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Volumn 15, Issue 11, 1996, Pages 2659-2667

The CXXC motif: Imperatives for the formation of native disulfide bonds in the cell

Author keywords

Chaperone; Disulfide bond; Protein disulfide isomerase; Protein folding; Thioredoxin

Indexed keywords

PROTEIN DISULFIDE ISOMERASE; THIOL GROUP; THIOREDOXIN;

EID: 0029934516     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb00626.x     Document Type: Article
Times cited : (164)

References (77)
  • 2
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell,J.C.A., McGovem,K. and Beckwith,J. (1991) Identification of a protein required for disulfide bond formation in vivo. Cell, 67, 581-589.
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.A.1    McGovem, K.2    Beckwith, J.3
  • 4
    • 0000410244 scopus 로고
    • Enzyme kinetics and molecular evolution
    • Benner,S.A. (1989) Enzyme kinetics and molecular evolution. Chem. Rev., 89, 789-806.
    • (1989) Chem. Rev. , vol.89 , pp. 789-806
    • Benner, S.A.1
  • 5
    • 0020685761 scopus 로고
    • A glycosylated protoxin in killer yeast: Models for its structure and maturation
    • Bostian,K.A., Jayachandran,S. and Tipper,D.J. (1983) A glycosylated protoxin in killer yeast: models for its structure and maturation. Cell, 32, 169-180.
    • (1983) Cell , vol.32 , pp. 169-180
    • Bostian, K.A.1    Jayachandran, S.2    Tipper, D.J.3
  • 7
    • 0028171569 scopus 로고
    • Thioredoxin: A multifunctional regulatory protein with a bright future in technology and medicine
    • Buchanan,B.B., Schürmann,P., Decottignies,P. and Lozano,R.M. (1994) Thioredoxin: a multifunctional regulatory protein with a bright future in technology and medicine. Arch. Biochem. Biophys., 314, 257-260.
    • (1994) Arch. Biochem. Biophys. , vol.314 , pp. 257-260
    • Buchanan, B.B.1    Schürmann, P.2    Decottignies, P.3    Lozano, R.M.4
  • 8
    • 0024388720 scopus 로고
    • Evolutionary optimization of the catalytic effectiveness of an enzyme
    • Burbaum,J.J., Raines,R.T., Albery,W.J. and Knowles,J.R. (1989) Evolutionary optimization of the catalytic effectiveness of an enzyme. Biochemistry, 28, 9293-9305.
    • (1989) Biochemistry , vol.28 , pp. 9293-9305
    • Burbaum, J.J.1    Raines, R.T.2    Albery, W.J.3    Knowles, J.R.4
  • 11
    • 0017389755 scopus 로고
    • Conformational restrictions on the pathway of folding and unfolding of the pancreatic trypsin inhibitor
    • Creighton,T.E. (1977) Conformational restrictions on the pathway of folding and unfolding of the pancreatic trypsin inhibitor. J. Mol. Biol., 113, 275-293.
    • (1977) J. Mol. Biol. , vol.113 , pp. 275-293
    • Creighton, T.E.1
  • 12
    • 0028953741 scopus 로고
    • Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase
    • Darby,N.J. and Creighton,T.E. (1995) Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase. Biochemistry, 34, 3576-3587.
    • (1995) Biochemistry , vol.34 , pp. 3576-3587
    • Darby, N.J.1    Creighton, T.E.2
  • 13
    • 0029032586 scopus 로고
    • Engineering ribonuclease A: Production, purification, and characterization of wild-type enzyme and mutants at Gln11
    • delCardayré,S.B., Ribó,M., Yokel,E.M., Quirk,D.J., Rutter,W.J. and Raines,R.T. (1995) Engineering ribonuclease A: production, purification, and characterization of wild-type enzyme and mutants at Gln11. Protein Engng, 8, 261-273.
    • (1995) Protein Engng , vol.8 , pp. 261-273
    • DelCardayré, S.B.1    Ribó, M.2    Yokel, E.M.3    Quirk, D.J.4    Rutter, W.J.5    Raines, R.T.6
  • 14
    • 0025208204 scopus 로고
    • Maintaining protein stability
    • Deutscher,M.P. (1990) Maintaining protein stability. Methods Enzymol., 182, 83-89.
