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Volumn 8, Issue 10, 2013, Pages

Establishment of an In Vitro Transport Assay That Reveals Mechanistic Differences in Cytosolic Events Controlling Cholera Toxin and T-Cell Receptor α Retro-Translocation

Author keywords

[No Author keywords available]

Indexed keywords

CHOLERA TOXIN; CHOLERA TOXIN A1; GANGLIOSIDE GM1; GUANOSINE TRIPHOSPHATE; PROTEASOME; T LYMPHOCYTE RECEPTOR ALPHA CHAIN; UNCLASSIFIED DRUG;

EID: 84885395221     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0075801     Document Type: Article
Times cited : (17)

References (50)
  • 2
    • 0037013269 scopus 로고    scopus 로고
    • Uncoupling of the cholera toxin-G(M1) ganglioside receptor complex from endocytosis, retrograde Golgi trafficking, and downstream signal transduction by depletion of membrane cholesterol
    • Wolf AA, Fujinaga Y, Lencer WI, (2002) Uncoupling of the cholera toxin-G(M1) ganglioside receptor complex from endocytosis, retrograde Golgi trafficking, and downstream signal transduction by depletion of membrane cholesterol. J Biol Chem 277: 16249-16256.
    • (2002) J Biol Chem , vol.277 , pp. 16249-16256
    • Wolf, A.A.1    Fujinaga, Y.2    Lencer, W.I.3
  • 3
    • 84866034926 scopus 로고    scopus 로고
    • Lipid sorting by ceramide structure from plasma membrane to ER for the cholera toxin receptor ganglioside GM1
    • Chinnapen DJ, Hsieh WT, te Welscher YM, Saslowsky DE, Kaoutzani L, et al. (2012) Lipid sorting by ceramide structure from plasma membrane to ER for the cholera toxin receptor ganglioside GM1. Dev Cell 23: 573-586.
    • (2012) Dev Cell , vol.23 , pp. 573-586
    • Chinnapen, D.J.1    Hsieh, W.T.2    te Welscher, Y.M.3    Saslowsky, D.E.4    Kaoutzani, L.5
  • 4
    • 6044235526 scopus 로고    scopus 로고
    • Trafficking of cholera toxin-ganglioside GM1 complex into Golgi and induction of toxicity depend on actin cytoskeleton
    • Badizadegan K, Wheeler HE, Fujinaga Y, Lencer WI, (2004) Trafficking of cholera toxin-ganglioside GM1 complex into Golgi and induction of toxicity depend on actin cytoskeleton. Am J Physiol Cell Physiol 287: C1453-1462.
    • (2004) Am J Physiol Cell Physiol , vol.287
    • Badizadegan, K.1    Wheeler, H.E.2    Fujinaga, Y.3    Lencer, W.I.4
  • 5
    • 78649855802 scopus 로고    scopus 로고
    • Intoxication of zebrafish and mammalian cells by cholera toxin depends on the flotillin/reggie proteins but not Derlin-1 or -2
    • Saslowsky DE, Cho JA, Chinnapen H, Massol RH, Chinnapen DJ, et al. (2010) Intoxication of zebrafish and mammalian cells by cholera toxin depends on the flotillin/reggie proteins but not Derlin-1 or-2. J Clin Invest 120: 4399-4409.
    • (2010) J Clin Invest , vol.120 , pp. 4399-4409
    • Saslowsky, D.E.1    Cho, J.A.2    Chinnapen, H.3    Massol, R.H.4    Chinnapen, D.J.5
  • 6
    • 84873253810 scopus 로고    scopus 로고
    • Investigating endocytic pathways to the endoplasmic reticulum and to the cytosol using SNAP-trap
    • Geiger R, Luisoni S, Johnsson K, Greber UF, Helenius A, (2013) Investigating endocytic pathways to the endoplasmic reticulum and to the cytosol using SNAP-trap. Traffic 14: 36-46.
