메뉴 건너뛰기




Volumn 11, Issue 5, 2000, Pages 1775-1787

The p21 Rho-activating toxin cytotoxic necrotizing factor 1 is endocytosed by a clathrin-independent mechanism and enters the cytosol by an acidic-dependent membrane translocation step

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL TOXIN; CAVEOLIN; CELL SURFACE RECEPTOR; CHOLERA TOXIN; CLATHRIN; CYTOTOXIC FACTOR; DIPHTHERIA TOXIN; DYNAMIN; FILIPIN; GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN P21; RHO FACTOR; RICIN; TRANSFERRIN;

EID: 0034108090     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.11.5.1775     Document Type: Article
Times cited : (80)

References (79)
  • 1
    • 0026612457 scopus 로고
    • Intracellular localization of the p21Rho proteins
    • Adamson, P., Paterson, H.F., and Hall, A. (1992). Intracellular localization of the p21Rho proteins. J. Cell Biol. 119, 617-627.
    • (1992) J. Cell Biol. , vol.119 , pp. 617-627
    • Adamson, P.1    Paterson, H.F.2    Hall, A.3
  • 3
  • 5
    • 0029916264 scopus 로고    scopus 로고
    • Staphylococcal alpha-toxin, streptolysin-O and Escherichia coli hemolysin: Prototypes of pore-forming bacterial cytolysins
    • Bhakdi, S., Bayley, H., Valeva, A., Walev, I., Walker, B., Weller, U., Kehoe, M., and Palmer, M. (1996). Staphylococcal alpha-toxin, streptolysin-O and Escherichia coli hemolysin: prototypes of pore-forming bacterial cytolysins. Arch. Microbiol. 165, 73-79.
    • (1996) Arch. Microbiol. , vol.165 , pp. 73-79
    • Bhakdi, S.1    Bayley, H.2    Valeva, A.3    Walev, I.4    Walker, B.5    Weller, U.6    Kehoe, M.7    Palmer, M.8
  • 6
    • 0029989699 scopus 로고    scopus 로고
    • Virulence factors and O groups of Escherichia coli isolates from patients with acute pyelonephritis, cystitis and asymptomatic bacteriuria
    • Blanco, M., Blanco, J.E., Alonso, M.P., and Blanco., J. (1996). Virulence factors and O groups of Escherichia coli isolates from patients with acute pyelonephritis, cystitis and asymptomatic bacteriuria. Eur. J. Epidemiol. 12, 191-198.
    • (1996) Eur. J. Epidemiol. , vol.12 , pp. 191-198
    • Blanco, M.1    Blanco, J.E.2    Alonso, M.P.3    Blanco, J.4
  • 7
    • 0028985139 scopus 로고
    • Gene clusters encoding the cytotoxic necrotizing factor type 1, Prs-fimbriae and α-hemolysin from the pathogenicity island II of the uropathogenic Escherichia coli strain J96
    • Blum, G., Falbo, V., Caprioli, A., and Hacker, J. (1995). Gene clusters encoding the cytotoxic necrotizing factor type 1, Prs-fimbriae and α-hemolysin from the pathogenicity island II of the uropathogenic Escherichia coli strain J96. FEMS Microbiol. Lett. 126, 189-195.
    • (1995) FEMS Microbiol. Lett. , vol.126 , pp. 189-195
    • Blum, G.1    Falbo, V.2    Caprioli, A.3    Hacker, J.4
  • 8
    • 0001026865 scopus 로고    scopus 로고
    • The cytotoxic necrotizing factor 1 (CNF1) from Escherichia coli
    • ed. K. Aktories and I. Just, Berlin: Springer-Verlag (in press)
    • Boquet, P., and Fiorentini, C. (2000). The cytotoxic necrotizing factor 1 (CNF1) from Escherichia coli. In: Handbook of Experimental Pharmacology: Bacterial Protein Toxins, ed. K. Aktories and I. Just, Berlin: Springer-Verlag (in press).
    • (2000) Handbook of Experimental Pharmacology: Bacterial Protein Toxins
    • Boquet, P.1    Fiorentini, C.2
  • 9
    • 0003707675 scopus 로고
    • Modulation of cell function by ADP-ribosylating bacterial toxins
    • ed. J.E. Alouf and J.H. Freer, London: Academic Press
    • Boquet, P., and Gill, D.M. (1991). Modulation of cell function by ADP-ribosylating bacterial toxins. In: Sourcebook of Bacterial Protein Toxins, ed. J.E. Alouf and J.H. Freer, London: Academic Press, 23-44.
