J. M. & Bardwell, J. C. DsbB catalyzes disulfide bond formation de novo. J. Biol. Chem. 277, 32706-32713 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 32706-32713
    • Regeimbal, J.M.1    Bardwell, J.C.2
  • 86
    • 0029822654 scopus 로고    scopus 로고
    • An in vivo pathway for disulfide bond isomerization in Escherichia coli
    • Rietsch, A., Belin, D., Martin, N. & Beckwith, J. An in vivo pathway for disulfide bond isomerization in Escherichia coli. Proc. Natl. Acad. Sci. USA 93, 13048-13053 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13048-13053
    • Rietsch, A.1    Belin, D.2    Martin, N.3    Beckwith, J.4
  • 87
    • 0032189925 scopus 로고    scopus 로고
    • Disulfide bond formation in the Escherichia coli cytoplasm: An in vivo role reversal for the thioredoxins
    • Stewart, E. J., Åslund, F. & Beckwith, J. Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins. EMBOJ, 17, 5543-5550(1998).
    • (1998) EMBO J. , vol.17 , pp. 5543-5550
    • Stewart, E.J.1    Åslund, F.2    Beckwith, J.3
  • 88
    • 0034673562 scopus 로고    scopus 로고
    • Regulation of the quiescence-induced genes: Quiescin Q6, decorin, and ribosomal protein S29
    • Coppock, D., Kopman,C.,Gudas, J. & Cina-Poppe, D.A. Regulation of the quiescence-induced genes: Quiescin Q6, decorin, and ribosomal protein S29. Biochem. Biophys. Res. Commun. 269, 604-610 (2000).
    • (2000) Biochem. Biophys. Res. Commun. , vol.269 , pp. 604-610
    • Coppock, D.1    Kopman, C.2    Gudas, J.3    Cina-Poppe, D.A.4
  • 89
    • 0034866458 scopus 로고    scopus 로고
    • An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins
    • Lange, H. et al. An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins. EMBO Rep. 2, 715-720 (2001).
    • (2001) EMBO Rep. , vol.2 , pp. 715-720
    • Lange, H.1
  • 90
    • 0027514241 scopus 로고
    • Functional replacement of the Saccharomyces cerevisiae Trg1/Pdi1 protein by members of the mammalian protein disulfide isomerase family
    • Günther, R, et al, Functional replacement of the Saccharomyces cerevisiae Trg1/Pdi1 protein by members of the mammalian protein disulfide isomerase family. J. Biol. Chem. 268, 7728-7732 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 7728-7732
    • Günther, R.1
  • 91
    • 0029899087 scopus 로고    scopus 로고
    • ERp60 does not substitute for protein disulphide isomerase as the β-subunit of prolyl 4-hydroxylase
    • Koivunen, P. et al. ERp60 does not substitute for protein disulphide isomerase as the β-subunit of prolyl 4-hydroxylase. Biochem. J. 316, 599-605 (1996).
    • (1996) Biochem. J. , vol.316 , pp. 599-605
    • Koivunen, P.1
  • 92
    • 0031035644 scopus 로고    scopus 로고
    • Interaction of the thiol-dependent reductase ERp 57 with nascent glycoproteins
    • Oliver, J, D., van der Wal, F. J., Bulleid, N. J. & High, S. Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science 275, 86-88 (1997).
    • (1997) Science , vol.275 , pp. 86-88
    • Oliver, J.D.1    Van der Wal, F.J.2    Bulleid, N.J.3    High, S.4
  • 93
    • 0033523910 scopus 로고    scopus 로고
    • Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells
    • Molinari, M. & Helenius, A. Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells. Nature 402, 90-93 (1999).
    • (1999) Nature , vol.402 , pp. 90-93
    • Molinari, M.1    Helenius, A.2
  • 94
    • 0030934557 scopus 로고    scopus 로고
    • Molecular characterization of a pancreas-specific protein disulfide isomerase, PDIp
    • Desilva, M. G., Notkins, A. L. & Lan, M. S. Molecular characterization of a pancreas-specific protein disulfide isomerase, PDIp. DNA Cell Biol. 16, 269-274 (1997).
