메뉴 건너뛰기




Volumn 6, Issue 12, 1999, Pages 871-879

A small-molecule catalyst of protein folding in vitro and in vivo

Author keywords

Catalysis; Cysteine; Disulfide bond; Enzyme mimic; Protein folding

Indexed keywords


EID: 0033485854     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(00)80006-X     Document Type: Article
Times cited : (79)

References (65)
  • 2
    • 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. (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
  • 3
    • 0024337857 scopus 로고
    • Protein disulfide isomerase: Multiple roles in the modification of nascent secretory pathways
    • Freedman, R.B. (1989). Protein disulfide isomerase: Multiple roles in the modification of nascent secretory pathways. Cell 57, 1069-1072.
    • (1989) Cell , vol.57 , pp. 1069-1072
    • Freedman, R.B.1
  • 4
    • 0028885790 scopus 로고
    • The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds
    • Laboissière, M.C.A., Sturley, S.L. & Raines, R.T. (1995). 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
  • 5
    • 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. (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
  • 6
    • 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. (1996). Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine. Biochemistry 35, 1972-1980.
    • (1996) Biochemistry , vol.35 , pp. 1972-1980
    • Walker, K.W.1    Lyles, M.M.2    Gilbert, H.F.3
  • 7
    • 0028953741 scopus 로고
    • Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase
    • Darby, N.J. & 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
  • 9
    • 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
  • 10
    • 0030934272 scopus 로고    scopus 로고
    • The CXXC motif: A rheostat in the active site
    • Chivers, P.T., Prehoda, K.E. & Raines, R.T. (1997). The CXXC motif: A rheostat in the active site. Biochemistry 36, 4061-4066.
    • (1997) Biochemistry , vol.36 , pp. 4061-4066
    • Chivers, P.T.1    Prehoda, K.E.2    Raines, R.T.3
  • 11
    • 0025801897 scopus 로고
    • The reactivities and ionization properties of the active-site dithiol groups of mammalian protein disulphide-isomerase
    • Hawkins, H.C. & 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
  • 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
    • Lundström, J. & 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
  • 13
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang, C., Sinskey, A.J. & 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
  • 14
    • 0029934516 scopus 로고    scopus 로고
    • The CXXC motif: Imperatives for the formation of native disulfide bonds in the cell
    • Chivers, P.T., Laboissière, M.C.A. & Raines, R.T. (1996). The CXXC motif: Imperatives for the formation of native disulfide bonds in the cell. EMBO J. 16, 2659-2667.
    • (1996) EMBO J. , vol.16 , pp. 2659-2667
    • Chivers, P.T.1    Laboissière, M.C.A.2    Raines, R.T.3
  • 16
    • 0028171569 scopus 로고
    • Thioredoxin: A multifunctional regulatory protein with a bright future in technology and medicine
    • Buchanan, B.B., Schürmann, P., Decottignies, P. & 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
  • 17
    • 0001432326 scopus 로고
    • Enzymatic synthesis of deoxyribonucleotides
    • Moore, E.C., Reichard, P. & Thelander, L. (1964). Enzymatic synthesis of deoxyribonucleotides. J. Biol. Chem. 239, 3445-3452.
    • (1964) J. Biol. Chem. , vol.239 , pp. 3445-3452
    • Moore, E.C.1    Reichard, P.2    Thelander, L.3
  • 19
    • 0022545039 scopus 로고
    • Tissue distribution properties of technetium-99m-diamide-dimercaptide complexes and potential use as renal radiopharmaceuticals
    • Kasina, S., Fritzberg, A.R., Johnson, D.L. & Eshima, D. (1986). Tissue distribution properties of technetium-99m-diamide-dimercaptide complexes and potential use as renal radiopharmaceuticals. J. Med. Chem. 29, 1933-1940.
    • (1986) J. Med. Chem. , vol.29 , pp. 1933-1940
    • Kasina, S.1    Fritzberg, A.R.2    Johnson, D.L.3    Eshima, D.4
  • 20
    • 0000999485 scopus 로고
    • Synthesis of dithiols as reducing agents for disulfides in neutral aqueous solution and comparison of reduction potentials
    • Lamoureux, G.V. & Whitesides, G.M. (1993). Synthesis of dithiols as reducing agents for disulfides in neutral aqueous solution and comparison of reduction potentials. J. Org. Chem. 58, 633-641.