    • (1991) Sourcebook of Bacterial Protein Toxins , pp. 23-44
    • Boquet, P.1    Gill, D.M.2
  • 10
    • 0017124132 scopus 로고
    • Interaction of diphtheria toxin with mammalian cell membranes
    • Boquet, P., and Pappenheimer, A.M., Jr. (1976). Interaction of diphtheria toxin with mammalian cell membranes. J. Biol. Chem. 251, 5770-5778.
    • (1976) J. Biol. Chem. , vol.251 , pp. 5770-5778
    • Boquet, P.1    Pappenheimer A.M., Jr.2
  • 12
    • 0027169924 scopus 로고
    • Hypersensitivity to diphtheria toxin by mouse cells expressing both diphtheria receptor and CD9 antigen
    • Brown, J.G., Almond, B.D., Naglich, J.G., and Eidels, L. (1993). Hypersensitivity to diphtheria toxin by mouse cells expressing both diphtheria receptor and CD9 antigen. Proc. Natl. Acad. Sci. USA 90, 8184-8188.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8184-8188
    • Brown, J.G.1    Almond, B.D.2    Naglich, J.G.3    Eidels, L.4
  • 14
    • 0024449589 scopus 로고
    • The mammalian G protein rhoC is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells
    • Chardin, P., Boquet, P., Madaule, P., Popoff, M.R., Rubin, E.J., and Gill, D.M. (1989). The mammalian G protein rhoC is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells. EMBO J. 8, 1087-1092.
    • (1989) EMBO J. , vol.8 , pp. 1087-1092
    • Chardin, P.1    Boquet, P.2    Madaule, P.3    Popoff, M.R.4    Rubin, E.J.5    Gill, D.M.6
  • 15
    • 0033574449 scopus 로고    scopus 로고
    • Brefeldin A: The advantage of being uncompetitive
    • Chardin, P., and McCormick, F. (1999). Brefeldin A: the advantage of being uncompetitive. Cell 97, 153-155.
    • (1999) Cell , vol.97 , pp. 153-155
    • Chardin, P.1    McCormick, F.2
  • 16
    • 0029134736 scopus 로고
    • Clathrin-independent pinocytosis is induced in cells overexpressing a temperature-sensitive mutant of dynamin
    • Damke, H., Baba, T., van der Bliek, A.M., and Schmid, S.L. (1995). Clathrin-independent pinocytosis is induced in cells overexpressing a temperature-sensitive mutant of dynamin. J. Cell Biol. 131, 69-80.
    • (1995) J. Cell Biol. , vol.131 , pp. 69-80
    • Damke, H.1    Baba, T.2    Van Der Bliek, A.M.3    Schmid, S.L.4
  • 17
    • 0028036513 scopus 로고
    • Induction of mutant dynamin specifically blocks endocytic coated vesicle formation
    • Damke, H., Baba, T., Warnock, D.E., and Schmid, S.L. (1994). Induction of mutant dynamin specifically blocks endocytic coated vesicle formation. J. Cell Biol. 127, 915-934.
    • (1994) J. Cell Biol. , vol.127 , pp. 915-934
    • Damke, H.1    Baba, T.2    Warnock, D.E.3    Schmid, S.L.4
  • 18
    • 0019287379 scopus 로고
    • The entry of diphtheria toxin into the mammalian cell cytoplasm: Evidence for lysosomal involvement
    • Draper, R.K., and Simon, M.I. (1980). The entry of diphtheria toxin into the mammalian cell cytoplasm: evidence for lysosomal involvement. J. Cell Biol. 87, 849-854.
    • (1980) J. Cell Biol. , vol.87 , pp. 849-854
    • Draper, R.K.1    Simon, M.I.2
  • 19
    • 0033065155 scopus 로고    scopus 로고
    • The 5′ region of cnf1 harbours a translational regulatory mechanism for CNF1 synthesis and encodes the cell-binding domain of the toxin
    • Fabbri, A., Gauthier, M., and Boquet, P. (1999). The 5′ region of cnf1 harbours a translational regulatory mechanism for CNF1 synthesis and encodes the cell-binding domain of the toxin. Mol. Microbiol. 33, 108-118.
