메뉴 건너뛰기




Volumn 280, Issue 1, 1998, Pages 85-102

Disulfide analysis reveals a role for macrophage migration inhibitory factor (MIF) as thiol-protein oxidoreductase

Author keywords

Cysteine mutants; Cytokine; Disulfide; Macrophage migration inhibitory factor (MIF); Thiol protein oxidoreductase

Indexed keywords

CYSTEINE; INSULIN; MACROPHAGE MIGRATION INHIBITION FACTOR; OXIDOREDUCTASE; SERINE;

EID: 0032479319     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1864     Document Type: Article
Times cited : (289)

References (69)
  • 2
    • 0027997701 scopus 로고
    • Purification, bioactivity, and secondary structure analysis of mouse and human macrophage migration Inhibitory factor (MIF)
    • Bernhagen J., Mitchell R.A., Calandra T., Voelter W., Cerami A., Bucala R. Purification, bioactivity, and secondary structure analysis of mouse and human macrophage migration Inhibitory factor (MIF). Biochemistry. 33:1994;14144-14155
    • (1994) Biochemistry , vol.33 , pp. 14144-14155
    • Bernhagen, J.1    Mitchell, R.A.2    Calandra, T.3    Voelter, W.4    Cerami, A.5    Bucala, R.6
  • 3
    • 0010588656 scopus 로고
    • Conformational and disulfid bond analysis of macrophage migration inhibitory factor (MIF)
    • H.S.L. Maia. Leiden, The Netherlands: ESCOM
    • Bernhagen J., Kapurniotu A., Stoeva S., Voelter W., Bucala R. Conformational and disulfid bond analysis of macrophage migration inhibitory factor (MIF). Maia H.S.L. Peptides. 1995;572-573 ESCOM, Leiden, The Netherlands
    • (1995) Peptides , pp. 572-573
    • Bernhagen, J.1    Kapurniotu, A.2    Stoeva, S.3    Voelter, W.4    Bucala, R.5
  • 4
    • 0030051176 scopus 로고    scopus 로고
    • An essential role for macrophage migration inhibitory factor in the tuberculin delayed-type hypersensitivity reaction
    • Bernhagen J., Bacher M., Calandra T., Metz C.N., Doty S.B., Donnelly T., Bucala R. An essential role for macrophage migration inhibitory factor in the tuberculin delayed-type hypersensitivity reaction. J. Exp. Med. 183:1996;277-282
    • (1996) J. Exp. Med. , vol.183 , pp. 277-282
    • Bernhagen, J.1    Bacher, M.2    Calandra, T.3    Metz, C.N.4    Doty, S.B.5    Donnelly, T.6    Bucala, R.7
  • 5
    • 0031931818 scopus 로고    scopus 로고
    • Regulation of the immune response by macrophage migration inhibitory factor: Biological and structural features
    • Bernhagen J., Calandra T., Bucala R. Regulation of the immune response by macrophage migration inhibitory factor biological and structural features. J. Mol. Med. 76:1998;151-161
    • (1998) J. Mol. Med. , vol.76 , pp. 151-161
    • Bernhagen, J.1    Calandra, T.2    Bucala, R.3
  • 6
    • 0026466890 scopus 로고
    • Rat liver protein linking chemical and immunological detoxification systems
    • Blocki F.A., Schlievert P.M., Wackett L.P. Rat liver protein linking chemical and immunological detoxification systems. Nature. 360:1992;269-270
    • (1992) Nature , vol.360 , pp. 269-270
    • Blocki, F.A.1    Schlievert, P.M.2    Wackett, L.P.3
  • 7
    • 0027330057 scopus 로고
    • MIF protein are theta-class glutathione S-transferase homologs
    • Blocki F.A., Ellis L.B., Wackett L.B. MIF protein are theta-class glutathione S-transferase homologs. Protein Sci. 2:1993;2095-2102
    • (1993) Protein Sci. , vol.2 , pp. 2095-2102
    • Blocki, F.A.1    Ellis, L.B.2    Wackett, L.B.3
  • 8
    • 0025022474 scopus 로고