    • (1997) DNA Cell Biol. , vol.16 , pp. 269-274
    • Desilva, M.G.1    Notkins, A.L.2    Lan, M.S.3
  • 95
    • 0029590754 scopus 로고
    • Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase
    • Darby, N. J. & Creighton, T. E. Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase. Biochemistry 34, 16770-16780(1995).
    • (1995) Biochemistry , vol.34 , pp. 16770-16780
    • Darby, N.J.1    Creighton, T.E.2
  • 96
    • 0032512878 scopus 로고    scopus 로고
    • The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency
    • Darby, N. J., Penka, E. & Vincentelli, R. The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency. J. Mol. Biol. 276, 239-247 (1998).
    • (1998) J. Mol. Biol. , vol.276 , pp. 239-247
    • Darby, N.J.1    Penka, E.2    Vincentelli, R.3
  • 97
    • 0028885790 scopus 로고
    • The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds
    • Laboissiere, M. C., Sturley, S. L. & Raines, R. T. The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J. Biol. Chem. 270, 28006-28009 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 28006-28009
    • Laboissiere, M.C.1    Sturley, S.L.2    Raines, R.T.3
  • 98
    • 0030061006 scopus 로고    scopus 로고
    • Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine
    • Walker, K. W., Lyles, M. M. & Gilbert, H. F. Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine. Biochemistry 35, 1972-1980 (1996).
    • (1996) Biochemistry , vol.35 , pp. 1972-1980
    • Walker, K.W.1    Lyles, M.M.2    Gilbert, H.F.3
  • 99
    • 0035881866 scopus 로고    scopus 로고
    • Mutation of yeast Eug1p CXXS active sites to CXXC results in a dramatic increase in protein disulphide isomerase activity
    • NØrgaard, R & Winther, J. R. Mutation of yeast Eug1 p CXXS active sites to CXXC results in a dramatic increase in protein disulphide isomerase activity. Biochem. J. 358, 269-274 (2001).
    • (2001) Biochem. J. , vol.358 , pp. 269-274
    • NØrgaard, R.1    Winther, J.R.2
  • 100
    • 0032535351 scopus 로고    scopus 로고
    • The quiescin Q6 gene (QSCN6) is a fusion of two ancient gene families: Thioredoxin and ERV1
    • Coppock, D. L., Cina-Poppe, D. & Gilleran, S. The quiescin Q6 gene (QSCN6) is a fusion of two ancient gene families: Thioredoxin and ERV1. Genomics 54, 460-468 (1998).
    • (1998) Genomics , vol.54 , pp. 460-468
    • Coppock, D.L.1    Cina-Poppe, D.2    Gilleran, S.3
  • 101
  • 102
    • 0027930477 scopus 로고
    • Augmenter of liver regeneration: Its place in the universe of hepatic growth factors
    • Francavillia, A. et al. Augmenter of liver regeneration: Its place in the universe of hepatic growth factors. Hepatology 20, 747-757 (1994).
    • (1994) Hepatology , vol.20 , pp. 747-757
    • Francavillia, A.1
  • 103
    • 0028122426 scopus 로고
    • Cloning and sequence analysis of the rat augmenter of liver regeneration (ALR) gene: Expression of biologically active recombinant ALR and demonstration of tissue distribution
    • , Hagiya, M. et al. Cloning and sequence analysis of the rat augmenter of liver regeneration (ALR) gene: Expression of biologically active recombinant ALR and demonstration of tissue distribution. Proc. Natl. Acad. Sci. USA 91, 8142-8146 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8142-8146
    • Hagiya, M.1
  • 104
    • 0035076003 scopus 로고    scopus 로고
    • Mammalian augmenter of liver regeneration protein is a sulfhydryl oxidase
    • Lisowsky, T., Lee, J. E., Polimeno, L., Francavilla, A. & Hofhaus, G. Mammalian augmenter of liver regeneration protein is a sulfhydryl oxidase. Dig. Liver Dis. 33, 173-180 (2001).