    • (1999) Mol. Microbiol. , vol.33 , pp. 108-118
    • Fabbri, A.1    Gauthier, M.2    Boquet, P.3
  • 20
    • 0027520011 scopus 로고
    • Isolation and nucleotide sequence of the gene encoding cytotoxic necrotizing factor 1 of Escherichia coli
    • Falbo, V., Pace, T., Picci, L., Pizzi, E., and Caprioli, A. (1993). Isolation and nucleotide sequence of the gene encoding cytotoxic necrotizing factor 1 of Escherichia coli. Infect. Immun. 61, 4909-4914.
    • (1993) Infect. Immun. , vol.61 , pp. 4909-4914
    • Falbo, V.1    Pace, T.2    Picci, L.3    Pizzi, E.4    Caprioli, A.5
  • 22
    • 0029088441 scopus 로고
    • Escherichia coli cytotoxic necrotizing factor 1: Evidence for induction of actin assembly by constitutive activation of the p21 Rho GTPase
    • Fiorentini, C., Donelli, G., Matarrese, P., Fabbri, A., Paradisi, S., and Boquet, P. (1995). Escherichia coli cytotoxic necrotizing factor 1: evidence for induction of actin assembly by constitutive activation of the p21 Rho GTPase. Infect. Immun. 63, 3936-3944.
    • (1995) Infect. Immun. , vol.63 , pp. 3936-3944
    • Fiorentini, C.1    Donelli, G.2    Matarrese, P.3    Fabbri, A.4    Paradisi, S.5    Boquet, P.6
  • 23
    • 0020854846 scopus 로고
    • Inhibition of the activity of Pseudomonas toxin by methylamine
    • Fitzgerald, D., Morris, R.E., and Salinger, C.B. (1983). Inhibition of the activity of Pseudomonas toxin by methylamine. Rev. Infect. Dis. 5(suppl 5), S985-S991.
    • (1983) Rev. Infect. Dis. , vol.5 , Issue.SUPPL. 5
    • Fitzgerald, D.1    Morris, R.E.2    Salinger, C.B.3
  • 25
    • 0029100974 scopus 로고
    • Membrane transport in the endocytic pathway
    • Gruenberg, J., and Maxfield, F.R. (1995). Membrane transport in the endocytic pathway. Curr. Opin. Cell Biol. 7, 552-563.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 552-563
    • Gruenberg, J.1    Maxfield, F.R.2
  • 26
    • 0022997339 scopus 로고
    • Internalization and recycling of transferrin and its receptor. Effect of trifluoroperazine on recycling in human erythroleukemic cells
    • Hunt, R.C., and Marshall-Carlson, L. (1986). Internalization and recycling of transferrin and its receptor. Effect of trifluoroperazine on recycling in human erythroleukemic cells. J. Biol. Chem. 261, 3681-3686.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3681-3686
    • Hunt, R.C.1    Marshall-Carlson, L.2
  • 27
    • 0015817362 scopus 로고
    • Diphtheria toxin: Specific competition for cell receptors
    • Ittelson, T.R., and Gill, D.M. (1973). Diphtheria toxin: specific competition for cell receptors. Nature 242, 330-332.
    • (1973) Nature , vol.242 , pp. 330-332
    • Ittelson, T.R.1    Gill, D.M.2
  • 28
    • 0025831433 scopus 로고
    • The ras-related gene rhoB is an immediate-early gene inducible by v-Fps, epidermal growth factor, and platelet-derived growth factor in rat fibroblasts
    • Jähner, D., and Hunter, T. (1991). The ras-related gene rhoB is an immediate-early gene inducible by v-Fps, epidermal growth factor, and platelet-derived growth factor in rat fibroblasts. Mol. Cell. Biol. 11, 3682-3690.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3682-3690
    • Jähner, D.1    Hunter, T.2
  • 29
    • 0031890793 scopus 로고    scopus 로고
    • Surfing on a retrograde wave: How does Shiga toxin reach the endoplasmic reticulum?
    • Johannes, L., and Goud, B. (1998). Surfing on a retrograde wave: how does Shiga toxin reach the endoplasmic reticulum? Trends Cell Biol. 8, 158-162.
