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Volumn 75, Issue 6, 2007, Pages 2946-2953

Evading the proteasome: Absence of lysine residues contributes to pertussis toxin activity by evasion of proteasome degradation

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; LYSINE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PERTUSSIS TOXIN; PROTEASOME; PROTEASOME INHIBITOR;

EID: 34249885064     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.02011-06     Document Type: Article
Times cited : (44)

References (56)
  • 1
    • 18144422732 scopus 로고    scopus 로고
    • p97 is in a complex with cholera toxin and influences the transport of cholera toxin and related toxins to the cytoplasm
    • Abujarour, R. J., S. Dalai, P. I. Hanson, and R. K. Draper. 2005. p97 is in a complex with cholera toxin and influences the transport of cholera toxin and related toxins to the cytoplasm. J. Biol. Chem. 280:15865- 15871.
    • (2005) J. Biol. Chem , vol.280 , pp. 15865-15871
    • Abujarour, R.J.1    Dalai, S.2    Hanson, P.I.3    Draper, R.K.4
  • 2
    • 0023877979 scopus 로고
    • Lectin-like binding of pertussis toxin to a 165-kilodalton Chinese hamster ovary cell glycoprotein
    • Brennan, M. J., J. L. David, J. G. Kenimer, and C. R. Manclark. 1988. Lectin-like binding of pertussis toxin to a 165-kilodalton Chinese hamster ovary cell glycoprotein. J. Biol. Chem. 263:4895-4899.
    • (1988) J. Biol. Chem , vol.263 , pp. 4895-4899
    • Brennan, M.J.1    David, J.L.2    Kenimer, J.G.3    Manclark, C.R.4
  • 3
    • 0033208984 scopus 로고    scopus 로고
    • ER protein quality control and proteasome-mediated protein degradation
    • Brodsky, J. L., and A. A. McCracken. 1999. ER protein quality control and proteasome-mediated protein degradation. Semin. Cell Dev. Biol. 10:507-513.
    • (1999) Semin. Cell Dev. Biol , vol.10 , pp. 507-513
    • Brodsky, J.L.1    McCracken, A.A.2
  • 4
    • 0242573090 scopus 로고    scopus 로고
    • NSF and p97/VCP: Similar at first, different at last
    • Brunger, A. T., and B. DeLaBarre. 2003. NSF and p97/VCP: similar at first, different at last. FEBS Lett. 555:126-133.
    • (2003) FEBS Lett , vol.555 , pp. 126-133
    • Brunger, A.T.1    DeLaBarre, B.2
  • 5
    • 0242286554 scopus 로고    scopus 로고
    • Pertussis toxin plays an early role in respiratory tract colonization by Bordetella pertussis
    • Carbonetti, N. H., G. V. Artamonova, R. M. Mays, and Z. E. Worthington. 2003. Pertussis toxin plays an early role in respiratory tract colonization by Bordetella pertussis. Infect. Immun. 71:6358-6366.
    • (2003) Infect. Immun , vol.71 , pp. 6358-6366
    • Carbonetti, N.H.1    Artamonova, G.V.2    Mays, R.M.3    Worthington, Z.E.4
  • 6
    • 0032936651 scopus 로고    scopus 로고
    • Intracellular delivery of a cytolytic T-lymphocyte epitope peptide by pertussis toxin to major histocompatibility complex class I without involvement of the cytosolic class I antigen processing pathway
    • Carbonetti, N. H., T. J. Irish, C. H. Chen, C. B. O'Connell, G. A. Hadley, U. McNamara, R. G. Tuskan, and G. K. Lewis. 1999. Intracellular delivery of a cytolytic T-lymphocyte epitope peptide by pertussis toxin to major histocompatibility complex class I without involvement of the cytosolic class I antigen processing pathway. Infect. Immun. 67:602-607.
    • (1999) Infect. Immun , vol.67 , pp. 602-607
    • Carbonetti, N.H.1    Irish, T.J.2    Chen, C.H.3    O'Connell, C.B.4    Hadley, G.A.5    McNamara, U.6    Tuskan, R.G.7    Lewis, G.K.8
  • 7
    • 15444368456 scopus 로고    scopus 로고
    • Proteolytic cleavage of pertussis toxin S1 subunit is not essential for its activity in mammalian cells
    • Carbonetti, N. H., R. M. Mays, G. V. Artamonova, R. D. Plaut, and Z. E. Worthington. 2005. Proteolytic cleavage of pertussis toxin S1 subunit is not essential for its activity in mammalian cells. BMC Microbiol. 5:7.
