메뉴 건너뛰기




Volumn 59, Issue 8, 2007, Pages 798-809

"Alternative" endocytic mechanisms exploited by pathogens: New avenues for therapeutic delivery?

(1)  Medina Kauwe, L K a  

a NONE

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; PATHOGENS; PROTEINS;

EID: 34548231783     PISSN: 0169409X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.addr.2007.06.009     Document Type: Review
Times cited : (59)

References (151)
  • 1
    • 28844460780 scopus 로고    scopus 로고
    • Intracellular trafficking of nonviral vectors
    • Medina-Kauwe L.K., Xie J., and Hamm-Alvarez S. Intracellular trafficking of nonviral vectors. Gene Ther. 12 (2005) 1734-1751
    • (2005) Gene Ther. , vol.12 , pp. 1734-1751
    • Medina-Kauwe, L.K.1    Xie, J.2    Hamm-Alvarez, S.3
  • 2
    • 33644593889 scopus 로고    scopus 로고
    • Uptake pathways and subsequent intracellular trafficking in nonviral gene delivery
    • Khalil I.A., Kogure K., Akita H., and Harashima H. Uptake pathways and subsequent intracellular trafficking in nonviral gene delivery. Pharmacol. Rev. 58 (2006) 32-45
    • (2006) Pharmacol. Rev. , vol.58 , pp. 32-45
    • Khalil, I.A.1    Kogure, K.2    Akita, H.3    Harashima, H.4
  • 4
    • 20744450629 scopus 로고    scopus 로고
    • Delivery into cells: lessons learned from plant and bacterial toxins
    • Sandvig K., and van Deurs B. Delivery into cells: lessons learned from plant and bacterial toxins. Gene Ther. 12 (2005) 865-872
    • (2005) Gene Ther. , vol.12 , pp. 865-872
    • Sandvig, K.1    van Deurs, B.2
  • 5
    • 30744471419 scopus 로고    scopus 로고
    • Protein toxins: intracellular trafficking for targeted therapy
    • Johannes L., and Decaudin D. Protein toxins: intracellular trafficking for targeted therapy. Gene Ther. 12 (2005) 1360-1368
    • (2005) Gene Ther. , vol.12 , pp. 1360-1368
    • Johannes, L.1    Decaudin, D.2
  • 6
    • 29144458927 scopus 로고    scopus 로고
    • Secrets of caveolae- and lipid raft-mediated endocytosis revealed by mammalian viruses
    • (Electronic publication 2005 Jul 2005)
    • Pelkmans L. Secrets of caveolae- and lipid raft-mediated endocytosis revealed by mammalian viruses. Biochim. Biophys Acta. 1746 (2005) 295-304 (Electronic publication 2005 Jul 2005)
    • (2005) Biochim. Biophys Acta. , vol.1746 , pp. 295-304
    • Pelkmans, L.1
  • 7
    • 32644435882 scopus 로고    scopus 로고
    • Surviving inside a macrophage: the many ways of Brucella
    • (Electronic publication 2005 Nov 2009)
    • Celli J. Surviving inside a macrophage: the many ways of Brucella. Res. Microbiol. 157 (2006) 93-98 (Electronic publication 2005 Nov 2009)
    • (2006) Res. Microbiol. , vol.157 , pp. 93-98
    • Celli, J.1
  • 10
    • 0032764932 scopus 로고    scopus 로고
    • Application of membrane-active peptides for nonviral gene delivery
    • Wagner E. Application of membrane-active peptides for nonviral gene delivery. Adv. Drug Deliv. Rev. 38 (1999) 279-289
    • (1999) Adv. Drug Deliv. Rev. , vol.38 , pp. 279-289
    • Wagner, E.1
  • 13
    • 0032559646 scopus 로고    scopus 로고
    • Toxin entry: retrograde transport through the secretory pathway
    • Lord J.M., and Roberts L.M. Toxin entry: retrograde transport through the secretory pathway. J. Cell. Biol. 140 (1998) 733-736
    • (1998) J. Cell. Biol. , vol.140 , pp. 733-736
    • Lord, J.M.1    Roberts, L.M.2
  • 14
    • 0034669117 scopus 로고    scopus 로고
    • Entry of ricin and Shiga toxin into cells: molecular mechanisms and medical perspectives
    • Sandvig K., and van Deurs B. Entry of ricin and Shiga toxin into cells: molecular mechanisms and medical perspectives. EMBO J. 19 (2000) 5943-5950
    • (2000) EMBO J. , vol.19 , pp. 5943-5950
    • Sandvig, K.1    van Deurs, B.2
  • 15
    • 0023219950 scopus 로고
    • RNA N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes
    • Endo Y., and Tsurugi K. RNA N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes. J. Biol. Chem. 262 (1987) 8128-8130
    • (1987) J. Biol. Chem. , vol.262 , pp. 8128-8130
    • Endo, Y.1    Tsurugi, K.2
  • 16
    • 0023854742 scopus 로고
    • Site of action of a Vero toxin (VT2) from Escherichia coli O157:H7 and of Shiga toxin on eukaryotic ribosomes. RNA N-glycosidase activity of the toxins
    • Endo Y., Tsurugi K., Yutsudo T., Takeda Y., Ogasawara T., and Igarashi K. Site of action of a Vero toxin (VT2) from Escherichia coli O157:H7 and of Shiga toxin on eukaryotic ribosomes. RNA N-glycosidase activity of the toxins. Eur. J. Biochem. 171 (1988) 45-50
    • (1988) Eur. J. Biochem. , vol.171 , pp. 45-50
    • Endo, Y.1    Tsurugi, K.2    Yutsudo, T.3    Takeda, Y.4    Ogasawara, T.5    Igarashi, K.6
  • 17
    • 0017329291 scopus 로고
    • Mechanism of action of choleragen. Evidence for ADP-ribosyltransferase activity with arginine as an acceptor
    • Moss J., and Vaughan M. Mechanism of action of choleragen. Evidence for ADP-ribosyltransferase activity with arginine as an acceptor. J. Biol. Chem. 252 (1977) 2455-2457
    • (1977) J. Biol. Chem. , vol.252 , pp. 2455-2457
    • Moss, J.1    Vaughan, M.2
  • 19
    • 0000838807 scopus 로고
    • NAD-dependent inhibition of protein synthesis by Pseudomonas aeruginosa toxin
    • Iglewski B.H., and Kabat D. NAD-dependent inhibition of protein synthesis by Pseudomonas aeruginosa toxin. Proc. Natl. Acad. Sci. U. S. A. 72 (1975) 2284-2288
    • (1975) Proc. Natl. Acad. Sci. U. S. A. , vol.72 , pp. 2284-2288
    • Iglewski, B.H.1    Kabat, D.2
  • 20
    • 0025028971 scopus 로고
    • Induction of verotoxin sensitivity in receptor-deficient cell lines using the receptor glycolipid globotriosylceramide
    • Waddell T., Cohen A., and Lingwood C.A. Induction of verotoxin sensitivity in receptor-deficient cell lines using the receptor glycolipid globotriosylceramide. Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 7898-7901
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 7898-7901
    • Waddell, T.1    Cohen, A.2    Lingwood, C.A.3
  • 21