    • (1998) Trends Cell Biol. , vol.8 , pp. 158-162
    • Johannes, L.1    Goud, B.2
  • 30
    • 0030876616 scopus 로고    scopus 로고
    • Retrograde transport of KDEL-bearing B-fragment of Shiga toxin
    • Johannes, L., Tenza, D., Antony, C., and Goud, B. (1997). Retrograde transport of KDEL-bearing B-fragment of Shiga toxin. J. Biol. Chem. 272, 19554-19561.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19554-19561
    • Johannes, L.1    Tenza, D.2    Antony, C.3    Goud, B.4
  • 31
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and organelle structure
    • Klausner, R.D., Donaldson, J.G., and Lippincott-Schwartz, J. (1992). Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell Biol. 116, 1071-1080.
    • (1992) J. Cell Biol. , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 32
    • 0030910603 scopus 로고    scopus 로고
    • Cytotoxic necrotizing factor 1 from Escherichia coli and dermonecrotic toxin from Bordetella bronchiseptica induce p21 (rho)-dependent tyrosine phosphorylation of focal adhesion kinase and paxillin in Swiss 3T3 cells
    • Lacerda, H.M., Pullinger, G.D., Lax, A.J., and Rozengurt, E. (1997). Cytotoxic necrotizing factor 1 from Escherichia coli and dermonecrotic toxin from Bordetella bronchiseptica induce p21 (rho)-dependent tyrosine phosphorylation of focal adhesion kinase and paxillin in Swiss 3T3 cells. J. Biol. Chem. 272, 9587-9596.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9587-9596
    • Lacerda, H.M.1    Pullinger, G.D.2    Lax, A.J.3    Rozengurt, E.4
  • 33
    • 0029117498 scopus 로고
    • The emergence of clathrin-independent pinocytic pathway
    • Lamaze, C., and Schmid, S.L. (1995). The emergence of clathrin-independent pinocytic pathway. Curr. Opin. Cell Biol. 7, 573-580.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 573-580
    • Lamaze, C.1    Schmid, S.L.2
  • 35
    • 0030742773 scopus 로고    scopus 로고
    • Molecular localization of the Escherichia coli cytotoxic necrotizing factor 1 cell-binding and catalytic domains
    • Lemichez, E., Flatau, G., Bruzzone, M., Boquet, P., and Gauthier, M. (1997b). Molecular localization of the Escherichia coli cytotoxic necrotizing factor 1 cell-binding and catalytic domains. Mol. Microbiol. 24, 1061-1070.
    • (1997) Mol. Microbiol. , vol.24 , pp. 1061-1070
    • Lemichez, E.1    Flatau, G.2    Bruzzone, M.3    Boquet, P.4    Gauthier, M.5
  • 36
    • 0032498544 scopus 로고    scopus 로고
    • Expression of mutant dynamin inhibits toxicity and trans-port of endocytosed ricin to the Golgi apparatus
    • Llorente, A., Rapak, A., Schmid, S.L., van Deurs, B., and Sandvig, K. (1998). Expression of mutant dynamin inhibits toxicity and trans-port of endocytosed ricin to the Golgi apparatus. J. Cell Biol. 140, 553-563.
    • (1998) J. Cell Biol. , vol.140 , pp. 553-563
    • Llorente, A.1    Rapak, A.2    Schmid, S.L.3    Van Deurs, B.4    Sandvig, K.5
  • 37
    • 0026492389 scopus 로고
    • How bacterial protein toxins enter cells: The role of partial unfolding in membrane translocation
    • London, E. (1992). How bacterial protein toxins enter cells: the role of partial unfolding in membrane translocation. Mol. Microbiol. 6, 3277-3282.
    • (1992) Mol. Microbiol. , vol.6 , pp. 3277-3282
    • London, E.1
  • 38
    • 0032559646 scopus 로고    scopus 로고
    • Toxin entry: Retrograde transport through the secretory pathway
    • Lord, J.M., and Roberts, L.M. (1998). Toxin entry: retrograde transport through the secretory pathway. J. Cell Biol. 140, 733-736.
    • (1998) J. Cell Biol. , vol.140 , pp. 733-736
    • Lord, J.M.1    Roberts, L.M.2
  • 39
    • 0021358020 scopus 로고
    • Gene clusters governing the production of hemolysin and mannose-resistant hemagglutination are closely linked in Escherichia coli se-rotype O4 and O6 isolates from urinary tract infections
    • Low, D., David, V., Lark, D., Schoolnick, G., and Falkow, S. (1984). Gene clusters governing the production of hemolysin and mannose-resistant hemagglutination are closely linked in Escherichia coli se-rotype O4 and O6 isolates from urinary tract infections. Infect. Immun. 43, 353-358.