    • (1990) Methods Enzymol. , vol.182 , pp. 83-89
    • Deutscher, M.P.1
  • 15
    • 0025261972 scopus 로고
    • Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy
    • Dyson,H.J., Gippert,G.P., Case,D.A., Holmgren,A. and Wright,P.E. (1990) Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy. Biochemistry, 29, 4129-4136.
    • (1990) Biochemistry , vol.29 , pp. 4129-4136
    • Dyson, H.J.1    Gippert, G.P.2    Case, D.A.3    Holmgren, A.4    Wright, P.E.5
  • 17
    • 0028180891 scopus 로고
    • Characterization by 1H-NMR of a C32S,C35S double mutant of Escherichia coli thioredoxin confirms its resemblence to the reduced wild-type protein
    • Dyson,H.J., Jeng,M.-F., Model,P. and Holmgren,A. (1994) Characterization by 1H-NMR of a C32S,C35S double mutant of Escherichia coli thioredoxin confirms its resemblence to the reduced wild-type protein. FEBS Lett., 339, 11-17.
    • (1994) FEBS Lett. , vol.339 , pp. 11-17
    • Dyson, H.J.1    Jeng, M.-F.2    Model, P.3    Holmgren, A.4
  • 18
    • 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. and Rutter,W.J. (1985) Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature, 317, 267-270.
    • (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
  • 19
    • 0025883245 scopus 로고
    • Structural and functional relations among thioredoxins of different species
    • Eklund,H., Gleason,F.K. and Holmgren,A. (1991) Structural and functional relations among thioredoxins of different species. Proteins, 11, 13-28.
    • (1991) Proteins , vol.11 , pp. 13-28
    • Eklund, H.1    Gleason, F.K.2    Holmgren, A.3
  • 20
    • 0026703547 scopus 로고
    • A simple and efficient procedure for transformation of yeasts
    • Elble,R. (1992) A simple and efficient procedure for transformation of yeasts. BioTechniques, 13, 18-20.
    • (1992) BioTechniques , vol.13 , pp. 18-20
    • Elble, R.1
  • 21
    • 0025909444 scopus 로고
    • High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution
    • Forman-Kay,J.D., Clore,G.M., Wingfield,P.T. and Gronenborn,A.M. (1991) High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution. Biochemistry, 30, 2685-2698.
    • (1991) Biochemistry , vol.30 , pp. 2685-2698
    • Forman-Kay, J.D.1    Clore, G.M.2    Wingfield, P.T.3    Gronenborn, A.M.4
  • 22
    • 0026511733 scopus 로고
    • Relationship between electrostatics and redox function in human thioredoxin: Characterization of pH titration shifts using two-dimensional homo-and heteronuclear NMR
    • Forman-Kay,J.D., Clore,G.M. and Gronenborn,A.M. (1992) Relationship between electrostatics and redox function in human thioredoxin: characterization of pH titration shifts using two-dimensional homo-and heteronuclear NMR. Biochemistry, 31, 3442-3452.
    • (1992) Biochemistry , vol.31 , pp. 3442-3452
    • Forman-Kay, J.D.1    Clore, G.M.2    Gronenborn, A.M.3
  • 23
    • 0002417413 scopus 로고
    • Protein folding in the cell
    • Creighton,T.E. (ed), W.H.Freeman and Co., New York
    • Freedman,R.B. (1992) Protein folding in the cell. In Creighton,T.E. (ed), Protein Folding. W.H.Freeman and Co., New York, pp. 455-539.
    • (1992) Protein Folding , pp. 455-539
    • Freedman, R.B.1
  • 24
    • 0025118967 scopus 로고
    • Molecular and cellular aspects of thiol-disulfide exchange
    • Gilbert,H.F. (1990) Molecular and cellular aspects of thiol-disulfide exchange. Adv. Enzymol., 63, 69-172.
