메뉴 건너뛰기




Volumn 18, Issue , 2002, Pages 1-24

Membrane traffic exploited by protein toxins

Author keywords

Endocytosis; Endoplasmic reticulum; Golgi; Rafts; Ricin

Indexed keywords

CELL SURFACE RECEPTOR; PROTEIN DERIVATIVE; TOXIN; PROTEIN;

EID: 0036441135     PISSN: 10810706     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.cellbio.18.011502.142107     Document Type: Review
Times cited : (203)

References (139)
  • 1
    • 0028171066 scopus 로고
    • The cytoplasmic domain of the diphtheria toxin receptor (HB-EGF precursor) is not required for receptor-mediated endocytosis
    • Almond BD, Eidels L. 1994. The cytoplasmic domain of the diphtheria toxin receptor (HB-EGF precursor) is not required for receptor-mediated endocytosis. J. Biol. Chem. 269:26635-41
    • (1994) J. Biol. Chem. , vol.269 , pp. 26635-26641
    • Almond, B.D.1    Eidels, L.2
  • 2
    • 0030459125 scopus 로고    scopus 로고
    • A role for phosphoinositide 3-kinase in the completion of macropinocytosis and phagocytosis by macrophages
    • Araki N, Johnson MT, Swanson JA. 1996. A role for phosphoinositide 3-kinase in the completion of macropinocytosis and phagocytosis by macrophages. J. Cell Biol. 135: 1249-60
    • (1996) J. Cell Biol. , vol.135 , pp. 1249-1260
    • Araki, N.1    Johnson, M.T.2    Swanson, J.A.3
  • 3
    • 0034255636 scopus 로고    scopus 로고
    • The effect of a monoclonal antibody coupled to ricin A chain-derived peptides on endothelial cells in vitro: Insights into toxin-mediated vascular damage
    • Baluna R, Coleman E, Jones C, Ghetie V, Vitetta ES. 2000. The effect of a monoclonal antibody coupled to ricin A chain-derived peptides on endothelial cells in vitro: Insights into toxin-mediated vascular damage. Exp. Cell Res. 258:417-24
    • (2000) Exp. Cell Res. , vol.258 , pp. 417-424
    • Baluna, R.1    Coleman, E.2    Jones, C.3    Ghetie, V.4    Vitetta, E.S.5
  • 4
    • 0039003839 scopus 로고    scopus 로고
    • Cellular uptake of Clostridium botulinum C2 toxin requires oligomerization and acidification
    • Barth H, Blöcker D, Behlke J, Bergsma-Schutter W, Brisson A, et al. 2001a. Cellular uptake of Clostridium botulinum C2 toxin requires oligomerization and acidification. J. Biol. Chem. 275:18704-11
    • (2001) J. Biol. Chem. , vol.275 , pp. 18704-18711
    • Barth, H.1    Blöcker, D.2    Behlke, J.3    Bergsma-Schutter, W.4    Brisson, A.5
  • 5
    • 0035815642 scopus 로고    scopus 로고
    • Low pH-induced formation of ion channels by Clostridium difficile toxin B in target cells
    • Barth H, Pfeifer G, Hofmann F, Maier E, Benz R, Aktories K. 2001b. Low pH-induced formation of ion channels by Clostridium difficile toxin B in target cells. J. Biol. Chem. 276:10670-76
    • (2001) J. Biol. Chem. , vol.276 , pp. 10670-10676
    • Barth, H.1    Pfeifer, G.2    Hofmann, F.3    Maier, E.4    Benz, R.5    Aktories, K.6
  • 6
    • 0034602956 scopus 로고    scopus 로고
    • Mapping of Eps15 domains involved in its targeting to clathrincoated pits
    • Benmerah A, Poupon V, Cerf-Bensussan N, Dautry-Varsat A. 2000. Mapping of Eps15 domains involved in its targeting to clathrincoated pits. J. Biol. Chem. 275:3288-95
    • (2000) J. Biol. Chem. , vol.275 , pp. 3288-3295
    • Benmerah, A.1    Poupon, V.2    Cerf-Bensussan, N.3    Dautry-Varsat, A.4
  • 7
    • 0023872946 scopus 로고
    • Cholera toxin and pertussis toxin stimulate prostaglandin E2 synthesis in a murine macrophage cell line
    • Burch RM, Jelsema C, Axelrod J. 1988. Cholera toxin and pertussis toxin stimulate prostaglandin E2 synthesis in a murine macrophage cell line. J. Pharmacol. Exp. Ther. 244: 765-73
    • (1988) J. Pharmacol. Exp. Ther. , vol.244 , pp. 765-773
    • Burch, R.M.1    Jelsema, C.2    Axelrod, J.3
  • 8
    • 0033614495 scopus 로고    scopus 로고
    • Free and N-linked oligomannosides as markers of the quality control of newly synthesized glycoproteins
    • Cacan R, Verbert A. 1999. Free and N-linked oligomannosides as markers of the quality control of newly synthesized glycoproteins. Biochem. Biophys. Res. Commun. 258:1-5
    • (1999) Biochem. Biophys. Res. Commun. , vol.258 , pp. 1-5
    • Cacan, R.1    Verbert, A.2
  • 9
    • 0025012987 scopus 로고
    • Pseudomonas exotoxin contains a specific sequence at the carboxyl terminus that is required for cytotoxicity
    • Chaudhary VK, Jinno Y, Fitzgerald D, Pastan I. 1990. Pseudomonas exotoxin contains a specific sequence at the carboxyl terminus that is required for cytotoxicity. Proc. Natl. Acad. Sci. USA 87:308-12
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 308-312
    • Chaudhary, V.K.1    Jinno, Y.2    Fitzgerald, D.3    Pastan, I.4
  • 10
    • 0034878448 scopus 로고    scopus 로고
    • Understanding the mode of action of diphtheria toxin: A perspective on progress during the 20th century
    • Collier RJ. 2001. Understanding the mode of action of diphtheria toxin: A perspective on progress during the 20th century. Toxicon 39:1793-803
    • (2001) Toxicon , vol.39 , pp. 1793-1803
    • Collier, R.J.1
  • 11
    • 0034698787 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Eps15 is required for ligand-regulated, but not constitutive, endocytosis
    • Confalonieri S, Salcini AE, Puri C, Tacchetti C, Di Fiore PP. 2000. Tyrosine phosphorylation of Eps15 is required for ligand-regulated, but not constitutive, endocytosis. J. Cell Biol. 150:905-12
    • (2000) J. Cell Biol. , vol.150 , pp. 905-912
    • Confalonieri, S.1    Salcini, A.E.2    Puri, C.3    Tacchetti, C.4    Di Fiore, P.P.5
  • 12
    • 0034108090 scopus 로고    scopus 로고
    • The p21 rhoactivating toxin cytotoxic necrotizing factor 1 is endocytosed by a clathrin-independent mechanism and enters the cytosol by an acidic-dependent membrane translocation step
    • Contamin S, Galmiche A, Doye A, Flatau G, Benmerah A, Boquet P. 2000. The p21 rhoactivating toxin cytotoxic necrotizing factor 1 is endocytosed by a clathrin-independent mechanism and enters the cytosol by an acidic-dependent membrane translocation step. Mol. Biol. Cell 11:1775-87
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1775-1787
    • Contamin, S.1    Galmiche, A.2    Doye, A.3    Flatau, G.4    Benmerah, A.5    Boquet, P.6
  • 13
    • 0029134736 scopus 로고
    • Clathrin-independent pinocytosis is induced in cells overexpressing a temperature-sensitive mutant of dynamin
    • Damke H, Baba T, van der Bliek AM, Schmid SL. 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
  • 14
    • 0030866249 scopus 로고    scopus 로고
    • Cellular pertussis vaccines containing genetically detoxified pertussis toxin induce long-lasting humoral and cellular responses in adults