    • 0022508584 scopus 로고
    • Pathogenesis of shigella diarrhea. XI. Isolation of a shigella toxin-binding glycolipid from rabbit jejunum and HeLa cells and its identification as globotriaosylceramide
    • Jacewicz M., Clausen H., Nudelman E., Donohue-Rolfe A., and Keusch G.T. Pathogenesis of shigella diarrhea. XI. Isolation of a shigella toxin-binding glycolipid from rabbit jejunum and HeLa cells and its identification as globotriaosylceramide. J. Exp. Med. 163 (1986) 1391-1404
    • (1986) J. Exp. Med. , vol.163 , pp. 1391-1404
    • Jacewicz, M.1    Clausen, H.2    Nudelman, E.3    Donohue-Rolfe, A.4    Keusch, G.T.5
  • 23
    • 0015819081 scopus 로고
    • Tissue receptor for cholera exotoxin: postulated structure from studies with GM1 ganglioside and related glycolipids
    • Holmgren J., Lonnroth I., and Svennerholm L. Tissue receptor for cholera exotoxin: postulated structure from studies with GM1 ganglioside and related glycolipids. Infect. Immun. 8 (1973) 208-214
    • (1973) Infect. Immun. , vol.8 , pp. 208-214
    • Holmgren, J.1    Lonnroth, I.2    Svennerholm, L.3
  • 24
    • 0015547008 scopus 로고
    • Fixation and inactivation of cholera toxin by GM1 ganglioside
    • Holmgren J., Lonnroth I., and Svennerholm L. Fixation and inactivation of cholera toxin by GM1 ganglioside. Scand. J. Infect. Dis. 5 (1973) 77-78
    • (1973) Scand. J. Infect. Dis. , vol.5 , pp. 77-78
    • Holmgren, J.1    Lonnroth, I.2    Svennerholm, L.3
  • 25
    • 0026690341 scopus 로고
    • The alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein binds and internalizes Pseudomonas exotoxin A
    • Kounnas M.Z., Morris R.E., Thompson M.R., FitzGerald D.J., Strickland D.K., and Saelinger C.B. The alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein binds and internalizes Pseudomonas exotoxin A. J. Biol. Chem. 267 (1992) 12420-12423
    • (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
  • 26
    • 0002169483 scopus 로고
    • Toxic lectins and related proteins
    • van Heyningen S. (Ed), Elsevier, Amsterdam
    • Olsnes S., and Pihl A. Toxic lectins and related proteins. In: van Heyningen S. (Ed). Molecular Action of Toxins and Viruses (1982), Elsevier, Amsterdam 51-105
    • (1982) Molecular Action of Toxins and Viruses , pp. 51-105
    • Olsnes, S.1    Pihl, A.2
  • 27
    • 33644867725 scopus 로고    scopus 로고
    • The association of Shiga-like toxin with detergent-resistant membranes is modulated by glucosylceramide and is an essential requirement in the endoplasmic reticulum for a cytotoxic effect
    • (Electronic publication 2005 Dec 1328)
    • Smith D.C., Sillence D.J., Falguieres T., Jarvis R.M., Johannes L., Lord J.M., Platt F.M., and Roberts L.M. The association of Shiga-like toxin with detergent-resistant membranes is modulated by glucosylceramide and is an essential requirement in the endoplasmic reticulum for a cytotoxic effect. Mol. Biol. Cell. 17 (2006) 1375-1387 (Electronic publication 2005 Dec 1328)
    • (2006) Mol. Biol. Cell. , vol.17 , pp. 1375-1387
    • Smith, D.C.1    Sillence, D.J.2    Falguieres, T.3    Jarvis, R.M.4    Johannes, L.5    Lord, J.M.6    Platt, F.M.7    Roberts, L.M.8
  • 29
    • 0027398577 scopus 로고
    • Rab9 functions in transport between late endosomes and the trans Golgi network
    • Lombardi D., Soldati T., Riederer M.A., Goda Y., Zerial M., and Pfeffer S.R. Rab9 functions in transport between late endosomes and the trans Golgi network. EMBO J. 12 (1993) 677-682
    • (1993) EMBO J. , vol.12 , pp. 677-682
    • Lombardi, D.1    Soldati, T.2    Riederer, M.A.3    Goda, Y.4    Zerial, M.5    Pfeffer, S.R.6
  • 31
    • 33748313351 scopus 로고    scopus 로고
    • Retrograde transport from endosomes to the trans-Golgi network
    • Bonifacino J.S., and Rojas R. Retrograde transport from endosomes to the trans-Golgi network. Nat. Rev., Mol. Cell Biol. 7 (2006) 568-579
    • (2006) Nat. Rev., Mol. Cell Biol. , vol.7 , pp. 568-579
    • Bonifacino, J.S.1    Rojas, R.2
  • 33
    • 0028920154 scopus 로고
    • The capacity to retrieve escaped ER proteins extends to the trans-most cisterna of the Golgi stack
    • Miesenbock G., and Rothman J.E. The capacity to retrieve escaped ER proteins extends to the trans-most cisterna of the Golgi stack. J. Cell Biol. 129 (1995) 309-319
    • (1995) J. Cell Biol. , vol.129 , pp. 309-319
    • Miesenbock, G.1    Rothman, J.E.2
  • 34
    • 0030760897 scopus 로고    scopus 로고
    • Coatomer (COPI)-coated vesicles: role in intracellular transport and protein sorting
    • Cosson P., and Letourneur F. Coatomer (COPI)-coated vesicles: role in intracellular transport and protein sorting. Curr. Opin. Cell Biol. 9 (1997) 484-487
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 484-487
    • Cosson, P.1    Letourneur, F.2
  • 36
    • 0025012987 scopus 로고
    • Pseudomonas exotoxin contains a specific sequence at the carboxyl terminus that is required for cytotoxicity
    • Chaudhary V.K., Jinno Y., FitzGerald D., and Pastan I. Pseudomonas exotoxin contains a specific sequence at the carboxyl terminus that is required for cytotoxicity. Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 308-312
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 308-312
    • Chaudhary, V.K.1    Jinno, Y.2    FitzGerald, D.3    Pastan, I.4
  • 37
    • 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 M.E., Simpson J.C., Girod A., Pepperkok R., Roberts L.M., and Lord J.M. 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 (1999) 467-475
    • (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
  • 38
    • 0028951457 scopus 로고
    • Importance of the glutamate residue of KDEL in increasing the cytotoxicity of Pseudomonas exotoxin derivatives and for increased binding to the KDEL receptor
    • Kreitman R.J., and Pastan I. Importance of the glutamate residue of KDEL in increasing the cytotoxicity of Pseudomonas exotoxin derivatives and for increased binding to the KDEL receptor. Biochem. J. 307 (1995) 29-37