    • (1993) J. Org. Chem. , vol.58 , pp. 633-641
    • Lamoureux, G.V.1    Whitesides, G.M.2
  • 21
    • 0000756406 scopus 로고
    • Equilibrium constants for thioldisulfide interchange reactions: A coherent, corrected set
    • Lees, W.J. & Whitesides, G.M. (1993). Equilibrium constants for thioldisulfide interchange reactions: A coherent, corrected set. J. Org. Chem. 58, 642-647.
    • (1993) J. Org. Chem. , vol.58 , pp. 642-647
    • Lees, W.J.1    Whitesides, G.M.2
  • 23
    • 0030666729 scopus 로고    scopus 로고
    • Role of Cue1 p in ubiquitination and degradation at the ER surface
    • Biederer, T., Volkwein, C. & Sommer, T. (1997). Role of Cue1 p in ubiquitination and degradation at the ER surface. Science 278, 1806-1809.
    • (1997) Science , vol.278 , pp. 1806-1809
    • Biederer, T.1    Volkwein, C.2    Sommer, T.3
  • 24
    • 0028219869 scopus 로고
    • Protein disulfide isomerase overexpression increases secretion of foreign proteins in Saccharomyces cerevisiae
    • Robinson, A.S., Hines, V. & Wittrup, K.D. (1994). Protein disulfide isomerase overexpression increases secretion of foreign proteins in Saccharomyces cerevisiae. BioTechnology 12, 381-384.
    • (1994) BioTechnology , vol.12 , pp. 381-384
    • Robinson, A.S.1    Hines, V.2    Wittrup, K.D.3
  • 25
    • 0031879861 scopus 로고    scopus 로고
    • Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments
    • Shusta, E.V., Raines, R.T., Plückthun, A. & Wittrup, K.D. (1998). Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments. Nat. Biotechnol. 16, 773-777.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 773-777
    • Shusta, E.V.1    Raines, R.T.2    Plückthun, A.3    Wittrup, K.D.4
  • 26
    • 0029094253 scopus 로고
    • Quality-control in the secretory pathway
    • Hammond, C. & Helenius, A. (1995). Quality-control in the secretory pathway. Curr. Opin. Cell Biol. 7, 523-529.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 523-529
    • Hammond, C.1    Helenius, A.2
  • 27
    • 0028943316 scopus 로고
    • Disulfide bond formation and eucaryotic secretory productivity
    • Wittrup, K.D. (1995). Disulfide bond formation and eucaryotic secretory productivity. Curr. Opin. Biotechnol. 6, 203-208.
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 203-208
    • Wittrup, K.D.1
  • 28
    • 0030912818 scopus 로고    scopus 로고
    • Nature's transitory covalent bond
    • Raines, R.T. (1997). Nature's transitory covalent bond. Nat. Struct. Biol. 4, 424-427.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 424-427
    • Raines, R.T.1
  • 29
    • 0001120296 scopus 로고
    • Side-chain interactions governing the pairing of half-cystine residues in ribonuclease
    • Haber, E. & Anfinsen, C.B. (1962). Side-chain interactions governing the pairing of half-cystine residues in ribonuclease. J. Biol. Chem. 237, 1839-1844.
    • (1962) J. Biol. Chem. , vol.237 , pp. 1839-1844
    • Haber, E.1    Anfinsen, C.B.2
  • 30
    • 0014937559 scopus 로고
    • Formation of three-dimensional structure in proteins. I.Rapid nonenzymic reactivation of reduced lysozyme
    • Saxena, V.P. & Wetlaufer, D.B. (1970). Formation of three-dimensional structure in proteins. I.Rapid nonenzymic reactivation of reduced lysozyme. Biochemistry 9, 5015-5022.
    • (1970) Biochemistry , vol.9 , pp. 5015-5022
    • Saxena, V.P.1    Wetlaufer, D.B.2
  • 31
    • 0016167164 scopus 로고
    • Pathways of folding of reduced bovine pancreatic ribonuclease
    • Hantgan, R.R., Hammes, G.G. & Scheraga, H.A. (1974). Pathways of folding of reduced bovine pancreatic ribonuclease. Biochemistry 13, 3421-3431.