    • (1990) Adv. Enzymol. , vol.63 , pp. 69-172
    • Gilbert, H.F.1
  • 25
    • 0003226410 scopus 로고
    • Oxidation and disulfide interchange in the reactivation of reduced ribonuclease
    • Givol,D., Goldberger,R.F. and Anfinsen,C.B. (1964) Oxidation and disulfide interchange in the reactivation of reduced ribonuclease. J. Biol. Chem., 239, PC3114-3116.
    • (1964) J. Biol. Chem. , vol.239
    • Givol, D.1    Goldberger, R.F.2    Anfinsen, C.B.3
  • 26
    • 73649177752 scopus 로고
    • Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver
    • Goldberger,R.F., Epstein,C.J. and Anfinsen,C.B. (1963) Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver. J. Biol. Chem., 238, 628-635.
    • (1963) J. Biol. Chem. , vol.238 , pp. 628-635
    • Goldberger, R.F.1    Epstein, C.J.2    Anfinsen, C.B.3
  • 27
    • 0027514241 scopus 로고
    • Functional replacement of the Saccharomyces cerevisiae Trg1/Pdi1 protein by members of the protein disulfide isomerase family
    • Günther,R., Srinivasan,M., Haugejordan,S., Green,M., Ehbrecht,J.-M. and Küntzel,H. (1993) Functional replacement of the Saccharomyces cerevisiae Trg1/Pdi1 protein by members of the protein disulfide isomerase family. J. Biol. Chem., 268, 7728-7732.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7728-7732
    • Günther, R.1    Srinivasan, M.2    Haugejordan, S.3    Green, M.4    Ehbrecht, J.-M.5    Küntzel, H.6
  • 28
    • 0023974872 scopus 로고
    • The Saccharomyces cerevisiae ACP2 gene encodes an essential HMG1-like protein
    • Haggren,W. and Kolodrubetz,D. (1988) The Saccharomyces cerevisiae ACP2 gene encodes an essential HMG1-like protein. Mol. Cell, Biol., 8, 1282-1289.
    • (1988) Mol. Cell, Biol. , vol.8 , pp. 1282-1289
    • Haggren, W.1    Kolodrubetz, D.2
  • 29
    • 0025801897 scopus 로고
    • The reactivities and ionization properties of the active-site dithiol groups of mammalian protein disulphide-isomerase
    • Hawkins,H.C. and Freedman,R.B. (1991) The reactivities and ionization properties of the active-site dithiol groups of mammalian protein disulphide-isomerase. Biochem J., 275, 335-339.
    • (1991) Biochem J. , vol.275 , pp. 335-339
    • Hawkins, H.C.1    Freedman, R.B.2
  • 30
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho,S.N., Hunt,H.D., Horton,R.M., Pullen,J.K. and Pease,L.R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene, 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 31
    • 0021978310 scopus 로고
    • The role of the α-helix dipole in protein function and structure
    • Hol,W.G. (1985) The role of the α-helix dipole in protein function and structure. Prog. Biophys. Mol. Biol., 45, 149-195.
    • (1985) Prog. Biophys. Mol. Biol. , vol.45 , pp. 149-195
    • Hol, W.G.1
  • 32
    • 0015500758 scopus 로고
    • Tryptophan fluorescence study of conformational transitions of the oxidized and reduced form of thioredoxin
    • Holmgren,A. (1972) Tryptophan fluorescence study of conformational transitions of the oxidized and reduced form of thioredoxin. J. Biol. Chem., 247, 1992-1998.
    • (1972) J. Biol. Chem. , vol.247 , pp. 1992-1998
    • Holmgren, A.1
  • 33
    • 2042476756 scopus 로고
    • Hydrogen donor system for Escherichia coli ribonucleotide-diphosphate reductase dependent on glutathione
    • Holmgren,A. (1976) Hydrogen donor system for Escherichia coli ribonucleotide-diphosphate reductase dependent on glutathione. Proc. Natl Acad. Sci. USA, 73, 2275-2279.