    • Di Tommaso A, Bartalini M, Peppoloni S, Podda A, Rappuoli R, De Magistris MT. 1997. Cellular pertussis vaccines containing genetically detoxified pertussis toxin induce long-lasting humoral and cellular responses in adults. Vaccine 15:1218-24
    • (1997) Vaccine , vol.15 , pp. 1218-1224
    • Di Tommaso, A.1    Bartalini, M.2    Peppoloni, S.3    Podda, A.4    Rappuoli, R.5    De Magistris, M.T.6
  • 15
    • 0033041377 scopus 로고    scopus 로고
    • Cytotoxic T-lymphocyte epitopes fused to anthrax toxin induce protective antiviral immunity
    • Doling AM, Ballard JD, Shen H, Krishna KM, Ahmed R, et al. 1999. Cytotoxic T-lymphocyte epitopes fused to anthrax toxin induce protective antiviral immunity. Infect. Immun. 67:3290-96
    • (1999) Infect. Immun. , vol.67 , pp. 3290-3296
    • Doling, A.M.1    Ballard, J.D.2    Shen, H.3    Krishna, K.M.4    Ahmed, R.5
  • 16
    • 0027471558 scopus 로고
    • Targeted delivery of peptide epitopes to class I major histocompatibility molecules modified by Pseudomonas exotoxin
    • Donnelly JJ, Ulmer JB, Hawe LA, Friedman A, Shi X-P, et al. 1993. Targeted delivery of peptide epitopes to class I major histocompatibility molecules modified by Pseudomonas exotoxin. Proc. Natl. Acad. Sci. USA. 90:3530-34
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3530-3534
    • Donnelly, J.J.1    Ulmer, J.B.2    Hawe, L.A.3    Friedman, A.4    Shi, X.-P.5
  • 17
    • 0019287379 scopus 로고
    • The entry of diphtheria toxin into the mammalian cell cytoplasm: Evidence for lysosomal involvement
    • Draper RK, Simon MI. 1980. The entry of diphtheria toxin into the mammalian cell cytoplasm: Evidence for lysosomal involvement. J. Cell Biol. 87:849-54
    • (1980) J. Cell Biol. , vol.87 , pp. 849-854
    • Draper, R.K.1    Simon, M.I.2
  • 18
    • 0004054832 scopus 로고
    • ed. F Himmelweit, M Marquardt, Sir S Dale: New York: Pergamon
    • Ehrlich P. 1957. The collected papers of Paul Ehrlich, ed. F Himmelweit, M Marquardt, Sir S Dale, pp. 596-618: New York: Pergamon
    • (1957) The Collected Papers of Paul Ehrlich , pp. 596-618
    • Ehrlich, P.1
  • 19
    • 0028241862 scopus 로고
    • Selective regulation of apical endocytosis in polarized MDCK cells by mastoparan and cAMP
    • Eker P, Holm PK, van Deurs B, Sandvig K. 1994. Selective regulation of apical endocytosis in polarized MDCK cells by mastoparan and cAMP. J. Biol. Chem. 269:18607-15
    • (1994) J. Biol. Chem. , vol.269 , pp. 18607-18615
    • Eker, P.1    Holm, P.K.2    Van Deurs, B.3    Sandvig, K.4
  • 20
    • 0030974747 scopus 로고    scopus 로고
    • Endocytosis and retrograde transport of pertussis toxin to the Golgi complex as a pre-requisite for cellular intoxication
    • el Baya A, Linnemann R, von Olleschik-Elbheim L, Robenek H, Schmidt MA. 1997. Endocytosis and retrograde transport of pertussis toxin to the Golgi complex as a pre-requisite for cellular intoxication. Eur. J. Cell Biol. 73:40-48
    • (1997) Eur. J. Cell Biol. , vol.73 , pp. 40-48
    • El Baya, A.1    Linnemann, R.2    Von Olleschik-Elbheim, L.3    Robenek, H.4    Schmidt, M.A.5
  • 21
    • 0035168061 scopus 로고    scopus 로고
    • Targeting of Shiga toxin β-subunit to retrograde transport route in association with detergent-resistant membranes
    • Falguieres T, Mallard F, Baron C, Hanau D, Lingwood C, et al. 2001. Targeting of Shiga toxin β-subunit to retrograde transport route in association with detergent-resistant membranes. Mol. Biol. Cell 12:2453-68
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2453-2468
    • Falguieres, T.1    Mallard, F.2    Baron, C.3    Hanau, D.4    Lingwood, C.5
  • 22
    • 0033922714 scopus 로고    scopus 로고
    • Penetration of protein toxins into cells
    • Falnes PO, Sandvig K. 2000. Penetration of protein toxins into cells. Curr. Opin. Cell Biol. 12:407-13
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 407-413
    • Falnes, P.O.1    Sandvig, K.2
  • 24
    • 0034975261 scopus 로고    scopus 로고
    • The use of Shiga-like toxin 1 in cancer therapy
    • Gariepy J. 2001. The use of Shiga-like toxin 1 in cancer therapy. Crit. Rev. Oncol. Hematol. 39:99-106
    • (2001) Crit. Rev. Oncol. Hematol. , vol.39 , pp. 99-106
    • Gariepy, J.1
  • 25
    • 0035105678 scopus 로고    scopus 로고
    • Reconstitution of clathrin-independent endocytosis at the apical domain of permeabilized MDCK II cells: Requirement for a Rho-family GTPase
    • Garred O, Rodal SK, van Deurs B, Sandvig K. 2001. Reconstitution of clathrin-independent endocytosis at the apical domain of permeabilized MDCK II cells: Requirement for a Rho-family GTPase. Traffic 2:26-36
    • (2001) Traffic , vol.2 , pp. 26-36
    • Garred, O.1    Rodal, S.K.2    Van Deurs, B.3    Sandvig, K.4
  • 26
    • 0032563568 scopus 로고    scopus 로고
    • An endocytosed TGN38 chimeric protein is delivered to the TGN after trafficking through the endocytic recycling compartment in CHO cells
    • Ghosh KN, Mallet WG, Soe TT, McGraw TE, Maxfield FR. 1998. An endocytosed TGN38 chimeric protein is delivered to the TGN after trafficking through the endocytic recycling compartment in CHO cells. J. Cell Biol. 142:923-36
    • (1998) J. Cell Biol. , vol.142 , pp. 923-936
    • Ghosh, K.N.1    Mallet, W.G.2    Soe, T.T.3    McGraw, T.E.4    Maxfield, F.R.5
  • 27
    • 0033224214 scopus 로고    scopus 로고
    • Evidence for a COP-I-independent transport route from the Golgi complex to the endoplasmic reticulum
    • Girod A, Storrie B, Simpson JC, Johannes L, Goud B, et al. 1999. Evidence for a COP-I-independent transport route from the Golgi complex to the endoplasmic reticulum. Nat. Cell Biol. 1:423-30
    • (1999) Nat. Cell Biol. , vol.1 , pp. 423-430
    • Girod, A.1    Storrie, B.2    Simpson, J.C.3    Johannes, L.4    Goud, B.5
  • 28
    • 0035169411 scopus 로고    scopus 로고
    • The number of subunits comprising the channel formed by the T domain of diphtheria toxin
    • Gordon M, Finkelstein A. 2001. The number of subunits comprising the channel formed by the T domain of diphtheria toxin. J. Gen. Physiol. 118:471-80
    • (2001) J. Gen. Physiol. , vol.118 , pp. 471-480
    • Gordon, M.1    Finkelstein, A.2
  • 29
    • 0028089159 scopus 로고
    • Proteolytic activation of bacterial toxins: Role of bacterial and host cell proteases
    • Gordon VM, Leppla SH. 1994. Proteolytic activation of bacterial toxins: Role of bacterial and host cell proteases. Infect. Immun. 62:333-40
    • (1994) Infect. Immun. , vol.62 , pp. 333-340
    • Gordon, V.M.1    Leppla, S.H.2
  • 30
    • 0028091981 scopus 로고
    • Localization of the Lys, Asp, Glu, Leu tetrapeptide receptor to the Golgi complex and the intermediate compartment in mammalian cells
