메뉴 건너뛰기




Volumn 288, Issue 11, 2013, Pages 7492-7505

Cellular interactions of the cytolethal distending toxins from Escherichia coli and Haemophilus ducreyi

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; CELLULAR INTERACTION; COMPETITIVE BINDING; ENDOPLASMIC RETICULUM; ENDOSOMAL COMPARTMENTS; EUKARYOTIC CELL CYCLE; NUCLEAR LOCALIZATION; PATHOGENIC BACTERIUM;

EID: 84875187695     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.448118     Document Type: Article
Times cited : (30)

References (68)
  • 1
    • 13644262252 scopus 로고    scopus 로고
    • Cytolethal distending toxin: A bacterial bullet targeted to nucleus
    • Ohara, M., Oswald, E., and Sugai, M. (2004) Cytolethal distending toxin: a bacterial bullet targeted to nucleus. J. Biochem. 136, 409-413
    • (2004) J. Biochem. , vol.136 , pp. 409-413
    • Ohara, M.1    Oswald, E.2    Sugai, M.3
  • 2
    • 30944456901 scopus 로고    scopus 로고
    • Cytolethal distending toxin generates cell death by inducing a bottleneck in the cell cycle
    • Ceelen, L. M., Decostere, A., Ducatelle, R., and Haesebrouck, F. (2006) Cytolethal distending toxin generates cell death by inducing a bottleneck in the cell cycle. Microbiol. Res. 161, 109-120
    • (2006) Microbiol. Res. , vol.161 , pp. 109-120
    • Ceelen, L.M.1    Decostere, A.2    Ducatelle, R.3    Haesebrouck, F.4
  • 3
    • 14644392194 scopus 로고    scopus 로고
    • Cyclomodulins: Bacterial effectors that modulate the eukaryotic cell cycle
    • Nougayrède, J. P., Taieb, F., De Rycke, J., and Oswald, E. (2005) Cyclomodulins: bacterial effectors that modulate the eukaryotic cell cycle. Trends Microbiol. 13, 103-110
    • (2005) Trends Microbiol , vol.13 , pp. 103-110
    • Nougayrède, J.P.1    Taieb, F.2    De Rycke, J.3    Oswald, E.4
  • 5
    • 84879475695 scopus 로고    scopus 로고
    • Bacterial toxin modulation of the eukaryotic cell cycle: Are all cytolethal distending toxins created equally?
    • Gargi, A., Reno, M., and Blanke, S. R. (2012) Bacterial toxin modulation of the eukaryotic cell cycle: are all cytolethal distending toxins created equally? Front. Cell. Infect. Microbiol. 2, 124
    • (2012) Front. Cell. Infect. Microbiol. , vol.2 , pp. 124
    • Gargi, A.1    Reno, M.2    Blanke, S.R.3
  • 6
    • 47549092184 scopus 로고    scopus 로고
    • In vivo virulence properties of bacterial cytolethal-distending toxin
    • Ge, Z., Schauer, D. B., and Fox, J. G. (2008) In vivo virulence properties of bacterial cytolethal-distending toxin. Cell. Microbiol. 10, 1599-1607
    • (2008) Cell. Microbiol. , vol.10 , pp. 1599-1607
    • Ge, Z.1    Schauer, D.B.2    Fox, J.G.3
  • 7
    • 33845222309 scopus 로고    scopus 로고
    • The contribution of cytolethal distending toxin to bacterial pathogenesis
    • Smith, J. L., and Bayles, D. O. (2006) The contribution of cytolethal distending toxin to bacterial pathogenesis. Crit. Rev. Microbiol. 32, 227-248
    • (2006) Crit. Rev. Microbiol. , vol.32 , pp. 227-248
    • Smith, J.L.1    Bayles, D.O.2
  • 9
    • 33845478725 scopus 로고    scopus 로고
    • Portals and pathways: Principles of bacterial toxin entry into host cells
    • Blanke, S. R. (2006) Portals and pathways: principles of bacterial toxin entry into host cells. Microbe 1, 26-32
    • (2006) Microbe , vol.1 , pp. 26-32
    • Blanke, S.R.1
  • 10
    • 0033854239 scopus 로고    scopus 로고
    • DNase i homologous residues in CdtB are critical for cytolethal distending toxin-mediated cell cycle arrest
    • Elwell, C. A., and Dreyfus, L. A. (2000) DNase I homologous residues in CdtB are critical for cytolethal distending toxin-mediated cell cycle arrest. Mol. Microbiol. 37, 952-963