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 2275-2279
    • Holmgren, A.1
  • 36
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang,C., Sinskey,A.J. and Lodish,H.F. (1992) Oxidized redox state of glutathione in the endoplasmic reticulum. Science, 257, 1496-1502.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 38
    • 0029057023 scopus 로고
    • Proton sharing between cysteine thiols in Escherichia coli thioredoxin: Implications for the mechanism of protein disulfide reduction
    • Jeng,M.-F, Holmgren,A. and Dyson,H.J. (1995) Proton sharing between cysteine thiols in Escherichia coli thioredoxin: implications for the mechanism of protein disulfide reduction. Biochemistry, 34, 1010-10105.
    • (1995) Biochemistry , vol.34 , pp. 1010-10105
    • Jeng, M.-F.1    Holmgren, A.2    Dyson, H.J.3
  • 39
    • 0025319619 scopus 로고
    • Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution
    • Katti,S.K., LeMaster,D.M. and Eklund,H. (1990) Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution. J. Mol. Biol., 212, 167-184.
    • (1990) J. Mol. Biol. , vol.212 , pp. 167-184
    • Katti, S.K.1    LeMaster, D.M.2    Eklund, H.3
  • 40
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis,P. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. April. Crystallogr., 24, 946-950.
    • (1991) J. April. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 41
    • 0025914427 scopus 로고
    • Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli ihioredoxin
    • Krause,G., Lundström,J., Barea,J.L., Pueyo de la Cuesta,C. and Holmgren,A. (1991) Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli ihioredoxin. J. Biol. Chem., 266, 9494-9500.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9494-9500
    • Krause, G.1    Lundström, J.2    Barea, J.L.3    Pueyo de la Cuesta, C.4    Holmgren, A.5
  • 42
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel,T.A. (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl Acad. Sci. USA, 82, 488-492.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 43
    • 0029379610 scopus 로고
    • Production of rat protein disulfide isomerase in Saccharomyces cerevisiae
    • Laboissière,M.C.A., Chivers,P.T. and Raines,R.T. (1995a) Production of rat protein disulfide isomerase in Saccharomyces cerevisiae. Protein Express. Purif., 6, 700-706.
    • (1995) Protein Express. Purif. , vol.6 , pp. 700-706
    • Laboissière, M.C.A.1    Chivers, P.T.2    Raines, R.T.3
  • 44
    • 0028885790 scopus 로고
    • The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds
    • Laboissière,M.C.A., Sturley,S.L. and Raines,R.T. (1995b) The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J. Biol. Chem., 270, 28006-28009.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28006-28009
    • Laboissière, M.C.A.1    Sturley, S.L.2    Raines, R.T.3
  • 45
    • 0027203922 scopus 로고
    • The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity
    • LaMantia,M. and Lennarz,W.J. (1993) The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity. Cell, 74, 899-908.
    • (1993) Cell , vol.74 , pp. 899-908
    • LaMantia, M.1    Lennarz, W.J.2
  • 46
    • 0344998885 scopus 로고
    • BH+ for aliphatic ketones from nuclear magnetic resonance chemical shift data
    • BH+ for aliphatic ketones from nuclear magnetic resonance chemical shift data. Can. J. Chem., 48, 1919-1923.
    • (1970) Can. J. Chem. , vol.48 , pp. 1919-1923
    • Lee, D.G.1
  • 47
    • 0021848701 scopus 로고
    • Cloning and nucleotide sequence of the trxA gene of Escherichia coli K-12
    • Lim,C.-J., Geraghty,D. and Fuchs,J.A. (1985) Cloning and nucleotide sequence of the trxA gene of Escherichia coli K-12. J. Bacteriol., 163, 311-316.
    • (1985) J. Bacteriol. , vol.163 , pp. 311-316
    • Lim, C.-J.1    Geraghty, D.2    Fuchs, J.A.3
  • 48
    • 0024324626 scopus 로고
    • Urea dependence of thiol-disulfide equilibrium in thioredoxin: Confirmation of the linkage relationship and a sensitive assay for structure
    • Lin,T.-Y. and Kim,P.S. (1989) Urea dependence of thiol-disulfide equilibrium in thioredoxin: confirmation of the linkage relationship and a sensitive assay for structure. Biochemistry, 28, 5282-5287.