    • Evidence for a novel thioredoxin-like catalytic property of gonadotropic hormones
    • Boniface J.J., Reichert J.L.E. Evidence for a novel thioredoxin-like catalytic property of gonadotropic hormones. Science. 247:1990;61-64
    • (1990) Science , vol.247 , pp. 61-64
    • Boniface, J.J.1    Reichert, J.L.E.2
  • 9
    • 0019005874 scopus 로고
    • Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism
    • Brahms S., Brahms J. Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism. J. Mol. Biol. 138:1980;149-178
    • (1980) J. Mol. Biol. , vol.138 , pp. 149-178
    • Brahms, S.1    Brahms, J.2
  • 11
    • 0028305693 scopus 로고
    • The macrophage is an important and previously unrecognized source of macrophage migration inhibitory factor
    • 1985-1902
    • Calandra T., Bernhagen J., Mitchell R.A., Bucala R. The macrophage is an important and previously unrecognized source of macrophage migration inhibitory factor. J. Exp. Med. 179:1994;. 1985-1902
    • (1994) J. Exp. Med. , vol.179
    • Calandra, T.1    Bernhagen, J.2    Mitchell, R.A.3    Bucala, R.4
  • 14
    • 0022555899 scopus 로고
    • Disulfide bonds as probes of protein folding pathways
    • Creighton T.E. Disulfide bonds as probes of protein folding pathways. Methods Enzymol. 131:1986;83-106
    • (1986) Methods Enzymol. , vol.131 , pp. 83-106
    • Creighton, T.E.1
  • 17
    • 0026719195 scopus 로고
    • Identification of the three-dimensional thioredoxin motif: Related structure in the ORF3 protein of the Staphylococcus aureus mer operon
    • Ellis L.B.M., Saurugger P., Woodward C. Identification of the three-dimensional thioredoxin motif related structure in the ORF3 protein of the Staphylococcus aureus mer operon. Biochemistry. 31:1992;4882-4891
    • (1992) Biochemistry , vol.31 , pp. 4882-4891
    • Ellis, L.B.M.1    Saurugger, P.2    Woodward, C.3
  • 18
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman G.L. Tissue sulfhydryl groups. Arch. Biophys. Acta. 82:1959;70-77
    • (1959) Arch. Biophys. Acta , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 19
    • 0027959156 scopus 로고
    • Protein disulphide isomerase: Building bridges in protein folding
    • Freedman R.B., Hirst T.R., Tuite M.F. Protein disulphide isomerase building bridges in protein folding. Trends Biochem. Sci. 19:1994;331-336
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 20
    • 0022636460 scopus 로고
    • Purification and properties of thioltransferase
    • Gan Z.R., Wells W.W. Purification and properties of thioltransferase. J. Biol. Chem. 261:1986;996-1001
    • (1986) J. Biol. Chem. , vol.261 , pp. 996-1001
    • Gan, Z.R.1    Wells, W.W.2
  • 21
    • 0023181023 scopus 로고
    • Preparation of homogeneous pig liver thioltransferase by a thiol: Disulfide mediated pI shift
    • Gan Z.R., Wells W.W. Preparation of homogeneous pig liver thioltransferase by a thiol disulfide mediated pI shift. Anal. Biochem. 162:1987;265-273
    • (1987) Anal. Biochem. , vol.162 , pp. 265-273
    • Gan, Z.R.1    Wells, W.W.2
  • 22
    • 0029065402 scopus 로고
    • Thiol/disulfide exchange equilibra and disulfide bond stability
    • Gilbert H.F. Thiol/disulfide exchange equilibra and disulfide bond stability. Methods Enzymol. 251:1995;8-28
    • (1995) Methods Enzymol. , vol.251 , pp. 8-28
    • Gilbert, H.F.1
  • 23
    • 0027217531 scopus 로고
    • Oxidoreductive regulation of nuclear factor kappa B. Involvement of a cellular reducing catalyst thioredoxin