    • (2005) BMC Microbiol , vol.5 , pp. 7
    • Carbonetti, N.H.1    Mays, R.M.2    Artamonova, G.V.3    Plaut, R.D.4    Worthington, Z.E.5
  • 8
    • 0035142273 scopus 로고    scopus 로고
    • Expression, activity and cytotoxicity of pertussis toxin S1 subunit in transfected mammalian cells
    • Castro, M. G., U. McNamara, and N. H. Carbonetti. 2001. Expression, activity and cytotoxicity of pertussis toxin S1 subunit in transfected mammalian cells. Cell Microbiol. 3:45-54.
    • (2001) Cell Microbiol , vol.3 , pp. 45-54
    • Castro, M.G.1    McNamara, U.2    Carbonetti, N.H.3
  • 9
    • 0742323006 scopus 로고    scopus 로고
    • Distinct roles for the AAA ATPases NSF and p97 in the secretory pathway
    • Dalal, S., M. F. Rosser, D. M. Cyr, and P. I. Hanson. 2004. Distinct roles for the AAA ATPases NSF and p97 in the secretory pathway. Mol. Biol. Cell 15:637-648.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 637-648
    • Dalal, S.1    Rosser, M.F.2    Cyr, D.M.3    Hanson, P.I.4
  • 10
    • 0037066109 scopus 로고    scopus 로고
    • The low lysine content of ricin A chain reduces the risk of proteolytic degradation after translocation from the endoplasmic reticulum to the cytosol
    • Deeks, E. D., J. P. Cook, P. J. Day, D. C. Smith, L. M. Roberts, and J. M. Lord. 2002. The low lysine content of ricin A chain reduces the risk of proteolytic degradation after translocation from the endoplasmic reticulum to the cytosol. Biochemistry 41:3405-3413.
    • (2002) Biochemistry , vol.41 , pp. 3405-3413
    • Deeks, E.D.1    Cook, J.P.2    Day, P.J.3    Smith, D.C.4    Roberts, L.M.5    Lord, J.M.6
  • 11
    • 18744402497 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation of ricin A chain has unique and plant-specific features
    • Di Cola, A., L. Frigerio, J. M. Lord, L. M. Roberts, and A. Ceriotti. 2005. Endoplasmic reticulum-associated degradation of ricin A chain has unique and plant-specific features. Plant Physiol. 137:287-296.
    • (2005) Plant Physiol , vol.137 , pp. 287-296
    • Di Cola, A.1    Frigerio, L.2    Lord, J.M.3    Roberts, L.M.4    Ceriotti, A.5
  • 13
    • 0028936760 scopus 로고
    • Degradation of ornithine decarboxylase by the mammalian and yeast 26S proteasome complexes requires all the components of the protease
    • Elias, S., B. Bercovich, C. Kahana, P. Conino, M. Fischer, W. Hilt, D. H. Wolf, and A. Ciechanover. 1995. Degradation of ornithine decarboxylase by the mammalian and yeast 26S proteasome complexes requires all the components of the protease. Eur. J. Biochem. 229:276-283.
    • (1995) Eur. J. Biochem , vol.229 , pp. 276-283
    • Elias, S.1    Bercovich, B.2    Kahana, C.3    Conino, P.4    Fischer, M.5    Hilt, W.6    Wolf, D.H.7    Ciechanover, A.8
  • 14
    • 1042278180 scopus 로고    scopus 로고
    • Distinct steps in dislocation of luminal endoplasmic reticulum-associated degradation substrates: Roles of endoplasmic reticulum-bound p97/Cdc48p and proteasome
    • Elkabetz, Y., I. Shapira, E. Rabinovich, and S. Bar-Nun. 2004. Distinct steps in dislocation of luminal endoplasmic reticulum-associated degradation substrates: roles of endoplasmic reticulum-bound p97/Cdc48p and proteasome. J. Biol. Chem. 279:3980-3989.