    • (1989) Biochemistry , vol.28 , pp. 5282-5287
    • Lin, T.-Y.1    Kim, P.S.2
  • 49
    • 0025748014 scopus 로고
    • Evaluating the effects of a single amino acid substitution on both the native and denatured states of a protein
    • Lin,T.-Y. and Kim,P.S. (1991) Evaluating the effects of a single amino acid substitution on both the native and denatured states of a protein. Proc. Natl Acad. Sci. USA, 88, 10573-10577.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 10573-10577
    • Lin, T.-Y.1    Kim, P.S.2
  • 50
    • 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
    • Lundström,J. and Holmgren,A. (1993) 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) Biochemistry , vol.32 , pp. 6649-6655
    • Lundström, J.1    Holmgren, A.2
  • 51
    • 0026793715 scopus 로고
    • A Pro to His mutation in active site of thioredoxin increase its disulfide-isomerase activity 10-fold
    • Lundström,J., Krause,G. and Holmgren,A. (1992) A Pro to His mutation in active site of thioredoxin increase its disulfide-isomerase activity 10-fold. J. Biol. Chem., 267, 9047-9052.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9047-9052
    • Lundström, J.1    Krause, G.2    Holmgren, A.3
  • 52
    • 0020488534 scopus 로고
    • Rat liver thioredoxin and thioredoxin reductase: Purification and characterization
    • Luthman,M. and Holmgren,A. (1982) Rat liver thioredoxin and thioredoxin reductase: purification and characterization. Biochemistry, 21, 6628-6633.
    • (1982) Biochemistry , vol.21 , pp. 6628-6633
    • Luthman, M.1    Holmgren, A.2
  • 53
    • 0025972887 scopus 로고
    • Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: Pre-steady-state kinetics and the utilization of the oxidizing equivalents of the isomerase
    • Lyles,M.M. and Gilbert,H.F. (1991) Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: pre-steady-state kinetics and the utilization of the oxidizing equivalents of the isomerase. Biochemistry, 30, 619-625.
    • (1991) Biochemistry , vol.30 , pp. 619-625
    • Lyles, M.M.1    Gilbert, H.F.2
  • 54
    • 0027373949 scopus 로고
    • Crystal structure of the DsbA protein required for disulphide bond formation in vivo
    • Martin,J.L., Bardwell,J.C.A. and 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.A.2    Kuriyan, J.3
  • 55
    • 0001432326 scopus 로고
    • Enzymatic synthesis of deoxyribonucleotides
    • Moore,E.G., Reichard,P. and Thelander,L. (1964) Enzymatic synthesis of deoxyribonucleotides. J. Biol. Chem., 239, 3445-3452.
    • (1964) J. Biol. Chem. , vol.239 , pp. 3445-3452
    • Moore, E.G.1    Reichard, P.2    Thelander, L.3
  • 56
    • 0025993780 scopus 로고
    • A putative glutathione binding site in T4 glutaredoxin investigated by site-directed mutagenesis
    • Nikkola,M., Gleason,F.K., Saarinen,M., Joelson,T., Björnberg,O. and Eklund,H. (1991) A putative glutathione binding site in T4 glutaredoxin investigated by site-directed mutagenesis. J. Biol. Chem., 266, 16105-16112.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16105-16112
    • Nikkola, M.1    Gleason, F.K.2    Saarinen, M.3    Joelson, T.4    Björnberg, O.5    Eklund, H.6
  • 57
    • 0027220866 scopus 로고
    • Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites
    • Noiva,R., Freedman,R.B. and Lennarz,W.J. (1993) Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites. J. Biol. Chem., 268, 19210-19217.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19210-19217
    • Noiva, R.1    Freedman, R.B.2    Lennarz, W.J.3
  • 58
    • 0024022478 scopus 로고
    • Sorting of soluble ER proteins in yeast
    • Pelham,H.R.B., Hardwick,K.G. and Lewis,M.J. (1988) Sorting of soluble ER proteins in yeast. EMBO J., 7, 1757-1762.
    • (1988) EMBO J. , vol.7 , pp. 1757-1762
    • Pelham, H.R.B.1    Hardwick, K.G.2    Lewis, M.J.3
  • 59
    • 0023303619 scopus 로고
    • Molecular cloning of the 13-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene
    • Pihlajaniemi,T., Helaakoski,T., Tasanen,K., Myllylä,R., Huhtala,M.-L., Koivu,J. and Kivirikko,K.I. (1987) Molecular cloning of the 13-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBO J., 6, 643-649.
