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Volumn 320, Issue 2, 2004, Pages 359-365

Functional differences between human and yeast protein disulfide isomerase family proteins

Author keywords

Chaperone activity; Isomerase activity; Protein disulfide isomerase; Tetrad analysis; Yeast

Indexed keywords

CHAPERONE; COMPLEMENTARY DNA; HUMAN PROTEIN DISULFIDE ISOMERASE; ISOMERASE; PROTEIN; PROTEIN EUG1P; PROTEIN MPD1P; PROTEIN MPD2P; UNCLASSIFIED DRUG; YEAST PROTEIN DISULFIDE ISOMERASE;

EID: 2942718758     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.05.178     Document Type: Article
Times cited : (25)

References (33)
  • 1
    • 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
  • 2
    • 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. Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature. 317:1985;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
    • 0029074071 scopus 로고
    • A possible role of ER-60 protease in the degradation of misfolded proteins in the endoplasmic reticulum
    • Otsu M., Urade R., Kito M., Omura F., Kikuchi M. A possible role of ER-60 protease in the degradation of misfolded proteins in the endoplasmic reticulum. J. Biol. Chem. 270:1995;14958-14961
    • (1995) J. Biol. Chem. , vol.270 , pp. 14958-14961
    • Otsu, M.1    Urade, R.2    Kito, M.3    Omura, F.4    Kikuchi, M.5
  • 5
    • 0029620311 scopus 로고
    • Protein disulfide isomerase mutant lacking its isomerase activity accelerates protein folding in the cell
    • Hayano T., Hirose M., Kikuchi M. Protein disulfide isomerase mutant lacking its isomerase activity accelerates protein folding in the cell. FEBS Lett. 377:1995;505-511
    • (1995) FEBS Lett. , vol.377 , pp. 505-511
    • Hayano, T.1    Hirose, M.2    Kikuchi, M.3
  • 6
    • 0028846534 scopus 로고
    • Cloning and sequencing of the cDNA encoding human P5
    • Hayano T., Kikuchi M. Cloning and sequencing of the cDNA encoding human P5. Gene. 164:1995;377-378
    • (1995) Gene , vol.164 , pp. 377-378
    • Hayano, T.1    Kikuchi, M.2
  • 7
    • 0029121158 scopus 로고
    • Molecular cloning of the cDNA encoding a novel protein disulfide isomerase-related protein (PDIR)
    • Hayano T., Kikuchi M. Molecular cloning of the cDNA encoding a novel protein disulfide isomerase-related protein (PDIR). FEBS Lett. 372:1995;210-214
    • (1995) FEBS Lett. , vol.372 , pp. 210-214
    • Hayano, T.1    Kikuchi, M.2
  • 8
    • 0036737949 scopus 로고    scopus 로고
    • Functional analysis of human P5, a protein disulfide isomerase homologue
    • Kikuchi M., Doi E., Tsujimoto I., Horibe T., Tsujimoto Y. Functional analysis of human P5, a protein disulfide isomerase homologue. J. Biochem. 132:2002;451-455
    • (2002) J. Biochem. , vol.132 , pp. 451-455
    • Kikuchi, M.1    Doi, E.2    Tsujimoto, I.3    Horibe, T.4    Tsujimoto, Y.5
  • 9
    • 1042266634 scopus 로고    scopus 로고
    • Different contributions of the three CXXC motifs of human protein disulfide isomerase-related protein to isomerase activity and oxidative refolding
    • Horibe T., Gomi M., Iguchi D., Ito H., Kitamura Y., Masuoka T., Tsujimoto I., Kimura T., Kikuchi M. Different contributions of the three CXXC motifs of human protein disulfide isomerase-related protein to isomerase activity and oxidative refolding. J. Biol. Chem. 279:2004;4604-4611
    • (2004) J. Biol. Chem. , vol.279 , pp. 4604-4611
    • Horibe, T.1    Gomi, M.2    Iguchi, D.3    Ito, H.4    Kitamura, Y.5    Masuoka, T.6    Tsujimoto, I.7    Kimura, T.8    Kikuchi, M.9
  • 10
    • 0036836665 scopus 로고    scopus 로고
    • Proteins of the PDI family: Unpredicted non-ER locations and functions
    • Turano C., Coppari S., Altieri F., Ferraro A. Proteins of the PDI family: unpredicted non-ER locations and functions. J. Cell Physiol. 193:2002;154-163
    • (2002) J. Cell Physiol. , vol.193 , pp. 154-163
    • Turano, C.1    Coppari, S.2    Altieri, F.3    Ferraro, A.4
  • 11
    • 0036790739 scopus 로고    scopus 로고
