메뉴 건너뛰기




Volumn 14, Issue 6, 2005, Pages 1630-1642

The prokaryotic enzyme DsbB may share key structural features with eukaryotic disulfide bond forming oxidoreductases

Author keywords

Disulfide; DsbB; Ero1; Erv2; Structure

Indexed keywords

DSBB PROTEIN; OXIDOREDUCTASE; PROTEIN; PROTEIN ERO1; PROTEIN ERV2; UNCLASSIFIED DRUG;

EID: 22444432755     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.051355705     Document Type: Article
Times cited : (38)

References (53)
  • 2
    • 0033597878 scopus 로고    scopus 로고
    • Oxidative protein folding is driven by the electron transport system
    • Bader, M., Muse, W., Ballou, D.P., Gassner, C., and Bardwell, J.C. 1999. Oxidative protein folding is driven by the electron transport system. Cell 98: 217-227.
    • (1999) Cell , vol.98 , pp. 217-227
    • Bader, M.1    Muse, W.2    Ballou, D.P.3    Gassner, C.4    Bardwell, J.C.5
  • 3
    • 0034714289 scopus 로고    scopus 로고
    • Disulfide bonds are generated by quinone reduction
    • Bader, M.W., Xie, T., Yu, C.A., and Bardwell, J.C. 2000. Disulfide bonds are generated by quinone reduction. J. Biol. Chem. 275: 26082-26088.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26082-26088
    • Bader, M.W.1    Xie, T.2    Yu, C.A.3    Bardwell, J.C.4
  • 5
    • 0034681340 scopus 로고    scopus 로고
    • ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
    • Cabibbo, A., Pagani, M., Fabbri, M., Rocchi, M., Farmery, M.R., Bulleid, N.J., and Sitia, R. 2000. ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum. J. Biol. Chem. 275: 4827-4833.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4827-4833
    • Cabibbo, A.1    Pagani, M.2    Fabbri, M.3    Rocchi, M.4    Farmery, M.R.5    Bulleid, N.J.6    Sitia, R.7
  • 6
    • 0036224573 scopus 로고    scopus 로고
    • Oxidative protein folding in bacteria
    • Collet, J.F. and Bardwell, J.C. 2002. Oxidative protein folding in bacteria. Mol. Microbiol. 44: 1-8.
    • (2002) Mol. Microbiol. , vol.44 , pp. 1-8
    • Collet, J.F.1    Bardwell, J.C.2
  • 7
    • 0034673562 scopus 로고    scopus 로고
    • Regulation of the quiescence-induced genes: Quiescin Q6, decorin, and ribosomal protein S29
    • Coppock, D., Kopman, C., Gudas, J., and Cina-Poppe, D.A. 2000. Regulation of the quiescence-induced genes: quiescin Q6, decorin, and ribosomal protein S29. Biochem. Biophys. Res. Commun. 269: 604-610.
    • (2000) Biochem. Biophys. Res. Commun. , vol.269 , pp. 604-610
    • Coppock, D.1    Kopman, C.2    Gudas, J.3    Cina-Poppe, D.A.4
  • 8
    • 0034663597 scopus 로고    scopus 로고
    • Application of multiple sequence alignment profiles to improve protein secondary structure prediction
    • Cuff, J.A. and Barton, G.J. 2000. Application of multiple sequence alignment profiles to improve protein secondary structure prediction. Proteins 40: 502-511.
    • (2000) Proteins , vol.40 , pp. 502-511
    • Cuff, J.A.1    Barton, G.J.2
  • 9
    • 0036186384 scopus 로고    scopus 로고
    • Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum
    • Fassio, A. and Sitia, R. 2002. Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum. Histochem. Cell Biol. 117: 151-157.
    • (2002) Histochem. Cell Biol. , vol.117 , pp. 151-157
    • Fassio, A.1    Sitia, R.2
  • 10
    • 0031609760 scopus 로고    scopus 로고
    • 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
  • 11
    • 0033213605 scopus 로고    scopus 로고
    • Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum
    • _. 1999. Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol. Cell 4: 469-477.
    • (1999) Mol. Cell , vol.4 , pp. 469-477
  • 12
    • 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
    • _. 2000. 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) Mol. Biol. Cell , vol.11 , pp. 2833-2843
  • 13
    • 0028009149 scopus 로고
    • SOPM: A self-optimized method for protein secondary structure prediction
    • Geourjon, C. and Deleage, G. 1994. SOPM: A self-optimized method for protein secondary structure prediction. Protein Eng. 7: 157-164.
    • (1994) Protein Eng. , vol.7 , pp. 157-164
    • Geourjon, C.1    Deleage, G.2
  • 14