    • (1984) Infect. Immun. , vol.43 , pp. 353-358
    • Low, D.1    David, V.2    Lark, D.3    Schoolnick, G.4    Falkow, S.5
  • 40
    • 0031041314 scopus 로고    scopus 로고
    • Quantitative analysis of bacterial toxin affinity and specificity for glycolipid receptors by surface plasmon resonance
    • MacKenzie, C.R., Hirama, T., Lee, K.K., Altman, E., and Young, N.M. (1997). Quantitative analysis of bacterial toxin affinity and specificity for glycolipid receptors by surface plasmon resonance. J. Biol. Chem. 272, 5533-5538.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5533-5538
    • MacKenzie, C.R.1    Hirama, T.2    Lee, K.K.3    Altman, E.4    Young, N.M.5
  • 41
    • 0030037845 scopus 로고    scopus 로고
    • Membranes and sorting
    • Mellman, I. (1996). Membranes and sorting. Curr. Opin. Cell Biol. 8, 497-498.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 497-498
    • Mellman, I.1
  • 42
    • 0032145173 scopus 로고    scopus 로고
    • Protein toxins and membrane transport
    • Montecucco, C. (1998). Protein toxins and membrane transport. Curr. Opin. Cell Biol. 100, 530-536.
    • (1998) Curr. Opin. Cell Biol. , vol.100 , pp. 530-536
    • Montecucco, C.1
  • 43
    • 0028236333 scopus 로고
    • Bacterial protein toxins penetrate cells via a four-step mechanism
    • Montecucco, C., Papini, E., and Schiavo, G. (1994). Bacterial protein toxins penetrate cells via a four-step mechanism. FEBS Lett. 346, 92-98.
    • (1994) FEBS Lett. , vol.346 , pp. 92-98
    • Montecucco, C.1    Papini, E.2    Schiavo, G.3
  • 44
    • 0019994630 scopus 로고
    • Non-coated membrane invaginations are involved in binding and internalization of cholera and tetanus toxins
    • Montesano, R., Roth, J., Robert, A., and Orci, L. (1982). Non-coated membrane invaginations are involved in binding and internalization of cholera and tetanus toxins. Nature 296, 651-653.
    • (1982) Nature , vol.296 , pp. 651-653
    • Montesano, R.1    Roth, J.2    Robert, A.3    Orci, L.4
  • 45
    • 0023866565 scopus 로고
    • Low pH-induced release of diphtheria toxin A-fragment in Vero cells. Biochemical evidence for transfer to the cytosol
    • Moskaug, J.O., Sandvig, K., and Olsnes, S. (1988). Low pH-induced release of diphtheria toxin A-fragment in Vero cells. Biochemical evidence for transfer to the cytosol. J. Biol. Chem. 263, 2518-2525.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2518-2525
    • Moskaug, J.O.1    Sandvig, K.2    Olsnes, S.3
  • 46
    • 0022005540 scopus 로고
    • Inhibition of coated pit formation in HEp-2 cells blocks the cytotoxicity of diphtheria toxin but not that of ricin toxin
    • Moya, M., Dautry-Varsat, A., Goud, B., Louvard, D., and Boquet, P. (1985). Inhibition of coated pit formation in HEp-2 cells blocks the cytotoxicity of diphtheria toxin but not that of ricin toxin. J. Cell Biol. 101, 548-559.
    • (1985) J. Cell Biol. , vol.101 , pp. 548-559
    • Moya, M.1    Dautry-Varsat, A.2    Goud, B.3    Louvard, D.4    Boquet, P.5
  • 47
    • 0027314536 scopus 로고
    • Brefeldin A blocks the response of cultured cells to cholera toxin. Implications for intracellular trafficking in toxin action
    • Orlandi, P.A., Curran, P.K., and Fishman, P.H. (1993). Brefeldin A blocks the response of cultured cells to cholera toxin. Implications for intracellular trafficking in toxin action. J. Biol. Chem. 268, 12010-12016.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12010-12016
    • Orlandi, P.A.1    Curran, P.K.2    Fishman, P.H.3
  • 48
    • 0031750101 scopus 로고    scopus 로고
    • Filipin-dependent inhibition of cholera toxin: Evidence for toxin internalization and activation through caveolae-like domains
    • Orlandi, P.A., and Fishman, P.H. (1998). Filipin-dependent inhibition of cholera toxin: evidence for toxin internalization and activation through caveolae-like domains. J. Cell Biol. 141, 905-915.