    • (2013) Traffic , vol.14 , pp. 36-46
    • Geiger, R.1    Luisoni, S.2    Johnsson, K.3    Greber, U.F.4    Helenius, A.5
  • 7
    • 0031006074 scopus 로고    scopus 로고
    • Proteolytic activation of cholera toxin and Escherichia coli labile toxin by entry into host epithelial cells. Signal transduction by a protease-resistant toxin variant
    • Lencer WI, Constable C, Moe S, Rufo PA, Wolf A, et al. (1997) Proteolytic activation of cholera toxin and Escherichia coli labile toxin by entry into host epithelial cells. Signal transduction by a protease-resistant toxin variant. J Biol Chem 272: 15562-15568.
    • (1997) J Biol Chem , vol.272 , pp. 15562-15568
    • Lencer, W.I.1    Constable, C.2    Moe, S.3    Rufo, P.A.4    Wolf, A.5
  • 8
    • 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, Read RJ, (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
  • 9
    • 84870907436 scopus 로고    scopus 로고
    • Cleaning up: ER-associated degradation to the rescue
    • Brodsky JL, (2012) Cleaning up: ER-associated degradation to the rescue. Cell 151: 1163-1167.
    • (2012) Cell , vol.151 , pp. 1163-1167
    • Brodsky, J.L.1
  • 10
    • 12244305596 scopus 로고    scopus 로고
    • Role of ubiquitination in retro-translocation of cholera toxin and escape of cytosolic degradation
    • Rodighiero C, Tsai B, Rapoport TA, Lencer WI, (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
  • 12
    • 79959347089 scopus 로고    scopus 로고
    • A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation
    • Wang Q, Liu Y, Soetandyo N, Baek K, Hegde R, et al. (2011) A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation. Mol Cell 42: 758-770.
    • (2011) Mol Cell , vol.42 , pp. 758-770
    • Wang, Q.1    Liu, Y.2    Soetandyo, N.3    Baek, K.4    Hegde, R.5
  • 13
    • 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 RJ, Dalal S, Hanson PI, Draper RK, (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    Dalal, S.2    Hanson, P.I.3    Draper, R.K.4
  • 14
    • 23044460010 scopus 로고    scopus 로고
    • Role of p97 AAA-ATPase in the retrotranslocation of the cholera toxin A1 chain, a non-ubiquitinated substrate
    • Kothe M, Ye Y, Wagner JS, De Luca HE, Kern E, et al. (2005) Role of p97 AAA-ATPase in the retrotranslocation of the cholera toxin A1 chain, a non-ubiquitinated substrate. J Biol Chem 280: 28127-28132.
    • (2005) J Biol Chem , vol.280 , pp. 28127-28132
    • Kothe, M.1    Ye, Y.2    Wagner, J.S.3    De Luca, H.E.4    Kern, E.5
  • 15
    • 33745224935 scopus 로고    scopus 로고
    • p97: The cell's molecular purgatory?
    • Halawani D, Latterich M, (2006) p97: The cell's molecular purgatory? Mol Cell 22: 713-717.
    • (2006) Mol Cell , vol.22 , pp. 713-717
    • Halawani, D.1    Latterich, M.2
  • 17
    • 80052451417 scopus 로고    scopus 로고
    • Endolysosomal sorting of ubiquitylated caveolin-1 is regulated by VCP and UBXD1 and impaired by VCP disease mutations
    • Ritz D, Vuk M, Kirchner P, Bug M, Schutz S, et al. (2011) Endolysosomal sorting of ubiquitylated caveolin-1 is regulated by VCP and UBXD1 and impaired by VCP disease mutations. Nat Cell Biol 13: 1116-1123.
    • (2011) Nat Cell Biol , vol.13 , pp. 1116-1123
    • Ritz, D.1    Vuk, M.2    Kirchner, P.3    Bug, M.4    Schutz, S.5
  • 18
    • 84856620090 scopus 로고    scopus 로고
    • The p97 ATPase associates with EEA1 to regulate the size of early endosomes
    • Ramanathan HN, Ye Y, (2012) The p97 ATPase associates with EEA1 to regulate the size of early endosomes. Cell Res 22: 346-359.