    • Hayashi T., Ueno Y., Okamoto T. Oxidoreductive regulation of nuclear factor kappa B. Involvement of a cellular reducing catalyst thioredoxin. J. Biol. Chem. 268:1993;11380-11388
    • (1993) J. Biol. Chem. , vol.268 , pp. 11380-11388
    • Hayashi, T.1    Ueno, Y.2    Okamoto, T.3
  • 24
    • 0018786584 scopus 로고
    • Glutathione-dependent synthesis of deoxyribonucleotides. Purification and characterization of glutaredoxin from Escherichia coli
    • Holmgren A. Glutathione-dependent synthesis of deoxyribonucleotides. Purification and characterization of glutaredoxin from Escherichia coli. J. Biol. Chem. 254:1979;3664-3671
    • (1979) J. Biol. Chem. , vol.254 , pp. 3664-3671
    • Holmgren, A.1
  • 25
    • 0018723651 scopus 로고
    • Thioredoxin catalyses the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • Holmgren A. Thioredoxin catalyses the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J. Biol. Chem. 254:1979;9627-9632
    • (1979) J. Biol. Chem. , vol.254 , pp. 9627-9632
    • Holmgren, A.1
  • 26
    • 0022272491 scopus 로고
    • Glutaredoxin from Escherichia coliand calf thymus
    • Holmgren A. Glutaredoxin from Escherichia coliand calf thymus. Methods Enzymol. 113:1985;525-528
    • (1985) Methods Enzymol. , vol.113 , pp. 525-528
    • Holmgren, A.1
  • 28
    • 0032167393 scopus 로고    scopus 로고
    • Migration inhibitory factor (MIF) induces killing of Leishmania major by macrophages: Dependence on reactive nitrogen intermediates and endogenous TNF-α
    • In the press
    • Jüttner S., Bernhagen J., Metz C.N., Röllinghoff M., Bucala R., Gessner A. Migration inhibitory factor (MIF) induces killing of Leishmania major by macrophages dependence on reactive nitrogen intermediates and endogenous TNF-α J. Immunol. 1998;. In the press
    • (1998) J. Immunol.
    • Jüttner, S.1    Bernhagen, J.2    Metz, C.N.3    Röllinghoff, M.4    Bucala, R.5    Gessner, A.6
  • 29
    • 0019163962 scopus 로고
    • Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cystein-35 present in the reduced form of thioredoxin from Escherichia coli
    • Kallis G.-B., Holmgren A. Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cystein-35 present in the reduced form of thioredoxin from Escherichia coli. J. Biol. Chem. 255:1980;10261-10265
    • (1980) J. Biol. Chem. , vol.255 , pp. 10261-10265
    • Kallis, G.-B.1    Holmgren, A.2
  • 31
    • 0024324626 scopus 로고
    • Urea dependence of thiol-disulfide equilibria in thioredoxin: Confirmation of the linkage relationship and a sensitive assay for structure
    • Lin T.Y., Kim P.S. Urea dependence of thiol-disulfide equilibria in thioredoxin confirmation of the linkage relationship and a sensitive assay for structure. Biochemistry. 28:1989;5282-5287
    • (1989) Biochemistry , vol.28 , pp. 5282-5287
    • Lin, T.Y.1    Kim, P.S.2
  • 32
    • 0027994720 scopus 로고
    • Requirement of posttranslational modifications for the generation of biologic activity of glycosylation-inhibiting factor
    • Liu Y.C., Nakano T., Elly C., Ishizaka K. Requirement of posttranslational modifications for the generation of biologic activity of glycosylation-inhibiting factor. Proc. Natl Acad. Sci. USA. 91:1994;11227-11231
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 11227-11231
    • Liu, Y.C.1    Nakano, T.2    Elly, C.3    Ishizaka, K.4
  • 33
    • 0028901726 scopus 로고