    • (2004) J. Biol. Chem , vol.279 , pp. 3980-3989
    • Elkabetz, Y.1    Shapira, I.2    Rabinovich, E.3    Bar-Nun, S.4
  • 15
    • 0023219950 scopus 로고
    • RNA N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes
    • Endo, Y., and K. Tsurugi. 1987. RNA N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes. J. Biol. Chem. 262:8128-8130.
    • (1987) J. Biol. Chem , vol.262 , pp. 8128-8130
    • Endo, Y.1    Tsurugi, K.2
  • 16
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific aminoterminal threonine modification by lactacystin
    • Fenteany, G., R. F. Standaert, W. S. Lane, S. Choi, E. J. Corey, and S. L. Schreiber. 1995. Inhibition of proteasome activities and subunit-specific aminoterminal threonine modification by lactacystin. Science 268:726-731.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 17
    • 0024237306 scopus 로고
    • Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum
    • Fujiwara, T., K. Oda, S. Yokota, A. Takatsuki, and Y. Ikehara. 1988. Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum. J. Biol. Chem. 263:18545-18552.
    • (1988) J. Biol. Chem , vol.263 , pp. 18545-18552
    • Fujiwara, T.1    Oda, K.2    Yokota, S.3    Takatsuki, A.4    Ikehara, Y.5
  • 18
    • 0037023764 scopus 로고    scopus 로고
    • A principal role for the proteasome in endoplasmic reticulum-associated degradation of misfolded intracellular cystic fibrosis transmembrane conductance regulator
    • Gelman, M. S., E. S. Kannegaard, and R. R. Kopito. 2002. A principal role for the proteasome in endoplasmic reticulum-associated degradation of misfolded intracellular cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 277:11709-11714.
    • (2002) J. Biol. Chem , vol.277 , pp. 11709-11714
    • Gelman, M.S.1    Kannegaard, E.S.2    Kopito, R.R.3
  • 19
    • 0032959440 scopus 로고    scopus 로고
    • Overview of N- and O-linked oligosaccharide structures found in various yeast species
    • Gemmili, T. R., and R. B. Trimble. 1999. Overview of N- and O-linked oligosaccharide structures found in various yeast species. Biochim. Biophys. Acta 1426:227-237.
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 227-237
    • Gemmili, T.R.1    Trimble, R.B.2
  • 20
    • 0030886889 scopus 로고    scopus 로고
    • Accumulating evidence suggests that several AB-toxins subvert the endoplasmic reticulum-associated protein degradation pathway to enter target cells
    • Hazes, B., and R. J. Read. 1997. Accumulating evidence suggests that several AB-toxins subvert the endoplasmic reticulum-associated protein degradation pathway to enter target cells. Biochemistry 36:11051-11054.
    • (1997) Biochemistry , vol.36 , pp. 11051-11054
    • Hazes, B.1    Read, R.J.2
  • 21
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 23
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen, T. J., M. A. Loo, S. Pind, D. B. Williams, A. L. Goldberg, and J. R. Riordan. 1995. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83:129-135.
    • (1995) Cell , vol.83 , pp. 129-135
    • Jensen, T.J.1    Loo, M.A.2    Pind, S.3    Williams, D.B.4    Goldberg, A.L.5    Riordan, J.R.6
  • 24
    • 0020791359 scopus 로고
    • The A protomer of islet-activating protein, pertussis toxin, as an active peptide catalyzing ADP-ribosylation of a membrane protein
    • Katada, T., M. Tamura, and M. Ui. 1983. The A protomer of islet-activating protein, pertussis toxin, as an active peptide catalyzing ADP-ribosylation of a membrane protein. Arch. Biochem. Biophys. 224:290-298.
    • (1983) Arch. Biochem. Biophys , vol.224 , pp. 290-298
    • Katada, T.1    Tamura, M.2    Ui, M.3
  • 25
    • 0025184648 scopus 로고
    • Pertussis toxin analog with reduced enzymatic and biological activities is a protective immunogen
    • Kimura, A., K. T. Mounlzouros, P. A. Schad, W. Cieplak, and J. L. Cowell. 1990. Pertussis toxin analog with reduced enzymatic and biological activities is a protective immunogen. Infect. Immun. 58:3337-3347.