    • (2012) Cell Res , vol.22 , pp. 346-359
    • Ramanathan, H.N.1    Ye, Y.2
  • 19
    • 17044386675 scopus 로고    scopus 로고
    • p97/p47-Mediated biogenesis of Golgi and ER
    • Uchiyama K, Kondo H, (2005) p97/p47-Mediated biogenesis of Golgi and ER. J Biochem 137: 115-119.
    • (2005) J Biochem , vol.137 , pp. 115-119
    • Uchiyama, K.1    Kondo, H.2
  • 20
    • 0029122698 scopus 로고
    • Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes
    • Latterich M, Frohlich KU, Schekman R, (1995) Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes. Cell 82: 885-893.
    • (1995) Cell , vol.82 , pp. 885-893
    • Latterich, M.1    Frohlich, K.U.2    Schekman, R.3
  • 21
    • 33745265260 scopus 로고    scopus 로고
    • Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation
    • Forster ML, Sivick K, Park YN, Arvan P, Lencer WI, et al. (2006) Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation. J Cell Biol 173: 853-859.
    • (2006) J Cell Biol , vol.173 , pp. 853-859
    • Forster, M.L.1    Sivick, K.2    Park, Y.N.3    Arvan, P.4    Lencer, W.I.5
  • 22
    • 77949894225 scopus 로고    scopus 로고
    • N-terminal extension of the cholera toxin A1-chain causes rapid degradation after retrotranslocation from endoplasmic reticulum to cytosol
    • Wernick NL, De Luca H, Kam WR, Lencer WI, (2010) N-terminal extension of the cholera toxin A1-chain causes rapid degradation after retrotranslocation from endoplasmic reticulum to cytosol. J Biol Chem 285: 6145-6152.
    • (2010) J Biol Chem , vol.285 , pp. 6145-6152
    • Wernick, N.L.1    De Luca, H.2    Kam, W.R.3    Lencer, W.I.4
  • 23
    • 77957817389 scopus 로고    scopus 로고
    • Hsp90 is required for transfer of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol
    • Taylor M, Navarro-Garcia F, Huerta J, Burress H, Massey S, et al. (2010) Hsp90 is required for transfer of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol. J Biol Chem 285: 31261-31267.
    • (2010) J Biol Chem , vol.285 , pp. 31261-31267
    • Taylor, M.1    Navarro-Garcia, F.2    Huerta, J.3    Burress, H.4    Massey, S.5
  • 24
    • 79960292775 scopus 로고    scopus 로고
    • TorsinA participates in endoplasmic reticulum-associated degradation
    • Nery FC, Armata IA, Farley JE, Cho JA, Yaqub U, et al. (2011) TorsinA participates in endoplasmic reticulum-associated degradation. Nat Commun 2: 393.
    • (2011) Nat Commun , vol.2 , pp. 393
    • Nery, F.C.1    Armata, I.A.2    Farley, J.E.3    Cho, J.A.4    Yaqub, U.5
  • 25
    • 79958051219 scopus 로고    scopus 로고
    • A large and intact viral particle penetrates the endoplasmic reticulum membrane to reach the cytosol
    • Inoue T, Tsai B, (2011) A large and intact viral particle penetrates the endoplasmic reticulum membrane to reach the cytosol. PLoS Pathog 7: e1002037.
    • (2011) PLoS Pathog , vol.7
    • Inoue, T.1    Tsai, B.2
  • 26
    • 84855195138 scopus 로고    scopus 로고
    • BiP and multiple DNAJ molecular chaperones in the endoplasmic reticulum are required for efficient simian virus 40 infection
    • Goodwin EC, Lipovsky A, Inoue T, Magaldi TG, Edwards AP, et al. (2011) BiP and multiple DNAJ molecular chaperones in the endoplasmic reticulum are required for efficient simian virus 40 infection. MBio 2: e00101-00111.