    • (2001) Dig. Liver Dis. , vol.33 , pp. 173-180
    • Lisowsky, T.1    Lee, J.E.2    Polimeno, L.3    Francavilla, A.4    Hofhaus, G.5
  • 105
    • 0035958044 scopus 로고    scopus 로고
    • Rat seminal vesicle FAD-dependent sulfhydryl oxidase. Biochemical characterization and molecular cloning of a member of the new sulfhydryl oxidase/qulescin Q6 gene family
    • Benayoun, B., Esnard-Feve, A., Castella, S., Courty, Y. & Esnard, F. Rat seminal vesicle FAD-dependent sulfhydryl oxidase. Biochemical characterization and molecular cloning of a member of the new sulfhydryl oxidase/qulescin Q6 gene family, J. Biol. Chem. 276, 13830-13837 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 13830-13837
    • Benayoun, B.1    Esnard-Feve, A.2    Castella, S.3    Courty, Y.4    Esnard, F.5
  • 106
    • 0035860281 scopus 로고    scopus 로고
    • Identification and expression of a new sulfhydryl oxidase SOx-3 during the cell cycle and the estrus cycle in uterine cells
    • Musard, J. F. et al, Identification and expression of a new sulfhydryl oxidase SOx-3 during the cell cycle and the estrus cycle in uterine cells. Biochem. Biophys. Res, Commun. 287, 83-91 (2001).
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 83-91
    • Musard, J.F.1
  • 107
    • 0034647976 scopus 로고    scopus 로고
    • Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase
    • Lee, J., Hofhaus, G. & Lisowsky, T. Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase. FEBS Lett. 477, 62-66 (2000).
    • (2000) FEBS Lett. , vol.477 , pp. 62-66
    • Lee, J.1    Hofhaus, G.2    Lisowsky, T.3
  • 108
    • 0026544596 scopus 로고
    • Dual function of a new nuclear gene for oxidative phosphorylation and vegetative growth in yeast
    • Lisowsky, T. Dual function of a new nuclear gene for oxidative phosphorylation and vegetative growth in yeast. Mol. Gen. Genet. 232, 58-64 (1992).
    • (1992) Mol. Gen. Genet. , vol.232 , pp. 58-64
    • Lisowsky, T.1
  • 109
    • 0032986628 scopus 로고    scopus 로고
    • Highly divergent amino termini of the homologous human ALR and yeast scERV1 gene products define species specific differences in cellular localization
    • Hofhaus, G., Stein, G., Polimeno, L., Francavilla, A. & Lisowsky, T. Highly divergent amino termini of the homologous human ALR and yeast scERV1 gene products define species specific differences in cellular localization. Eur. J. Cell Biol. 78, 349-356 (1999).
    • (1999) Eur. J. Cell Biol. , vol.78 , pp. 349-356
    • Hofhaus, G.1    Stein, G.2    Polimeno, L.3    Francavilla, A.4    Lisowsky, T.5
  • 110
    • 0034610226 scopus 로고    scopus 로고
    • Vaccinia virus E 1OR protein is associated with the membranes of intracellular mature virions and has a role in morphogenesis
    • Senkevich, T. G., Weisberg, A. S. & Moss, B. Vaccinia virus E1OR protein is associated with the membranes of intracellular mature virions and has a role in morphogenesis. Virology 278, 244-252 (2000).
    • (2000) Virology , vol.278 , pp. 244-252
    • Senkevich, T.G.1    Weisberg, A.S.2    Moss, B.3
  • 111
    • 0022387362 scopus 로고
    • Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin
    • Edman, J. C., Ellis, L., Blacher, R. W., Roth, R. A. & Rutter, W. J. Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature 317, 267-270 (1985).
