메뉴 건너뛰기




Volumn 13, Issue 7, 2004, Pages 1902-1907

Zinc-dependent dimerization of the folding catalyst, protein disulfide isomerase

Author keywords

Disulfide; Oligomerization; Protein disulfide isomerase; Protein folding; Zinc

Indexed keywords

CADMIUM; CHAPERONE; CYSTEINE DERIVATIVE; DIVALENT CATION; MERCURY; MONOMER; PROTEIN DISULFIDE ISOMERASE; SERINE; THIOREDOXIN; ZINC DERIVATIVE;

EID: 3042572562     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.04716104     Document Type: Article
Times cited : (54)

References (20)
  • 1
    • 0016272861 scopus 로고
    • The subcellular distribution of copper, zinc and iron in liver and kidney: Changes during copper deficiency in the rat
    • Alfaro, B. and Heaton, F.W. 1974. The subcellular distribution of copper, zinc and iron in liver and kidney: Changes during copper deficiency in the rat. Br. J. Nutr. 32: 435-445.
    • (1974) Br. J. Nutr. , vol.32 , pp. 435-445
    • Alfaro, B.1    Heaton, F.W.2
  • 2
    • 0029564658 scopus 로고
    • Interaction of calreticulin with protein disulfide isomerase
    • Baksh, S., Burns, K., Andrin, C., and Michalak, M. 1995. Interaction of calreticulin with protein disulfide isomerase. J. Biol. Chem. 270: 31338-31344.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31338-31344
    • Baksh, S.1    Burns, K.2    Andrin, C.3    Michalak, M.4
  • 3
    • 0022854081 scopus 로고
    • Immunocytochemical localization of metallothionein in the rat prostate gland
    • Bataineh, Z.M., Heidger, P.M., Thompson, S.A., and Timms, B.G. 1986. Immunocytochemical localization of metallothionein in the rat prostate gland. Prostate 9: 397-410.
    • (1986) Prostate , vol.9 , pp. 397-410
    • Bataineh, Z.M.1    Heidger, P.M.2    Thompson, S.A.3    Timms, B.G.4
  • 4
    • 0037119369 scopus 로고    scopus 로고
    • Surplus zinc is handled by Zym1 metallothionein and Zhf endoplasmic reticulum transporter in Schizosaccharomyces pombe
    • Borrelly, G.P., Harrison, M.D., Robinson, A.K., Cox, S.G., Robinson, N.J., and Whitehall, S.K. 2002. Surplus zinc is handled by Zym1 metallothionein and Zhf endoplasmic reticulum transporter in Schizosaccharomyces pombe. J. Biol. Chem. 277: 30394-30400.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30394-30400
    • Borrelly, G.P.1    Harrison, M.D.2    Robinson, A.K.3    Cox, S.G.4    Robinson, N.J.5    Whitehall, S.K.6
  • 5
    • 0018787261 scopus 로고
    • Interchangeable forms of thiol:protein disulfide oxidoreductase
    • Carmichael, D.F., Keefe, M., Pace, M., and Dixon, J.E. 1979. Interchangeable forms of thiol:protein disulfide oxidoreductase. J. Biol. Chem. 234: 8386-8390.
    • (1979) J. Biol. Chem. , vol.234 , pp. 8386-8390
    • Carmichael, D.F.1    Keefe, M.2    Pace, M.3    Dixon, J.E.4
  • 6
    • 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
  • 7
    • 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
  • 8
    • 0026135014 scopus 로고
    • Expression and purification of recombinant protein disulfide isomerase in E. coli
    • Gilbert, H.F., Kruzel, M.L., Lyles, M.M., and Harper, J.W. 1991. Expression and purification of recombinant protein disulfide isomerase in E. coli. Protein Expr. Purif. 2: 194-198.
    • (1991) Protein Expr. Purif. , vol.2 , pp. 194-198
    • Gilbert, H.F.1    Kruzel, M.L.2    Lyles, M.M.3    Harper, J.W.4
  • 9
    • 0025819371 scopus 로고
    • Redox properties and cross-linking of the dithiol/disulphide active sites of mammalian protein disulphide-isomerase
    • Hawkins, H.C., de Nardi, M., and Freedman, R.B. 1991. Redox properties and cross-linking of the dithiol/disulphide active sites of mammalian protein disulphide-isomerase. Biochem. J. 275: 341-348.