    • (2000) Mol. Microbiol. , vol.37 , pp. 952-963
    • Elwell, C.A.1    Dreyfus, L.A.2
  • 11
    • 0034644631 scopus 로고    scopus 로고
    • A bacterial toxin that controls cell cycle progression as a deoxyribonuclease I-like protein
    • Lara-Tejero, M., and Galán, J. E. (2000) A bacterial toxin that controls cell cycle progression as a deoxyribonuclease I-like protein. Science 290, 354-357
    • (2000) Science , vol.290 , pp. 354-357
    • Lara-Tejero, M.1    Galán, J.E.2
  • 12
    • 1842840103 scopus 로고    scopus 로고
    • Nuclear localization of the Escherichia coli cytolethal distending toxin CdtB subunit
    • McSweeney, L. A., and Dreyfus, L. A. (2004) Nuclear localization of the Escherichia coli cytolethal distending toxin CdtB subunit. Cell. Microbiol. 6, 447-458
    • (2004) Cell. Microbiol. , vol.6 , pp. 447-458
    • McSweeney, L.A.1    Dreyfus, L.A.2
  • 13
    • 0346118865 scopus 로고    scopus 로고
    • An N-terminal segment of the active component of the bacterial genotoxin cytolethal distending toxin B (CDTB) directs CDTB into the nucleus
    • Nishikubo, S., Ohara, M., Ueno, Y., Ikura, M., Kurihara, H., Komatsuzawa, H., Oswald, E., and Sugai, M. (2003) An N-terminal segment of the active component of the bacterial genotoxin cytolethal distending toxin B (CDTB) directs CDTB into the nucleus. J. Biol. Chem. 278, 50671-50681
    • (2003) J. Biol. Chem. , vol.278 , pp. 50671-50681
    • Nishikubo, S.1    Ohara, M.2    Ueno, Y.3    Ikura, M.4    Kurihara, H.5    Komatsuzawa, H.6    Oswald, E.7    Sugai, M.8
  • 14
    • 75649099370 scopus 로고    scopus 로고
    • Toxic activity of the CdtB component of Haemophilus ducreyi cytolethal distending toxin expressed from an adenovirus 5 vector
    • Wising, C., Magnusson, M., Ahlman, K., Lindholm, L., and Lagergård, T. (2010) Toxic activity of the CdtB component of Haemophilus ducreyi cytolethal distending toxin expressed from an adenovirus 5 vector. APMIS 118, 143-149
    • (2010) APMIS , vol.118 , pp. 143-149
    • Wising, C.1    Magnusson, M.2    Ahlman, K.3    Lindholm, L.4    Lagergård, T.5
  • 15
    • 16244386487 scopus 로고    scopus 로고
    • Carbohydrate-binding specificity of the Escherichia coli cytolethal distending toxin CdtA-II and CdtC-II subunits
    • McSweeney, L. A., and Dreyfus, L. A. (2005) Carbohydrate-binding specificity of the Escherichia coli cytolethal distending toxin CdtA-II and CdtC-II subunits. Infect. Immun. 73, 2051-2060
    • (2005) Infect. Immun. , vol.73 , pp. 2051-2060
    • McSweeney, L.A.1    Dreyfus, L.A.2
  • 16
    • 46449100439 scopus 로고    scopus 로고
    • Role of aromatic amino acids in receptor binding activity and subunit assembly of the cytolethal distending toxin of Aggregatibacter actinomycetemcomitans
    • Cao, L., Bandelac, G., Volgina, A., Korostoff, J., and DiRienzo, J. M. (2008) Role of aromatic amino acids in receptor binding activity and subunit assembly of the cytolethal distending toxin of Aggregatibacter actinomycetemcomitans. Infect. Immun. 76, 2812-2821
    • (2008) Infect. Immun. , vol.76 , pp. 2812-2821
    • Cao, L.1    Bandelac, G.2    Volgina, A.3    Korostoff, J.4    Dirienzo, J.M.5
  • 17
    • 28244481086 scopus 로고    scopus 로고
    • Characterization of point mutations in the cdtA gene of the cytolethal distending toxin of Actinobacillus actinomycetemcomitans
    • Cao, L., Volgina, A., Huang, C. M., Korostoff, J., and DiRienzo, J. M. (2005) Characterization of point mutations in the cdtA gene of the cytolethal distending toxin of Actinobacillus actinomycetemcomitans. Mol. Microbiol. 58, 1303-1321