    • (1987) EMBO J. , vol.6 , pp. 643-649
    • Pihlajaniemi, T.1    Helaakoski, T.2    Tasanen, K.3    Myllylä, R.4    Huhtala, M.-L.5    Koivu, J.6    Kivirikko, K.I.7
  • 61
    • 0028321726 scopus 로고
    • Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme
    • Puig,A. and Gilbert,H.F. (1994) Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme. J. Biol. Chem., 269, 7764-7771.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7764-7771
    • Puig, A.1    Gilbert, H.F.2
  • 62
    • 0028242359 scopus 로고
    • The role of the thiol/disulfide centers and peptide binding site in the chaperone and anti-chaperone activities of protein disulfide isomerase
    • Puig,A., Lyles,M.M., Noiva,R. and Gilbert,H.F. (1994) The role of the thiol/disulfide centers and peptide binding site in the chaperone and anti-chaperone activities of protein disulfide isomerase. J. Biol. Chem., 269, 19128-19135.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19128-19135
    • Puig, A.1    Lyles, M.M.2    Noiva, R.3    Gilbert, H.F.4
  • 63
    • 0023643438 scopus 로고
    • Enzyme relaxation in the reaction catalyzed by triosephosphate isomerase: Detection and kinetic characterization of two unliganded forms of the enzyme
    • Raines,R.T. and Knowles,J.R. (1987) Enzyme relaxation in the reaction catalyzed by triosephosphate isomerase: detection and kinetic characterization of two unliganded forms of the enzyme. Biochemistry, 26, 7014-7020.
    • (1987) Biochemistry , vol.26 , pp. 7014-7020
    • Raines, R.T.1    Knowles, J.R.2
  • 64
    • 0019877092 scopus 로고
    • A conformational study of thioredoxin and its tryptic fragments
    • Reutimann,H., Straub,B., Luisi,P.L. and Holmgren,A. (1981) A conformational study of thioredoxin and its tryptic fragments. J. Biol. Chem., 256, 6796-6803.
    • (1981) J. Biol. Chem. , vol.256 , pp. 6796-6803
    • Reutimann, H.1    Straub, B.2    Luisi, P.L.3    Holmgren, A.4
  • 65
    • 0029257263 scopus 로고
    • Constitutive overexpression of secreted heterologous proteins decreases extractable BiP and protein disulfide isomerase levels in Saccharomyces cerevisiae
    • Robinson,A.S. and Wittrup,K.D. (1995) Constitutive overexpression of secreted heterologous proteins decreases extractable BiP and protein disulfide isomerase levels in Saccharomyces cerevisiae. Biotechnol. Prog., 11, 171-177.
    • (1995) Biotechnol. Prog. , vol.11 , pp. 171-177
    • Robinson, A.S.1    Wittrup, K.D.2
  • 66
    • 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. and Messenguy,F. (1991) 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) Yeast , vol.7 , pp. 185-193
    • Scherens, B.1    Dubois, E.2    Messenguy, F.3
  • 67
    • 0002018792 scopus 로고
    • Solvent isotope effects on enzymic reactions
    • Cleland,W.W., O'Leary,M.H. and Northrop,D.B. (eds), University Park Press, Baltimore, MD
    • Schowen,R.L. (1977) Solvent isotope effects on enzymic reactions. In Cleland,W.W., O'Leary,M.H. and Northrop,D.B. (eds), Isotope Effects on Enzyme-Catalyzed Reactions. University Park Press, Baltimore, MD, pp. 64-99.
    • (1977) Isotope Effects on Enzyme-Catalyzed Reactions , pp. 64-99
    • Schowen, R.L.1
  • 68
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Guthrie,C. and Fink,G.R. (eds). Academic Press, San Diego, CA
    • Shermann,F. (1991) Getting started with yeast. In Guthrie,C. and Fink,G.R. (eds). Guide to Yeast Genetics and Molecular Biology. Academic Press, San Diego, CA, pp. 3-21.