    • Griffiths G, Ericsson M, Krijnse-Locker J, Nilsson T, Goud B, et al. 1994. Localization of the Lys, Asp, Glu, Leu tetrapeptide receptor to the Golgi complex and the intermediate compartment in mammalian cells. J. Cell Biol. 127:1557-74
    • (1994) J. Cell Biol. , vol.127 , pp. 1557-1574
    • Griffiths, G.1    Ericsson, M.2    Krijnse-Locker, J.3    Nilsson, T.4    Goud, B.5
  • 31
    • 0033634889 scopus 로고    scopus 로고
    • Endosome to Golgi transport of ricin is regulated by cholesterol
    • Grimmer S, Iversen TG, van Deurs B, Sandvig K. 2000. Endosome to Golgi transport of ricin is regulated by cholesterol. Mol. Biol. Cell 11:4205-16
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4205-4216
    • Grimmer, S.1    Iversen, T.G.2    Van Deurs, B.3    Sandvig, K.4
  • 32
    • 0034665096 scopus 로고    scopus 로고
    • The B subunit of Shiga toxin fused to a tumor antigen elicits CTL and targets dendritic cells to allow MHC class I-restricted presentation of peptides derived from exogenous antigens
    • Haicheur N, Bismuth E, Bosset S, Adotevi O, Warnier G, et al. 2000. The B subunit of Shiga toxin fused to a tumor antigen elicits CTL and targets dendritic cells to allow MHC class I-restricted presentation of peptides derived from exogenous antigens. J. Immunol. 165:3301-8
    • (2000) J. Immunol. , vol.165 , pp. 3301-3308
    • Haicheur, N.1    Bismuth, E.2    Bosset, S.3    Adotevi, O.4    Warnier, G.5
  • 33
  • 34
    • 0034681410 scopus 로고    scopus 로고
    • Cholesterol depletion of enterocytes. Effect on the Golgi complex and apical membrane trafficking
    • Hansen GH, Nielschr LL, Thorsen E, Immerdal L, Danielsen EM. 2000. Cholesterol depletion of enterocytes. Effect on the Golgi complex and apical membrane trafficking. J. Biol. Chem. 275:5136-42
    • (2000) J. Biol. Chem. , vol.275 , pp. 5136-5142
    • Hansen, G.H.1    Nielschr, L.L.2    Thorsen, E.3    Immerdal, L.4    Danielsen, E.M.5
  • 35
    • 0027361965 scopus 로고
    • Molecules internalized by clathrin-independent endocytosis are delivered to endosomes containing transferrin receptors
    • Hansen SH, Sandvig K, van Deurs B. 1993. Molecules internalized by clathrin-independent endocytosis are delivered to endosomes containing transferrin receptors. J. Cell Biol. 123:89-97
    • (1993) J. Cell Biol. , vol.123 , pp. 89-97
    • Hansen, S.H.1    Sandvig, K.2    Van Deurs, B.3
  • 36
    • 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 36:11051-54
    • (1997) Biochemistry , vol.36 , pp. 11051-11054
    • Hazes, B.1    Read, R.J.2
  • 38
    • 0035168442 scopus 로고    scopus 로고
    • Lipid rafts act as specialized domains for tetanus toxin binding and internalization into neurons
    • Herreros J, Ng T, Schiavo G. 2001. Lipid rafts act as specialized domains for tetanus toxin binding and internalization into neurons. Mol. Biol. Cell 12:2947-60
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2947-2960
    • Herreros, J.1    Ng, T.2    Schiavo, G.3
  • 39
    • 0028956320 scopus 로고
    • Phorbol myristate acetate selectively stimulates apical endocytosis via protein kinase C in polarized MDCK cells
    • Holm PK, Eker P, Sandvig K, van Deurs B. 1995. Phorbol myristate acetate selectively stimulates apical endocytosis via protein kinase C in polarized MDCK cells. Exp. Cell Res. 217:157-68
    • (1995) Exp. Cell Res. , vol.217 , pp. 157-168
    • Holm, P.K.1    Eker, P.2    Sandvig, K.3    Van Deurs, B.4
  • 41
    • 0035423556 scopus 로고    scopus 로고
    • Roles of lipid rafts in membrane transport
    • Ikonen E. 2001. Roles of lipid rafts in membrane transport. Curr. Opin. Cell Biol. 13:470-77
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 470-477
    • Ikonen, E.1
  • 43
    • 0032969203 scopus 로고    scopus 로고
    • The KDEL retrieval system is exploited by Pseudomonas exotoxin A, but not by Shiga-like toxin-1, during retrograde transport from the Golgi complex to the endoplasmic reticulum
    • Jackson ME, Simpson JC, Girod A, Pepperkok R, Roberts LM, Lord JM. 1999. The KDEL retrieval system is exploited by Pseudomonas exotoxin A, but not by Shiga-like toxin-1, during retrograde transport from the Golgi complex to the endoplasmic reticulum. J. Cell Sci. 112:467-75
    • (1999) J. Cell Sci. , vol.112 , pp. 467-475
    • Jackson, M.E.1    Simpson, J.C.2    Girod, A.3    Pepperkok, R.4    Roberts, L.M.5    Lord, J.M.6
  • 44
    • 0034139657 scopus 로고    scopus 로고
    • Facing inward from compartment shores: How many pathways were we looking for?
    • Johannes L, Goud B. 2000. Facing inward from compartment shores: How many pathways were we looking for? Traffic 1:119-23
    • (2000) Traffic , vol.1 , pp. 119-123
    • Johannes, L.1    Goud, B.2
  • 45
    • 0018743649 scopus 로고
    • Endocytosis of cholera toxin in GERL-like structures of murine neuroblastoma cells pre-treated with GM1 ganglioside
    • Joseph KC, Stieber A, Gonatas NK. 1979. Endocytosis of cholera toxin in GERL-like structures of murine neuroblastoma cells pre-treated with GM1 ganglioside. J. Cell Biol. 81:543-54
    • (1979) J. Cell Biol. , vol.81 , pp. 543-554
    • Joseph, K.C.1    Stieber, A.2    Gonatas, N.K.3
  • 46
    • 0033280324 scopus 로고    scopus 로고
    • Adaptors for clathrin-mediated traffic
    • Kirchhausen T. 1999. Adaptors for clathrin-mediated traffic. Annu. Rev. Cell Dev. Biol. 15:705-32
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 705-732
    • Kirchhausen, T.1
  • 47
    • 0034628502 scopus 로고    scopus 로고
    • Shiga-like toxins are neutralized by tailored multivalent carbohydrate ligands
    • Kitov PI, Sadowska JM, Mulvey G, Armstrong GD, Ling H, et al. 2000. Shiga-like toxins are neutralized by tailored multivalent carbohydrate ligands. Nature 403:669-72
    • (2000) Nature , vol.403 , pp. 669-672
    • Kitov, P.I.1    Sadowska, J.M.2    Mulvey, G.3    Armstrong, G.D.4    Ling, H.5
  • 48
    • 0033725154 scopus 로고    scopus 로고
    • Export of antigenic peptides from the endoplasmic reticulum intersects with retrograde protein translocation through the Sec61p channel
    • Koopmann JO, Albring J, Huter E, Bulbuc N, Spee P, et al. 2000. Export of antigenic peptides from the endoplasmic reticulum intersects with retrograde protein translocation through the Sec61p channel. Immunity 13:117-27
    • (2000) Immunity , vol.13 , pp. 117-127
    • Koopmann, J.O.1    Albring, J.2    Huter, E.3    Bulbuc, N.4    Spee, P.5
  • 49
    • 0026690341 scopus 로고
    • The alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein binds and internalizes Pseudomonas exotoxin A
    • Kounnas MZ, Morris RE, Thompson MR, FitzGerald DJ, Strickland DK, Saelinger CB. 1992. The alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein binds and internalizes Pseudomonas exotoxin A. J. Biol. Chem. 267:12420-23