    • A protein disulfide isomerase expressed in the embryonic midline is required for left/right asymmetries
    • Hoshijima K., Metherall J.E., Grunwald D.J. A protein disulfide isomerase expressed in the embryonic midline is required for left/right asymmetries. Genes Dev. 16:2002;2518-2529
    • (2002) Genes Dev. , vol.16 , pp. 2518-2529
    • Hoshijima, K.1    Metherall, J.E.2    Grunwald, D.J.3
  • 12
    • 0026334073 scopus 로고
    • The Saccharomyces cerevisiae TRG1 gene is essential for growth and encodes a lumenal endoplasmic reticulum glycoprotein involved in the maturation of vascular carboxypeptidase
    • Günther R., Brauer C., Janetzky B., Foster H.H., Ehbrecht I.M., Lehle L., Küntzel H. The Saccharomyces cerevisiae TRG1 gene is essential for growth and encodes a lumenal endoplasmic reticulum glycoprotein involved in the maturation of vascular carboxypeptidase. J. Biol. Chem. 266:1991;24557-24563
    • (1991) J. Biol. Chem. , vol.266 , pp. 24557-24563
    • Günther, R.1    Brauer, C.2    Janetzky, B.3    Foster, H.H.4    Ehbrecht, I.M.5    Lehle, L.6    Küntzel, H.7
  • 13
    • 0035832893 scopus 로고    scopus 로고
    • Studies on the function of yeast protein disulfide isomerase in renaturation of proteins
    • Katiyar S., Till E.A., Lennarz W.J. Studies on the function of yeast protein disulfide isomerase in renaturation of proteins. Biochim. Biophys. Acta. 1548:2001;47-56
    • (2001) Biochim. Biophys. Acta , vol.1548 , pp. 47-56
    • Katiyar, S.1    Till, E.A.2    Lennarz, W.J.3
  • 14
    • 0029115691 scopus 로고
    • Isolation and characterization of a yeast gene, MPD1, the overexpression of which suppresses inviability caused by protein disulfide isomerase depletion
    • Tachikawa H., Takeuchi Y., Funahashi W., Miura T., Gao X.D., Fujimoto D., Mizunaga T., Onodera K. Isolation and characterization of a yeast gene, MPD1, the overexpression of which suppresses inviability caused by protein disulfide isomerase depletion. FEBS Lett. 369:1995;212-216
    • (1995) FEBS Lett. , vol.369 , pp. 212-216
    • Tachikawa, H.1    Takeuchi, Y.2    Funahashi, W.3    Miura, T.4    Gao, X.D.5    Fujimoto, D.6    Mizunaga, T.7    Onodera, K.8
  • 16
    • 0026738643 scopus 로고
    • The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase
    • Tachibana C., Stevens T.H. The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase. Mol. Cell. Biol. 12:1992;4601-4611
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4601-4611
    • Tachibana, C.1    Stevens, T.H.2
  • 18
    • 0035881866 scopus 로고    scopus 로고
    • Mutation of yeast Eug1p CXXS active sites to CXXC results ir a dramatic increase in protein disulphide isomerase activity
    • Nørgaard P., Winther J.R. Mutation of yeast Eug1p CXXS active sites to CXXC results ir a dramatic increase in protein disulphide isomerase activity. Biochem. J. 358:2001;269-274
    • (2001) Biochem. J. , vol.358 , pp. 269-274
    • Nørgaard, P.1    Winther, J.R.2
  • 19
    • 0035958920 scopus 로고    scopus 로고
    • Combinations of protein-disulfide isomerase domains show that there is little correlation between isomerase activity and wild-type growth
    • Xiao R., Solovyov A., Gilbert H.F., Holmgren A., Lundstrom-Ljung J. Combinations of protein-disulfide isomerase domains show that there is little correlation between isomerase activity and wild-type growth. J. Biol. Chem. 276:2001;27975-27980
    • (2001) J. Biol. Chem. , vol.276 , pp. 27975-27980
    • Xiao, R.1    Solovyov, A.2    Gilbert, H.F.3    Holmgren, A.4    Lundstrom-Ljung, J.5
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 2942720981 scopus 로고    scopus 로고
    • Functional analysis of the CXXC motif with phage antibodies that cross-react with protein disulphide-isomerase family proteins
    • (in press)
    • T. Kimura, A. Nishida, N. Ohara, D. Yamagishi, T. Horibe, M. Kikuchi, Functional analysis of the CXXC motif with phage antibodies that cross-react with protein disulphide-isomerase family proteins, Biochem. J. (2004) (in press)
    • (2004) Biochem. J.