    • (1985) Nature , vol.317 , pp. 267-270
    • Edman, J.C.1    Ellis, L.2    Blacher, R.W.3    Roth, R.A.4    Rutter, W.J.5
  • 112
    • 0032481380 scopus 로고    scopus 로고
    • The b'domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins
    • Klappa, P., Ruddock, L. W, Darby, N. J. & Freedman, R. B. The b'domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins. EMBOJ. 17, 927-935 (1998).
    • (1998) EMBO J. , vol.17 , pp. 927-935
    • Klappa, P.1    Ruddock, L.W.2    Darby, N.J.3    Freedman, R.B.4
  • 113
    • 0028823248 scopus 로고
    • Molecular cloning of the human glucose-regulated protein ERp57/GRP58, a thiol-dependent reductase. Identification of its secretory form and inducible expression by the oncogenic transformation
    • Hirano, N. et al. Molecular cloning of the human glucose-regulated protein ERp57/GRP58, a thiol-dependent reductase. Identification of its secretory form and inducible expression by the oncogenic transformation. Eur. J. Biochem, 234, 336-342 (1995).
    • (1995) Eur. J. Biochem. , vol.234 , pp. 336-342
    • Hirano, N.1
  • 114
    • 0037133347 scopus 로고    scopus 로고
    • TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain
    • Frickel, E. M. et al. TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain. Proc. Natl. Acad. Sci. USA 99, 1954-1959 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1954-1959
    • Frickel, E.M.1
  • 115
    • 0030960372 scopus 로고    scopus 로고
    • The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins
    • Elliott, J. G., Oliver, J. D. & High, S. The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins. J. Biol. Chem. 272, 13849-13855(1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 13849-13855
    • Elliott, J.G.1    Oliver, J.D.2    High, S.3
  • 116
    • 0025070112 scopus 로고
    • ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase
    • Mazzarella, R. A., Srinivasan, M., Haugejorden, S. M. & Green, M. ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase. J. Biol. Chem, 265, 1094-1101 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 1094-1101
    • Mazzarella, R.A.1    Srinivasan, M.2    Haugejorden, S.M.3    Green, M.4
  • 117
    • 0027957793 scopus 로고
    • +-binding proteins and members of the thioredoxin superfamily
    • +-binding proteins and members of the thioredoxin superfamily. J. Biol. Chem. 269, 1744-1749(1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 1744-1749
    • Nigam, S.K.1
  • 118
    • 0028795422 scopus 로고
    • Two resident ER-proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: Comparison with protein disulfide isomerase
    • Lundstrom-Ljung, J., Bimbach, U., Rupp, K., Soling, H, D. & Holmgren, A. Two resident ER-proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: comparison with protein disulfide isomerase. FEBS Lett. 357, 305-308(1995).
    • (1995) FEBS Lett. , vol.357 , pp. 305-308
    • Lundstrom-Ljung, J.1    Bimbach, U.2    Rupp, K.3    Soling, H.D.4    Holmgren, A.5
  • 119
    • 0028001714 scopus 로고
    • CaBP1, a calcium binding protein of the thioredoxin family, is a resident KDEL protein of the ER and not of the intermediate compartment
    • Fullekrug, J. et al. CaBP1, a calcium binding protein of the thioredoxin family, is a resident KDEL protein of the ER and not of the intermediate compartment. J. Cell Sci. 107, 2719-2727(1994),
    • (1994) J. Cell Sci. , vol.107 , pp. 2719-2727
    • Fullekrug, J.1
  • 120
    • 0030068301 scopus 로고    scopus 로고
    • Characterization and chromosonmal localization of a new protein disulfide isomerase, PDIp, highly expressed in human pancreas
    • Desilva, M. G. et al. Characterization and chromosonmal localization of a new protein disulfide isomerase, PDIp, highly expressed in human pancreas. DNA Cell Biol. 15, 9-16 (1996).