    • (2005) Mol. Microbiol. , vol.58 , pp. 1303-1321
    • Cao, L.1    Volgina, A.2    Huang, C.M.3    Korostoff, J.4    Dirienzo, J.M.5
  • 18
    • 77951036332 scopus 로고    scopus 로고
    • Mechanisms of assembly and cellular interactions for the bacterial genotoxin CDT
    • Nesic, D., and Stebbins, C. E. (2005) Mechanisms of assembly and cellular interactions for the bacterial genotoxin CDT. PLoS Pathog. 1, e28
    • (2005) PLoS Pathog. , vol.1
    • Nesic, D.1    Stebbins, C.E.2
  • 19
    • 0033167976 scopus 로고    scopus 로고
    • The cytolethal distending toxin family
    • Pickett, C. L., and Whitehouse, C. A. (1999) The cytolethal distending toxin family. Trends Microbiol. 7, 292-297
    • (1999) Trends Microbiol , vol.7 , pp. 292-297
    • Pickett, C.L.1    Whitehouse, C.A.2
  • 20
    • 30144440665 scopus 로고    scopus 로고
    • Comparative structure-function analysis of cytolethal distending toxins
    • Hu, X., Nesic, D., and Stebbins, C. E. (2006) Comparative structure-function analysis of cytolethal distending toxins. Proteins 62, 421-434
    • (2006) Proteins , vol.62 , pp. 421-434
    • Hu, X.1    Nesic, D.2    Stebbins, C.E.3
  • 21
    • 77953299606 scopus 로고    scopus 로고
    • Cytolethal distending toxin family members are differentially affected by alterations in host glycans and membrane cholesterol
    • Eshraghi, A., Maldonado-Arocho, F. J., Gargi, A., Cardwell, M. M., Prouty, M. G., Blanke, S. R., and Bradley, K. A. (2010) Cytolethal distending toxin family members are differentially affected by alterations in host glycans and membrane cholesterol. J. Biol. Chem. 285, 18199-18207
    • (2010) J. Biol. Chem. , vol.285 , pp. 18199-18207
    • Eshraghi, A.1    Maldonado-Arocho, F.J.2    Gargi, A.3    Cardwell, M.M.4    Prouty, M.G.5    Blanke, S.R.6    Bradley, K.A.7
  • 22
    • 2642550772 scopus 로고    scopus 로고
    • Ssembly and function of a bacterial genotoxin
    • Nesić, D., Hsu, Y., and Stebbins, C. E. (2004) Assembly and function of a bacterial genotoxin. Nature 429, 429-433
    • (2004) Nature , vol.429 , pp. 429-433
    • Nesić, D.1    Hsu, Y.2    Stebbins, C.E.3
  • 23
    • 0041322857 scopus 로고    scopus 로고
    • Interactions of Campylobacter jejuni cytolethal distending toxin subunits CdtA and CdtC with HeLa cells
    • Lee, R. B., Hassane, D. C., Cottle, D. L., and Pickett, C. L. (2003) Interactions of Campylobacter jejuni cytolethal distending toxin subunits CdtA and CdtC with HeLa cells. Infect. Immun. 71, 4883-4890
    • (2003) Infect. Immun. , vol.71 , pp. 4883-4890
    • Lee, R.B.1    Hassane, D.C.2    Cottle, D.L.3    Pickett, C.L.4
  • 24
    • 0001661419 scopus 로고
    • Analysis of extreme values
    • Dixon, W. (1950) Analysis of extreme values. Ann. Math. Stat. 21, 488-506
    • (1950) Ann. Math. Stat. , vol.21 , pp. 488-506
    • Dixon, W.1
  • 25
    • 0032893106 scopus 로고    scopus 로고
    • The cytolethal distending toxin from the chancroid bacterium Haemophilus ducreyi induces cell-cycle arrest in the G2 phase
    • Cortes-Bratti, X., Chaves-Olarte, E., Lagergård, T., and Thelestam, M. (1999) The cytolethal distending toxin from the chancroid bacterium Haemophilus ducreyi induces cell-cycle arrest in the G2 phase. J. Clin. Invest. 103, 107-115
    • (1999) J. Clin. Invest. , vol.103 , pp. 107-115
    • Cortes-Bratti, X.1    Chaves-Olarte, E.2    Lagergård, T.3    Thelestam, M.4
  • 26
    • 0032722556 scopus 로고    scopus 로고
    • Cytolethal distending toxin of Haemophilus ducreyi induces apoptotic death of JurkatTcells
