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Volumn 219, Issue 3, 1996, Pages 686-689

DSBC protein: A new member of the thioredoxin fold-containing family

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BACTERIAL PROTEIN; THIOREDOXIN;

EID: 0029980415     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.1996.0295     Document Type: Article
Times cited : (12)

References (16)
  • 1
    • 0028028387 scopus 로고
    • Building bridges: Disulphide bond formation in the cell
    • Bardwell, J. C. A. (1994) Building bridges: Disulphide bond formation in the cell. Mol. Microbiol. 14, 199-205.
    • (1994) Mol. Microbiol. , vol.14 , pp. 199-205
    • Bardwell, J.C.A.1
  • 2
    • 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
  • 3
    • 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
  • 5
    • 0028215226 scopus 로고
    • Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity
    • Shevchik, V. E., Condemine, G., and Robert-Baudouy, J. (1994) Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity. EMBO J. 13, 2007-2012.
    • (1994) EMBO J. , vol.13 , pp. 2007-2012
    • Shevchik, V.E.1    Condemine, G.2    Robert-Baudouy, J.3
  • 6
    • 0028296940 scopus 로고
    • The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation
    • Missiakas, D., Georgopoulos, C., and Raina, S. (1994) The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. EMBO J. 13, 2013-2020.
    • (1994) EMBO J. , vol.13 , pp. 2013-2020
    • Missiakas, D.1    Georgopoulos, C.2    Raina, S.3
  • 7
    • 0028949156 scopus 로고
    • Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli
    • Zapun, A., Missiakas, D., Raina, S., and Creighton, T. E. (1995) Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. Biochemistry 34, 5075-5089.
    • (1995) Biochemistry , vol.34 , pp. 5075-5089
    • Zapun, A.1    Missiakas, D.2    Raina, S.3    Creighton, T.E.4
  • 8
    • 0027177451 scopus 로고
    • The SWISS-PROT protein sequence data bank, recent developments
    • Bairoch, A., and Boeckmann, B. (1993) The SWISS-PROT protein sequence data bank, recent developments. Nucleic. Acids. Res. 21, 3093-3096.
    • (1993) Nucleic. Acids. Res. , vol.21 , pp. 3093-3096
    • Bairoch, A.1    Boeckmann, B.2
  • 9
    • 0029996162 scopus 로고    scopus 로고
    • Incorporation of non-local interactions in protein secondary structure prediction from the amino acid sequence
    • in press. Network access: Protein sequences can be submitted for secondary structure prediction either or through electronic mail to predator@embl-heildelberg.de. A mail message containing HELP in the first line will be answered with appropriate instructions
    • Frishman, D., and Argos, P. (1996) Incorporation of non-local interactions in protein secondary structure prediction from the amino acid sequence. Protein Engineering, in press. (Network access: Protein sequences can be submitted for secondary structure prediction either to WWW URL http://www.embl-heidelberg.de/predator/predator_info.html or through electronic mail to predator@embl-heildelberg.de. A mail message containing HELP in the first line will be answered with appropriate instructions).
    • (1996) Protein Engineering
    • Frishman, D.1    Argos, P.2
  • 11
    • 0029644246 scopus 로고
    • Thioredoxin structure and mechanism: Conformational changes on oxidation of the active-site sulfhydryls to a disulfide
    • Holmgren, A. (1995) Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide. Holmgren-A Structure 3, 239-243.
    • (1995) Holmgren-A Structure , vol.3 , pp. 239-243
    • Holmgren, A.1
  • 12
    • 0027209602 scopus 로고
    • Structure determination and refinement of human alpha class glutathione transferase Al-I, and a comparison with the Mu and Pi class enzymes
    • Sinning, I., Kleywegt, G. J., Cowan, S. W., Reinemer, P., Dirr, H. W., Huber, R., Gilliland, G. L., Armstrong, R. N., Ji, X., and Board, P. G., et al. (1993) Structure determination and refinement of human alpha class glutathione transferase Al-I, and a comparison with the Mu and Pi class enzymes. J. Mol. Biol. 232, 192-212.
    • (1993) J. Mol. Biol. , vol.232 , pp. 192-212
    • Sinning, I.1    Kleywegt, G.J.2    Cowan, S.W.3    Reinemer, P.4    Dirr, H.W.5    Huber, R.6    Gilliland, G.L.7    Armstrong, R.N.8    Ji, X.9    Board, P.G.10
  • 13
    • 0026460365 scopus 로고
    • The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2 Å resolution
    • Ji, X., Zhang, P., Armstrong, R. N., and Gilliland, G. L. (1992) The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2 Å resolution. Biochemistry 31, 10169-10184.
    • (1992) Biochemistry , vol.31 , pp. 10169-10184
    • Ji, X.1    Zhang, P.2    Armstrong, R.N.3    Gilliland, G.L.4
  • 14
    • 0028181442 scopus 로고
    • The nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin(C14S) and glutathione
    • Bushweller, J. H., Billeter, M., Holmgren, A., and Wuthrich, K. (1994) J. Mol. Biol. The nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin(C14S) and glutathione. 235, 1585-1597.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1585-1597
    • Bushweller, J.H.1    Billeter, M.2    Holmgren, A.3    Wuthrich, K.4
  • 15
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure
    • Kraulis, P. J. J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure. Appl. Crtyst. 24, 946-950.
    • (1991) Appl. Crtyst. , vol.24 , pp. 946-950
    • Kraulis, P.J.J.1
  • 16
    • 0029149907 scopus 로고
    • Protein secondary structure prediction
    • Barton, G. J. (1995) Protein secondary structure prediction. Curr. Opinion Struct. Biol. 5, 372-376.
    • (1995) Curr. Opinion Struct. Biol. , vol.5 , pp. 372-376
    • Barton, G.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.