    • (1992) J. Biol. Chem. , vol.267 , pp. 12420-12423
    • Kounnas, M.Z.1    Morris, R.E.2    Thompson, M.R.3    FitzGerald, D.J.4    Strickland, D.K.5    Saelinger, C.B.6
  • 51
    • 0032879545 scopus 로고    scopus 로고
    • Immunotoxins in cancer therapy
    • Kreitman RJ. 1999. Immunotoxins in cancer therapy. Curr. Opin. Immunol. 11:570-78
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 570-578
    • Kreitman, R.J.1
  • 52
    • 13044254786 scopus 로고    scopus 로고
    • + hematopoietic stem cells: Implications for ex vivo tumor purging and autologous stem cell transplantation
    • + hematopoietic stem cells: Implications for ex vivo tumor purging and autologous stem cell transplantation. Blood 94:2901-10
    • (1999) Blood , vol.94 , pp. 2901-2910
    • LaCasse, E.C.1    Bray, M.R.2    Patterson, B.3    Lim, W.-M.4    Perampalam, S.5
  • 54
    • 0035265834 scopus 로고    scopus 로고
    • Interleukin 2 receptors and detergent-resistant membrane domains define a clathrin-independent endocytic pathway
    • Lamaze C, Dujeancourt A, Baba T, Lo CG, Benmerah A, Dautry-Varsat A. 2001. Interleukin 2 receptors and detergent-resistant membrane domains define a clathrin-independent endocytic pathway. Mol. Cell 7:661-71
    • (2001) Mol. Cell , vol.7 , pp. 661-671
    • Lamaze, C.1    Dujeancourt, A.2    Baba, T.3    Lo, C.G.4    Benmerah, A.5    Dautry-Varsat, A.6
  • 55
    • 0022425912 scopus 로고
    • Nucleotide sequence of cloned cRNA coding for preproricin
    • Lamb FI, Roberts LM, Lord JM. 1985. Nucleotide sequence of cloned cRNA coding for preproricin. Eur. J. Biochem. 148:265-70
    • (1985) Eur. J. Biochem. , vol.148 , pp. 265-270
    • Lamb, F.I.1    Roberts, L.M.2    Lord, J.M.3
  • 56
    • 0031692642 scopus 로고    scopus 로고
    • Major histocompatibility complex class I presentation of exogenous tumor antigen fused to the B-fragment of Shiga toxin
    • Lee R-S, Tartour E, van der Bruggen P, Vantomme V, Joyeux I, et al. 1998. Major histocompatibility complex class I presentation of exogenous tumor antigen fused to the B-fragment of Shiga toxin. Eur. J. Immunol. 28:2726-37
    • (1998) Eur. J. Immunol. , vol.28 , pp. 2726-2737
    • Lee, R.-S.1    Tartour, E.2    Van der Bruggen, P.3    Vantomme, V.4    Joyeux, I.5
  • 57
    • 0028809828 scopus 로고
    • Targeting of cholera toxin and Escherichia coli heat labile toxin in polarized epithelia: Role of COOH-terminal KDEL
    • Lencer WI, Constable C, Moe S, Jobling MG, Webb HM, et al. 1995. Targeting of cholera toxin and Escherichia coli heat labile toxin in polarized epithelia: Role of COOH-terminal KDEL. J. Cell Biol. 131:951-62
    • (1995) J. Cell Biol. , vol.131 , pp. 951-962
    • Lencer, W.I.1    Constable, C.2    Moe, S.3    Jobling, M.G.4    Webb, H.M.5
  • 58
    • 0035903198 scopus 로고    scopus 로고
    • Recombinant forms of tetanus toxin engineered for examining and exploiting neuronal trafficking pathways
    • Li Y, Foran P, Lawrence G, Mohammed N, Chan-Kwo-Chion CK, et al. 2001. Recombinant forms of tetanus toxin engineered for examining and exploiting neuronal trafficking pathways. J. Biol. Chem. 276:31394-401
    • (2001) J. Biol. Chem. , vol.276 , pp. 31394-31401
    • Li, Y.1    Foran, P.2    Lawrence, G.3    Mohammed, N.4    Chan-Kwo-Chion, C.K.5
  • 59
    • 0032833409 scopus 로고    scopus 로고
    • Glycolipid receptors for verotoxin and Helicobacter pylori: Role in pathology
    • Lingwood CA. 1999. Glycolipid receptors for verotoxin and Helicobacter pylori: Role in pathology. Biochim. Biophys. Acta 1455: 375-86
    • (1999) Biochim. Biophys. Acta , vol.1455 , pp. 375-386
    • Lingwood, C.A.1
  • 60
    • 0032498544 scopus 로고    scopus 로고
    • Expression of mutant dynamin inhibits toxicity and transport of endocytosed ricin to the Golgi apparatus
    • Llorente A, Rapak A, Schmid SL, van Deurs B, Sandvig K. 1998. Expression of mutant dynamin inhibits toxicity and transport of endocytosed ricin to the Golgi apparatus. J. Cell Biol. 140:1-11
    • (1998) J. Cell Biol. , vol.140 , pp. 1-11
    • Llorente, A.1    Rapak, A.2    Schmid, S.L.3    Van Deurs, B.4    Sandvig, K.5
  • 61
    • 0034011995 scopus 로고    scopus 로고
    • Apical endocytosis of ricin in MDCK cells is regulated by the cyclooxygenase pathway
    • Llorente A, van Deurs B, Garred Ø, Eker P, Sandvig K. 2000. Apical endocytosis of ricin in MDCK cells is regulated by the cyclooxygenase pathway. J. Cell Sci. 113:1213-21
    • (2000) J. Cell Sci. , vol.113 , pp. 1213-1221
    • Llorente, A.1    Van Deurs, B.2    Garred, Ø.3    Eker, P.4    Sandvig, K.5
  • 63
    • 0033609049 scopus 로고    scopus 로고
    • Intranuclear delivery of an antiviral peptide mediated by the B subunit of Escherichia coli heat-labile enterotoxin
    • Loregian A, Papini E, Satin B, Marsden B, Hirst TR. 1999. Intranuclear delivery of an antiviral peptide mediated by the B subunit of Escherichia coli heat-labile enterotoxin. Proc. Natl. Acad. Sci. USA 96:5221-26
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5221-5226
    • Loregian, A.1    Papini, E.2    Satin, B.3    Marsden, B.4    Hirst, T.R.5
  • 64
    • 0023191512 scopus 로고
    • Effect of potassium depletion of Hep 2 cells on intracellular pH and on chloride uptake by anion antiport
    • Madshus IH, Tönnessen TI, Olsnes S, Sandvig K. 1987. Effect of potassium depletion of Hep 2 cells on intracellular pH and on chloride uptake by anion antiport. J. Cell Physiol. 131:6-13
    • (1987) J. Cell Physiol. , vol.131 , pp. 6-13
    • Madshus, I.H.1    Tönnessen, T.I.2    Olsnes, S.3    Sandvig, K.4
  • 65
    • 0029898287 scopus 로고    scopus 로고
    • Transport of an external Lys-Asp-Glu-Leu (KDEL) protein from the plasma membrane to the endoplasmic reticulum: Studies with cholera toxin in Vero cells
    • Majoul IV, Bastiaens PIH, Söling H-D. 1996. Transport of an external Lys-Asp-Glu-Leu (KDEL) protein from the plasma membrane to the endoplasmic reticulum: Studies with cholera toxin in Vero cells. J. Cell Biol. 133:777-89
    • (1996) J. Cell Biol. , vol.133 , pp. 777-789
    • Majoul, I.V.1    Bastiaens, P.I.H.2    Söling, H.-D.3
  • 66
    • 0032538927 scopus 로고    scopus 로고
    • Direct pathway from early/recycling endosomes to the Golgi apparatus revealed through the study of shiga toxin B-fragment transport
    • Mallard F, Antony C, Tenza D, Salamero J, Goud B, Johannes L. 1998. Direct pathway from early/recycling endosomes to the Golgi apparatus revealed through the study of shiga toxin B-fragment transport. J. Cell Biol. 143:973-90
    • (1998) J. Cell Biol. , vol.143 , pp. 973-990
    • Mallard, F.1    Antony, C.2    Tenza, D.3    Salamero, J.4    Goud, B.5    Johannes, L.6
  • 67
    • 0033606772 scopus 로고    scopus 로고