    • Gelfanova, V., Hansen, E. J., and Spinola, S. M. (1999) Cytolethal distending toxin of Haemophilus ducreyi induces apoptotic death of JurkatTcells. Infect. Immun. 67, 6394-6402
    • (1999) Infect. Immun. , vol.67 , pp. 6394-6402
    • Gelfanova, V.1    Hansen, E.J.2    Spinola, S.M.3
  • 27
    • 0141725786 scopus 로고    scopus 로고
    • The Haemophilus ducreyi cytolethal distending toxin induces DNA double-strand breaks and promotes ATM-dependent activation of RhoA
    • Frisan, T., Cortes-Bratti, X., Chaves-Olarte, E., Stenerlöw, B., and Thelestam, M. (2003) The Haemophilus ducreyi cytolethal distending toxin induces DNA double-strand breaks and promotes ATM-dependent activation of RhoA. Cell. Microbiol. 5, 695-707
    • (2003) Cell. Microbiol. , vol.5 , pp. 695-707
    • Frisan, T.1    Cortes-Bratti, X.2    Chaves-Olarte, E.3    Stenerlöw, B.4    Thelestam, M.5
  • 28
    • 0023889126 scopus 로고
    • A new heat-labile cytolethal distending toxin (CLDT) produced by Campylobacter SPP
    • Johnson, W. M., and Lior, H. (1988) A new heat-labile cytolethal distending toxin (CLDT) produced by Campylobacter spp. Microb. Pathog. 4, 115-126
    • (1988) Microb. Pathog. , vol.4 , pp. 115-126
    • Johnson, W.M.1    Lior, H.2
  • 29
    • 0023891492 scopus 로고
    • A new heat-labile cytolethal distending toxin (CLDT) produced by Escherichia coli isolates from clinical material
    • Johnson, W. M., and Lior, H. (1988) A new heat-labile cytolethal distending toxin (CLDT) produced by Escherichia coli isolates from clinical material. Microb. Pathog. 4, 103-113
    • (1988) Microb. Pathog. , vol.4 , pp. 103-113
    • Johnson, W.M.1    Lior, H.2
  • 31
    • 0031715028 scopus 로고    scopus 로고
    • The cell cyclespecific growth-inhibitory factor produced by Actinobacillus actinomycetemcomitans is a cytolethal distending toxin
    • Sugai, M., Kawamoto, T., Pérès, S. Y., Ueno, Y., Komatsuzawa, H., Fujiwara, T., Kurihara, H., Suginaka, H., and Oswald, E. (1998) The cell cyclespecific growth-inhibitory factor produced by Actinobacillus actinomycetemcomitans is a cytolethal distending toxin. Infect. Immun. 66, 5008-5019
    • (1998) Infect. Immun. , vol.66 , pp. 5008-5019
    • Sugai, M.1    Kawamoto, T.2    Pérès, S.Y.3    Ueno, Y.4    Komatsuzawa, H.5    Fujiwara, T.6    Kurihara, H.7    Suginaka, H.8    Oswald, E.9
  • 32
    • 0030964567 scopus 로고    scopus 로고
    • Effect of cytolethal distending toxin on F-actin assembly and cell division in Chinese hamster ovary cells
    • Aragon, V., Chao, K., and Dreyfus, L. A. (1997) Effect of cytolethal distending toxin on F-actin assembly and cell division in Chinese hamster ovary cells. Infect. Immun. 65, 3774-3780
    • (1997) Infect. Immun. , vol.65 , pp. 3774-3780
    • Aragon, V.1    Chao, K.2    Dreyfus, L.A.3
  • 33
    • 0027445226 scopus 로고
    • Evidence for the presence of a receptor for the cytolethal distending toxin (CLDT) of Campylobacter jejuni on CHO and HeLa cell membranes and development of a receptor-based enzyme-linked immunosorbent assay for detection of CLDT
    • Bag, P. K., Ramamurthy, T., and Nair, U. B. (1993) Evidence for the presence of a receptor for the cytolethal distending toxin (CLDT) of Campylobacter jejuni on CHO and HeLa cell membranes and development of a receptor-based enzyme-linked immunosorbent assay for detection of CLDT. FEMS Microbiol. Lett. 114, 285-291
    • (1993) FEMS Microbiol. Lett. , vol.114 , pp. 285-291
    • Bag, P.K.1    Ramamurthy, T.2    Nair, U.B.3
  • 34
    • 0024987434 scopus 로고