    • (1995) Biochem. J. , vol.307 , pp. 29-37
    • Kreitman, R.J.1    Pastan, I.2
  • 39
    • 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. Increased cytotoxic activity of Pseudomonas exotoxin and two chimeric toxins ending in KDEL. J. Biol. Chem. 266 (1991) 17376-17381
    • (1991) J. Biol. Chem. , vol.266 , pp. 17376-17381
    • Seetharam, S.1    Chaudhary, V.K.2    FitzGerald, D.3    Pastan, I.4
  • 40
    • 0037128205 scopus 로고    scopus 로고
    • Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform
    • (Electronic publication 2002 Feb 2011)
    • Mallard F., Tang B.L., Galli T., Tenza D., Saint-Pol A., Yue X., Antony C., Hong W., Goud B., and Johannes L. Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform. J. Cell Biol. 156 (2002) 653-664 (Electronic publication 2002 Feb 2011)
    • (2002) J. Cell Biol. , vol.156 , pp. 653-664
    • Mallard, F.1    Tang, B.L.2    Galli, T.3    Tenza, D.4    Saint-Pol, A.5    Yue, X.6    Antony, C.7    Hong, W.8    Goud, B.9    Johannes, L.10
  • 43
    • 0036221752 scopus 로고    scopus 로고
    • Characterization of novel Rab6-interacting proteins involved in endosome-to-TGN transport
    • Monier S., Jollivet F., Janoueix-Lerosey I., Johannes L., and Goud B. Characterization of novel Rab6-interacting proteins involved in endosome-to-TGN transport. Traffic 3 (2002) 289-297
    • (2002) Traffic , vol.3 , pp. 289-297
    • Monier, S.1    Jollivet, F.2    Janoueix-Lerosey, I.3    Johannes, L.4    Goud, B.5
  • 44
    • 4344571004 scopus 로고    scopus 로고
    • Retrograde transport of cholera toxin from the plasma membrane to the endoplasmic reticulum requires the trans-Golgi network but not the Golgi apparatus in Exo2-treated cells
    • (Electronic publication 2004 May 2021)
    • Feng Y., Jadhav A.P., Rodighiero C., Fujinaga Y., Kirchhausen T., and Lencer W.I. Retrograde transport of cholera toxin from the plasma membrane to the endoplasmic reticulum requires the trans-Golgi network but not the Golgi apparatus in Exo2-treated cells. EMBO Rep. 5 (2004) 596-601 (Electronic publication 2004 May 2021)
    • (2004) EMBO Rep. , vol.5 , pp. 596-601
    • Feng, Y.1    Jadhav, A.P.2    Rodighiero, C.3    Fujinaga, Y.4    Kirchhausen, T.5    Lencer, W.I.6
  • 45
    • 0035831558 scopus 로고    scopus 로고
    • An interaction between ricin and calreticulin that may have implications for toxin trafficking
    • (Electronic publication 2000 Dec 7211)
    • Day P.J., Owens S.R., Wesche J., Olsnes S., Roberts L.M., and Lord J.M. An interaction between ricin and calreticulin that may have implications for toxin trafficking. J. Biol. Chem. 276 (2001) 7202-7208 (Electronic publication 2000 Dec 7211)
    • (2001) J. Biol. Chem. , vol.276 , pp. 7202-7208
    • Day, P.J.1    Owens, S.R.2    Wesche, J.3    Olsnes, S.4    Roberts, L.M.5    Lord, J.M.6
  • 46
    • 0041326901 scopus 로고    scopus 로고
    • Evidence that the transport of ricin to the cytoplasm is independent of both Rab6A and COPI
    • (Electronic publication 2003 Jul 3515)
    • Chen A., AbuJarour R.J., and Draper R.K. Evidence that the transport of ricin to the cytoplasm is independent of both Rab6A and COPI. J. Cell Sci. 116 (2003) 3503-3510 (Electronic publication 2003 Jul 3515)
    • (2003) J. Cell Sci. , vol.116 , pp. 3503-3510
    • Chen, A.1    AbuJarour, R.J.2    Draper, R.K.3
  • 49
    • 0030886889 scopus 로고    scopus 로고
    • Accumulating evidence suggests that several AB-toxins subvert the endoplasmic reticulum-associated protein degradation pathway to enter target cells
    • Hazes B., and Read R.J. Accumulating evidence suggests that several AB-toxins subvert the endoplasmic reticulum-associated protein degradation pathway to enter target cells. Biochemistry 36 (1997) 11051-11054
    • (1997) Biochemistry , vol.36 , pp. 11051-11054
    • Hazes, B.1    Read, R.J.2
  • 50
    • 0031026351 scopus 로고    scopus 로고
    • The transmembrane domain of diphtheria toxin improves molecular conjugate gene transfer
    • Fisher K.J., and Wilson J.M. The transmembrane domain of diphtheria toxin improves molecular conjugate gene transfer. Biochem. J. 321 (1997) 49-58
    • (1997) Biochem. J. , vol.321 , pp. 49-58
    • Fisher, K.J.1    Wilson, J.M.2
  • 51
    • 0026652890 scopus 로고
    • Membrane translocation of diphtheria toxin carrying passenger protein domains
    • Madshus I.H., Olsnes S., and Stenmark H. Membrane translocation of diphtheria toxin carrying passenger protein domains. Infect. Immun. 60 (1992) 3296-3302
    • (1992) Infect. Immun. , vol.60 , pp. 3296-3302
    • Madshus, I.H.1    Olsnes, S.2    Stenmark, H.3
  • 52
    • 0025872046 scopus 로고
    • Peptides fused to the amino-terminal end of diphtheria toxin are translocated to the cytosol
    • Stenmark H., Moskaug J.O., Madshus I.H., Sandvig K., and Olsnes S. Peptides fused to the amino-terminal end of diphtheria toxin are translocated to the cytosol. J. Cell Biol. 113 (1991) 1025-1032
    • (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
  • 53
    • 0031891120 scopus 로고    scopus 로고
    • A chimeric fusion protein containing transforming growth factor-α mediates gene transfer via binding to the EGF receptor
    • Fominaya J., Uherek C., and Wels W. A chimeric fusion protein containing transforming growth factor-α mediates gene transfer via binding to the EGF receptor. Gene Ther. 5 (1998) 521-530
    • (1998) Gene Ther. , vol.5 , pp. 521-530
    • Fominaya, J.1    Uherek, C.2    Wels, W.3
  • 54
    • 15844404886 scopus 로고    scopus 로고
    • Target cell-specific DNA transfer mediated by a chimeric multidomain protein. Novel non-viral gene delivery system
    • Fominaya J., and Wels W. Target cell-specific DNA transfer mediated by a chimeric multidomain protein. Novel non-viral gene delivery system. J. Biol. Chem. 271 (1996) 10560-10568
    • (1996) J. Biol. Chem. , vol.271 , pp. 10560-10568
    • Fominaya, J.1    Wels, W.2
  • 58
    • 0035840213 scopus 로고    scopus 로고
    • A verotoxin 1 B subunit-lambda CRO chimeric protein specifically binds both DNA and globotriaosylceramide (Gb(3)) to effect nuclear targeting of exogenous DNA in Gb(3) positive cells
    • Facchini L.M., and Lingwood C.A. A verotoxin 1 B subunit-lambda CRO chimeric protein specifically binds both DNA and globotriaosylceramide (Gb(3)) to effect nuclear targeting of exogenous DNA in Gb(3) positive cells. Exp. Cell Res. 269 (2001) 117-129
    • (2001) Exp. Cell Res. , vol.269 , pp. 117-129
    • Facchini, L.M.1    Lingwood, C.A.2
  • 59
    • 0036789039 scopus 로고    scopus 로고
    • 1st class ticket to class I: protein toxins as pathfinders for antigen presentation
    • Smith D.C., Lord J.M., Roberts L.M., Tartour E., and Johannes L. 1st class ticket to class I: protein toxins as pathfinders for antigen presentation. Traffic 3 (2002) 697-704
    • (2002) Traffic , vol.3 , pp. 697-704
    • Smith, D.C.1    Lord, J.M.2    Roberts, L.M.3    Tartour, E.4    Johannes, L.5
  • 60
    • 1942502913 scopus 로고    scopus 로고
    • pH-sensitive toxins: interactions with membrane bilayers and application to drug delivery
    • Cabiaux V. pH-sensitive toxins: interactions with membrane bilayers and application to drug delivery. Adv. Drug Deliv. Rev. 56 (2004) 987-997
    • (2004) Adv. Drug Deliv. Rev. , vol.56 , pp. 987-997
    • Cabiaux, V.1
  • 63
    • 0141515196 scopus 로고    scopus 로고
    • Putative functions of PrP(C)
    • Lasmezas C.I. Putative functions of PrP(C). Br. Med. Bull. 66 (2003) 61-70
    • (2003) Br. Med. Bull. , vol.66 , pp. 61-70
    • Lasmezas, C.I.1
  • 66
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: their causes and molecular basis
    • Collinge J. Prion diseases of humans and animals: their causes and molecular basis. Annu. Rev. Neurosci. 24 (2001) 519-550
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 519-550
    • Collinge, J.1
  • 67
    • 2942620539 scopus 로고    scopus 로고
    • Propagating prions in fungi and mammals
    • Tuite M.F., and Koloteva-Levin N. Propagating prions in fungi and mammals. Mol. Cell 14 (2004) 541-552
    • (2004) Mol. Cell , vol.14 , pp. 541-552
    • Tuite, M.F.1    Koloteva-Levin, N.2
  • 68
    • 0344021409 scopus 로고    scopus 로고
    • Prions and the immune system: a journey through gut, spleen, and nerves
    • Aguzzi A. Prions and the immune system: a journey through gut, spleen, and nerves. Adv. Immunol. 81 (2003) 123-171
    • (2003) Adv. Immunol. , vol.81 , pp. 123-171
    • Aguzzi, A.1
  • 69
    • 7444254877 scopus 로고    scopus 로고
    • Brain targeting through the autonomous nervous system: lessons from prion diseases
    • Haik S., Faucheux B.A., and Hauw J.J. Brain targeting through the autonomous nervous system: lessons from prion diseases. Trends Mol. Med. 10 (2004) 107-112
    • (2004) Trends Mol. Med. , vol.10 , pp. 107-112
    • Haik, S.1    Faucheux, B.A.2    Hauw, J.J.3
  • 70
    • 0034796073 scopus 로고    scopus 로고
    • The immunobiology of TSE diseases
    • Mabbott N.A., and Bruce M.E. The immunobiology of TSE diseases. J. Gen. Virol. 82 (2001) 2307-2318
    • (2001) J. Gen. Virol. , vol.82 , pp. 2307-2318
    • Mabbott, N.A.1    Bruce, M.E.2
  • 71
    • 0036917840 scopus 로고    scopus 로고
    • The immune system and prion diseases: a relationship of complicity and blindness
    • Aucouturier P., and Carnaud C. The immune system and prion diseases: a relationship of complicity and blindness. J. Leukoc. Biol. 72 (2002) 1075-1083
    • (2002) J. Leukoc. Biol. , vol.72 , pp. 1075-1083
    • Aucouturier, P.1    Carnaud, C.2
  • 73
    • 13244295520 scopus 로고    scopus 로고
    • The highways and byways of prion protein trafficking
    • Campana V., Sarnataro D., and Zurzolo C. The highways and byways of prion protein trafficking. Trends Cell Biol. 15 (2005) 102-111
    • (2005) Trends Cell Biol. , vol.15 , pp. 102-111
    • Campana, V.1    Sarnataro, D.2    Zurzolo, C.3
  • 74
    • 0141626391 scopus 로고    scopus 로고
    • Trafficking, turnover and membrane topology of PrP
    • Harris D.A. Trafficking, turnover and membrane topology of PrP. Br. Med. Bull. 66 (2003) 71-85
    • (2003) Br. Med. Bull. , vol.66 , pp. 71-85
    • Harris, D.A.1
  • 75
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., and Ikonen E. Functional rafts in cell membranes. Nature 387 (1997) 569-572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 77
    • 0028305135 scopus 로고
    • A glycolipid-anchored prion protein is endocytosed via clathrin-coated pits
    • Shyng S.L., Heuser J.E., and Harris D.A. A glycolipid-anchored prion protein is endocytosed via clathrin-coated pits. J. Cell Biol. 125 (1994) 1239-1250
    • (1994) J. Cell Biol. , vol.125 , pp. 1239-1250
    • Shyng, S.L.1    Heuser, J.E.2    Harris, D.A.3
  • 79
    • 0027333415 scopus 로고
    • Signal-dependent membrane protein trafficking in the endocytic pathway
    • Trowbridge I.S., Collawn J.F., and Hopkins C.R. Signal-dependent membrane protein trafficking in the endocytic pathway. Annu. Rev. Cell Biol. 9 (1993) 129-161
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 129-161
    • Trowbridge, I.S.1    Collawn, J.F.2    Hopkins, C.R.3
  • 81
    • 12444347534 scopus 로고    scopus 로고
    • A protein's final ESCRT
    • Babst M. A protein's final ESCRT. Traffic 6 (2005) 2-9
    • (2005) Traffic , vol.6 , pp. 2-9
    • Babst, M.1
  • 83
    • 0036500554 scopus 로고    scopus 로고
    • Conversion of raft associated prion protein to the protease-resistant state requires insertion of PrP-res (PrP(Sc)) into contiguous membranes
    • Baron G.S., Wehrly K., Dorward D.W., Chesebro B., and Caughey B. Conversion of raft associated prion protein to the protease-resistant state requires insertion of PrP-res (PrP(Sc)) into contiguous membranes. EMBO J. 21 (2002) 1031-1040
    • (2002) EMBO J. , vol.21 , pp. 1031-1040
    • Baron, G.S.1    Wehrly, K.2    Dorward, D.W.3    Chesebro, B.4    Caughey, B.5
  • 84
    • 0026775909 scopus 로고
    • Evidence for synthesis of scrapie prion proteins in the endocytic pathway
    • Borchelt D.R., Taraboulos A., and Prusiner S.B. Evidence for synthesis of scrapie prion proteins in the endocytic pathway. J. Biol. Chem. 267 (1992) 16188-16199
    • (1992) J. Biol. Chem. , vol.267 , pp. 16188-16199
    • Borchelt, D.R.1    Taraboulos, A.2    Prusiner, S.B.3
  • 85
    • 0025991466 scopus 로고
    • The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive
    • Caughey B., and Raymond G.J. The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive. J. Biol. Chem. 266 (1991) 18217-18223
    • (1991) J. Biol. Chem. , vol.266 , pp. 18217-18223
    • Caughey, B.1    Raymond, G.J.2
  • 87
    • 0035287755 scopus 로고    scopus 로고
    • VP22 enhanced intercellular trafficking of HSV thymidine kinase reduced the level of ganciclovir needed to cause suicide cell death
    • Liu C.S., Kong B., Xia H.H., Ellem K.A., and Wei M.Q. VP22 enhanced intercellular trafficking of HSV thymidine kinase reduced the level of ganciclovir needed to cause suicide cell death. J. Gene Med. 3 (2001) 145-152
    • (2001) J. Gene Med. , vol.3 , pp. 145-152
    • Liu, C.S.1    Kong, B.2    Xia, H.H.3    Ellem, K.A.4    Wei, M.Q.5
  • 88
    • 0034797798 scopus 로고    scopus 로고
    • Mapping of herpes simplex virus-1 VP22 functional domains for inter- and subcellular protein targeting
    • Aints A., Guven H., Gahrton G., Smith C.I., and Dilber M.S. Mapping of herpes simplex virus-1 VP22 functional domains for inter- and subcellular protein targeting. Gene Ther. 8 (2001) 1051-1056
    • (2001) Gene Ther. , vol.8 , pp. 1051-1056
    • Aints, A.1    Guven, H.2    Gahrton, G.3    Smith, C.I.4    Dilber, M.S.5
  • 89
    • 0031471203 scopus 로고    scopus 로고
    • Intercellular trafficking and protein delivery by a herpesvirus structural protein
    • Elliott G., and O'Hare P. Intercellular trafficking and protein delivery by a herpesvirus structural protein. Cell 88 (1997) 223-233
    • (1997) Cell , vol.88 , pp. 223-233
    • Elliott, G.1    O'Hare, P.2
  • 90
    • 77049234363 scopus 로고
    • The fine structure of the gall bladder epithelium of the mouse
    • Yamada E. The fine structure of the gall bladder epithelium of the mouse. J. Biophys. Biochem. Cytol. 1 (1955) 445-458
    • (1955) J. Biophys. Biochem. Cytol. , vol.1 , pp. 445-458
    • Yamada, E.1
  • 92
    • 0026640940 scopus 로고
    • VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles
    • Kurzchalia T.V., Dupree P., Parton R.G., Kellner R., Virta H., Lehnert M., and Simons K. VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles. J. Cell Biol. 118 (1992) 1003-1014
    • (1992) J. Cell Biol. , vol.118 , pp. 1003-1014
    • Kurzchalia, T.V.1    Dupree, P.2    Parton, R.G.3    Kellner, R.4    Virta, H.5    Lehnert, M.6    Simons, K.7
  • 93
    • 0028920139 scopus 로고
    • Caveolin is palmitoylated on multiple cysteine residues. Palmitoylation is not necessary for localization of caveolin to caveolae
    • Dietzen D.J., Hastings W.R., and Lublin D.M. Caveolin is palmitoylated on multiple cysteine residues. Palmitoylation is not necessary for localization of caveolin to caveolae. J. Biol. Chem. 270 (1995) 6838-6842
    • (1995) J. Biol. Chem. , vol.270 , pp. 6838-6842
    • Dietzen, D.J.1    Hastings, W.R.2    Lublin, D.M.3
  • 95
    • 4644224284 scopus 로고    scopus 로고
    • Role of caveolae and caveolins in health and disease
    • Cohen A.W., Hnasko R., Schubert W., and Lisanti M.P. Role of caveolae and caveolins in health and disease. Physiol. Rev. 84 (2004) 1341-1379
    • (2004) Physiol. Rev. , vol.84 , pp. 1341-1379
    • Cohen, A.W.1    Hnasko, R.2    Schubert, W.3    Lisanti, M.P.4
  • 96
    • 0034755553 scopus 로고    scopus 로고
    • Caveolae are involved in the trafficking of mouse polyomavirus virions and artificial VP1 pseudocapsids toward cell nuclei
    • Richterova Z., Liebl D., Horak M., Palkova Z., Stokrova J., Hozak P., Korb J., and Forstova J. Caveolae are involved in the trafficking of mouse polyomavirus virions and artificial VP1 pseudocapsids toward cell nuclei. J. Virol. 75 (2001) 10880-10891
    • (2001) J. Virol. , vol.75 , pp. 10880-10891
    • Richterova, Z.1    Liebl, D.2    Horak, M.3    Palkova, Z.4    Stokrova, J.5    Hozak, P.6    Korb, J.7    Forstova, J.8
  • 97
    • 6344275643 scopus 로고    scopus 로고
    • Echovirus 1 endocytosis into caveosomes requires lipid rafts, dynamin II, and signaling events
    • (Electronic publication 2004 Sep 4918)
    • Pietiainen V., Marjomaki V., Upla P., Pelkmans L., Helenius A., and Hyypia T. Echovirus 1 endocytosis into caveosomes requires lipid rafts, dynamin II, and signaling events. Mol. Biol. Cell 15 (2004) 4911-4925 (Electronic publication 2004 Sep 4918)
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4911-4925
    • Pietiainen, V.1    Marjomaki, V.2    Upla, P.3    Pelkmans, L.4    Helenius, A.5    Hyypia, T.6
  • 101
    • 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., and Helenius A. Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER. Nat. Cell Biol. 3 (2001) 473-483
    • (2001) Nat. Cell Biol. , vol.3 , pp. 473-483
    • Pelkmans, L.1    Kartenbeck, J.2    Helenius, A.3
  • 102
    • 13444273098 scopus 로고    scopus 로고
    • Clathrin- and caveolin-1-independent endocytosis: entry of simian virus 40 into cells devoid of caveolae
    • (Electronic publication 2005 Jan 2024)
    • Damm E.M., Pelkmans L., Kartenbeck J., Mezzacasa A., Kurzchalia T., and Helenius A. Clathrin- and caveolin-1-independent endocytosis: entry of simian virus 40 into cells devoid of caveolae. J. Cell Biol. 168 (2005) 477-488 (Electronic publication 2005 Jan 2024)
    • (2005) J. Cell Biol. , vol.168 , pp. 477-488
    • Damm, E.M.1    Pelkmans, L.2    Kartenbeck, J.3    Mezzacasa, A.4    Kurzchalia, T.5    Helenius, A.6
  • 103
    • 0029987340 scopus 로고    scopus 로고
    • Bound simian virus 40 translocates to caveolin-enriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae
    • Anderson H.A., Chen Y., and Norkin L.C. Bound simian virus 40 translocates to caveolin-enriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae. Mol. Biol. Cell. 7 (1996) 1825-1834
    • (1996) Mol. Biol. Cell. , vol.7 , pp. 1825-1834
    • Anderson, H.A.1    Chen, Y.2    Norkin, L.C.3
  • 104
    • 0037134014 scopus 로고    scopus 로고
    • Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae
    • Pelkmans L., Puntener D., and Helenius A. Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae. Science 296 (2002) 535-539
    • (2002) Science , vol.296 , pp. 535-539
    • Pelkmans, L.1    Puntener, D.2    Helenius, A.3
  • 106
    • 8744221758 scopus 로고    scopus 로고
    • Characterization of simian virus 40 on its infectious entry pathway in cells using fluorescence correlation spectroscopy
    • Bernacchi S., Mueller G., Langowski J., and Waldeck W. Characterization of simian virus 40 on its infectious entry pathway in cells using fluorescence correlation spectroscopy. Biochem. Soc. Trans. 32 (2004) 746-749
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 746-749
    • Bernacchi, S.1    Mueller, G.2    Langowski, J.3    Waldeck, W.4
  • 107
    • 0031861436 scopus 로고    scopus 로고
    • MHC class I molecules are enriched in caveolae but do not enter with simian virus 40
    • Anderson H.A., Chen Y., and Norkin L.C. MHC class I molecules are enriched in caveolae but do not enter with simian virus 40. J. Gen. Virol. 79 (1998) 1469-1477
    • (1998) J. Gen. Virol. , vol.79 , pp. 1469-1477
    • Anderson, H.A.1    Chen, Y.2    Norkin, L.C.3
  • 108
    • 0030745673 scopus 로고    scopus 로고
    • Major histocompatibility complex class I molecules mediate association of SV40 with caveolae
    • Stang E., Kartenbeck J., and Parton R.G. Major histocompatibility complex class I molecules mediate association of SV40 with caveolae. Mol. Biol. Cell 8 (1997) 47-57
    • (1997) Mol. Biol. Cell , vol.8 , pp. 47-57
    • Stang, E.1    Kartenbeck, J.2    Parton, R.G.3
  • 109
    • 0029818007 scopus 로고    scopus 로고
    • Extracellular simian virus 40 induces an ERK/MAP kinase-independent signalling pathway that activates primary response genes and promotes virus entry
    • Dangoria N.S., Breau W.C., Anderson H.A., Cishek D.M., and Norkin L.C. Extracellular simian virus 40 induces an ERK/MAP kinase-independent signalling pathway that activates primary response genes and promotes virus entry. J. Gen. Virol. 77 (1996) 2173-2182
    • (1996) J. Gen. Virol. , vol.77 , pp. 2173-2182
    • Dangoria, N.S.1    Breau, W.C.2    Anderson, H.A.3    Cishek, D.M.4    Norkin, L.C.5
  • 110
    • 0037113074 scopus 로고    scopus 로고
    • Dual control of caveolar membrane traffic by microtubules and the actin cytoskeleton
    • Mundy D.I., Machleidt T., Ying Y.S., Anderson R.G., and Bloom G.S. Dual control of caveolar membrane traffic by microtubules and the actin cytoskeleton. J. Cell Sci. 115 (2002) 4327-4339
    • (2002) J. Cell Sci. , vol.115 , pp. 4327-4339
    • Mundy, D.I.1    Machleidt, T.2    Ying, Y.S.3    Anderson, R.G.4    Bloom, G.S.5
  • 111
    • 4544375506 scopus 로고    scopus 로고
    • Caveolin-stabilized membrane domains as multifunctional transport and sorting devices in endocytic membrane traffic
    • Pelkmans L., Burli T., Zerial M., and Helenius A. Caveolin-stabilized membrane domains as multifunctional transport and sorting devices in endocytic membrane traffic. Cell 118 (2004) 767-780
    • (2004) Cell , vol.118 , pp. 767-780
    • Pelkmans, L.1    Burli, T.2    Zerial, M.3    Helenius, A.4
  • 112
    • 0035817629 scopus 로고    scopus 로고
    • Clathrin-dependent and -independent internalization of plasma membrane sphingolipids initiates two Golgi targeting pathways
    • (Electronic publication 2001 Jul 2030)
    • Puri V., Watanabe R., Singh R.D., Dominguez M., Brown J.C., Wheatley C.L., Marks D.L., and Pagano R.E. Clathrin-dependent and -independent internalization of plasma membrane sphingolipids initiates two Golgi targeting pathways. J. Cell Biol. 154 (2001) 535-547 (Electronic publication 2001 Jul 2030)
    • (2001) J. Cell Biol. , vol.154 , pp. 535-547
    • Puri, V.1    Watanabe, R.2    Singh, R.D.3    Dominguez, M.4    Brown, J.C.5    Wheatley, C.L.6    Marks, D.L.7    Pagano, R.E.8
  • 113
    • 0036094927 scopus 로고    scopus 로고
    • A distinct class of endosome mediates clathrin-independent endocytosis to the Golgi complex
    • Nichols B.J. A distinct class of endosome mediates clathrin-independent endocytosis to the Golgi complex. Nat. Cell Biol. 4 (2002) 374-378
    • (2002) Nat. Cell Biol. , vol.4 , pp. 374-378
    • Nichols, B.J.1
  • 114
    • 0037598870 scopus 로고    scopus 로고
    • Distinct endocytic pathways regulate TGF-beta receptor signalling and turnover
    • Di Guglielmo G.M., Le Roy C., Goodfellow A.F., and Wrana J.L. Distinct endocytic pathways regulate TGF-beta receptor signalling and turnover. Nat. Cell Biol. 5 (2003) 410-421
    • (2003) Nat. Cell Biol. , vol.5 , pp. 410-421
    • Di Guglielmo, G.M.1    Le Roy, C.2    Goodfellow, A.F.3    Wrana, J.L.4
  • 115
    • 0037684840 scopus 로고    scopus 로고
    • Caveolae/raft-dependent endocytosis
    • Nabi I.R., and Le P.U. Caveolae/raft-dependent endocytosis. J. Cell Biol. 161 (2003) 673-677
    • (2003) J. Cell Biol. , vol.161 , pp. 673-677
    • Nabi, I.R.1    Le, P.U.2
  • 116
    • 0036000023 scopus 로고    scopus 로고
    • Inhibitors of COP-mediated transport and cholera toxin action inhibit simian virus 40 infection
    • Richards A.A., Stang E., Pepperkok R., and Parton R.G. Inhibitors of COP-mediated transport and cholera toxin action inhibit simian virus 40 infection. Mol. Biol Cell. 13 (2002) 1750-1764
    • (2002) Mol. Biol Cell. , vol.13 , pp. 1750-1764
    • Richards, A.A.1    Stang, E.2    Pepperkok, R.3    Parton, R.G.4
  • 117
    • 0031785929 scopus 로고    scopus 로고
    • How do animal DNA viruses get to the nucleus?
