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Volumn 12, Issue 2, 2010, Pages 233-247

Selective and specific internalization of clostridial C3 ADP-ribosyltransferases into macrophages and monocytes

Author keywords

[No Author keywords available]

Indexed keywords

BAFILOMYCIN A1; EXOENZYME C3; RHO FACTOR; MACROLIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE;

EID: 77649216057     PISSN: 14625814     EISSN: 14625822     Source Type: Journal    
DOI: 10.1111/j.1462-5822.2009.01393.x     Document Type: Article
Times cited : (50)

References (59)
  • 2
    • 0023656574 scopus 로고
    • ADP-ribosylation of a 21-24 kDa eukaryotic protein(s) by C3, a novel botulinum ADP-ribosyltransferase, is regulated by guanine nucleotide
    • Aktories K, Frevert J. ADP-ribosylation of a 21-24 kDa eukaryotic protein(s) by C3, a novel botulinum ADP-ribosyltransferase, is regulated by guanine nucleotide. