메뉴 건너뛰기




Volumn 379, Issue 3, 1998, Pages 321-328

Experimental and theoretical analyses of the domain architecture of mammalian protein disulphide-isomerase

Author keywords

Limited proteolysis; Protein folding; Structure prediction; Tertiary structure

Indexed keywords

PROTEIN DISULFIDE ISOMERASE; RECOMBINANT PROTEIN; THIOREDOXIN;

EID: 0031954077     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/bchm.1998.379.3.321     Document Type: Article
Times cited : (51)

References (25)
  • 1
    • 0029093531 scopus 로고
    • Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase
    • Darby, N.J., and Creighton, T.E. (1995). Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase. Biochemistry 34, 1725-1735.
    • (1995) Biochemistry , vol.34 , pp. 1725-1735
    • Darby, N.J.1    Creighton, T.E.2
  • 2
    • 0032512878 scopus 로고    scopus 로고
    • The multi-domain structure of protein disulphide isomerase is essential for high catalytic efficiency
    • in press
    • Darby, N.J., Penka, E., and Vincentelli, R. (1998). The multi-domain structure of protein disulphide isomerase is essential for high catalytic efficiency. J. Mol. Biol., in press.
    • (1998) J. Mol. Biol.
    • Darby, N.J.1    Penka, E.2    Vincentelli, R.3
  • 3
    • 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
  • 4
    • 0023084055 scopus 로고
    • Progressive sequence alignment as a prerequisite to correct phylogenetic trees
    • Feng, D.F. and Doolittle, R.F. (1987). Progressive sequence alignment as a prerequisite to correct phylogenetic trees. J. Molec. Evol. 25, 351-360.
    • (1987) J. Molec. Evol. , vol.25 , pp. 351-360
    • Feng, D.F.1    Doolittle, R.F.2
  • 5
    • 0000294372 scopus 로고    scopus 로고
    • Protein disulphide-isomerase: A catalyst of thiol:disulphide interchange and associated protein folding
    • B. Bukau, ed. (London: Harwood Academic Press), in press
    • Freedman, R.B., and Klappa, P. (1998). Protein disulphide-isomerase: a catalyst of thiol:disulphide interchange and associated protein folding. In: Molecular Biology of Chaperones and Folding Catalysts, B. Bukau, ed. (London: Harwood Academic Press), in press.
    • (1998) Molecular Biology of Chaperones and Folding Catalysts
    • Freedman, R.B.1    Klappa, P.2
  • 6
    • 0024603788 scopus 로고
    • The role of protein disulphide-isomerase in the expression of native proteins
    • Freedman, R.B., Bulleid, N.J., Hawkins, H.C., and Paver, J.L. (1989). The role of protein disulphide-isomerase in the expression of native proteins. Biochem. Soc. Symp. 55, 167-192.
    • (1989) Biochem. Soc. Symp. , vol.55 , pp. 167-192
    • Freedman, R.B.1    Bulleid, N.J.2    Hawkins, H.C.3    Paver, J.L.4
  • 7
    • 0027959156 scopus 로고
    • Protein disulphide isomerase: Building bridges in protein folding
    • Freedman, R.B., Hirst, T.R., and Tuite, M.F. (1994). Protein disulphide isomerase: building bridges in protein folding. TIBS 19, 331-336.
    • (1994) TIBS , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 10
    • 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
  • 11
    • 0028946033 scopus 로고
    • The effect of denaturants on PDI conformation and activity
    • Hawkins, H.C., and Freedman, R.B. (1995). The effect of denaturants on PDI conformation and activity. Biochem. Soc. Trans. 23, 65S.
    • (1995) Biochem. Soc. Trans. , vol.23
    • Hawkins, H.C.1    Freedman, R.B.2
  • 12
    • 0025904916 scopus 로고
    • Comparison of the activities of protein disulphide isomerase and thioredoxin in catalyzing disulphide isomerization in a protein substrate
    • Hawkins, H.C., Blackburn, E.C., and Freedman, R.B. (1991). Comparison of the activities of protein disulphide isomerase and thioredoxin in catalyzing disulphide isomerization in a protein substrate. Biochem. J. 275, 349-353.
    • (1991) Biochem. J. , vol.275 , pp. 349-353
    • Hawkins, H.C.1    Blackburn, E.C.2    Freedman, R.B.3
  • 13
    • 0029973729 scopus 로고    scopus 로고
    • Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy
    • Kemmink, J., Darby, N.J., Dijkstra, K., Nilges, M., and Creighton, T.E. (1996). Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy. Biochemistry 35, 7684-7691.
    • (1996) Biochemistry , vol.35 , pp. 7684-7691
    • Kemmink, J.1    Darby, N.J.2    Dijkstra, K.3    Nilges, M.4    Creighton, T.E.5
  • 14
    • 0031127294 scopus 로고    scopus 로고
    • The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules
    • Kemmink, J., Darby, N.J., Dijkstra, K., Nilges, M., and Creighton, T.E. (1997). The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules. Current Biology 7, 239-245.