    • Kasamatsu H., and Nakanishi A. How do animal DNA viruses get to the nucleus?. Annu. Rev. Microbiol. 52 (1998) 627-686
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 627-686
    • Kasamatsu, H.1    Nakanishi, A.2
  • 118
    • 0032498628 scopus 로고    scopus 로고
    • Caveolin transfection results in caveolae formation but not apical sorting of glycosylphosphatidylinositol (GPI)-anchored proteins in epithelial cells
    • Lipardi C., Mora R., Colomer V., Paladino S., Nitsch L., Rodriguez-Boulan E., and Zurzolo C. Caveolin transfection results in caveolae formation but not apical sorting of glycosylphosphatidylinositol (GPI)-anchored proteins in epithelial cells. J. Cell Biol. 140 (1998) 617-626
    • (1998) J. Cell Biol. , vol.140 , pp. 617-626
    • Lipardi, C.1    Mora, R.2    Colomer, V.3    Paladino, S.4    Nitsch, L.5    Rodriguez-Boulan, E.6    Zurzolo, C.7
  • 119
    • 0034605039 scopus 로고    scopus 로고
    • Endothelial cell-surface gp60 activates vesicle formation and trafficking via G(i)-coupled Src kinase signaling pathway
    • Minshall R.D., Tiruppathi C., Vogel S.M., Niles W.D., Gilchrist A., Hamm H.E., and Malik A.B. Endothelial cell-surface gp60 activates vesicle formation and trafficking via G(i)-coupled Src kinase signaling pathway. J. Cell Biol. 150 (2000) 1057-1070
    • (2000) J. Cell Biol. , vol.150 , pp. 1057-1070
    • Minshall, R.D.1    Tiruppathi, C.2    Vogel, S.M.3    Niles, W.D.4    Gilchrist, A.5    Hamm, H.E.6    Malik, A.B.7
  • 120
    • 0036151510 scopus 로고    scopus 로고
    • Caveolae are highly immobile plasma membrane microdomains, which are not involved in constitutive endocytic trafficking
    • Thomsen P., Roepstorff K., Stahlhut M., and van Deurs B. Caveolae are highly immobile plasma membrane microdomains, which are not involved in constitutive endocytic trafficking. Mol Biol. Cell 13 (2002) 238-250
    • (2002) Mol Biol. Cell , vol.13 , pp. 238-250
    • Thomsen, P.1    Roepstorff, K.2    Stahlhut, M.3    van Deurs, B.4
  • 123
    • 13644257020 scopus 로고    scopus 로고
    • Insights into the mechanism of magnetofection using PEI-based magnetofectins for gene transfer
    • Huth S., Lausier J., Gersting S.W., Rudolph C., Plank C., Welsch U., and Rosenecker J. Insights into the mechanism of magnetofection using PEI-based magnetofectins for gene transfer. J.Gene Med. 6 (2004) 923-936
    • (2004) J.Gene Med. , vol.6 , pp. 923-936
    • Huth, S.1    Lausier, J.2    Gersting, S.W.3    Rudolph, C.4    Plank, C.5    Welsch, U.6    Rosenecker, J.7
  • 124
    • 1642575957 scopus 로고    scopus 로고
    • Size-dependent internalization of particles via the pathways of clathrin- and caveolae-mediated endocytosis
    • Rejman J., Oberle V., Zuhorn I.S., and Hoekstra D. Size-dependent internalization of particles via the pathways of clathrin- and caveolae-mediated endocytosis. Biochem. J. 377 (2004) 159-169
    • (2004) Biochem. J. , vol.377 , pp. 159-169
    • Rejman, J.1    Oberle, V.2    Zuhorn, I.S.3    Hoekstra, D.4
  • 126
    • 4344697827 scopus 로고    scopus 로고
    • Macropinocytosis of polyplexes and recycling of plasmid via the clathrin-dependent pathway impair the transfection efficiency of human hepatocarcinoma cells
    • Goncalves C., Mennesson E., Fuchs R., Gorvel J.P., Midoux P., and Pichon C. Macropinocytosis of polyplexes and recycling of plasmid via the clathrin-dependent pathway impair the transfection efficiency of human hepatocarcinoma cells. Mol. Ther. 10 (2004) 373-385
    • (2004) Mol. Ther. , vol.10 , pp. 373-385
    • Goncalves, C.1    Mennesson, E.2    Fuchs, R.3    Gorvel, J.P.4    Midoux, P.5    Pichon, C.6
  • 127
    • 0030825703 scopus 로고    scopus 로고
    • When intracellular pathogens invade the frontiers of cell biology and immunology
    • Pizarro-Cerda J., Moreno E., Desjardins M., and Gorvel J.P. When intracellular pathogens invade the frontiers of cell biology and immunology. Histol. Histopathol. 12 (1997) 1027-1038
    • (1997) Histol. Histopathol. , vol.12 , pp. 1027-1038
    • Pizarro-Cerda, J.1    Moreno, E.2    Desjardins, M.3    Gorvel, J.P.4
  • 129
    • 0041920932 scopus 로고    scopus 로고
    • Brucella evades macrophage killing via VirB-dependent sustained interactions with the endoplasmic reticulum
    • Celli J., de Chastellier C., Franchini D.M., Pizarro-Cerda J., Moreno E., and Gorvel J.P. Brucella evades macrophage killing via VirB-dependent sustained interactions with the endoplasmic reticulum. J. Exp. Med. 198 (2003) 545-556
    • (2003) J. Exp. Med. , vol.198 , pp. 545-556
    • Celli, J.1    de Chastellier, C.2    Franchini, D.M.3    Pizarro-Cerda, J.4    Moreno, E.5    Gorvel, J.P.6
  • 130
    • 0037146657 scopus 로고    scopus 로고
    • Brucella intracellular life: from invasion to intracellular replication
    • Gorvel J.P., and Moreno E. Brucella intracellular life: from invasion to intracellular replication. Vet. Microbiol. 90 (2002) 281-297
    • (2002) Vet. Microbiol. , vol.90 , pp. 281-297
    • Gorvel, J.P.1    Moreno, E.2
  • 131
    • 0033224556 scopus 로고    scopus 로고
    • Characterization and intracellular trafficking pattern of vacuoles containing Chlamydia pneumoniae in human epithelial cells