    • (1998) J. Cell Biol. , vol.141 , pp. 905-915
    • Orlandi, P.A.1    Fishman, P.H.2
  • 49
    • 0028231764 scopus 로고
    • Cytotoxic necrotizing factor 2 produced by virulent Escherichia coli modifies the small GTP-binding protein Rho involved in assembly of actin stress fibers
    • Oswald, E., Sugai, M., Labigne, A., Wu, H.C., Fiorentini, C., Boquet, P., and O'Brien, A.D. (1994). Cytotoxic necrotizing factor 2 produced by virulent Escherichia coli modifies the small GTP-binding protein Rho involved in assembly of actin stress fibers. Proc. Natl. Acad. Sci. USA 91, 3814-3818.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3814-3818
    • Oswald, E.1    Sugai, M.2    Labigne, A.3    Wu, H.C.4    Fiorentini, C.5    Boquet, P.6    O'Brien, A.D.7
  • 50
    • 0027510933 scopus 로고
    • Cell penetration of diphtheria toxin. Reduction of the interchain disulfide bridge is the rate-limiting step of translocation in the cytosol
    • Papini, E., Rappuoli, R., Murgia, M., and Montecucco, C. (1993). Cell penetration of diphtheria toxin. Reduction of the interchain disulfide bridge is the rate-limiting step of translocation in the cytosol. J. Biol. Chem. 268, 1567-1574.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1567-1574
    • Papini, E.1    Rappuoli, R.2    Murgia, M.3    Montecucco, C.4
  • 51
    • 0032563187 scopus 로고    scopus 로고
    • Dap160, a neural-specific Eps15 homology and multiple SH3 domain-containing protein that interacts with Drosophila dynamin
    • Roos, J., and Kelly, R.B. (1998). Dap160, a neural-specific Eps15 homology and multiple SH3 domain-containing protein that interacts with Drosophila dynamin. J. Biol. Chem. 273, 19108-19119.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19108-19119
    • Roos, J.1    Kelly, R.B.2
  • 53
    • 0026684124 scopus 로고
    • Retrograde transport of endocytosed Shiga toxin to the endoplasmic reticulum
    • Sandvig, K., Garred, O., Prydz, K., Kozlov, J.V., Hansen, S.H., and van Deurs, B. (1992). Retrograde transport of endocytosed Shiga toxin to the endoplasmic reticulum. Nature 358, 510-512.
    • (1992) Nature , vol.358 , pp. 510-512
    • Sandvig, K.1    Garred, O.2    Prydz, K.3    Kozlov, J.V.4    Hansen, S.H.5    Van Deurs, B.6
  • 54
    • 0019271816 scopus 로고
    • Diphtheria toxin entry into cells is facilitated by low pH
    • Sandvig, K., and Olsnes, S. (1980). Diphtheria toxin entry into cells is facilitated by low pH. J. Cell Biol. 87, 828-832.
    • (1980) J. Cell Biol. , vol.87 , pp. 828-832
    • Sandvig, K.1    Olsnes, S.2
  • 55
    • 0003707675 scopus 로고
    • Membrane translocation of diphtheria toxin
    • ed. J.E. Alouf and J.H. Freer, London: Academic Press
    • Sandvig, K., and Olsnes, S. (1991). Membrane translocation of diphtheria toxin. In: Sourcebook of Bacterial Protein Toxins, ed. J.E. Alouf and J.H. Freer, London: Academic Press, 57-73.
    • (1991) Sourcebook of Bacterial Protein Toxins , pp. 57-73
    • Sandvig, K.1    Olsnes, S.2
  • 56
    • 0023582912 scopus 로고
    • Acidification of the cytosol inhibits endocytosis from coated pits
    • Sandvig, K., Olsnes, S., Petersen, O.W., and van Deurs, B. (1987). Acidification of the cytosol inhibits endocytosis from coated pits. J. Cell Biol. 105, 679-689.
    • (1987) J. Cell Biol. , vol.105 , pp. 679-689
    • Sandvig, K.1    Olsnes, S.2    Petersen, O.W.3    Van Deurs, B.4
  • 57
    • 0028302595 scopus 로고
    • Endocytosis without clathrin
    • Sandvig, K., and van Deurs, B. (1994). Endocytosis without clathrin. Trends Cell Biol. 4, 275-277.