    • (1974) Biochemistry , vol.13 , pp. 3421-3431
    • Hantgan, R.R.1    Hammes, G.G.2    Scheraga, H.A.3
  • 32
    • 0020482340 scopus 로고
    • Regeneration of ribonuclease A from the reduced protein. Rate-limiting steps
    • Konishi, Y., Ooi, T. & Scheraga, H.A. (1982). Regeneration of ribonuclease A from the reduced protein. Rate-limiting steps. Biochemistry 21, 4734-4740.
    • (1982) Biochemistry , vol.21 , pp. 4734-4740
    • Konishi, Y.1    Ooi, T.2    Scheraga, H.A.3
  • 33
    • 0023290034 scopus 로고
    • The oxidative folding of proteins by disulfide plus thiol does not correlate with redox potential
    • Wetlaufer, D.B., Branca, P.A. & Chen, G.-X. (1987). The oxidative folding of proteins by disulfide plus thiol does not correlate with redox potential. Protein Eng. 1, 141-146.
    • (1987) Protein Eng. , vol.1 , pp. 141-146
    • Wetlaufer, D.B.1    Branca, P.A.2    Chen, G.-X.3
  • 34
    • 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. & 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
  • 35
    • 0029153845 scopus 로고
    • Active site peptides with CXXC motif on MAP-resin can mimic protein disulfide isomerase activity
    • Ookura, T., Kainuma, K., Kim, H.-j., Otaka, A., Fujii, N. & Kawamura, Y. (1995). Active site peptides with CXXC motif on MAP-resin can mimic protein disulfide isomerase activity. Biochem. Biophys. Res. Comm. 213, 746-751.
    • (1995) Biochem. Biophys. Res. Comm. , vol.213 , pp. 746-751
    • Ookura, T.1    Kainuma, K.2    Kim, H.-J.3    Otaka, A.4    Fujii, N.5    Kawamura, Y.6
  • 36
    • 0028886558 scopus 로고
    • a values in proteins of the thioredoxin family
    • a values in proteins of the thioredoxin family. J. Mol. Biol. 253, 799-812.
    • (1995) J. Mol. Biol. , vol.253 , pp. 799-812
    • Kortemme, T.1    Creighton, T.E.2
  • 37
    • 0001566670 scopus 로고
    • Regeneration and reduction of native bovine pancreatic ribonuclease A with oxidized and reduced dithiothreitol
    • Rothwarf, D.M. & Scheraga, H.A. (1991). Regeneration and reduction of native bovine pancreatic ribonuclease A with oxidized and reduced dithiothreitol. J. Am. Chem. Soc. 113, 6293-6294.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 6293-6294
    • Rothwarf, D.M.1    Scheraga, H.A.2
  • 38
    • 0027413488 scopus 로고
    • Regeneration of bovine pancreatic ribonuclease A. 1. Steady-state distribution
    • Rothwarf, D.M. & Scheraga, H.A. (1993). Regeneration of bovine pancreatic ribonuclease A. 1. Steady-state distribution. Biochemistry 32, 2671-2679.
    • (1993) Biochemistry , vol.32 , pp. 2671-2679
    • Rothwarf, D.M.1    Scheraga, H.A.2
  • 39
    • 0027506109 scopus 로고
    • Regeneration of bovine pancreatic ribonuclease A. 3. Dependence on the nature of the redox reagent
    • Rothwarf, D.M. & Scheraga, H.A. (1993). Regeneration of bovine pancreatic ribonuclease A. 3. Dependence on the nature of the redox reagent. Biochemistry 32, 2690-2697.
    • (1993) Biochemistry , vol.32 , pp. 2690-2697
    • Rothwarf, D.M.1    Scheraga, H.A.2
  • 41
    • 0001008982 scopus 로고
    • Acidic dissociation constants of thiols
    • Danehy, J.P. & Parameswaran, K.N. (1968). Acidic dissociation constants of thiols. J. Chem. Eng. Data 13, 386-389.