    • Chimeric forms of furin and TGN38 are transported from the plasma membrane to the trans-Golgi network via distinct endosomal pathways
    • Mallet WG, Maxfield FR. 1999. Chimeric forms of furin and TGN38 are transported from the plasma membrane to the trans-Golgi network via distinct endosomal pathways. J. Cell Biol. 146:345-59
    • (1999) J. Cell Biol. , vol.146 , pp. 345-359
    • Mallet, W.G.1    Maxfield, F.R.2
  • 68
    • 0028564905 scopus 로고
    • Specific inhibition of herpes virus replication by receptor-mediated entry of an antiviral peptide linked to Escherichia coli enterotoxin B subunit
    • Marcello A, Loregian A, Cross A, Marsden H, Hirst TR, Palù G. 1994. Specific inhibition of herpes virus replication by receptor-mediated entry of an antiviral peptide linked to Escherichia coli enterotoxin B subunit. Proc. Natl. Acad. Sci. USA 91:8994-98
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8994-8998
    • Marcello, A.1    Loregian, A.2    Cross, A.3    Marsden, H.4    Hirst, T.R.5    Palù, G.6
  • 69
    • 0032488845 scopus 로고    scopus 로고
    • Protein translocation: Tunnel vision
    • Matlack KES, Mothes W, Rapoport TA. 1998. Protein translocation: Tunnel vision. Cell 92:381-90
    • (1998) Cell , vol.92 , pp. 381-390
    • Matlack, K.E.S.1    Mothes, W.2    Rapoport, T.A.3
  • 70
    • 0024495932 scopus 로고
    • Actin involvement in exocytosis from PC12 cells: Studies on influence of botulinum C2 toxin on stimulated noradrenaline release
    • Matter K, Dreyer F, Aktories K. 1989. Actin involvement in exocytosis from PC12 cells: Studies on influence of botulinum C2 toxin on stimulated noradrenaline release. J. Neurochem. 52:370-76
    • (1989) J. Neurochem. , vol.52 , pp. 370-376
    • Matter, K.1    Dreyer, F.2    Aktories, K.3
  • 71
    • 0035963866 scopus 로고    scopus 로고
    • The role of caveolae and caveolin in vesicle-dependent and vesicle-independent trafficking
    • Matveev S, Li X, Everson W, Smart EJ. 2001. The role of caveolae and caveolin in vesicle-dependent and vesicle-independent trafficking. Adv. Drug Deliv. Rev. 49:237-50
    • (2001) Adv. Drug Deliv. Rev. , vol.49 , pp. 237-250
    • Matveev, S.1    Li, X.2    Everson, W.3    Smart, E.J.4
  • 72
    • 0034161330 scopus 로고    scopus 로고
    • The dynamin family of mechanoenzymes: Pinching in new places
    • McNiven MA, Cao H, Pitts KR, Yoon Y. 2000. The dynamin family of mechanoenzymes: Pinching in new places. Trends. Biochem. Sci. 25:115-20
    • (2000) Trends. Biochem. Sci. , vol.25 , pp. 115-120
    • McNiven, M.A.1    Cao, H.2    Pitts, K.R.3    Yoon, Y.4
  • 73
    • 0028920154 scopus 로고
    • The capacity to retrieve escaped ER proteins extends to the trans-most cisterna of the Golgi stack
    • Miesenböck G, Rothman JE. 1995. The capacity to retrieve escaped ER proteins extends to the trans-most cisterna of the Golgi stack. J. Cell Biol. 129:309-19
    • (1995) J. Cell Biol. , vol.129 , pp. 309-319
    • Miesenböck, G.1    Rothman, J.E.2
  • 74
    • 0019994630 scopus 로고
    • Non-coated membrane invaginations are involved in binding internalization of cholera and tetanus toxins
    • Montesano R, Roth J, Robert A, Orci L. 1982. Non-coated membrane invaginations are involved in binding internalization of cholera and tetanus toxins. Nature 296:651-53
    • (1982) Nature , vol.296 , pp. 651-653
    • Montesano, R.1    Roth, J.2    Robert, A.3    Orci, L.4
  • 75
    • 0033786156 scopus 로고    scopus 로고
    • Globotriaosyl ceramide (CD77/Gb3) in the glycolipid-enriched membrane domain participates in B-cell receptor-mediated apoptosis by regulating lyn kinase activity in human B cells
    • Mori T, Kiyokawa N, Katagiri YU, Taguchi T, Suzuki T, et al. 2000. Globotriaosyl ceramide (CD77/Gb3) in the glycolipid-enriched membrane domain participates in B-cell receptor-mediated apoptosis by regulating lyn kinase activity in human B cells. Exp. Hematol. 28:1260-68
    • (2000) Exp. Hematol. , vol.28 , pp. 1260-1268
    • Mori, T.1    Kiyokawa, N.2    Katagiri, Y.U.3    Taguchi, T.4    Suzuki, T.5
  • 77
    • 0022005540 scopus 로고
    • Inhibition of coated pit formation in Hep2 cells blocks the cytotoxicity of diphtheria toxin but not that of ricin
    • Moya M, Dautry-Varsat A, Goud B, Louvard D, Boquet P. 1985. Inhibition of coated pit formation in Hep2 cells blocks the cytotoxicity of diphtheria toxin but not that of ricin. J. Cell Biol. 101:548-59
    • (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
  • 78
    • 0344791683 scopus 로고    scopus 로고
    • Endocytic sorting of lipid analogues differing solely in the chemistry of their hydrophobic tails
    • Mukherjee S, Soe TT, Maxfield FR. 1999. Endocytic sorting of lipid analogues differing solely in the chemistry of their hydrophobic tails. J. Cell Biol. 144:1271-84
    • (1999) J. Cell Biol. , vol.144 , pp. 1271-1284
    • Mukherjee, S.1    Soe, T.T.2    Maxfield, F.R.3
  • 79
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro S, Pelham HRB. 1987. A C-terminal signal prevents secretion of luminal ER proteins. Cell 48:899-907
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.B.2
  • 80
    • 0026747170 scopus 로고
    • Expression cloning of a diphtheria toxin receptor: Identity with a heparin-binding EGF-like growth factor precursor
    • Naglich JG, Metherall JE, Russell DW, Eidels L. 1992. Expression cloning of a diphtheria toxin receptor: Identity with a heparin-binding EGF-like growth factor precursor. Cell 69:1051-61
    • (1992) Cell , vol.69 , pp. 1051-1061
    • Naglich, J.G.1    Metherall, J.E.2    Russell, D.W.3    Eidels, L.4
  • 81
    • 0032854066 scopus 로고    scopus 로고
    • Regulated expression of Shiga toxin B gene induces apoptosis in mammalian fibroblastic cells
    • Nakagawa I, Nakata M, Kawabata S, Hamada S. 1999. Regulated expression of Shiga toxin B gene induces apoptosis in mammalian fibroblastic cells. Mol. Microbiol. 33:1190-99
    • (1999) Mol. Microbiol. , vol.33 , pp. 1190-1199
    • Nakagawa, I.1    Nakata, M.2    Kawabata, S.3    Hamada, S.4
  • 82
    • 0029083578 scopus 로고
    • Ilimaquinone inhibits the cytotoxicities of ricin, diphtheria toxin, and other protein toxins in Vero cells
    • Nambiar MP, Wu HC. 1995. Ilimaquinone inhibits the cytotoxicities of ricin, diphtheria toxin, and other protein toxins in Vero cells. Exp. Cell Res. 219:671-78
    • (1995) Exp. Cell Res. , vol.219 , pp. 671-678
    • Nambiar, M.P.1    Wu, H.C.2
  • 84
    • 0033995518 scopus 로고    scopus 로고
    • Involvement of dynamin in endosome-to-TGN recycling of the cation-independent mannose 6-phosphate receptor
    • Nicoziani P, Vilhardt F, Llorente A, Hilout L, Courtoy PJ, et al. 2000. Involvement of dynamin in endosome-to-TGN recycling of the cation-independent mannose 6-phosphate receptor. Mol. Biol. Cell 11:481-95