    • Al-Younes H.M., Rudel T., and Meyer T.F. Characterization and intracellular trafficking pattern of vacuoles containing Chlamydia pneumoniae in human epithelial cells. Cell Microbiol. 1 (1999) 237-247
    • (1999) Cell Microbiol. , vol.1 , pp. 237-247
    • Al-Younes, H.M.1    Rudel, T.2    Meyer, T.F.3
  • 134
    • 0036175876 scopus 로고    scopus 로고
    • Role of cholesterol and the ganglioside GM(1) in entry and short-term survival of Brucella suis in murine macrophages
    • Naroeni A., and Porte F. Role of cholesterol and the ganglioside GM(1) in entry and short-term survival of Brucella suis in murine macrophages. Infect. Immun. 70 (2002) 1640-1644
    • (2002) Infect. Immun. , vol.70 , pp. 1640-1644
    • Naroeni, A.1    Porte, F.2
  • 136
    • 0031899678 scopus 로고    scopus 로고
    • Virulent Brucella abortus prevents lysosome fusion and is distributed within autophagosome-like compartments
    • Pizarro-Cerda J., Moreno E., Sanguedolce V., Mege J.L., and Gorvel J.P. Virulent Brucella abortus prevents lysosome fusion and is distributed within autophagosome-like compartments. Infect. Immun. 66 (1998) 2387-2392
    • (1998) Infect. Immun. , vol.66 , pp. 2387-2392
    • Pizarro-Cerda, J.1    Moreno, E.2    Sanguedolce, V.3    Mege, J.L.4    Gorvel, J.P.5
  • 137
    • 1242329005 scopus 로고    scopus 로고
    • Organelle robbery: Brucella interactions with the endoplasmic reticulum
    • Celli J., and Gorvel J.P. Organelle robbery: Brucella interactions with the endoplasmic reticulum. Curr. Opin. Microbiol. 7 (2004) 93-97
    • (2004) Curr. Opin. Microbiol. , vol.7 , pp. 93-97
    • Celli, J.1    Gorvel, J.P.2
  • 138
    • 0032783141 scopus 로고    scopus 로고
    • Early acidification of phagosomes containing Brucella suis is essential for intracellular survival in murine macrophages
    • Porte F., Liautard J.P., and Kohler S. Early acidification of phagosomes containing Brucella suis is essential for intracellular survival in murine macrophages. Infect. Immun. 67 (1999) 4041-4047
    • (1999) Infect. Immun. , vol.67 , pp. 4041-4047
    • Porte, F.1    Liautard, J.P.2    Kohler, S.3
  • 139
    • 0036903907 scopus 로고    scopus 로고
    • Legionella phagosomes intercept vesicular traffic from endoplasmic reticulum exit sites
    • Kagan J.C., and Roy C.R. Legionella phagosomes intercept vesicular traffic from endoplasmic reticulum exit sites. Nat. Cell Biol. 4 (2002) 945-954
    • (2002) Nat. Cell Biol. , vol.4 , pp. 945-954
    • Kagan, J.C.1    Roy, C.R.2
  • 141
    • 0032868454 scopus 로고    scopus 로고
    • A homologue of the Agrobacterium tumefaciens VirB and Bordetella pertussis Ptl type IV secretion systems is essential for intracellular survival of Brucella suis
    • O'Callaghan D., Cazevieille C., Allardet-Servent A., Boschiroli M.L., Bourg G., Foulongne V., Frutos P., Kulakov Y., and Ramuz M. A homologue of the Agrobacterium tumefaciens VirB and Bordetella pertussis Ptl type IV secretion systems is essential for intracellular survival of Brucella suis. Mol. Microbiol. 33 (1999) 1210-1220
    • (1999) Mol. Microbiol. , vol.33 , pp. 1210-1220
    • O'Callaghan, D.1    Cazevieille, C.2    Allardet-Servent, A.3    Boschiroli, M.L.4    Bourg, G.5    Foulongne, V.6    Frutos, P.7    Kulakov, Y.8    Ramuz, M.9
  • 142
    • 0034985282 scopus 로고    scopus 로고
    • Intracellular survival of Brucella spp. in human monocytes involves conventional uptake but special phagosomes
    • Rittig M.G., Alvarez-Martinez M.T., Porte F., Liautard J.P., and Rouot B. Intracellular survival of Brucella spp. in human monocytes involves conventional uptake but special phagosomes. Infect. Immun. 69 (2001) 3995-4006
    • (2001) Infect. Immun. , vol.69 , pp. 3995-4006
    • Rittig, M.G.1    Alvarez-Martinez, M.T.2    Porte, F.3    Liautard, J.P.4    Rouot, B.5
  • 143
    • 0038528218 scopus 로고    scopus 로고
    • Subversion and utilization of the host cell cyclic adenosine 5′-monophosphate/protein kinase A pathway by Brucella during macrophage infection
    • Gross A., Bouaboula M., Casellas P., Liautard J.P., and Dornand J. Subversion and utilization of the host cell cyclic adenosine 5′-monophosphate/protein kinase A pathway by Brucella during macrophage infection. J. Immunol. 170 (2003) 5607-5614
    • (2003) J. Immunol. , vol.170 , pp. 5607-5614
    • Gross, A.1    Bouaboula, M.2    Casellas, P.3    Liautard, J.P.4    Dornand, J.5
  • 145
    • 14144253164 scopus 로고    scopus 로고
    • Gene therapy put on hold as third child develops cancer
    • Check E. Gene therapy put on hold as third child develops cancer. Nature 433 (2005) 561
    • (2005) Nature , vol.433 , pp. 561
    • Check, E.1
  • 148
    • 0030280036 scopus 로고    scopus 로고
    • The potential of extrachromosomal replicating vectors for gene therapy
    • Calos M.P. The potential of extrachromosomal replicating vectors for gene therapy. Trends Genet. 12 (1996) 463-466
    • (1996) Trends Genet. , vol.12 , pp. 463-466
    • Calos, M.P.1
  • 149
    • 33645243935 scopus 로고    scopus 로고
    • Use of bacteria in anti-cancer therapies
    • Ryan R.M., Green J., and Lewis C.E. Use of bacteria in anti-cancer therapies. Bioessays 28 (2006) 84-94
    • (2006) Bioessays , vol.28 , pp. 84-94
    • Ryan, R.M.1    Green, J.2    Lewis, C.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.