    • 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., Lill, R., and Lisowsky, T. 2001. Yeast ERV2p is the first microsomal FAD-linked sulfhydryl oxidase of the Erv1p/Alrp protein family. J. Biol. Chem. 276: 23486-23491.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23486-23491
    • Gerber, J.1    Muhlenhoff, U.2    Hofhaus, G.3    Lill, R.4    Lisowsky, T.5
  • 15
    • 0042815104 scopus 로고    scopus 로고
    • Mechanism of the electron transfer catalyst DsbB from Escherichia coli
    • Grauschopf, U., Fritz, A., and Glockshuber, R. 2003. Mechanism of the electron transfer catalyst DsbB from Escherichia coli. EMBO J. 22: 3503-3513.
    • (2003) EMBO J. , vol.22 , pp. 3503-3513
    • Grauschopf, U.1    Fritz, A.2    Glockshuber, R.3
  • 16
    • 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., and Fass, D. 2002. A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Nat. Struct. Biol. 9: 61-67.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 61-67
    • Gross, E.1    Sevier, C.S.2    Vala, A.3    Kaiser, C.A.4    Fass, D.5
  • 17
    • 2542475140 scopus 로고    scopus 로고
    • Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell
    • Gross, E., Kastner, D.B., Kaiser, C.A., and 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
  • 18
    • 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., and Beckwith, J. 1995. Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA. Proc. Natl. Acad. Sci. 92: 9895-9899.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 9895-9899
    • Guilhot, C.1    Jander, G.2    Martin, N.L.3    Beckwith, J.4
  • 19
    • 0037119945 scopus 로고    scopus 로고
    • The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: Crystal structure of the DsbC-DsbDα complex
    • Haebel, P.W., Goldstone, D., Katzen, F., Beckwith, J., and Metcalf, P. 2002. The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: Crystal structure of the DsbC-DsbDα complex. EMBO J. 21: 4774-4784.
    • (2002) EMBO J. , vol.21 , pp. 4774-4784
    • Haebel, P.W.1    Goldstone, D.2    Katzen, F.3    Beckwith, J.4    Metcalf, P.5
  • 20
    • 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., and Thorpe, C. 1999. 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) 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
  • 21
    • 0037013828 scopus 로고    scopus 로고
    • Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade
    • Inaba, K. and Ito, K. 2002. Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade. EMBO J. 21: 2646-2654.
    • (2002) EMBO J. , vol.21 , pp. 2646-2654
    • Inaba, K.1    Ito, K.2
  • 22
    • 1342304093 scopus 로고    scopus 로고
    • DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation
    • Inaba, K., Takahashi, Y.H., Fujieda, N., Kano, K., Miyoshi, H., and Ito, K. 2004. DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation. J. Biol. Chem. 279: 6761-6768.
    • (2004) J. Biol. Chem. , vol.279 , pp. 6761-6768
    • Inaba, K.1    Takahashi, Y.H.2    Fujieda, N.3    Kano, K.4    Miyoshi, H.5    Ito, K.6
  • 23
    • 0028154918 scopus 로고
    • Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation
    • Jander, G., Martin, N.L., and Beckwith, J. 1994. Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation. EMBO J. 13: 5121-5127.
    • (1994) EMBO J. , vol.13 , pp. 5121-5127
    • Jander, G.1    Martin, N.L.2    Beckwith, J.3
  • 24
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones, D.T. 1999. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292: 195-202.
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 25
    • 0037093512 scopus 로고    scopus 로고
    • Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA
    • Kadokura, H. and Beckwith, J. 2002. Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA. EMBO J. 21: 2354-2363.
    • (2002) EMBO J. , vol.21 , pp. 2354-2363
    • Kadokura, H.1    Beckwith, J.2
  • 26
    • 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., and Beckwith, J. 2000. 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. 97: 10884-10889.
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 10884-10889
    • Kadokura, H.1    Bader, M.2    Tian, H.3    Bardwell, J.C.4    Beckwith, J.5
  • 27