    • (1994) Trends Cell Biol. , vol.4 , pp. 275-277
    • Sandvig, K.1    Van Deurs, B.2
  • 58
    • 28244497552 scopus 로고
    • Drug antagonism and pAx
    • Schild, H.O. (1957). Drug antagonism and pAx. Pharmacol. Rev. 9, 242-246.
    • (1957) Pharmacol. Rev. , vol.9 , pp. 242-246
    • Schild, H.O.1
  • 59
    • 0030610785 scopus 로고    scopus 로고
    • Gln 63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1
    • Schmidt, G., Sehr, P., Wilm, M., Selzer, J., Mann, M., and Aktories, K. (1997). Gln 63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1. Nature 387, 725-729.
    • (1997) Nature , vol.387 , pp. 725-729
    • Schmidt, G.1    Sehr, P.2    Wilm, M.3    Selzer, J.4    Mann, M.5    Aktories, K.6
  • 60
    • 0032577588 scopus 로고    scopus 로고
    • The Rho-deamidating cytotoxic necrotizing factor 1 from Escherichia coli possesses transglutaminase activity. Cysteine 866 and histidine 881 are essential for enzyme activity
    • Schmidt, G., Selzer, J., Lerm, M., and Aktories, K. (1998). The Rho-deamidating cytotoxic necrotizing factor 1 from Escherichia coli possesses transglutaminase activity. Cysteine 866 and histidine 881 are essential for enzyme activity. J. Biol. Chem. 273, 13669-13674.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13669-13674
    • Schmidt, G.1    Selzer, J.2    Lerm, M.3    Aktories, K.4
  • 61
    • 0029942531 scopus 로고    scopus 로고
    • Enteric bacterial toxins: Mechanisms of action and linkage to intestinal secretion
    • Sears, C.L., and Kaper, J.B. (1996). Enteric bacterial toxins: mechanisms of action and linkage to intestinal secretion. Microbiol. Rev. 60, 167-215.
    • (1996) Microbiol. Rev. , vol.60 , pp. 167-215
    • Sears, C.L.1    Kaper, J.B.2
  • 62
    • 0026000526 scopus 로고
    • Increased cytotoxic activity of Pseudomonas exotoxin and two chimeric toxins ending in KDEL
    • Seetharam, S., Chaudhary, V.K., Fitzgerald, D., and Pastan, I. (1991). Increased cytotoxic activity of Pseudomonas exotoxin and two chimeric toxins ending in KDEL. J. Biol. Chem. 266, 17376-17381.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17376-17381
    • Seetharam, S.1    Chaudhary, V.K.2    Fitzgerald, D.3    Pastan, I.4
  • 63
    • 0033106167 scopus 로고    scopus 로고
    • The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15
    • Sengar, A.S., Wang, W., Bishay, J., Cohen, S., and Egan, S.E. (1999). The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15. EMBO J. 18, 1159-1171.
    • (1999) EMBO J. , vol.18 , pp. 1159-1171
    • Sengar, A.S.1    Wang, W.2    Bishay, J.3    Cohen, S.4    Egan, S.E.5
  • 64
    • 0031714548 scopus 로고    scopus 로고
    • The Diphtheria toxin channel-forming T domain translocates its own NH2-terminal region across planar bilayers
    • Senzel, L., Huynh, P.D., Jakes, K.S., Collier, R.J., and Finkelstein, A. (1998). The Diphtheria toxin channel-forming T domain translocates its own NH2-terminal region across planar bilayers. J. Gen. Physiol. 112, 317-324.
    • (1998) J. Gen. Physiol. , vol.112 , pp. 317-324
    • Senzel, L.1    Huynh, P.D.2    Jakes, K.S.3    Collier, R.J.4    Finkelstein, A.5
  • 65
    • 0028269946 scopus 로고
    • Structure-function relationships in diphtheria toxin channels: Determining a minimal channel-forming domain
    • Silverman, J.A., Mindell, J.A., Zhan, H., Finkelstein, A., Shen, W.H., and Collier, R.J. (1994). Structure-function relationships in diphtheria toxin channels: determining a minimal channel-forming domain. J. Membr. Biol. 137, 17-28.