    • (1990) Infect. Immun , vol.58 , pp. 3337-3347
    • Kimura, A.1    Mounlzouros, K.T.2    Schad, P.A.3    Cieplak, W.4    Cowell, J.L.5
  • 26
    • 31044445642 scopus 로고    scopus 로고
    • Pertussis toxin inhibits neutrophil recruitment to delay antibody-mediated clearance of Bordetella pertussis
    • Kirimanjeswara, G. S., L. M. Agosto, M. J. Kennett, O. N. Bjornstad, and E. T. Harvill. 2005. Pertussis toxin inhibits neutrophil recruitment to delay antibody-mediated clearance of Bordetella pertussis. J. Clin. Investig. 115:3594-3601.
    • (2005) J. Clin. Investig , vol.115 , pp. 3594-3601
    • Kirimanjeswara, G.S.1    Agosto, L.M.2    Kennett, M.J.3    Bjornstad, O.N.4    Harvill, E.T.5
  • 27
    • 29144434531 scopus 로고    scopus 로고
    • Raft trafficking of AB5 subunit bacterial toxins
    • Lencer, W. I., and D. Saslowsky. 2005. Raft trafficking of AB5 subunit bacterial toxins. Biochim. Biophys. Acta 1746:314-321.
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 314-321
    • Lencer, W.I.1    Saslowsky, D.2
  • 28
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • Lilley, B. N., and H. L. Ploegh. 2004. A membrane protein required for dislocation of misfolded proteins from the ER. Nature 429:834-840.
    • (2004) Nature , vol.429 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 29
    • 0021100134 scopus 로고
    • Activation by thiol of the latent NAD glycohydrolase and ADP-ribosyltransferase activities of Bordetella pertussis toxin (islet-activating protein)
    • Moss, J., S. J. Stanley, D. L. Burns, J. A. Hsia, D. A. Yost, G. A. Myers, and E. L. Hewlett. 1983. Activation by thiol of the latent NAD glycohydrolase and ADP-ribosyltransferase activities of Bordetella pertussis toxin (islet-activating protein). J. Biol. Chem. 258:11879-11882.
    • (1983) J. Biol. Chem , vol.258 , pp. 11879-11882
    • Moss, J.1    Stanley, S.J.2    Burns, D.L.3    Hsia, J.A.4    Yost, D.A.5    Myers, G.A.6    Hewlett, E.L.7
  • 30
    • 33751229337 scopus 로고    scopus 로고
    • The pertussis toxin S1 subunit is a thermally unstable protein susceptible to degradation by the 20S proteasome
    • Pande, A. H., D. Moe, M. Jamnadas, S. A. Tatulian, and K. Teter. 2006. The pertussis toxin S1 subunit is a thermally unstable protein susceptible to degradation by the 20S proteasome. Biochemistry 45:13734-13740.
    • (2006) Biochemistry , vol.45 , pp. 13734-13740
    • Pande, A.H.1    Moe, D.2    Jamnadas, M.3    Tatulian, S.A.4    Teter, K.5
  • 31
    • 0034327504 scopus 로고    scopus 로고
    • Ubiquitin in chains
    • Pickart, C. M. 2000. Ubiquitin in chains. Trends Biochem. Sci. 25:544-548.
    • (2000) Trends Biochem. Sci , vol.25 , pp. 544-548
    • Pickart, C.M.1
  • 32
    • 0030789680 scopus 로고    scopus 로고
    • Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation
    • Pilon, M., R. Schekman, and K. Romisch. 1997. Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation. EMBO J. 16:4540-4548.
    • (1997) EMBO J , vol.16 , pp. 4540-4548
    • Pilon, M.1    Schekman, R.2    Romisch, K.3
  • 34
    • 1842409617 scopus 로고    scopus 로고
    • Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
    • Plemper, R. K., S. Bohmler, J. Bordallo, T. Sommer, and D. H. Wolf. 1997. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 388:891-895.
    • (1997) Nature , vol.388 , pp. 891-895
    • Plemper, R.K.1    Bohmler, S.2    Bordallo, J.3    Sommer, T.4    Wolf, D.H.5
  • 35
    • 0032484024 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation of a mutated ATP-binding cassette transporter Pdr5 proceeds in a concerted action of Sec61 and the proteasome
    • Plemper, R. K., R. Egner, K. Kuchler, and D. H. Wolf. 1998. Endoplasmic reticulum degradation of a mutated ATP-binding cassette transporter Pdr5 proceeds in a concerted action of Sec61 and the proteasome. J. Biol. Chem. 273:32848-32856.