    • (2011) MBio , vol.2
    • Goodwin, E.C.1    Lipovsky, A.2    Inoue, T.3    Magaldi, T.G.4    Edwards, A.P.5
  • 27
    • 80455143829 scopus 로고    scopus 로고
    • BAP31 and BiP are essential for dislocation of SV40 from the endoplasmic reticulum to the cytosol
    • Geiger R, Andritschke D, Friebe S, Herzog F, Luisoni S, et al. (2011) BAP31 and BiP are essential for dislocation of SV40 from the endoplasmic reticulum to the cytosol. Nat Cell Biol 13: 1305-1314.
    • (2011) Nat Cell Biol , vol.13 , pp. 1305-1314
    • Geiger, R.1    Andritschke, D.2    Friebe, S.3    Herzog, F.4    Luisoni, S.5
  • 28
    • 0033055636 scopus 로고    scopus 로고
    • Membrane traffic and the cellular uptake of cholera toxin
    • Lencer WI, Hirst TR, Holmes RK, (1999) Membrane traffic and the cellular uptake of cholera toxin. Biochim Biophys Acta 1450: 177-190.
    • (1999) Biochim Biophys Acta , vol.1450 , pp. 177-190
    • Lencer, W.I.1    Hirst, T.R.2    Holmes, R.K.3
  • 29
    • 0035937408 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
    • Tsai B, Rodighiero C, Lencer WI, Rapoport TA, (2001) Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell 104: 937-948.
    • (2001) Cell , vol.104 , pp. 937-948
    • Tsai, B.1    Rodighiero, C.2    Lencer, W.I.3    Rapoport, T.A.4
  • 30
    • 0030744415 scopus 로고    scopus 로고
    • The alpha chain of the T cell antigen receptor is degraded in the cytosol
    • Huppa JB, Ploegh HL, (1997) The alpha chain of the T cell antigen receptor is degraded in the cytosol. Immunity 7: 113-122.
    • (1997) Immunity , vol.7 , pp. 113-122
    • Huppa, J.B.1    Ploegh, H.L.2
  • 31
    • 0030817978 scopus 로고    scopus 로고
    • Cytosolic degradation of T-cell receptor alpha chains by the proteasome
    • Yu H, Kaung G, Kobayashi S, Kopito RR, (1997) Cytosolic degradation of T-cell receptor alpha chains by the proteasome. J Biol Chem 272: 20800-20804.
    • (1997) J Biol Chem , vol.272 , pp. 20800-20804
    • Yu, H.1    Kaung, G.2    Kobayashi, S.3    Kopito, R.R.4
  • 32
    • 33646535590 scopus 로고    scopus 로고
    • Central pore residues mediate the p97/VCP activity required for ERAD
    • DeLaBarre B, Christianson JC, Kopito RR, Brunger AT, (2006) Central pore residues mediate the p97/VCP activity required for ERAD. Mol Cell 22: 451-462.
    • (2006) Mol Cell , vol.22 , pp. 451-462
    • DeLaBarre, B.1    Christianson, J.C.2    Kopito, R.R.3    Brunger, A.T.4
  • 33
    • 33748988214 scopus 로고    scopus 로고
    • Regulation of retrotranslocation by p97-associated deubiquitinating enzyme ataxin-3
    • Wang Q, Li L, Ye Y, (2006) Regulation of retrotranslocation by p97-associated deubiquitinating enzyme ataxin-3. J Cell Biol 174: 963-971.
    • (2006) J Cell Biol , vol.174 , pp. 963-971
    • Wang, Q.1    Li, L.2    Ye, Y.3
  • 34
    • 34248561455 scopus 로고    scopus 로고
    • A novel function of VCP (valosin-containing protein; p97) in the control of N-glycosylation of proteins in the endoplasmic reticulum
    • Lass A, McConnell E, Nowis D, Mechref Y, Kang P, et al. (2007) A novel function of VCP (valosin-containing protein; p97) in the control of N-glycosylation of proteins in the endoplasmic reticulum. Arch Biochem Biophys 462: 62-73.