    • (1994) J. Membr. Biol. , vol.137 , pp. 17-28
    • Silverman, J.A.1    Mindell, J.A.2    Zhan, H.3    Finkelstein, A.4    Shen, W.H.5    Collier, R.J.6
  • 66
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., and Ikonen, E. (1997). Functional rafts in cell membranes. Nature 387, 569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 68
    • 0029147513 scopus 로고
    • Ricin cytotoxicity is sensitive to recycling between the endoplasmic reticulum and the Golgi complex
    • Simpson, J.C., Dascher, C., Roberts, L.M., Lord, J.M., and Balch, W.E. (1995). Ricin cytotoxicity is sensitive to recycling between the endoplasmic reticulum and the Golgi complex. J. Biol. Chem. 270, 20078-20083.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20078-20083
    • Simpson, J.C.1    Dascher, C.2    Roberts, L.M.3    Lord, J.M.4    Balch, W.E.5
  • 69
    • 0029127063 scopus 로고
    • The endocytic activity of dendritic cells
    • Steinman, R.M., and Swanson, J. (1995). The endocytic activity of dendritic cells. J. Exp. Med. 182, 283-288.
    • (1995) J. Exp. Med. , vol.182 , pp. 283-288
    • Steinman, R.M.1    Swanson, J.2
  • 70
    • 0027446864 scopus 로고
    • Differential effects of brefeldin A on transport of secretory and lysosomal proteins
    • Strous, G.J., van Kerkhof, P., van Meer, G., Rijnboutt, S., and Stoorvogel, W. (1993). Differential effects of brefeldin A on transport of secretory and lysosomal proteins. J. Biol. Chem. 268, 2341-2347.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2341-2347
    • Strous, G.J.1    Van Kerkhof, P.2    Van Meer, G.3    Rijnboutt, S.4    Stoorvogel, W.5
  • 71
    • 0033168456 scopus 로고    scopus 로고
    • Is dynamin a regulator motor or a master regulator?
    • van der Bliek, A.M. (1999). Is dynamin a regulator motor or a master regulator? Trends Cell Biol. 9, 253-254.
    • (1999) Trends Cell Biol. , vol.9 , pp. 253-254
    • Van Der Bliek, A.M.1
  • 74
    • 0023878452 scopus 로고
    • Estimation of the amount of internalized ricin that reaches the trans-Golgi network
    • van Deurs, B., Sandvig, K., Petersen, O.W., Olsnes, S., Simons, K., and Griffiths, G. (1988). Estimation of the amount of internalized ricin that reaches the trans-Golgi network. J. Cell Biol. 106, 253-267.
    • (1988) J. Cell Biol. , vol.106 , pp. 253-267
    • Van Deurs, B.1    Sandvig, K.2    Petersen, O.W.3    Olsnes, S.4    Simons, K.5    Griffiths, G.6
  • 75
    • 0027520440 scopus 로고
    • Mis-assembly of clathrin lattices on endosomes reveals a regulatory switch for coated pit formation
    • Wang, L.H., Rothberg, K.G., and Anderson, R.G. (1993). Mis-assembly of clathrin lattices on endosomes reveals a regulatory switch for coated pit formation. J. Cell Biol. 123, 1107-1117.
    • (1993) J. Cell Biol. , vol.123 , pp. 1107-1117
    • Wang, L.H.1    Rothberg, K.G.2    Anderson, R.G.3
  • 76
    • 0024836461 scopus 로고
    • Distinct endocytotic pathways in epidermal growth factor-stimulated human carcinoma A431 cells
    • West, M.A., Bretscher, M.S., and Watts, C. (1989). Distinct endocytotic pathways in epidermal growth factor-stimulated human carcinoma A431 cells. J. Cell Biol. 109, 2731-2739.
    • (1989) J. Cell Biol. , vol.109 , pp. 2731-2739
    • West, M.A.1    Bretscher, M.S.2    Watts, C.3
  • 77
    • 0026713586 scopus 로고
    • The morphology but not the function of lysosomes is altered by brefeldin A
    • Wood, S.A., and Brown, W.J. (1992). The morphology but not the function of lysosomes is altered by brefeldin A. J. Cell Biol. 119, 273-285.
    • (1992) J. Cell Biol. , vol.119 , pp. 273-285
    • Wood, S.A.1    Brown, W.J.2
  • 79
    • 0018167496 scopus 로고
    • One molecule of diphteria toxin fragment A introduced into a cell can kill the cell
    • Yamaizumi, M., Mekada, E., Uchida, T., and Okada, Y. (1978). One molecule of diphteria toxin fragment A introduced into a cell can kill the cell. Cell 15, 245-250.
    • (1978) Cell , vol.15 , pp. 245-250
    • Yamaizumi, M.1    Mekada, E.2    Uchida, T.3    Okada, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.