    • (1998) J. Biol. Chem , vol.273 , pp. 32848-32856
    • Plemper, R.K.1    Egner, R.2    Kuchler, K.3    Wolf, D.H.4
  • 36
    • 12244305596 scopus 로고    scopus 로고
    • Role of ubiquitination in retro-translocation of cholera toxin and escape of cytosolic degradation
    • Rodighiero, C., B. Tsai, T. A. Rapoport, and W. I. Lencer. 2002. Role of ubiquitination in retro-translocation of cholera toxin and escape of cytosolic degradation. EMBO Rep. 3:1222-1227.
    • (2002) EMBO Rep , vol.3 , pp. 1222-1227
    • Rodighiero, C.1    Tsai, B.2    Rapoport, T.A.3    Lencer, W.I.4
  • 38
    • 0025259884 scopus 로고
    • Selective modulation of the endocytic uptake of ricin and fluid phase markers without alteration in transferrin endocytosis
    • Sandvig, K., and B. van Deurs. 1990. Selective modulation of the endocytic uptake of ricin and fluid phase markers without alteration in transferrin endocytosis. J. Biol. Chem. 265:6382-6388.
    • (1990) J. Biol. Chem , vol.265 , pp. 6382-6388
    • Sandvig, K.1    van Deurs, B.2
  • 39
    • 0034689054 scopus 로고    scopus 로고
    • Cholera toxin is exported from microsomes by the Sec61p complex
    • Schmitz, A., H. Herrgen, A. Winkeler, and V. Herzog. 2000. Cholera toxin is exported from microsomes by the Sec61p complex. J. Cell Biol. 148:1203-1212.
    • (2000) J. Cell Biol , vol.148 , pp. 1203-1212
    • Schmitz, A.1    Herrgen, H.2    Winkeler, A.3    Herzog, V.4
  • 41
    • 0032879634 scopus 로고    scopus 로고
    • Ricin A chain utilises the endoplasmic reticulum-associated protein degradation pathway to enter the cytosol of yeast
    • Simpson, J. C., L. M. Roberts, K. Romisch, J. Davey, D. H. Wolf, and J. M. Lord. 1999. Ricin A chain utilises the endoplasmic reticulum-associated protein degradation pathway to enter the cytosol of yeast. FEBS Lett. 459:80-84.
    • (1999) FEBS Lett , vol.459 , pp. 80-84
    • Simpson, J.C.1    Roberts, L.M.2    Romisch, K.3    Davey, J.4    Wolf, D.H.5    Lord, J.M.6
  • 42
    • 0014862345 scopus 로고
    • A simple chemically defined medium for the production of phase I Bordetella pertussis
    • Stainer, D. W., and M. J. Scholte. 1970. A simple chemically defined medium for the production of phase I Bordetella pertussis. J. Gen. Microbiol. 63:211-220.
    • (1970) J. Gen. Microbiol , vol.63 , pp. 211-220
    • Stainer, D.W.1    Scholte, M.J.2
  • 44
    • 0036839684 scopus 로고    scopus 로고
    • Transfer of the cholera toxin A1 polypeptide from the endoplasmic reticulum to the cytosol is a rapid process facilitated by the endoplasmic reticulum-associated degradation pathway
    • Teter, K., R. L. Allyn, M. G. Jobling, and R. K. Holmes. 2002. Transfer of the cholera toxin A1 polypeptide from the endoplasmic reticulum to the cytosol is a rapid process facilitated by the endoplasmic reticulum-associated degradation pathway. Infect. Immun. 70:6166-6171.
    • (2002) Infect. Immun , vol.70 , pp. 6166-6171
    • Teter, K.1    Allyn, R.L.2    Jobling, M.G.3    Holmes, R.K.4
  • 45
    • 33645505579 scopus 로고    scopus 로고
    • 3 subdomain is essential for interaction with ADP-ribosylation factor 6 and full toxic activity but is not required for translocation from the endoplasmic reticulum to the cytosol
    • 3 subdomain is essential for interaction with ADP-ribosylation factor 6 and full toxic activity but is not required for translocation from the endoplasmic reticulum to the cytosol. Infect. Immun. 74:2259-2267.