    • Cytolethal distending toxin (CLDT) production by enteropathogenic Escherichia coli (EPEC
    • Bouzari, S., and Varghese, A. (1990) Cytolethal distending toxin (CLDT) production by enteropathogenic Escherichia coli (EPEC). FEMS Microbiol. Lett. 59, 193-198
    • (1990) FEMS Microbiol. Lett. , vol.59 , pp. 193-198
    • Bouzari, S.1    Varghese, A.2
  • 35
    • 0033009746 scopus 로고    scopus 로고
    • Identification of a cytolethal distending toxin gene locus and features of a virulence-associated region in Actinobacillus actinomycetemcomitans
    • Mayer, M. P., Bueno, L. C., Hansen, E. J., and DiRienzo, J. M. (1999) Identification of a cytolethal distending toxin gene locus and features of a virulence-associated region in Actinobacillus actinomycetemcomitans. Infect. Immun. 67, 1227-1237
    • (1999) Infect. Immun. , vol.67 , pp. 1227-1237
    • Mayer, M.P.1    Bueno, L.C.2    Hansen, E.J.3    Dirienzo, J.M.4
  • 36
    • 0029008918 scopus 로고
    • Distribution of the cytolethal distending toxin A gene (cdtA) among species of Shigella and Vibrio, and cloning and sequencing of the cdt gene from Shigella dysenteriae
    • Okuda, J., Kurazono, H., and Takeda, Y. (1995) Distribution of the cytolethal distending toxin A gene (cdtA) among species of Shigella and Vibrio, and cloning and sequencing of the cdt gene from Shigella dysenteriae. Microb. Pathog. 18, 167-172
    • (1995) Microb. Pathog. , vol.18 , pp. 167-172
    • Okuda, J.1    Kurazono, H.2    Takeda, Y.3
  • 37
    • 33748084389 scopus 로고    scopus 로고
    • Role of intrachain disulfides in the activities of the CdtA and CdtC subunits of the cytolethal distending toxin of Actinobacillus actinomycetemcomitans
    • Cao, L., Volgina, A., Korostoff, J., and DiRienzo, J. M. (2006) Role of intrachain disulfides in the activities of the CdtA and CdtC subunits of the cytolethal distending toxin of Actinobacillus actinomycetemcomitans. Infect. Immun. 74, 4990-5002
    • (2006) Infect. Immun. , vol.74 , pp. 4990-5002
    • Cao, L.1    Volgina, A.2    Korostoff, J.3    Dirienzo, J.M.4
  • 38
    • 0036123023 scopus 로고    scopus 로고
    • The Haemophilus ducreyi cytolethal distending toxin activates sensors of DNA damage and repair complexes in proliferating and nonproliferating cells
    • Li, L., Sharipo, A., Chaves-Olarte, E., Masucci, M. G., Levitsky, V., Thelestam, M., and Frisan, T. (2002) The Haemophilus ducreyi cytolethal distending toxin activates sensors of DNA damage and repair complexes in proliferating and nonproliferating cells. Cell. Microbiol. 4, 87-99
    • (2002) Cell. Microbiol. , vol.4 , pp. 87-99
    • Li, L.1    Sharipo, A.2    Chaves-Olarte, E.3    Masucci, M.G.4    Levitsky, V.5    Thelestam, M.6    Frisan, T.7
  • 39
    • 0037219984 scopus 로고    scopus 로고
    • Campylobacter jejuni cytolethal distending toxin promotes DNA repair responses in normal human cells
    • Hassane, D. C., Lee, R. B., and Pickett, C. L. (2003) Campylobacter jejuni cytolethal distending toxin promotes DNA repair responses in normal human cells. Infect. Immun. 71, 541-545
    • (2003) Infect. Immun. , vol.71 , pp. 541-545
    • Hassane, D.C.1    Lee, R.B.2    Pickett, C.L.3
  • 40
    • 0034953016 scopus 로고    scopus 로고
    • The role of different protein components from the Haemophilus ducreyi cytolethal distending toxin in the generation of cell toxicity
    • Frisk, A., Lebens, M., Johansson, C., Ahmed, H., Svensson, L., Ahlman, K., and Lagergård, T. (2001) The role of different protein components from the Haemophilus ducreyi cytolethal distending toxin in the generation of cell toxicity. Microb. Pathog. 30, 313-324