    • (2007) Arch Biochem Biophys , vol.462 , pp. 62-73
    • Lass, A.1    McConnell, E.2    Nowis, D.3    Mechref, Y.4    Kang, P.5
  • 35
    • 0034757165 scopus 로고    scopus 로고
    • Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast
    • Zhang Y, Nijbroek G, Sullivan ML, McCracken AA, Watkins SC, et al. (2001) Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast. Mol Biol Cell 12: 1303-1314.
    • (2001) Mol Biol Cell , vol.12 , pp. 1303-1314
    • Zhang, Y.1    Nijbroek, G.2    Sullivan, M.L.3    McCracken, A.A.4    Watkins, S.C.5
  • 36
    • 34548857070 scopus 로고    scopus 로고
    • Cytoplasmic Hsp70 promotes ubiquitination for endoplasmic reticulum-associated degradation of a misfolded mutant of the yeast plasma membrane ATPase, PMA1
    • Han S, Liu Y, Chang A, (2007) Cytoplasmic Hsp70 promotes ubiquitination for endoplasmic reticulum-associated degradation of a misfolded mutant of the yeast plasma membrane ATPase, PMA1. J Biol Chem 282: 26140-26149.
    • (2007) J Biol Chem , vol.282 , pp. 26140-26149
    • Han, S.1    Liu, Y.2    Chang, A.3
  • 37
    • 37649025515 scopus 로고    scopus 로고
    • Dissecting the ER-associated degradation of a misfolded polytopic membrane protein
    • Nakatsukasa K, Huyer G, Michaelis S, Brodsky JL, (2008) Dissecting the ER-associated degradation of a misfolded polytopic membrane protein. Cell 132: 101-112.
    • (2008) Cell , vol.132 , pp. 101-112
    • Nakatsukasa, K.1    Huyer, G.2    Michaelis, S.3    Brodsky, J.L.4
  • 38
    • 3042543543 scopus 로고    scopus 로고
    • Uncoupling retro-translocation and degradation in the ER-associated degradation of a soluble protein
    • Lee RJ, Liu CW, Harty C, McCracken AA, Latterich M, et al. (2004) Uncoupling retro-translocation and degradation in the ER-associated degradation of a soluble protein. EMBO J 23: 2206-2215.
    • (2004) EMBO J , vol.23 , pp. 2206-2215
    • Lee, R.J.1    Liu, C.W.2    Harty, C.3    McCracken, A.A.4    Latterich, M.5
  • 39
    • 0033523771 scopus 로고    scopus 로고
    • The pathway of US11-dependent degradation of MHC class I heavy chains involves a ubiquitin-conjugated intermediate
    • Shamu CE, Story CM, Rapoport TA, Ploegh HL, (1999) The pathway of US11-dependent degradation of MHC class I heavy chains involves a ubiquitin-conjugated intermediate. J Cell Biol 147: 45-58.
    • (1999) J Cell Biol , vol.147 , pp. 45-58
    • Shamu, C.E.1    Story, C.M.2    Rapoport, T.A.3    Ploegh, H.L.4
  • 40
    • 4344568526 scopus 로고    scopus 로고
    • Carbohydrates act as sorting determinants in ER-associated degradation of tyrosinase
    • Svedine S, Wang T, Halaban R, Hebert DN, (2004) Carbohydrates act as sorting determinants in ER-associated degradation of tyrosinase. J Cell Sci 117: 2937-2949.