    • (2006) Infect. Immun , vol.74 , pp. 2259-2267
    • Teter, K.1    Jobling, M.G.2    Sentz, D.3    Holmes, R.K.4
  • 46
    • 0034602845 scopus 로고    scopus 로고
    • Recognition of the polyubiquitin proteolytic signal
    • Thrower, J. S., L. Hoffman, M. Rechsteiner, and C. M. Pickart. 2000. Recognition of the polyubiquitin proteolytic signal. EMBO J. 19:94-102.
    • (2000) EMBO J , vol.19 , pp. 94-102
    • Thrower, J.S.1    Hoffman, L.2    Rechsteiner, M.3    Pickart, C.M.4
  • 47
    • 0020514310 scopus 로고
    • Adherence of Bordetella pertussis to human respiratory epithelial cells
    • Tuomanen, E. I., and J. O. Hendley. 1983. Adherence of Bordetella pertussis to human respiratory epithelial cells. J. Infect. Dis. 148:125-130.
    • (1983) J. Infect. Dis , vol.148 , pp. 125-130
    • Tuomanen, E.I.1    Hendley, J.O.2
  • 48
    • 0030447659 scopus 로고    scopus 로고
    • Proteasome-dependent endoplasmic reticulum-associated protein degradation: An unconventional route to a familiar fate
    • Werner, E. D., J. L. Brodsky, and A. A. McCracken. 1996. Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate. Proc. Natl. Acad. Sci. USA 93:13797-13801.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13797-13801
    • Werner, E.D.1    Brodsky, J.L.2    McCracken, A.A.3
  • 49
    • 0033607688 scopus 로고    scopus 로고
    • Dependence of ricin toxicity on translocation of the toxin A-chain from the endoplasmic reticulum to the cytosol
    • Wesche, J., A. Rapak, and S. Olsnes. 1999. Dependence of ricin toxicity on translocation of the toxin A-chain from the endoplasmic reticulum to the cytosol. J. Biol. Chem. 274:34443-34449.
    • (1999) J. Biol. Chem , vol.274 , pp. 34443-34449
    • Wesche, J.1    Rapak, A.2    Olsnes, S.3
  • 51
    • 0030034114 scopus 로고    scopus 로고
    • Pertussis toxin-catalyzed ADP-ribosylation of Gi-2 and Gi-3 in CHO cells is modulated by inhibitors of intracellular trafficking
    • Xu, Y., and J. T. Barbieri. 1996. Pertussis toxin-catalyzed ADP-ribosylation of Gi-2 and Gi-3 in CHO cells is modulated by inhibitors of intracellular trafficking. Infect. Immun. 64:593-599.
    • (1996) Infect. Immun , vol.64 , pp. 593-599
    • Xu, Y.1    Barbieri, J.T.2
  • 52
    • 0028905448 scopus 로고
    • Pertussis toxin-mediated ADP-ribosylation of target proteins in Chinese hamster ovary cells involves a vesicle trafficking mechanism
    • Xu, Y., and J. T. Barbieri. 1995. Pertussis toxin-mediated ADP-ribosylation of target proteins in Chinese hamster ovary cells involves a vesicle trafficking mechanism. Infect. Immun. 63:825-832.
    • (1995) Infect. Immun , vol.63 , pp. 825-832
    • Xu, Y.1    Barbieri, J.T.2
  • 53
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye, Y., H. H. Meyer, and T. A. Rapoport. 2001. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414:652-656.
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 54
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-Ufd1-Np14 complex in retrotranslocation from the ER to the cytosol: Dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • Ye, Y., H. H. Meyer, and T. A. Rapoport. 2003. Function of the p97-Ufd1-Np14 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J. Cell Biol. 162:71-84.
    • (2003) J. Cell Biol , vol.162 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 55
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
    • Ye, Y., Y. Shibata, C. Yun, D. Ron, and T. A. Rapoport. 2004. A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 429:841-847.
    • (2004) Nature , vol.429 , pp. 841-847
    • Ye, Y.1    Shibata, Y.2    Yun, C.3    Ron, D.4    Rapoport, T.A.5
  • 56
    • 0033382189 scopus 로고    scopus 로고
    • The engagement of Sec61p in the ER dislocation process
    • Zhou, M., and R. Schekman. 1999. The engagement of Sec61p in the ER dislocation process. Mol. Cell 4:925-934.
    • (1999) Mol. Cell , vol.4 , pp. 925-934
    • Zhou, M.1    Schekman, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.