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Volumn 402, Issue 6757, 1999, Pages 90-93

Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells

Author keywords

[No Author keywords available]

Indexed keywords

CALNEXIN; CALRETICULIN; CELL PROTEIN; DISULFIDE; GLYCOPROTEIN; OXIDOREDUCTASE; PROTEIN DISULFIDE ISOMERASE;

EID: 0033523910     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/47062     Document Type: Article
Times cited : (281)

References (19)
  • 1
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.-J. & Sambrook, J. Protein folding in the cell. Nature 355, 33-45 (1992).
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.-J.1    Sambrook, J.2
  • 2
    • 0026659680 scopus 로고
    • The endoplasmic reticulum as a protein folding compartment
    • Helenius, A., Marquardt, T. & Braakman, I. The endoplasmic reticulum as a protein folding compartment. Trends Cell Biol. 2, 227-231 (1992).
    • (1992) Trends Cell Biol. , vol.2 , pp. 227-231
    • Helenius, A.1    Marquardt, T.2    Braakman, I.3
  • 3
    • 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, 331-336 (1994).
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 4
    • 0031939209 scopus 로고    scopus 로고
    • Protein disulfide isomerase
    • Gilbert, H. F. Protein disulfide isomerase. Methods Enzymol. 290, 27-50 (1998).
    • (1998) Methods Enzymol. , vol.290 , pp. 27-50
    • Gilbert, H.F.1
  • 5
    • 73649177752 scopus 로고
    • Acceleration of reactivation of reduced bovine pancreatic ribonudease by a microsomal system of rat liver
    • Goldberger, R. F., Epstein, C. F. & Anfinsen, C. B. Acceleration of reactivation of reduced bovine pancreatic ribonudease by a microsomal system of rat liver. J. Biol. Chem. 238, 628-635 (1963).
    • (1963) J. Biol. Chem. , vol.238 , pp. 628-635
    • Goldberger, R.F.1    Epstein, C.F.2    Anfinsen, C.B.3
  • 6
    • 0027270735 scopus 로고
    • Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase
    • Weissman, I. S. & Kim, P. S. Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase. Nature 365, 185-188 (1993).
    • (1993) Nature , vol.365 , pp. 185-188
    • Weissman, I.S.1    Kim, P.S.2
  • 7
    • 0032559297 scopus 로고    scopus 로고
    • The eS-Sence of -SH in the ER
    • Huppa, J. B. & Ploegh, H. L. The eS-Sence of -SH in the ER. Cell 92, 145-148 (1998).
    • (1998) Cell , vol.92 , pp. 145-148
    • Huppa, J.B.1    Ploegh, H.L.2
  • 8
    • 0031030579 scopus 로고    scopus 로고
    • Assisted protein folding
    • Ruddon, R. W. & Bedows, E. Assisted protein folding. J. Biol. Chem. 272, 3125-3128 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 3125-3128
    • Ruddon, R.W.1    Bedows, E.2
  • 9
    • 0026508087 scopus 로고
    • Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum
    • Braakman, I., Helenius, J. & Helenius, A. Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum. Nature 356, 260-262 (1992).
    • (1992) Nature , vol.356 , pp. 260-262
    • Braakman, I.1    Helenius, J.2    Helenius, A.3
  • 10
    • 0033601739 scopus 로고    scopus 로고
    • An unconventional role for cytoplasmic disulfide bonds in Vaccinia virus proteins
    • Krijnse-Locker, J. & Griffiths, G. An unconventional role for cytoplasmic disulfide bonds in Vaccinia virus proteins, J. Cell Biol. 144, 267-279 (1999).
    • (1999) J. Cell Biol. , vol.144 , pp. 267-279
    • Krijnse-Locker, J.1    Griffiths, G.2
  • 11
    • 0025949415 scopus 로고
    • Reexamination of the folding of BPTI: Predominance of native intermediates