    • (2001) Microb. Pathog. , vol.30 , pp. 313-324
    • Frisk, A.1    Lebens, M.2    Johansson, C.3    Ahmed, H.4    Svensson, L.5    Ahlman, K.6    Lagergård, T.7
  • 41
    • 0035058434 scopus 로고    scopus 로고
    • Escherichia coli CdtB mediates cytolethal distending toxin cell cycle arrest
    • Elwell, C., Chao, K., Patel, K., and Dreyfus, L. (2001) Escherichia coli CdtB mediates cytolethal distending toxin cell cycle arrest. Infect. Immun. 69, 3418-3422
    • (2001) Infect. Immun. , vol.69 , pp. 3418-3422
    • Elwell, C.1    Chao, K.2    Patel, K.3    Dreyfus, L.4
  • 42
    • 0034441256 scopus 로고    scopus 로고
    • Cellular internalization of cytolethal distending toxin from Haemophilus ducreyi
    • Cortes-Bratti, X., Chaves-Olarte, E., Lagergård, T., and Thelestam, M. (2000) Cellular internalization of cytolethal distending toxin from Haemophilus ducreyi. Infect. Immun. 68, 6903-6911
    • (2000) Infect. Immun. , vol.68 , pp. 6903-6911
    • Cortes-Bratti, X.1    Chaves-Olarte, E.2    Lagergård, T.3    Thelestam, M.4
  • 44
    • 0022555867 scopus 로고
    • Acidification of the endo-cytic and exocytic pathways
    • Mellman, I., Fuchs, R., and Helenius, A. (1986) Acidification of the endo-cytic and exocytic pathways. Annu. Rev. Biochem. 55, 663-700
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 663-700
    • Mellman, I.1    Fuchs, R.2    Helenius, A.3
  • 45
    • 0011913143 scopus 로고
    • Bafilomycins: A class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells
    • Bowman, E. J., Siebers, A., and Altendorf, K. (1988) Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells. Proc. Natl. Acad. Sci. U.S.A. 85, 7972-7976
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 7972-7976
    • Bowman, E.J.1    Siebers, A.2    Altendorf, K.3
  • 46
    • 0025240867 scopus 로고
    • Alteration of intracellular traffic by monensin; Mechanism, specificity, and relationship to toxicity
    • Mollenhauer, H. H., Morré, D. J., and Rowe, L. D. (1990) Alteration of intracellular traffic by monensin; mechanism, specificity, and relationship to toxicity. Biochim. Biophys. Acta 1031, 225-246
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 225-246
    • Mollenhauer, H.H.1    Morré, D.J.2    Rowe, L.D.3
  • 47
    • 84864805951 scopus 로고    scopus 로고
    • Localization of Aggregatibacter actinomycetemcomitans cytolethal distending toxin subunits during intoxication of live cells
    • Damek-Poprawa, M., Jang, J. Y., Volgina, A., Korostoff, J., and DiRienzo, J. M. (2012) Localization of Aggregatibacter actinomycetemcomitans cytolethal distending toxin subunits during intoxication of live cells. Infect. Immun. 80, 2761-2770
    • (2012) Infect. Immun. , vol.80 , pp. 2761-2770
    • Damek-Poprawa, M.1    Jang, J.Y.2    Volgina, A.3    Korostoff, J.4    Dirienzo, J.M.5
  • 49
    • 22744447453 scopus 로고    scopus 로고
    • Rab7 associates with early endosomes to mediate sorting and transport of Semliki forest virus to late endosomes
    • Vonderheit, A., and Helenius, A. (2005) Rab7 associates with early endosomes to mediate sorting and transport of Semliki forest virus to late endosomes. PLoS Biol. 3, e233
    • (2005) PLoS Biol , vol.3
    • Vonderheit, A.1    Helenius, A.2
  • 50
    • 39549098329 scopus 로고    scopus 로고
    • Functional characterization of Rab7 mutant proteins associated with Charcot-Marie-Tooth type 2B disease
    • Spinosa, M. R., Progida, C., De Luca, A., Colucci, A. M., Alifano, P., and Bucci, C. (2008) Functional characterization of Rab7 mutant proteins associated with Charcot-Marie-Tooth type 2B disease. J. Neurosci. 28, 1640-1648