    • (2000) Mol. Biol. Cell , vol.11 , pp. 481-495
    • Nicoziani, P.1    Vilhardt, F.2    Llorente, A.3    Hilout, L.4    Courtoy, P.J.5
  • 85
    • 0032790257 scopus 로고    scopus 로고
    • Exploiting retrograde transport of Shiga-like toxin 1 for delivery of exogenous antigens into MHC class I presentation pathway
    • Noakes KL, Teisserenc HT, Lord JM, Dunbar PR, Cerundolo V, Roberts LM. 1999. Exploiting retrograde transport of Shiga-like toxin 1 for delivery of exogenous antigens into MHC class I presentation pathway. FEBS Lett. 453:95-99
    • (1999) FEBS Lett. , vol.453 , pp. 95-99
    • Noakes, K.L.1    Teisserenc, H.T.2    Lord, J.M.3    Dunbar, P.R.4    Cerundolo, V.5    Roberts, L.M.6
  • 86
    • 0032489880 scopus 로고    scopus 로고
    • Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium
    • Oh P, McIntosh DP, Schnitzer JE. 1998. Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium. J. Cell Biol. 141:101-4
    • (1998) J. Cell Biol. , vol.141 , pp. 101-104
    • Oh, P.1    McIntosh, D.P.2    Schnitzer, J.E.3
  • 87
    • 0027373613 scopus 로고
    • Brefeldin A protects ricin-induced cytotoxicity in human cancer KB cell line, but not in its resistant counterpart with altered Golgi structures
    • Okimoto T, Seguchi T, Ono M, Nakayama Y, Funatsu G, et al. 1993. Brefeldin A protects ricin-induced cytotoxicity in human cancer KB cell line, but not in its resistant counterpart with altered Golgi structures. Cell Struct. Funct. 18:241-51
    • (1993) Cell Struct. Funct. , vol.18 , pp. 241-251
    • Okimoto, T.1    Seguchi, T.2    Ono, M.3    Nakayama, Y.4    Funatsu, G.5
  • 88
    • 0035434215 scopus 로고    scopus 로고
    • Interrogation by toxin
    • Palmiter R. 2001. Interrogation by toxin. Nat. Biotechnol. 19:731-32
    • (2001) Nat. Biotechnol. , vol.19 , pp. 731-732
    • Palmiter, R.1
  • 89
    • 0028057494 scopus 로고
    • Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae
    • Parton RG. 1994. Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae. J. Histochem. Cytochem. 42:155-66
    • (1994) J. Histochem. Cytochem. , vol.42 , pp. 155-166
    • Parton, R.G.1
  • 90
  • 91
    • 0034059721 scopus 로고    scopus 로고
    • A new biological agent for treatment of Shiga toxigenic Escherichia coli infections and dysentery in humans
    • Paton AW, Morona R, Paton JC. 2000. A new biological agent for treatment of Shiga toxigenic Escherichia coli infections and dysentery in humans. Nat. Med. 6:265-70
    • (2000) Nat. Med. , vol.6 , pp. 265-270
    • Paton, A.W.1    Morona, R.2    Paton, J.C.3
  • 92
    • 0034792596 scopus 로고    scopus 로고
    • Mutation of specific acidic residues of the CNF1 T domain into lysine alters cell membrane translocation of the toxin
    • Pei S, Doye A, Boquet P. 2001. Mutation of specific acidic residues of the CNF1 T domain into lysine alters cell membrane translocation of the toxin. Mol. Microbiol. 41:1237-47
    • (2001) Mol. Microbiol. , vol.41 , pp. 1237-1247
    • Pei, S.1    Doye, A.2    Boquet, P.3
  • 93
    • 0035017308 scopus 로고    scopus 로고
    • Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER
    • Pelkmans L, Kartenbeck J, Helenius A. 2001. Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER. Nat. Cell Biol. 3:473-83
    • (2001) Nat. Cell Biol. , vol.3 , pp. 473-483
    • Pelkmans, L.1    Kartenbeck, J.2    Helenius, A.3
  • 94
    • 0026779146 scopus 로고
    • Effects of brefeldin A on endocytosis, transcytosis and transport to the Golgi complex in polarized MDCK cells
    • Prydz K, Hansen SH, Sandvig K, van Deurs B. 1992. Effects of brefeldin A on endocytosis, transcytosis and transport to the Golgi complex in polarized MDCK cells. J. Cell Biol. 119:259-72
    • (1992) J. Cell Biol. , vol.119 , pp. 259-272
    • Prydz, K.1    Hansen, S.H.2    Sandvig, K.3    Van Deurs, B.4
  • 95
    • 0035817629 scopus 로고    scopus 로고
    • Clathrin-dependent and -independent internalization of plasma membrane sphingolipids initiates two Golgi targeting pathways
    • Puri V, Watanabe R, Singh RD, Dominguez M, Brown JC, et al. 2001. Clathrin-dependent and -independent internalization of plasma membrane sphingolipids initiates two Golgi targeting pathways. J. Cell Biol. 154:535-48
    • (2001) J. Cell Biol. , vol.154 , pp. 535-548
    • Puri, V.1    Watanabe, R.2    Singh, R.D.3    Dominguez, M.4    Brown, J.C.5
  • 96
    • 0034605038 scopus 로고    scopus 로고
    • Molecular links between endocytosis and the actin cytoskeleton
    • Qualmann B, Kessels MM, Kelly RB. 2000. Molecular links between endocytosis and the actin cytoskeleton. J. Cell Biol. 150:F111-16
    • (2000) J. Cell Biol. , vol.150
    • Qualmann, B.1    Kessels, M.M.2    Kelly, R.B.3
  • 97
    • 0030929658 scopus 로고    scopus 로고
    • Retrograde transport of mutant ricin to the endoplasmic reticulum with subsequent translocation to cytosol
    • Rapak A, Falnes PO, Olsnes S. 1997. Retrograde transport of mutant ricin to the endoplasmic reticulum with subsequent translocation to cytosol. Proc. Natl. Acad. Sci. USA 94:3783-88
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3783-3788
    • Rapak, A.1    Falnes, P.O.2    Olsnes, S.3
  • 98
    • 0028224561 scopus 로고
    • Lysosome biogenesis requires Rab function and receptor recycling from endosomes to the trans-Golgi network
    • Riederer MA, Soldati T, Shapiro J, Lin J, Pfeffer SR. 1994. Lysosome biogenesis requires Rab function and receptor recycling from endosomes to the trans-Golgi network. J. Cell Biol. 125:573-82
    • (1994) J. Cell Biol. , vol.125 , pp. 573-582
    • Riederer, M.A.1    Soldati, T.2    Shapiro, J.3    Lin, J.4    Pfeffer, S.R.5
  • 99
    • 0032931988 scopus 로고    scopus 로고
    • Extraction of cholesterol with methyl-β-cyclodextrin perturbs formation of clathrin-coated endocytic vesicles
    • Rodal SK, Skretting G, Garred Ø, Vilhardt F, van Deurs B, Sandvig K. 1999. Extraction of cholesterol with methyl-β-cyclodextrin perturbs formation of clathrin-coated endocytic vesicles. Mol. Biol. Cell 10:961-74
    • (1999) Mol. Biol. Cell , vol.10 , pp. 961-974
    • Rodal, S.K.1    Skretting, G.2    Garred, Ø.3    Vilhardt, F.4    Van Deurs, B.5    Sandvig, K.6
  • 100
    • 0025695634 scopus 로고
    • Cholesterol controls the clustering of glycosphingolipid-anchored membrane receptor for 5-methyltetrahydrofolate
    • Rothberg KG, Ying YS, Kamen BA, Anderson RG. 1990. Cholesterol controls the clustering of glycosphingolipid-anchored membrane receptor for 5-methyltetrahydrofolate. J. Cell Biol. 111:2931-38
    • (1990) J. Cell Biol. , vol.111 , pp. 2931-2938
    • Rothberg, K.G.1    Ying, Y.S.2    Kamen, B.A.3    Anderson, R.G.4
  • 101