    • (1968) J. Chem. Eng. Data , vol.13 , pp. 386-389
    • Danehy, J.P.1    Parameswaran, K.N.2
  • 42
    • 0015518039 scopus 로고
    • Dissoziationsgleichgewichte von glutathion-eine Fourier-transform-13C-NMR spektroskopische untersuchung der pH-abhängigkeit der ladungsverteilung
    • Jung, G., Breitmaier, E. & Voelter, W. (1972). Dissoziationsgleichgewichte von glutathion-eine Fourier-transform-13C-NMR spektroskopische untersuchung der pH-abhängigkeit der ladungsverteilung. [Dissociation equilibrium of glutathione. A Fourier transform-13C-NMR spectroscopic study of pH-dependence and of charge densities.] Eur. J. Biochem. 24, 438-445.
    • (1972) Eur. J. Biochem. , vol.24 , pp. 438-445
    • Jung, G.1    Breitmaier, E.2    Voelter, W.3
  • 43
    • 33947087226 scopus 로고
    • Nuclear magnetic resonance studies of the acid - Base chemistry of amino acids and peptides. I. Microscopic ionization constants of glutathione and methylmercury-complexed glutathione
    • Rabenstein, D.L. (1973). Nuclear magnetic resonance studies of the acid - Base chemistry of amino acids and peptides. I. Microscopic ionization constants of glutathione and methylmercury-complexed glutathione. J. Am. Chem. Soc. 95, 2797-2803.
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 2797-2803
    • Rabenstein, D.L.1
  • 44
    • 0001106718 scopus 로고
    • Reaction of thiol anions with benzene oxide and malachite green
    • Reuben, D.M.E. & Bruice, T.C. (1976). Reaction of thiol anions with benzene oxide and malachite green. J. Am. Chem. Soc. 98, 114-121.
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 114-121
    • Reuben, D.M.E.1    Bruice, T.C.2
  • 45
    • 0000382603 scopus 로고
    • Acyl substituent effects on thiohemiacetal equilibria
    • Kanchuger, M.S. & Byers, L.D. (1979). Acyl substituent effects on thiohemiacetal equilibria. J. Am. Chem. Soc. 101, 3005-3010.
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 3005-3010
    • Kanchuger, M.S.1    Byers, L.D.2
  • 46
    • 0030724094 scopus 로고    scopus 로고
    • Protein disulfide isomerase and assisted protein folding
    • Gilbert, H.F. (1997). Protein disulfide isomerase and assisted protein folding. J. Biol. Chem. 272, 29399-29402.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29399-29402
    • Gilbert, H.F.1
  • 49
    • 0001133785 scopus 로고
    • Binding energy and enzymatic catalysis
    • Hansen, D.E. & Raines, R.T. (1990). Binding energy and enzymatic catalysis. J. Chem. Ed. 67, 483-489.
    • (1990) J. Chem. Ed. , vol.67 , pp. 483-489
    • Hansen, D.E.1    Raines, R.T.2
  • 50
    • 0030898705 scopus 로고    scopus 로고
    • Scanning and escape during protein-disulfide isomerase-assisted protein folding
    • Walker, K.W. & Gilbert, H.F. (1997). Scanning and escape during protein-disulfide isomerase-assisted protein folding. J. Biol. Chem. 272, 8845-8848.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8845-8848
    • Walker, K.W.1    Gilbert, H.F.2
  • 51
    • 0026604334 scopus 로고
    • Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum
    • Braakman, I., Helenius, J. & Helenius, A. (1992). Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum. EMBO J. 11, 1717-1722.
    • (1992) EMBO J. , vol.11 , pp. 1717-1722
    • Braakman, I.1    Helenius, J.2    Helenius, A.3
  • 52
    • 0001050205 scopus 로고
    • Improvement in the alkaline stability of subtilisin using an efficient random mutagenesis and screening procedure
    • Cunningham, B.C. & Wells, J.A. (1987). Improvement in the alkaline stability of subtilisin using an efficient random mutagenesis and screening procedure. Protein Eng. 1, 319-325.
    • (1987) Protein Eng. , vol.1 , pp. 319-325
    • Cunningham, B.C.1    Wells, J.A.2
  • 54
    • 0029798402 scopus 로고    scopus 로고
    • Functional mimicry of protein hormone by a peptide agonist: The EPO receptor complex at 2.8 Å resolution
    • Livnah, O., et al., & Wilson, I.A. (1996). Functional mimicry of protein hormone by a peptide agonist: The EPO receptor complex at 2.8 Å resolution. Science 273, 464-471.