    • (2008) J. Neurosci. , vol.28 , pp. 1640-1648
    • Spinosa, M.R.1    Progida, C.2    De Luca, A.3    Colucci, A.M.4    Alifano, P.5    Bucci, C.6
  • 51
    • 9444223942 scopus 로고    scopus 로고
    • Rab9 GTPase regulates late endosome size and requires effector interaction for its stability
    • Ganley, I. G., Carroll, K., Bittova, L., and Pfeffer, S. (2004) Rab9 GTPase regulates late endosome size and requires effector interaction for its stability. Mol. Biol. Cell 15, 5420-5430
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5420-5430
    • Ganley, I.G.1    Carroll, K.2    Bittova, L.3    Pfeffer, S.4
  • 52
    • 23344447887 scopus 로고    scopus 로고
    • Involvement of ganglioside GM3 in G2/M cell cycle arrest of human monocytic cells induced by Actinobacillus actinomycetemcomitans cytolethal distending toxin
    • Mise, K., Akifusa, S., Watarai, S., Ansai, T., Nishihara, T., and Takehara, T. (2005) Involvement of ganglioside GM3 in G2/M cell cycle arrest of human monocytic cells induced by Actinobacillus actinomycetemcomitans cytolethal distending toxin. Infect. Immun. 73, 4846-4852
    • (2005) Infect. Immun. , vol.73 , pp. 4846-4852
    • Mise, K.1    Akifusa, S.2    Watarai, S.3    Ansai, T.4    Nishihara, T.5    Takehara, T.6
  • 53
    • 0031425955 scopus 로고    scopus 로고
    • Inhibition of endosome function inCHOcells bearing a temperature- sensitive defect in the coatomer (COPI) component ε-COP
    • Daro, E., Sheff, D., Gomez, M., Kreis, T., and Mellman, I. (1997) Inhibition of endosome function inCHOcells bearing a temperature-sensitive defect in the coatomer (COPI) component ε-COP. J. Cell Biol. 139, 1747-1759
    • (1997) J. Cell Biol. , vol.139 , pp. 1747-1759
    • Daro, E.1    Sheff, D.2    Gomez, M.3    Kreis, T.4    Mellman, I.5
  • 54
    • 20744450629 scopus 로고    scopus 로고
    • Delivery into cells. Lessons learned from plant and bacterial toxins
    • Sandvig, K., and van Deurs, B. (2005) Delivery into cells. Lessons learned from plant and bacterial toxins. Gene. Ther. 12, 865-872
    • (2005) Gene. Ther. , vol.12 , pp. 865-872
    • Sandvig, K.1    Van Deurs, B.2
  • 55
    • 12944322216 scopus 로고    scopus 로고
    • Anthrax toxin: The long and winding road that leads to the kill
    • Abrami, L., Reig, N., and van der Goot, F. G. (2005) Anthrax toxin: the long and winding road that leads to the kill. Trends Microbiol. 13, 72-78
    • (2005) Trends Microbiol. , vol.13 , pp. 72-78
    • Abrami, L.1    Reig, N.2    Van Der Goot, F.G.3
  • 56
    • 25444452398 scopus 로고    scopus 로고
    • Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins
    • Tweten, R. K. (2005) Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins. Infect. Immun. 73, 6199-6209
    • (2005) Infect. Immun. , vol.73 , pp. 6199-6209
    • Tweten, R.K.1
  • 57
    • 3542998744 scopus 로고    scopus 로고
    • Diverse and essential roles of mammalian vacuolar-type proton pump ATPase: Toward the physiological understanding of inside acidic compartments
    • Sun-Wada, G. H., Wada, Y., and Futai, M. (2004) Diverse and essential roles of mammalian vacuolar-type proton pump ATPase: toward the physiological understanding of inside acidic compartments. Biochim. Biophys. Acta 1658, 106-114
    • (2004) Biochim. Biophys. Acta , vol.1658 , pp. 106-114
    • Sun-Wada, G.H.1    Wada, Y.2    Futai, M.3
  • 58
    • 1342310842 scopus 로고    scopus 로고
    • Lysosome and lysosomerelated organelles responsible for specialized functions in higher organisms, with special emphasis on vacuolar-type proton ATPase