    • Glutaredoxin accelerates glutathione-dependent folding of reduced ribonuclease a together with protein disulfide-isomerase
    • Lundström-Ljung J., Holmgren A. Glutaredoxin accelerates glutathione-dependent folding of reduced ribonuclease A together with protein disulfide-isomerase. J. Biol. Chem. 270:1995;7822-7828
    • (1995) J. Biol. Chem. , vol.270 , pp. 7822-7828
    • Lundström-Ljung, J.1    Holmgren, A.2
  • 34
    • 0027373949 scopus 로고
    • Crystal structure of the DsbA protein required for disulphide bond formation in vivo
    • Martin J.L., Bardwell J.C.A., Kuriyan J. Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Nature. 365:1993;464-468
    • (1993) Nature , vol.365 , pp. 464-468
    • Martin, J.L.1    Bardwell, J.C.A.2    Kuriyan, J.3
  • 35
    • 0031154718 scopus 로고    scopus 로고
    • Macrophage migration inhibitory factor is involved in the pathogenesis of collagen type II-induced arthritis in mice
    • Mikulowska A., Metz C.N., Bucala R., Holmdahl R. Macrophage migration inhibitory factor is involved in the pathogenesis of collagen type II-induced arthritis in mice. J. Immunol. 158:1997;5514-5517
    • (1997) J. Immunol. , vol.158 , pp. 5514-5517
    • Mikulowska, A.1    Metz, C.N.2    Bucala, R.3    Holmdahl, R.4
  • 36
    • 0031559878 scopus 로고    scopus 로고
    • Structure activity studies of the cytokine macrophage migration inhibitory factor (MIF) reveal a critical role for its carboxy terminus
    • Mischke R., Gessner A., Kapurniotu A., Jüttner S., Kleemann R., Brunner H., Bernhagen J. Structure activity studies of the cytokine macrophage migration inhibitory factor (MIF) reveal a critical role for its carboxy terminus. FEBS Letters. 414:1997;226-232
    • (1997) FEBS Letters , vol.414 , pp. 226-232
    • Mischke, R.1    Gessner, A.2    Kapurniotu, A.3    Jüttner, S.4    Kleemann, R.5    Brunner, H.6    Bernhagen, J.7
  • 37
    • 0032080006 scopus 로고    scopus 로고
    • Cross-linking and mutational analysis of the oligomerization state of the cytokine macrophage migration inhibitory factor (MIF)
    • Mischke R., Kleemann R., Brunner H., Bernhagen J. Cross-linking and mutational analysis of the oligomerization state of the cytokine macrophage migration inhibitory factor (MIF). FEBS Letters. 427:1998;85-90
    • (1998) FEBS Letters , vol.427 , pp. 85-90
    • Mischke, R.1    Kleemann, R.2    Brunner, H.3    Bernhagen, J.4
  • 38
    • 0015072222 scopus 로고
    • Alterations of macrophage functions by mediators from lymphocytes
    • Nathan C.F., Karnovsky M.L., David J.R. Alterations of macrophage functions by mediators from lymphocytes. J. Exp. Med. 133:1971;1356-1376
    • (1971) J. Exp. Med. , vol.133 , pp. 1356-1376
    • Nathan, C.F.1    Karnovsky, M.L.2    David, J.R.3
  • 39
    • 85030336865 scopus 로고
    • Basensubstitution
    • A. Graham. Heidelberg: Spektrum Akademischer Verlag
    • Newton C.R., Graham A. Basensubstitution. Graham A. PCR. 1994;105-114 Spektrum Akademischer Verlag, Heidelberg
    • (1994) PCR , pp. 105-114
    • Newton, C.R.1    Graham, A.2
  • 40
    • 0029410736 scopus 로고
    • Localization of macrophage migration inhibitory factor (MIF) to secretory granules within the corticotrophic and thyrotrophic cells of the pituitary gland
    • Nishino T., Bernhagen J., Shiiki H., Calandra T., Dohi K., Bucala R. Localization of macrophage migration inhibitory factor (MIF) to secretory granules within the corticotrophic and thyrotrophic cells of the pituitary gland. Mol. Med. 1:1995;781-788