    • (2004) J Cell Sci , vol.117 , pp. 2937-2949
    • Svedine, S.1    Wang, T.2    Halaban, R.3    Hebert, D.N.4
  • 41
    • 33746851268 scopus 로고    scopus 로고
    • E2-25K mediates US11-triggered retro-translocation of MHC class I heavy chains in a permeabilized cell system
    • Flierman D, Coleman CS, Pickart CM, Rapoport TA, Chau V, (2006) E2-25K mediates US11-triggered retro-translocation of MHC class I heavy chains in a permeabilized cell system. Proc Natl Acad Sci U S A 103: 11589-11594.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 11589-11594
    • Flierman, D.1    Coleman, C.S.2    Pickart, C.M.3    Rapoport, T.A.4    Chau, V.5
  • 42
    • 84863620865 scopus 로고    scopus 로고
    • A viral deubiquitylating enzyme restores dislocation of substrates from the endoplasmic reticulum (ER) in semi-intact cells
    • Sanyal S, Claessen JH, Ploegh HL, (2012) A viral deubiquitylating enzyme restores dislocation of substrates from the endoplasmic reticulum (ER) in semi-intact cells. J Biol Chem 287: 23594-23603.
    • (2012) J Biol Chem , vol.287 , pp. 23594-23603
    • Sanyal, S.1    Claessen, J.H.2    Ploegh, H.L.3
  • 43
  • 44
    • 0030447659 scopus 로고    scopus 로고
    • Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate
    • Werner ED, Brodsky JL, McCracken AA, (1996) Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate. Proc Natl Acad Sci U S A 93: 13797-13801.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 13797-13801
    • Werner, E.D.1    Brodsky, J.L.2    McCracken, A.A.3
  • 45
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley D, (2009) Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu Rev Biochem 78: 477-513.
    • (2009) Annu Rev Biochem , vol.78 , pp. 477-513
    • Finley, D.1
  • 47
    • 56249144175 scopus 로고    scopus 로고
    • Cytosolic chaperones influence the fate of a toxin dislocated from the endoplasmic reticulum
    • Spooner RA, Hart PJ, Cook JP, Pietroni P, Rogon C, et al. (2008) Cytosolic chaperones influence the fate of a toxin dislocated from the endoplasmic reticulum. Proc Natl Acad Sci U S A 105: 17408-17413.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 17408-17413
    • Spooner, R.A.1    Hart, P.J.2    Cook, J.P.3    Pietroni, P.4    Rogon, C.5
  • 48
    • 43149093941 scopus 로고    scopus 로고
    • A proteasomal ATPase contributes to dislocation of endoplasmic reticulum-associated degradation (ERAD) substrates
    • Lipson C, Alalouf G, Bajorek M, Rabinovich E, Atir-Lande A, et al. (2008) A proteasomal ATPase contributes to dislocation of endoplasmic reticulum-associated degradation (ERAD) substrates. J Biol Chem 283: 7166-7175.
    • (2008) J Biol Chem , vol.283 , pp. 7166-7175
    • Lipson, C.1    Alalouf, G.2    Bajorek, M.3    Rabinovich, E.4    Atir-Lande, A.5
  • 49
    • 80053257157 scopus 로고    scopus 로고
    • How viruses and toxins disassemble to enter host cells
    • Inoue T, Moore P, Tsai B, (2011) How viruses and toxins disassemble to enter host cells. Annu Rev Microbiol 65: 287-305.
    • (2011) Annu Rev Microbiol , vol.65 , pp. 287-305
    • Inoue, T.1    Moore, P.2    Tsai, B.3
  • 50
    • 84857880542 scopus 로고    scopus 로고
    • How ricin and Shiga toxin reach the cytosol of target cells: retrotranslocation from the endoplasmic reticulum
    • Spooner RA, Lord JM, (2012) How ricin and Shiga toxin reach the cytosol of target cells: retrotranslocation from the endoplasmic reticulum. Curr Top Microbiol Immunol 357: 19-40.
    • (2012) Curr Top Microbiol Immunol , vol.357 , pp. 19-40
    • Spooner, R.A.1    Lord, J.M.2


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