    • Sun-Wada, G. H., Wada, Y., and Futai, M. (2003) Lysosome and lysosomerelated organelles responsible for specialized functions in higher organisms, with special emphasis on vacuolar-type proton ATPase. Cell Struct. Funct. 28, 455-463
    • (2003) Cell Struct. Funct. , vol.28 , pp. 455-463
    • Sun-Wada, G.H.1    Wada, Y.2    Futai, M.3
  • 59
    • 0036481562 scopus 로고    scopus 로고
    • The vacuolar (H+)-ATPases-nature's most versatile proton pumps
    • Nishi, T., and Forgac, M. (2002) The vacuolar (H+)-ATPases-nature's most versatile proton pumps. Nat. Rev. Mol. Cell Biol. 3, 94-103
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 94-103
    • Nishi, T.1    Forgac, M.2
  • 60
    • 0028236333 scopus 로고
    • Bacterial protein toxins penetrate cells via a four-step mechanism
    • Montecucco, C., Papini, E., and Schiavo, G. (1994) Bacterial protein toxins penetrate cells via a four-step mechanism. FEBS Lett. 346, 92-98
    • (1994) FEBS Lett , vol.346 , pp. 92-98
    • Montecucco, C.1    Papini, E.2    Schiavo, G.3
  • 61
    • 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. (1993) Rab9 functions in transport between late endosomes and the trans Golgi network. EMBO J. 12, 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
  • 62
    • 0028224561 scopus 로고
    • Lysosome biogenesis requires Rab9 function and receptor recycling from endosomes to the trans-Golgi network
    • Riederer, M. A., Soldati, T., Shapiro, A. D., Lin, J., and Pfeffer, S. R. (1994) Lysosome biogenesis requires Rab9 function and receptor recycling from endosomes to the trans-Golgi network. J. Cell Biol. 125, 573-582
    • (1994) J. Cell Biol. , vol.125 , pp. 573-582
    • Riederer, M.A.1    Soldati, T.2    Shapiro, A.D.3    Lin, J.4    Pfeffer, S.R.5
  • 63
    • 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., and 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, 973-990
    • (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
  • 64
    • 0028787861 scopus 로고
    • Signal transduction by cholera toxin: Processing in vesicular compartments does not require acidification
    • Lencer, W. I., Strohmeier, G., Moe, S., Carlson, S. L., Constable, C. T., and Madara, J. L. (1995) Signal transduction by cholera toxin: processing in vesicular compartments does not require acidification. Am. J. Physiol. 269, G548-G557
    • (1995) Am. J. Physiol. , vol.269
    • Lencer, W.I.1    Strohmeier, G.2    Moe, S.3    Carlson, S.L.4    Constable, C.T.5    Madara, J.L.6
  • 65
    • 0027314536 scopus 로고
    • Brefeldin A blocks the response of cultured cells to cholera toxin. Implications for intracellular trafficking in toxin action
    • Orlandi, P. A., Curran, P. K., and Fishman, P. H. (1993) Brefeldin A blocks the response of cultured cells to cholera toxin. Implications for intracellular trafficking in toxin action. J. Biol. Chem. 268, 12010-12016
    • (1993) J. Biol. Chem. , vol.268 , pp. 12010-12016
    • Orlandi, P.A.1    Curran, P.K.2    Fishman, P.H.3
  • 66
    • 0029147513 scopus 로고
    • Ricin cytotoxicity is sensitive to recycling between the endoplasmic reticulum and the Golgi complex
    • Simpson, J. C., Dascher, C., Roberts, L. M., Lord, J. M., and Balch, W. E. (1995) Ricin cytotoxicity is sensitive to recycling between the endoplasmic reticulum and the Golgi complex. J. Biol. Chem. 270, 20078-20083
    • (1995) J. Biol. Chem. , vol.270 , pp. 20078-20083
    • Simpson, J.C.1    Dascher, C.2    Roberts, L.M.3    Lord, J.M.4    Balch, W.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.