    • (1996) DNA Cell Biol. , vol.15 , pp. 9-16
    • Desilva, M.G.1
  • 121
    • 0029121158 scopus 로고
    • Molecular cloning of the cDNA encoding a novel protein disulfide isomerase-related protein (PDIR)
    • Hayano, T. & Kikuchi, M. Molecular cloning of the cDNA encoding a novel protein disulfide isomerase-related protein (PDIR). FEBS Lett. 372, 210-214 (1995),
    • (1995) FEBS Lett. , vol.372 , pp. 210-214
    • Hayano, T.1    Kikuchi, M.2
  • 122
    • 0026013390 scopus 로고
    • Determination of the sequence of the yeast YCL313 gene localized on chromosome III. Homology with the protein disulfide isomerase (PDI gene product) of other organisms
    • Scherens, B., Dubois, E. & Messenguy, F. Determination of the sequence of the yeast YCL313 gene localized on chromosome III. Homology with the protein disulfide isomerase (PDI gene product) of other organisms. Yeast 7, 185-193 (1991).
    • (1991) Yeast , vol.7 , pp. 185-193
    • Scherens, B.1    Dubois, E.2    Messenguy, F.3
  • 123
    • 0026334073 scopus 로고
    • The Saccharomyces cerevisiae TRG 1 gene is essential for growth and encodes a lumenal endoplasmic reticulum glycoprotein involved in the maturation of vacuolar carboxypeptidase
    • Gunther, R. et al. The Saccharomyces cerevisiae TRG1 gene is essential for growth and encodes a lumenal endoplasmic reticulum glycoprotein involved in the maturation of vacuolar carboxypeptidase. J. Biol. Chem. 266, 24557-24563 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 24557-24563
    • Gunther, R.1
  • 124
    • 0027203922 scopus 로고
    • The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity
    • LaMantia, M. L. & Lennarz, W. J. The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity. Cell 74, 899-908 (1993).
    • (1993) Cell , vol.74 , pp. 899-908
    • LaMantia, M.L.1    Lennarz, W.J.2
  • 125
    • 0033230434 scopus 로고    scopus 로고
    • Eps1, a novel PDI-related protein involved in ER quality control in yeast
    • Wang, Q. & Chang, A, Eps1, a novel PDI-related protein involved in ER quality control in yeast. EMBO J. 18, 5972-5982(1999).
    • (1999) EMBO J. , vol.18 , pp. 5972-5982
    • Wang, Q.1    Chang, A.2
  • 126
    • 0026738643 scopus 로고
    • The yeast EUG 1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase
    • Tachibana, C. & Stevens, T. H. The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase. Mol. Cell. Biol. 12, 4601-4611 (1992).
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4601-4611
    • Tachibana, C.1    Stevens, T.H.2
  • 127
    • 0029115691 scopus 로고
    • Isolation and characterization of a yeast gene, MPD 1, the overexpression of which suppresses inviability caused by protein disulfide isomerase depletion
    • Tachikawa, H. et al. Isolation and characterization of a yeast gene, MPD1, the overexpression of which suppresses inviability caused by protein disulfide isomerase depletion. FEBS Lett. 369, 212-216 (1995).
    • (1995) FEBS Lett. , vol.369 , pp. 212-216
    • Tachikawa, H.1
  • 128
    • 0031590425 scopus 로고    scopus 로고
    • Overproduction of Mpd2p suppresses the lethality of protein disulfide isomerase depletion in a Cxxc sequence dependent manner
    • Tachikawa, H. et al. Overproduction of Mpd2p suppresses the lethality of protein disulfide isomerase depletion in a Cxxc sequence dependent manner. Biochem. Biophys. Res. Commun. 239, 710-714 (1997).
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 710-714
    • Tachikawa, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.