    • (1995) Mol. Med. , vol.1 , pp. 781-788
    • Nishino, T.1    Bernhagen, J.2    Shiiki, H.3    Calandra, T.4    Dohi, K.5    Bucala, R.6
  • 41
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131:1986;266-280
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 42
    • 0025019350 scopus 로고
    • Conformational stability of globular proteins
    • Pace C.N. Conformational stability of globular proteins. Trends Biochem. Sci. 15:1990;14-17
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 14-17
    • Pace, C.N.1
  • 43
    • 0002343673 scopus 로고
    • Measuring the conformational stability of a protein
    • T.E. Creighton. Oxford,New York,Tokyo: Oxford University Press
    • Pace C.N., Shirley B.A., Thomson J.A. Measuring the conformational stability of a protein. Creighton T.E. Protein Structure. 1989;311-330 Oxford University Press, Oxford,New York,Tokyo
    • (1989) Protein Structure , pp. 311-330
    • Pace, C.N.1    Shirley, B.A.2    Thomson, J.A.3
  • 44
    • 0026696116 scopus 로고
    • Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: A practical guide
    • Perczel A., Park K., Fasman G.D. Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm a practical guide. Anal. Biochem. 203:1992;83-93
    • (1992) Anal. Biochem. , vol.203 , pp. 83-93
    • Perczel, A.1    Park, K.2    Fasman, G.D.3
  • 45
    • 0002940127 scopus 로고
    • Protein folding
    • T.E. Creighton. New York: Freeman, W. H
    • Ptitsyn O.B. Protein folding. Creighton T.E. Protein Folding. 1992;243-300 Freeman, W. H, New York
    • (1992) Protein Folding , pp. 243-300
    • Ptitsyn, O.B.1
  • 46
    • 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., Gilbert H.F. 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. 269:1994;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
  • 47
    • 0025816448 scopus 로고
    • The three-dimensional structure of class π glutathione S-transferase in complex with glutathione sulfonate at 2.3 Å
    • Reinemer P., Dirr H.W., Ladenstein R., Schäffer J., Gallay O.I., Huber R. The three-dimensional structure of class π glutathione S-transferase in complex with glutathione sulfonate at 2.3 Å EMBO J. 10:1991;1997-2005
    • (1991) EMBO J. , vol.10 , pp. 1997-2005
    • Reinemer, P.1    Dirr, H.W.2    Ladenstein, R.3    Schäffer, J.4    Gallay, O.I.5    Huber, R.6
  • 50
    • 0029669190 scopus 로고    scopus 로고
    • The immunoregulatory mediator macrophage migration inhibitory factor (MIF) catalyzes a tautomerization reaction
    • Rosengren E., Bucala R., Åman P., Jacobsson L., Odh G., Metz C.N., Rorsman H. The immunoregulatory mediator macrophage migration inhibitory factor (MIF) catalyzes a tautomerization reaction. Mol. Med. 2:1996;143-149
    • (1996) Mol. Med. , vol.2 , pp. 143-149
    • Rosengren, E.1    Bucala, R.2    Åman, P.3    Jacobsson, L.4    Odh, G.5    Metz, C.N.6    Rorsman, H.7
  • 51
    • 0342275186 scopus 로고    scopus 로고
    • Effect of glutaredoxin and protein disulfide isomerase on the glutathion-dependent folding of ribonuclease a
    • Ruoppolo M., Lundström-Ljung J., Talamo F., Pucci P., Marino G. Effect of glutaredoxin and protein disulfide isomerase on the glutathion-dependent folding of ribonuclease A. Biochemistry. 36:1997;12259-12267
    • (1997) Biochemistry , vol.36 , pp. 12259-12267