    • (1997) Current Biology , vol.7 , pp. 239-245
    • Kemmink, J.1    Darby, N.J.2    Dijkstra, K.3    Nilges, M.4    Creighton, T.E.5
  • 15
    • 0032481380 scopus 로고    scopus 로고
    • The b‰ domain provides the principal peptide binding site of protein disulphide isomerase but all domains contribute to the binding of misfolded proteins
    • in press
    • Klappa, P., Ruddock, L.W., Darby, N.J., and Freedman, R.B. (1998). The b‰ domain provides the principal peptide binding site of protein disulphide isomerase but all domains contribute to the binding of misfolded proteins. EMBO J., in press.
    • (1998) EMBO J.
    • Klappa, P.1    Ruddock, L.W.2    Darby, N.J.3    Freedman, R.B.4
  • 16
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and Doolittle, R.F. (1982). A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 17
    • 0029996044 scopus 로고    scopus 로고
    • The role of protein disulphide isomerase in the microsomal triacylglycerol transfer protein does not reside in its isomerase activity
    • Lamberg, A., Jauhiainen, M., Metso, J., Enholm, C., Shoulders, C., Scott, J., Pihlajaniemi, T., and Kivirikko, K.I. (1996). The role of protein disulphide isomerase in the microsomal triacylglycerol transfer protein does not reside in its isomerase activity. Biochem. J. 315, 533-536.
    • (1996) Biochem. J. , vol.315 , pp. 533-536
    • Lamberg, A.1    Jauhiainen, M.2    Metso, J.3    Enholm, C.4    Shoulders, C.5    Scott, J.6    Pihlajaniemi, T.7    Kivirikko, K.I.8
  • 18
    • 0028080915 scopus 로고
    • Mutations in the thioredoxin sites of protein disulfide isomerase reveal functional non-equivalence of the N- and C-terminal domains
    • Lyles, M.M., and Gilbert, H.F. (1994). Mutations in the thioredoxin sites of protein disulfide isomerase reveal functional non-equivalence of the N- and C-terminal domains. J. Biol. Chem. 269, 30946-30952.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30946-30952
    • Lyles, M.M.1    Gilbert, H.F.2
  • 19
    • 0029165589 scopus 로고
    • Thioredoxin - A fold for all reasons
    • Martin, J.L. (1995). Thioredoxin - a fold for all reasons. Structure 3, 245-250.
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 20
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto PVDF membranes
    • Matsudaira, P. (1987). Sequence from picomole quantities of proteins electroblotted onto PVDF membranes. J. Biol. Chem. 262, 10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 21
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C.N. (1986). Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods in Enzymology 131, 266-280.
    • (1986) Methods in Enzymology , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 22
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W.R., and Lipman, D.J. (1988). Improved tools for biological sequence comparison Proc. Nat. Acad. Sci. USA 85, 2444-2448.
    • (1988) Proc. Nat. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 23
    • 0023815684 scopus 로고
    • Characterisation of the human gene for a polypeptide that acts both as the beta subunit of prolyl-4-hydroxylase and as protein disulfide isomerase
    • Tasanen, K., Parkkonen, T., Chow, L.T., Kivirikko, K.I. and Pihlajaniemi, T. (1988). Characterisation of the human gene for a polypeptide that acts both as the beta subunit of prolyl-4-hydroxylase and as protein disulfide isomerase. J. Biol. Chem. 263, 16218-16224.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16218-16224
    • Tasanen, K.1    Parkkonen, T.2    Chow, L.T.3    Kivirikko, K.I.4    Pihlajaniemi, T.5
  • 24
    • 0026672695 scopus 로고
    • Site-directed mutagenesis of human protein disulphide isomerase: Effect on the assembly, activity and endoplasmic reticulum retention of human prolyl-4-hydroxylase in Spodoptera frugiperda insect cells
    • Vuori, K., Myllyla, R., Pihlajaniemi, T., and Kivirikko, K.I. (1992). Site-directed mutagenesis of human protein disulphide isomerase: effect on the assembly, activity and endoplasmic reticulum retention of human prolyl-4-hydroxylase in Spodoptera frugiperda insect cells. EMBO J. 11, 4213-4217.
    • (1992) EMBO J. , vol.11 , pp. 4213-4217
    • Vuori, K.1    Myllyla, R.2    Pihlajaniemi, T.3    Kivirikko, K.I.4
  • 25
    • 0023660653 scopus 로고
    • Prediction of protein secondary structure and active sites using the alignment of homologous sequences
    • Zvelebil, M.J. (1987). Prediction of protein secondary structure and active sites using the alignment of homologous sequences. J. Mol. Biol. 195, 957-961.
    • (1987) J. Mol. Biol. , vol.195 , pp. 957-961
    • Zvelebil, M.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.