    • (1991) Biochem. J. , vol.275 , pp. 341-348
    • Hawkins, H.C.1    De Nardi, M.2    Freedman, R.B.3
  • 10
    • 0026514649 scopus 로고
    • C-terminal truncation of bovine protein disulfide isomerase increases its activity
    • Hu, C.H. and Tsou, C.L. 1992. C-terminal truncation of bovine protein disulfide isomerase increases its activity. Biochem. Biophys. Res. Commun. 183: 714-718.
    • (1992) Biochem. Biophys. Res. Commun. , vol.183 , pp. 714-718
    • Hu, C.H.1    Tsou, C.L.2
  • 11
    • 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
  • 13
    • 0026062381 scopus 로고
    • Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: Dependence of the rate on the composition of the redox buffer
    • Lyles, M.M. and Gilbert, H.F. 1991. Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: Dependence of the rate on the composition of the redox buffer. Biochemistry 30: 613-619.
    • (1991) Biochemistry , vol.30 , pp. 613-619
    • Lyles, M.M.1    Gilbert, H.F.2
  • 14
    • 0028080915 scopus 로고
    • Mutations in the thioredoxin sites of protein disulfide isomerase reveal functional non-equivalence of the N- and C-terminal domains
    • -. 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
  • 15
    • 0038670762 scopus 로고    scopus 로고
    • Cellular zinc and redox states converge in the metallothionein/thionein pair
    • Maret, W. 2003. Cellular zinc and redox states converge in the metallothionein/thionein pair. J. Nutr. 133: 1460S-1462S.
    • (2003) J. Nutr. , vol.133
    • Maret, W.1
  • 16
    • 0034633293 scopus 로고    scopus 로고
    • Colorimetric and fluorimetric assays to quantitate micromolar concentrations of transition metals
    • McCall, K.A. and Fierke, C.A. 2000. Colorimetric and fluorimetric assays to quantitate micromolar concentrations of transition metals. Anal. Biochem. 284: 307-315.
    • (2000) Anal. Biochem. , vol.284 , pp. 307-315
    • McCall, K.A.1    Fierke, C.A.2
  • 17
    • 0027407353 scopus 로고
    • Guanidine hydrochloride stabilization of a partially unfolded intermediate during the reversible denaturation of protein disulfide isomerase
    • Morjana, N.A., McKeone, B.J., and Gilbert, H.F. 1993. Guanidine hydrochloride stabilization of a partially unfolded intermediate during the reversible denaturation of protein disulfide isomerase. Proc. Natl. Acad. Sci. 90: 2107-2111.
    • (1993) Proc. Natl. Acad. Sci. , vol.90 , pp. 2107-2111
    • Morjana, N.A.1    McKeone, B.J.2    Gilbert, H.F.3
  • 18
    • 0018626775 scopus 로고
    • The nature of the multiple forms of bovine thiol:protein disulfide oxidoreductase
    • Pace, M. and Dixon, J.E. 1979. The nature of the multiple forms of bovine thiol:protein disulfide oxidoreductase. Intl. J. Peptide Protein Res. 14: 409-413.
    • (1979) Intl. J. Peptide Protein Res. , vol.14 , pp. 409-413
    • Pace, M.1    Dixon, J.E.2
  • 19
    • 0345096663 scopus 로고    scopus 로고
    • Trace elements in human physiology and pathology: Zinc and metallothioneins
    • Tapiero, H. and Tew, K.D. 2003. Trace elements in human physiology and pathology: Zinc and metallothioneins. Biomed. Pharmacother. 57: 399-411.
    • (2003) Biomed. Pharmacother. , vol.57 , pp. 399-411
    • Tapiero, H.1    Tew, K.D.2
  • 20
    • 0028070283 scopus 로고
    • Association and dissociation of protein disulfide isomerase
    • Yu, X., Wang, C., and Tsou, C. 1994. Association and dissociation of protein disulfide isomerase. Biochim. Biophys. Acta 1207: 109-113.
    • (1994) Biochim. Biophys. Acta , vol.1207 , pp. 109-113
    • Yu, X.1    Wang, C.2    Tsou, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.