    • 0034899321 scopus 로고    scopus 로고
    • Diphtheria toxin receptor-mediated conditional and targeted cell ablation in transgenic mice
    • Saito M, Iwawaki T, Taya C, Yonekawa H, Noda M, et al. 2001. Diphtheria toxin receptor-mediated conditional and targeted cell ablation in transgenic mice. Nat. Biotechnol. 19:746-50
    • (2001) Nat. Biotechnol. , vol.19 , pp. 746-750
    • Saito, M.1    Iwawaki, T.2    Taya, C.3    Yonekawa, H.4    Noda, M.5
  • 102
    • 0034877295 scopus 로고    scopus 로고
    • Shiga toxins
    • Sandvig K. 2001. Shiga toxins. Toxicon 39: 1629-35
    • (2001) Toxicon , vol.39 , pp. 1629-1635
    • Sandvig, K.1
  • 104
    • 0029861240 scopus 로고    scopus 로고
    • Regulated transport of cholera toxin to the endoplasmic reticulum: Correlation with cAMP production
    • Sandvig K, Garred Ø, van Deurs B. 1996. Regulated transport of cholera toxin to the endoplasmic reticulum: Correlation with cAMP production. Proc. Natl. Acad. Sci. USA 93:12339-43
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12339-12343
    • Sandvig, K.1    Garred, Ø.2    Van Deurs, B.3
  • 106
    • 0019271816 scopus 로고
    • Diphtheria toxin entry into cells is facilitated by low pH
    • Sandvig K, Olsnes S. 1980. Diphtheria toxin entry into cells is facilitated by low pH. J. Cell Biol. 87:828-32
    • (1980) J. Cell Biol. , vol.87 , pp. 828-832
    • Sandvig, K.1    Olsnes, S.2
  • 107
    • 0024564286 scopus 로고
    • Endocytosis from coated pits of Shiga toxin: A glycolipid-binding protein from Shigella dysenteriae 1
    • Sandvig K, Olsnes S, Brown JE, Petersen OW, van Deurs B. 1989. Endocytosis from coated pits of Shiga toxin: A glycolipid-binding protein from Shigella dysenteriae 1. J. Cell Biol. 108:1331-43
    • (1989) J. Cell Biol. , vol.108 , pp. 1331-1343
    • Sandvig, K.1    Olsnes, S.2    Brown, J.E.3    Petersen, O.W.4    Van Deurs, B.5
  • 108
    • 0029909329 scopus 로고    scopus 로고
    • Endocytosis, intracellular transport, and cytotoxic action of Shiga toxin and ricin
    • Sandvig K, van Deurs B. 1996. Endocytosis, intracellular transport, and cytotoxic action of Shiga toxin and ricin. Physiol. Rev. 76:949-66
    • (1996) Physiol. Rev. , vol.76 , pp. 949-966
    • Sandvig, K.1    Van Deurs, B.2
  • 109
    • 0034669117 scopus 로고    scopus 로고
    • Entry of ricin and shiga toxin into cells: Molecular mechanisms and medical perspectives
    • Sandvig K, van Deurs B. 2000. Entry of ricin and shiga toxin into cells: Molecular mechanisms and medical perspectives. EMBO J. 19:5943-50
    • (2000) EMBO J. , vol.19 , pp. 5943-5950
    • Sandvig, K.1    Van Deurs, B.2
  • 112
    • 0034689054 scopus 로고    scopus 로고
    • Cholera toxin is exported from microsomes by the Sec61p complex
    • Schmitz A, Herrgen H, Winkeler A, Herzog V. 2000. Cholera toxin is exported from microsomes by the Sec61p complex. J. Cell Biol. 148:1203-12
    • (2000) J. Cell Biol. , vol.148 , pp. 1203-1212
    • Schmitz, A.1    Herrgen, H.2    Winkeler, A.3    Herzog, V.4
  • 113
    • 0029809310 scopus 로고    scopus 로고
    • Role of GTP hydrolysis in fission of caveolae directly from plasma membranes
    • Schnitzer JE, Oh P, McIntosh DP. 1996. Role of GTP hydrolysis in fission of caveolae directly from plasma membranes. Science 274:239-42
    • (1996) Science , vol.274 , pp. 239-242
    • Schnitzer, J.E.1    Oh, P.2    McIntosh, D.P.3
  • 114
    • 0023001183 scopus 로고
    • Complete amino acid sequence of Shigella toxin B-chain. A novel polypeptide containing 69 amino acids and one disulfide bridge
    • Seidah NG, Donohue-Rolfe A, Lazure C, Au-Clair F, Keusch GT, Chretien M. 1986. Complete amino acid sequence of Shigella toxin B-chain. A novel polypeptide containing 69 amino acids and one disulfide bridge. J. Biol. Chem. 261:13928-31
    • (1986) J. Biol. Chem. , vol.261 , pp. 13928-13931
    • Seidah, N.G.1    Donohue-Rolfe, A.2    Lazure, C.3    Au-Clair, F.4    Keusch, G.T.5    Chretien, M.6
  • 115
    • 0035957753 scopus 로고    scopus 로고
    • Dominant-negative mutants of a toxin subunit: An approach to therapy of anthrax
    • Sellman BR, Mourez M, Collier RJ. 2001. Dominant-negative mutants of a toxin subunit: An approach to therapy of anthrax. Science 292:695-97
    • (2001) Science , vol.292 , pp. 695-697
    • Sellman, B.R.1    Mourez, M.2    Collier, R.J.3
  • 116
    • 0034189032 scopus 로고    scopus 로고
    • Garrotes, springs, ratchets, and whips: Putting dynamin models to the test
    • Sever S, Damke H, Schmid SL. 2000. Garrotes, springs, ratchets, and whips: Putting dynamin models to the test. Traffic 1:385-92
    • (2000) Traffic , vol.1 , pp. 385-392
    • Sever, S.1    Damke, H.2    Schmid, S.L.3
  • 117
    • 0035877840 scopus 로고    scopus 로고
    • Abrin triggers cell death by inactivating a thiol-specific antioxidant protein
    • Shih SF, Wu YH, Hung CH, Yang HY, Lin JY. 2001. Abrin triggers cell death by inactivating a thiol-specific antioxidant protein. J. Biol. Chem. 276:21870-77
    • (2001) J. Biol. Chem. , vol.276 , pp. 21870-21877
    • Shih, S.F.1    Wu, Y.H.2    Hung, C.H.3    Yang, H.Y.4    Lin, J.Y.5
  • 118
    • 0035937752 scopus 로고    scopus 로고
    • Cholera toxin is found in detergent-insoluble rafts/domains at the cell surface of hippocampal neurons but is internalized via a raft-independent mechanism
    • Shogomori H, Futerman AH. 2001a. Cholera toxin is found in detergent-insoluble rafts/domains at the cell surface of hippocampal neurons but is internalized via a raft-independent mechanism. J. Biol. Chem. 276:9182-88
    • (2001) J. Biol. Chem. , vol.276 , pp. 9182-9188
    • Shogomori, H.1    Futerman, A.H.2
  • 119
    • 0034851545 scopus 로고    scopus 로고
    • Cholesterol depletion by methyl-beta-cyclodextrin blocks cholera toxin transport from endosomes to the Golgi apparatus in hippocampal neurons
    • Shogomori H, Futerman AH. 2001b. Cholesterol depletion by methyl-beta-cyclodextrin blocks cholera toxin transport from endosomes to the Golgi apparatus in hippocampal neurons. J. Neurochem. 78:991-99
    • (2001) J. Neurochem. , vol.78 , pp. 991-999
    • Shogomori, H.1    Futerman, A.H.2
  • 120
    • 0032879634 scopus 로고    scopus 로고
    • Ricin A chain utilises the endoplasmic reticulum-associated protein degradation pathway to enter the cytosol of yeast
    • Simpson JC, Roberts LM, Römisch K, Davey J, Wolf DH, Lord JM. 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    Römisch, K.3    Davey, J.4    Wolf, D.H.5    Lord, J.M.6
  • 121
    • 0031868419 scopus 로고    scopus 로고
    • Expression of mutant dynamin protects cells against diphtheria toxin but not against ricin
    • Simpson JC, Smith DC, Roberts LM, Lord JM. 1998. Expression of mutant dynamin protects cells against diphtheria toxin but not against ricin. Exp. Cell Res. 239:293-300