    • Weissman, J. S. & Kim, P. S. Reexamination of the folding of BPTI: predominance of native intermediates. Science 253, 1386-1393 (1991).
    • (1991) Science , vol.253 , pp. 1386-1393
    • Weissman, J.S.1    Kim, P.S.2
  • 12
    • 0029049090 scopus 로고
    • Cotranslational folding and calnexin binding during glycoprotein synthesis
    • Chen, W., Helenius, J., Braakman, I. & Helenius, A. Cotranslational folding and calnexin binding during glycoprotein synthesis. Proc. Natl Acad. Sci. USA 92, 6229-6233 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6229-6233
    • Chen, W.1    Helenius, J.2    Braakman, I.3    Helenius, A.4
  • 13
    • 0016292624 scopus 로고
    • Diagonal polyacrylamide-dodecyl sulfate gel electrophoresis for the identification of ribosomal proteins crosslinked with methyl-4-mercaptobutyrimidate
    • Sommer, A. & Traut, R. R. Diagonal polyacrylamide-dodecyl sulfate gel electrophoresis for the identification of ribosomal proteins crosslinked with methyl-4-mercaptobutyrimidate. Proc. Natl Acad. Sci. USA 71, 3946-3950 (1974).
    • (1974) Proc. Natl Acad. Sci. USA , vol.71 , pp. 3946-3950
    • Sommer, A.1    Traut, R.R.2
  • 14
    • 0028088152 scopus 로고
    • The alphaviruses: Gene expression, replication, and evolution
    • Strauss, J. H. & Strauss, E. G. The alphaviruses: gene expression, replication, and evolution. Mocrobiol. Rev. 58, 491-562 (1994).
    • (1994) Mocrobiol. Rev. , vol.58 , pp. 491-562
    • Strauss, J.H.1    Strauss, E.G.2
  • 15
    • 0018177156 scopus 로고
    • Assembly of the Semliki Forest virus membrane glycoproteins in the membrane of the endoplasmic reticulum in vitro
    • Garoff, H., Simons, K. & Dobberstein, B. Assembly of the Semliki Forest virus membrane glycoproteins in the membrane of the endoplasmic reticulum in vitro. J. Mol. Biol. 124, 587-600 (1978).
    • (1978) J. Mol. Biol. , vol.124 , pp. 587-600
    • Garoff, H.1    Simons, K.2    Dobberstein, B.3
  • 16
    • 0026563680 scopus 로고
    • Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum
    • Marquardt, T. & Helenius, A. Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum. J. Cell Biol. 117, 505-513 (1992).
    • (1992) J. Cell Biol. , vol.117 , pp. 505-513
    • Marquardt, T.1    Helenius, A.2
  • 17
    • 0031035644 scopus 로고    scopus 로고
    • Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
    • Oliver, J. D., van der Wal, F. J., Bulleid, N. J. & High, S. Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science 275, 86-88 (1997).
    • (1997) Science , vol.275 , pp. 86-88
    • Oliver, J.D.1    Van Der Wal, F.J.2    Bulleid, N.J.3    High, S.4
  • 18
    • 0032807338 scopus 로고    scopus 로고
    • ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin
    • Oliver, J. D., Roderick, H. L., Llewellyn, D. H. & High, S. ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin. Mol. Biol. Cell. 10, 2573-2582 (1999).
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 2573-2582
    • Oliver, J.D.1    Roderick, H.L.2    Llewellyn, D.H.3    High, S.4
  • 19
    • 0030467255 scopus 로고    scopus 로고
    • Deglucosylation of N-linked glycans is an important step in the dissociation of calreticulin-class 1-TAP complexes
    • Van Leeuwen, J. E. M. & Kearse, K. P. Deglucosylation of N-linked glycans is an important step in the dissociation of calreticulin-class 1-TAP complexes. Proc. Natl Acad. Sci. USA 93, 13997-14001 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 13997-14001
    • Van Leeuwen, J.E.M.1    Kearse, K.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.