    • (1996) Science , vol.273 , pp. 464-471
    • Livnah, O.1    Wilson, I.A.2
  • 55
    • 9444236174 scopus 로고    scopus 로고
    • Small peptides as potent mimetics of the protein hormone erythropoietin
    • Wrighton, N.C., et al., & Dower, W.J. (1996). Small peptides as potent mimetics of the protein hormone erythropoietin. Science 273, 458-463.
    • (1996) Science , vol.273 , pp. 458-463
    • Wrighton, N.C.1    Dower, W.J.2
  • 56
    • 0029619255 scopus 로고
    • Minimization of a polypeptide hormone
    • Li, B., et al., & Cunningham, B.C. (1995). Minimization of a polypeptide hormone. Science 270, 1657-1660.
    • (1995) Science , vol.270 , pp. 1657-1660
    • Li, B.1    Cunningham, B.C.2
  • 57
    • 33746204093 scopus 로고    scopus 로고
    • Enzyme mechanisms, models, and mimics
    • Kirby, A.J. (1996). Enzyme mechanisms, models, and mimics. Angew. Chem. Int. Ed. Engl. 35, 707-724.
    • (1996) Angew. Chem. Int. Ed. Engl. , vol.35 , pp. 707-724
    • Kirby, A.J.1
  • 58
    • 0027453389 scopus 로고
    • Synthesis, structure and activity of artificial, rationally designed catalytic polypeptides
    • Johnsson, K., Allemann, R.K., Widmer, H. & Benner, S.A. (1993). Synthesis, structure and activity of artificial, rationally designed catalytic polypeptides. Nature 365, 530-532.
    • (1993) Nature , vol.365 , pp. 530-532
    • Johnsson, K.1    Allemann, R.K.2    Widmer, H.3    Benner, S.A.4
  • 59
    • 33845182896 scopus 로고
    • Development of synthetic compounds with glutathione peroxidase activity
    • Wilson, S.R., Zucker, P.A., Ruey-Ruey, C.H. & Spector, A. (1989). Development of synthetic compounds with glutathione peroxidase activity. J. Am. Chem. Soc. 111, 5936-5939.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 5936-5939
    • Wilson, S.R.1    Zucker, P.A.2    Ruey-Ruey, C.H.3    Spector, A.4
  • 60
    • 0023050642 scopus 로고
    • The purification of eukaryotic proteins synthesized in Escherichia coli
    • Marston, F.A.O. (1986). The purification of eukaryotic proteins synthesized in Escherichia coli. Biochem. J. 240, 1-12.
    • (1986) Biochem. J. , vol.240 , pp. 1-12
    • Marston, F.A.O.1
  • 61
    • 0028859841 scopus 로고
    • Folding intermediates are involved in genetic diseases?
    • Bychkova, V.E. & Ptitsyn, O.B. (1995). Folding intermediates are involved in genetic diseases? FEBS Lett. 359, 6-8.
    • (1995) FEBS Lett. , vol.359 , pp. 6-8
    • Bychkova, V.E.1    Ptitsyn, O.B.2
  • 62
    • 0028856292 scopus 로고
    • Defective protein folding as a basis of human disease
    • Thomas, P.J., Qu, B.-H. & Pedersen, P.L. (1995). Defective protein folding as a basis of human disease. Trends Biochem. Sci. 20, 456-459.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 456-459
    • Thomas, P.J.1    Qu, B.-H.2    Pedersen, P.L.3
  • 63
    • 0031531472 scopus 로고    scopus 로고
    • Quality control of protein folding: Participation in human disease
    • Choudhury, P., Liu, Y. & Sifers, R.N. (1997). Quality control of protein folding: Participation in human disease. New Physiol. Sci. 12, 162-166.
    • (1997) New Physiol. Sci. , vol.12 , pp. 162-166
    • Choudhury, P.1    Liu, Y.2    Sifers, R.N.3
  • 64
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman, G.L. (1959). Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82, 70-77.
    • (1959) Arch. Biochem. Biophys. , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 65
    • 0029379610 scopus 로고
    • Production of rat protein disulfide isomerase in Saccharomyces cerevisiae
    • Laboissière, M.C.A., Chivers, P.T. & Raines, R.T. (1995). 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.