    • Kimura, T.1    Nishida, A.2    Ohara, N.3    Yamagishi, D.4    Horibe, T.5    Kikuchi, M.6
  • 23
    • 0017144476 scopus 로고
    • Thiol-protein disulphide oxidoreductases. Assay of microsomal membrane-bound glutathione-insulin transhydrogenase and comparison with protein disulphide-isomerase
    • Ibbetson A.L., Freedman R.B. Thiol-protein disulphide oxidoreductases. Assay of microsomal membrane-bound glutathione-insulin transhydrogenase and comparison with protein disulphide-isomerase. Biochem. J. 159:1976;377-384
    • (1976) Biochem. J. , vol.159 , pp. 377-384
    • Ibbetson, A.L.1    Freedman, R.B.2
  • 24
    • 0026416043 scopus 로고
    • Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
    • Martin J., Langer T., Boteva R., Schramel A., Horwich A.L., Hartle F.-U. Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature. 352:1991;36-42
    • (1991) Nature , vol.352 , pp. 36-42
    • Martin, J.1    Langer, T.2    Boteva, R.3    Schramel, A.4    Horwich, A.L.5    Hartle, F.-U.6
  • 25
    • 0027514241 scopus 로고
    • Functional replacement of the Saccharomyces cerevisiae Trg1/Pdi1 protein by members of the mammalian protein disulfide isomerase family
    • Günther R., Srinivasan M., Haugejorden S., Green M., Ehbrecht I.M., Küntzel H. Functional replacement of the Saccharomyces cerevisiae Trg1/Pdi1 protein by members of the mammalian protein disulfide isomerase family. J. Biol. Chem. 268:1993;7728-7732
    • (1993) J. Biol. Chem. , vol.268 , pp. 7728-7732
    • Günther, R.1    Srinivasan, M.2    Haugejorden, S.3    Green, M.4    Ehbrecht, I.M.5    Küntzel, H.6
  • 27
    • 0030875033 scopus 로고    scopus 로고
    • Interaction between protein disulphide isomerase and peptides
    • Klappa P., Hawkins H.C., Freedman R.B. Interaction between protein disulphide isomerase and peptides. Eur. J. Biochem. 248:1997;37-42
    • (1997) Eur. J. Biochem. , vol.248 , pp. 37-42
    • Klappa, P.1    Hawkins, H.C.2    Freedman, R.B.3
  • 28
    • 0027203922 scopus 로고
    • The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity
    • LaMantia M.L., Lennarz W.J. The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity. Cell. 74:1993;899-908
    • (1993) Cell , vol.74 , pp. 899-908
    • Lamantia, M.L.1    Lennarz, W.J.2
  • 30
    • 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., Pihlajaniemi T., Myllyla R., Kivirikko K.L. 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. 11:1992;4213-4217
    • (1992) EMBO J. , vol.11 , pp. 4213-4217
    • Vuori, K.1    Pihlajaniemi, T.2    Myllyla, R.3    Kivirikko, K.L.4
  • 31
    • 0025329901 scopus 로고
    • Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex
    • Wetterau J.R., Combs K.A., Spinnner S.N., Joiner B.J. Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex. J. Biol. Chem. 265:1990;9800-9807
    • (1990) J. Biol. Chem. , vol.265 , pp. 9800-9807
    • Wetterau, J.R.1    Combs, K.A.2    Spinnner, S.N.3    Joiner, B.J.4
  • 32
    • 0028257964 scopus 로고
    • Inhibition of human immunodeficiency virus infection by agents that interfere with thiol-disulfide interchange upon virus-receptor interaction
    • Ryser H.J., Levy E.M., Mandel R., Disciullo G.J. Inhibition of human immunodeficiency virus infection by agents that interfere with thiol-disulfide interchange upon virus-receptor interaction. Proc. Natl. Acad. Sci. USA. 91:1994;4559-4563
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4559-4563
    • Ryser, H.J.1    Levy, E.M.2    Mandel, R.3    Disciullo, G.J.4
  • 33
    • 0036850222 scopus 로고    scopus 로고
    • Conserved regions of protein disulfide isomerase are targeted by natural IgA antibodies in humans
    • Meek B., Back J.W., Klaren V.N.A., Speijer D., Peek R. Conserved regions of protein disulfide isomerase are targeted by natural IgA antibodies in humans. Int. Immunol. 14:2002;1291-1301
    • (2002) Int. Immunol. , vol.14 , pp. 1291-1301
    • Meek, B.1    Back, J.W.2    Klaren, V.N.A.3    Speijer, D.4    Peek, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.