    • (1991) Guide to Yeast Genetics and Molecular Biology , pp. 3-21
    • Shermann, F.1
  • 69
    • 0026090063 scopus 로고
    • In vitro mutagenesis and plasmid shuffling: From cloned gene to mutant yeast
    • Sikorski,R.S. and Boeke,J. (1991) In vitro mutagenesis and plasmid shuffling: from cloned gene to mutant yeast. Methods Enzymol., 194, 302-318.
    • (1991) Methods Enzymol. , vol.194 , pp. 302-318
    • Sikorski, R.S.1    Boeke, J.2
  • 70
    • 0021760477 scopus 로고
    • Polymer support oligonucleotide synthesis. XVIII: Use of β-cyanoethyl-N,N-dialkylamino-/N-morpholino phosphoramidite of deoxynucleosides for the synthesis of DNA fragment simplifying deprotection and isolation of the final product
    • Sinha,N.D., Biernat,J., McManus,J. and Köster,H. (1984) Polymer support oligonucleotide synthesis. XVIII: Use of β-cyanoethyl-N,N-dialkylamino-/N-morpholino phosphoramidite of deoxynucleosides for the synthesis of DNA fragment simplifying deprotection and isolation of the final product. Nucleic Acids Res., 12, 4539-4557.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 4539-4557
    • Sinha, N.D.1    Biernat, J.2    McManus, J.3    Köster, H.4
  • 71
    • 0026738643 scopus 로고
    • The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase
    • Tachibana,C. and Stevens,T.H. (1992) The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase. Mol. Cell. Biol., 12, 4601-4611.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4601-4611
    • Tachibana, C.1    Stevens, T.H.2
  • 72
    • 0142019685 scopus 로고
    • The enzymic reactivation of reduced ribonuclease
    • Venetianer,P. and Straub,F.B. (1963) The enzymic reactivation of reduced ribonuclease. Biochim. Biophys. Acta, 67, 166-168.
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 166-168
    • Venetianer, P.1    Straub, F.B.2
  • 73
    • 0027136018 scopus 로고
    • Protein disulfide isomerase is both an enzyme and a chaperone
    • Wang,C.-C. and Tsou,C.-L. (1993) Protein disulfide isomerase is both an enzyme and a chaperone. FASEB J., 7, 1515-1517.
    • (1993) FASEB J. , vol.7 , pp. 1515-1517
    • Wang, C.-C.1    Tsou, C.-L.2
  • 74
    • 0025949415 scopus 로고
    • Reexamination of the folding of BPTI: Predominance of native intermediates
    • Weissman,J.S. and Kim,P.S. (1991) Reexamination of the folding of BPTI: predominance of native intermediates. Science, 253, 1386-1393.
    • (1991) Science , vol.253 , pp. 1386-1393
    • Weissman, J.S.1    Kim, P.S.2
  • 75
    • 0025329901 scopus 로고
    • Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex
    • Wetterau,J.R., Combs,K.A., Spinner,S.N. and Joiner,B.J. (1990) Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex. J. Biol. Chem., 265, 9800-9807.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9800-9807
    • Wetterau, J.R.1    Combs, K.A.2    Spinner, S.N.3    Joiner, B.J.4
  • 76
    • 0027481123 scopus 로고
    • Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli
    • Wunderlich,M. and Glockshuber,R. (1993) Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli. Protein Sci., 2, 717-726.
    • (1993) Protein Sci. , vol.2 , pp. 717-726
    • Wunderlich, M.1    Glockshuber, R.2
  • 77
    • 0028956318 scopus 로고
    • Efficient catalysis of disulfide formation during protein folding with a single active-site cysteine
    • Wunderlich,M., Otto,A., Maskos,K., Mücke,M., Seckler,R. and Glockshuber,R. (1995) Efficient catalysis of disulfide formation during protein folding with a single active-site cysteine. J. Mol. Biol., 247, 28-33.
    • (1995) J. Mol. Biol. , vol.247 , pp. 28-33
    • Wunderlich, M.1    Otto, A.2    Maskos, K.3    Mücke, M.4    Seckler, R.5    Glockshuber, R.6


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