    • (1998) Exp. Cell Res. , vol.239 , pp. 293-300
    • Simpson, J.C.1    Smith, D.C.2    Roberts, L.M.3    Lord, J.M.4
  • 122
    • 0033492265 scopus 로고    scopus 로고
    • Endocytic mechanisms responsible for uptake of GPI-linked diphtheria toxin receptor
    • Skretting G, Torgersen ML, van Deurs B, Sandvig K. 1999. Endocytic mechanisms responsible for uptake of GPI-linked diphtheria toxin receptor. J. Cell Sci. 112:3899-909
    • (1999) J. Cell Sci. , vol.112 , pp. 3899-3909
    • Skretting, G.1    Torgersen, M.L.2    Van Deurs, B.3    Sandvig, K.4
  • 123
    • 0025872046 scopus 로고
    • Peptides fused to the amino-terminal end of diphtheria toxin are translocated to the cytosol
    • Stenmark H, Moskaug JO, Madshus IH, Sandvig K, Olsnes S. 1991. Peptides fused to the amino-terminal end of diphtheria toxin are translocated to the cytosol. J. Cell Biol. 113:1025-32
    • (1991) J. Cell Biol. , vol.113 , pp. 1025-1032
    • Stenmark, H.1    Moskaug, J.O.2    Madshus, I.H.3    Sandvig, K.4    Olsnes, S.5
  • 124
    • 0023840545 scopus 로고
    • Cloning and sequencing of the genes for Shiga toxin from Shigella dysenteriae type 1
    • Strockbine NA, Jackson MP, Sung LM, Holmes RK, O'Brien A. 1988. Cloning and sequencing of the genes for Shiga toxin from Shigella dysenteriae type 1. J. Bacteriol. 170:1116-22
    • (1988) J. Bacteriol. , vol.170 , pp. 1116-1122
    • Strockbine, N.A.1    Jackson, M.P.2    Sung, L.M.3    Holmes, R.K.4    O'Brien, A.5
  • 126
    • 0032562703 scopus 로고    scopus 로고
    • Complex, two-way traffic of molecules across the membrane of the endoplasmic reticulum
    • Suzuki T, Yan Q, Lennardz WJ. 1998. Complex, two-way traffic of molecules across the membrane of the endoplasmic reticulum. J. Biol. Chem. 273:10083-86
    • (1998) J. Biol. Chem. , vol.273 , pp. 10083-10086
    • Suzuki, T.1    Yan, Q.2    Lennardz, W.J.3
  • 128
    • 0027519575 scopus 로고
    • Vero toxins (Shiga-like toxins) produced by enterohemorrhagic Escherichia coli (Verocytotoxin-producing E. coli)
    • Takeda Y, Kurazono H, Yamasaki S. 1993. Vero toxins (Shiga-like toxins) produced by enterohemorrhagic Escherichia coli (Verocytotoxin-producing E. coli). Microbiol. Immunol. 37:591-99
    • (1993) Microbiol. Immunol. , vol.37 , pp. 591-599
    • Takeda, Y.1    Kurazono, H.2    Yamasaki, S.3
  • 129
    • 0035446006 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis: Membrane factors pull the trigger
    • Takei K, Haucke V. 2001. Clathrin-mediated endocytosis: Membrane factors pull the trigger. Trends Cell Biol. 11:385-91
    • (2001) Trends Cell Biol. , vol.11 , pp. 385-391
    • Takei, K.1    Haucke, V.2
  • 131
    • 0036151510 scopus 로고    scopus 로고
    • Caveolae are highly immobile plasma membrane microdomains, which are not involved in constitutive endocytic trafficking
    • Thomson P, Roepstorff K, Stahlhut M, van Deurs B. 2002. Caveolae are highly immobile plasma membrane microdomains, which are not involved in constitutive endocytic trafficking. Mol. Biol. Cell. 13:238-50
    • (2002) Mol. Biol. Cell , vol.13 , pp. 238-250
    • Thomson, P.1    Roepstorff, K.2    Stahlhut, M.3    Van Deurs, B.4
  • 132
    • 0034762332 scopus 로고    scopus 로고
    • Internalization of cholera toxin by different endocytic mechanisms
    • Torgersen ML, Skretting G, van Deurs B, Sandvig K. 2001. Internalization of cholera toxin by different endocytic mechanisms. J. Cell Sci. 114:3737-47
    • (2001) J. Cell Sci. , vol.114 , pp. 3737-3747
    • Torgersen, M.L.1    Skretting, G.2    Van Deurs, B.3    Sandvig, K.4
  • 133
    • 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 104:937-48
    • (2001) Cell , vol.104 , pp. 937-948
    • Tsai, B.1    Rodighiero, C.2    Lencer, W.I.3    Rapoport, T.A.4
  • 134
    • 0035159679 scopus 로고    scopus 로고
    • Proteasome inhibitors block a late step in lysosomal transport of selected membrane but not soluble proteins
    • van Kerkhof P, Alves dos Santos CM, Sachse M, Klumperman J, Bu G, Strous GJ. 2001. Proteasome inhibitors block a late step in lysosomal transport of selected membrane but not soluble proteins. Mol. Biol. Cell 12:2556-66
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2556-2566
    • Van Kerkhof, P.1    Alves dos Santos, C.M.2    Sachse, M.3    Klumperman, J.4    Bu, G.5    Strous, G.J.6
  • 135
    • 0035082123 scopus 로고    scopus 로고
    • Segregation of gangliosides GM1 and GD3 on cell membranes, isolated membrane rafts, and defined supported lipid monolayers
    • Vyas KA, Patel HV, Vyas AA, Schnaar RL. 2001. Segregation of gangliosides GM1 and GD3 on cell membranes, isolated membrane rafts, and defined supported lipid monolayers. Biol. Chem. 382:241-50
    • (2001) Biol. Chem. , vol.382 , pp. 241-250
    • Vyas, K.A.1    Patel, H.V.2    Vyas, A.A.3    Schnaar, R.L.4
  • 136
    • 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, Rapak A, Olsnes S. 1999. Dependence of ricin toxicity on translocation of the toxin A-chain from the endoplasmic reticulum to the cytosol. J. Biol. Chem. 274:3443-49
    • (1999) J. Biol. Chem. , vol.274 , pp. 3443-3449
    • Wesche, J.1    Rapak, A.2    Olsnes, S.3
  • 137
    • 0033571602 scopus 로고    scopus 로고
    • Rab6 coordinates a novel Golgi to ER retrograde transport pathway in live cells
    • White J, Johannes L, Mallard F, Girod A, Grill S, et al. 1999. Rab6 coordinates a novel Golgi to ER retrograde transport pathway in live cells. J. Cell Biol. 147:743-60
    • (1999) J. Cell Biol. , vol.147 , pp. 743-760
    • White, J.1    Johannes, L.2    Mallard, F.3    Girod, A.4    Grill, S.5
  • 138
    • 0028328846 scopus 로고
    • Dual mode of signal transduction by externally added acidic fibroblast growth factor
    • Wiedlocha A, Falnes PO, Madshus IH, Sandvig K, Olsnes S. 1994. Dual mode of signal transduction by externally added acidic fibroblast growth factor. Cell 76:1039-51
    • (1994) Cell , vol.76 , pp. 1039-1051
    • Wiedlocha, A.1    Falnes, P.O.2    Madshus, I.H.3    Sandvig, K.4    Olsnes, S.5
  • 139
    • 0034638828 scopus 로고    scopus 로고
    • Rab11 regulates the compartmentalization of early endosomes required for efficient transport from early endosomes to the trans-Golgi network
    • Wilcke M, Johannes L, Galli T, Mayau V, Goud B, Salamero J. 2000. Rab11 regulates the compartmentalization of early endosomes required for efficient transport from early endosomes to the trans-Golgi network. J. Cell Biol. 151:1207-20
    • (2000) J. Cell Biol. , vol.151 , pp. 1207-1220
    • Wilcke, M.1    Johannes, L.2    Galli, T.3    Mayau, V.4    Goud, B.5    Salamero, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.