    • Ruoppolo, M.1    Lundström-Ljung, J.2    Talamo, F.3    Pucci, P.4    Marino, G.5
  • 52
    • 0026554163 scopus 로고
    • Identification of cyclophilin as a pro-inflammatory secretory product of lipopolysaccaride-activated macrophages
    • Sherry B., Yarlett N., Strupp A., Cerami A. Identification of cyclophilin as a pro-inflammatory secretory product of lipopolysaccaride-activated macrophages. Proc. Natl Acad. Sci. USA. 89:1992;3511-3515
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 3511-3515
    • Sherry, B.1    Yarlett, N.2    Strupp, A.3    Cerami, A.4
  • 53
    • 0027308079 scopus 로고
    • Redox potentials of active-site bis(cysteinyl) fragments of thiol-protein oxidoreductases
    • Siedler F., Rudolph-Böhner S., Doi M., Musiol H.J., Moroder L. Redox potentials of active-site bis(cysteinyl) fragments of thiol-protein oxidoreductases. Biochemistry. 32:1993;7488-7495
    • (1993) Biochemistry , vol.32 , pp. 7488-7495
    • Siedler, F.1    Rudolph-Böhner, S.2    Doi, M.3    Musiol, H.J.4    Moroder, L.5
  • 54
    • 0029042407 scopus 로고
    • Glucocorticoid receptor thiols and steroid-binding activity
    • Simons S.S. Jr, Pratt W.B. Glucocorticoid receptor thiols and steroid-binding activity. Methods Enzymol. 251:1995;406-422
    • (1995) Methods Enzymol. , vol.251 , pp. 406-422
    • Simons Jr., S.S.1    Pratt, W.B.2
  • 55
  • 56
    • 0030060180 scopus 로고    scopus 로고
    • Enzymatic ketonization of 2-hydroxymuconate: Specificity and mechanism investigated by the crystal structures of two isomerases
    • Subramanya H.S., Roper D.I., Dauter Z., Dodson E.J., Davies G.J., Wilson K.S., Wigley D.B. Enzymatic ketonization of 2-hydroxymuconate specificity and mechanism investigated by the crystal structures of two isomerases. Biochemistry. 35:1996;792-802
    • (1996) Biochemistry , vol.35 , pp. 792-802
    • Subramanya, H.S.1    Roper, D.I.2    Dauter, Z.3    Dodson, E.J.4    Davies, G.J.5    Wilson, K.S.6    Wigley, D.B.7
  • 57
    • 0029895838 scopus 로고    scopus 로고
    • Crystal structure at 2.6 Å resolution of human macrophage migration inhibitory factor
    • Sun H., Bernhagen J., Bucala R., Lolis E. Crystal structure at 2.6 Å resolution of human macrophage migration inhibitory factor. Proc. Natl Acad. Sci. USA. 93:1996;5191-5196
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5191-5196
    • Sun, H.1    Bernhagen, J.2    Bucala, R.3    Lolis, E.4
  • 59
    • 0024461420 scopus 로고
    • ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin; Possible involvement of dithiol-reduction in the IL-2 receptor induction
    • Tagaya Y., Maeda Y., Mitsui A., Kondo, Matsui H., Hamuro J., Brown R., Arai K., Yokota T., Wakasugi N., Yodoi J. ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin; possible involvement of dithiol-reduction in the IL-2 receptor induction. EMBO J. 8:1989;757-764
    • (1989) EMBO J. , vol.8 , pp. 757-764
    • Tagaya, Y.1    Maeda, Y.2    Mitsui, A.3    Kondo4    Matsui, H.5    Hamuro, J.6    Brown, R.7    Arai, K.8    Yokota, T.9    Wakasugi, N.10    Yodoi, J.11
  • 60
    • 0030018518 scopus 로고    scopus 로고
    • On the reactivity and ionization of the active site cysteine residues of Escherichia colithioredoxin
    • Takahashi N., Creighton T.E. On the reactivity and ionization of the active site cysteine residues of Escherichia colithioredoxin. Biochemistry. 35:1996;8342-8353
    • (1996) Biochemistry , vol.35 , pp. 8342-8353