    • 0042768090 scopus 로고    scopus 로고
    • Protein disulfide bond formation in prokaryotes
    • Kadokura, H., Katzen, F., and 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
  • 28
    • 0032438987 scopus 로고    scopus 로고
    • Hidden Markov models for detecting remote protein homologies
    • Karplus, K., Barrett, C., and Hughey, R. 1998. Hidden Markov models for detecting remote protein homologies. Bioinformatics 14: 846-856.
    • (1998) Bioinformatics , vol.14 , pp. 846-856
    • Karplus, K.1    Barrett, C.2    Hughey, R.3
  • 29
    • 0036682611 scopus 로고    scopus 로고
    • Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD
    • Katzen, F., Deshmukh, M., Daldal, F., and Beckwith, J. 2002. Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD. EMBO J. 21: 3960-3969.
    • (2002) EMBO J. , vol.21 , pp. 3960-3969
    • Katzen, F.1    Deshmukh, M.2    Daldal, F.3    Beckwith, J.4
  • 30
    • 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. and Ito, K. 1996. 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) Genes Cells , vol.1 , pp. 201-208
    • Kishigami, S.1    Ito, K.2
  • 31
    • 0028948780 scopus 로고
    • Redox states of DsbA in the periplasm of Escherichia coli
    • Kishigami, S., Akiyama, Y., and Ito, K. 1995a. Redox states of DsbA in the periplasm of Escherichia coli. FEBS Lett. 364: 55-58.
    • (1995) FEBS Lett. , vol.364 , pp. 55-58
    • Kishigami, S.1    Akiyama, Y.2    Ito, K.3
  • 32
    • 0029161150 scopus 로고
    • DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA
    • Kishigami, S., Kanaya, E., Kikuchi, M., and Ito, K. 1995b. DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA. J. Biol. Chem. 270: 17072-17074.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17072-17074
    • Kishigami, S.1    Kanaya, E.2    Kikuchi, M.3    Ito, K.4
  • 33
    • 0033106153 scopus 로고    scopus 로고
    • Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway
    • Kobayashi, T. and Ito, K. 1999. Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway. EMBO J. 18: 1192-1198.
    • (1999) EMBO J. , vol.18 , pp. 1192-1198
    • Kobayashi, T.1    Ito, K.2
  • 34
    • 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., and 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. 94: 11857-11862.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 11857-11862
    • Kobayashi, T.1    Kishigami, S.2    Sone, M.3    Inokuchi, H.4    Mogi, T.5    Ito, K.6
  • 35
    • 0034647976 scopus 로고    scopus 로고
    • Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase
    • Lee, J., Hofhaus, G., and Lisowsky, T. 2000. Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase. FEBS Lett. 477: 62-66.
    • (2000) FEBS Lett. , vol.477 , pp. 62-66
    • Lee, J.1    Hofhaus, G.2    Lisowsky, T.3
  • 36
    • 0035076003 scopus 로고    scopus 로고
    • Mammalian augmenter of liver regeneration protein is a sulfhydryl oxidase
    • Lisowsky, T., Lee, J.E., Polimeno, L., Francavilla, A., and Hofhaus, G. 2001. Mammalian augmenter of liver regeneration protein is a sulfhydryl oxidase. Dig. Liver Dis. 33: 173-180.
    • (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
  • 37
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L.J., Bryson, K., and Jones, D.T. 2000. The PSIPRED protein structure prediction server. Bioinformatics 16: 404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 38
    • 0035890070 scopus 로고    scopus 로고
    • Manipulation of oxidative protein folding and PDI redox state in mammalian cells
    • Mezghrani, A., Fassio, A., Benham, A., Simmen, T., Braakman, I., and Sitia, R. 2001. Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO J. 20: 6288-6296.
    • (2001) EMBO J. , vol.20 , pp. 6288-6296
    • Mezghrani, A.1    Fassio, A.2    Benham, A.3    Simmen, T.4    Braakman, I.5    Sitia, R.6
  • 39
    • 0033933636 scopus 로고    scopus 로고
    • Cascaded multiple classifiers for secondary structure prediction
    • Ouali, M. and King, R.D. 2000. Cascaded multiple classifiers for secondary structure prediction. Protein Sci. 9: 1162-1176.
    • (2000) Protein Sci. , vol.9 , pp. 1162-1176
    • Ouali, M.1    King, R.D.2
  • 40