    • Takahashi, N.1    Creighton, T.E.2
  • 61
    • 0019881763 scopus 로고
    • Disulphide bridges in globular proteins
    • Thornton J.M. Disulphide bridges in globular proteins. J. Mol. Biol. 151:1981;261-287
    • (1981) J. Mol. Biol. , vol.151 , pp. 261-287
    • Thornton, J.M.1
  • 62
    • 0028027386 scopus 로고
    • Interleukin-10 inhibits antimicrobial activity against Leishmania major in murine macrophages
    • Vieth M., Will A., Schröppel K., Röllinghoff M., Gessner A. Interleukin-10 inhibits antimicrobial activity against Leishmania major in murine macrophages. Scan. J. Immunol. 40:1994;403-409
    • (1994) Scan. J. Immunol. , vol.40 , pp. 403-409
    • Vieth, M.1    Will, A.2    Schröppel, K.3    Röllinghoff, M.4    Gessner, A.5
  • 63
    • 0027406831 scopus 로고
    • A macrophage migration inhibitory factor is expressed in the differentiating cells of the eye lens
    • Wistow G.J., Shaughnessy M.P., Lee D.C., Hodin J., Zelenka P.S. A macrophage migration inhibitory factor is expressed in the differentiating cells of the eye lens. Proc. Natl Acad. Sci. USA. 90:1993;1271-1280
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 1271-1280
    • Wistow, G.J.1    Shaughnessy, M.P.2    Lee, D.C.3    Hodin, J.4    Zelenka, P.S.5
  • 65
    • 0028956318 scopus 로고
    • Efficient catalysis of disulfide formation during protein folding with a single active-site cysteine
    • Wunderlich M., Otto A., Maskos K., Mucke M., Seckler R., Glockshuber R. Efficient catalysis of disulfide formation during protein folding with a single active-site cysteine. J. Mol. Biol. 247:1995;28-33
    • (1995) J. Mol. Biol. , vol.247 , pp. 28-33
    • Wunderlich, M.1    Otto, A.2    Maskos, K.3    Mucke, M.4    Seckler, R.5    Glockshuber, R.6
  • 66
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang J.T., Wu C.S., Martinez H.M. Calculation of protein conformation from circular dichroism. Methods Enzymol. 130:1974;208-269
    • (1974) Methods Enzymol. , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.S.2    Martinez, H.M.3
  • 67
    • 0025788552 scopus 로고
    • Identification and characterization of the functional amino acids at the active center of pig liver thioltransferase by site-directed mutagenesis
    • Yang Y.F., Wells W.W. Identification and characterization of the functional amino acids at the active center of pig liver thioltransferase by site-directed mutagenesis. J. Biol. Chem. 266:1991;12759-12765
    • (1991) J. Biol. Chem. , vol.266 , pp. 12759-12765
    • Yang, Y.F.1    Wells, W.W.2
  • 68
    • 0028355571 scopus 로고
    • Replacement of the active-site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo
    • Zapun A., Cooper L., Creighton T.E. Replacement of the active-site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo. Biochemistry. 33:1994;1907-1914
    • (1994) Biochemistry , vol.33 , pp. 1907-1914
    • Zapun, A.1    Cooper, L.2    Creighton, T.E.3
  • 69
    • 0024428106 scopus 로고
    • Dependence of formation of small disulfide loops in two-cysteine peptides on the number and types of intervening amino acids
    • Zhang R., Snyder G.H. Dependence of formation of small disulfide loops in two-cysteine peptides on the number and types of intervening amino acids. J. Biol. Chem. 264:1989;18472-18479
    • (1989) J. Biol. Chem. , vol.264 , pp. 18472-18479
    • Zhang, R.1    Snyder, G.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.