    • 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., 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
  • 41
    • 32744472972 scopus 로고    scopus 로고
    • Porter: A new, accurate server for protein secondary structure prediction
    • e-pub Dec 7
    • Pollastri, G. and McLysaght, A. 2004. Porter: A new, accurate server for protein secondary structure prediction. Bioinformatics e-pub Dec 7.
    • (2004) Bioinformatics
    • Pollastri, G.1    McLysaght, A.2
  • 42
    • 0036568279 scopus 로고    scopus 로고
    • Improving the prediction of protein secondary structure in three and eight classes using recurrent neural networks and profiles
    • Pollastri, G., Przybylski, D., Rost, B., and Baldi, P. 2002. Improving the prediction of protein secondary structure in three and eight classes using recurrent neural networks and profiles. Proteins 47: 228-235.
    • (2002) Proteins , vol.47 , pp. 228-235
    • Pollastri, G.1    Przybylski, D.2    Rost, B.3    Baldi, P.4
  • 43
    • 0037031882 scopus 로고    scopus 로고
    • DsbB catalyzes disulfide bond formation de novo
    • Regeimbal, J. and Bardwell, J.C. 2002. DsbB catalyzes disulfide bond formation de novo. J. Biol. Chem. 277: 32706-32713.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32706-32713
    • Regeimbal, J.1    Bardwell, J.C.2
  • 44
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost, B. and Sander, C. 1993. Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232: 584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 45
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • _. 1994. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19: 55-72.
    • (1994) Proteins , vol.19 , pp. 55-72
  • 46
    • 0037076339 scopus 로고    scopus 로고
    • Complete pathway for protein disulfide bond formation encoded by poxviruses
    • Senkevich, T.G., White, C.L., Koonin, E.V., and Moss, B. 2002. Complete pathway for protein disulfide bond formation encoded by poxviruses. Proc. Natl. Acad. Sci. 99: 6667-6672.
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 6667-6672
    • Senkevich, T.G.1    White, C.L.2    Koonin, E.V.3    Moss, B.4
  • 47
    • 0036842559 scopus 로고    scopus 로고
    • Formation and transfer of disulphide bonds in living cells
    • Sevier, C.S. and Kaiser, C.A. 2002. Formation and transfer of disulphide bonds in living cells. Nat. Rev. Mol. Cell Biol. 3: 836-847.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 836-847
    • Sevier, C.S.1    Kaiser, C.A.2
  • 48
    • 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., Aslund, F., and Kaiser, C.A. 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
  • 49
    • 8744256714 scopus 로고    scopus 로고
    • Characterization of the menaquinone dependent disulfide bond formation pathway of Escherichia coli
    • Takahashi, Y., Inaba, K., and Ito, K. 2004. Characterization of the menaquinone dependent disulfide bond formation pathway of Escherichia coli. J. Biol. Chem. 279: 47057-47065.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47057-47065
    • Takahashi, Y.1    Inaba, K.2    Ito, K.3
  • 51
    • 0036862532 scopus 로고    scopus 로고
    • The FAD- and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum
    • Tu, B.P. and Weissman, J.S. 2002. The FAD- and O(2)-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
  • 52
    • 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., and Weissman, J.S. 2000. Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science 290: 1571-1574.
    • (2000) Science , vol.290 , pp. 1571-1574
    • Tu, B.P.1    Ho-Schleyer, S.C.2    Travers, K.J.3    Weissman, J.S.4
  • 53
    • 0037127202 scopus 로고    scopus 로고
    • Identification of the ubiquinone-binding domain in the disulfide catalyst disulfide bond protein B
    • Xie, T., Yu, L., Bader, M.W., Bardwell, J.C., and Yu, C.A. 2002. Identification of the ubiquinone-binding domain in the disulfide catalyst disulfide bond protein B. J. Biol. Chem. 277: 1649-1652.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1649-1652
    • Xie, T.1    Yu, L.2    Bader, M.W.3    Bardwell, J.C.4    Yu, C.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.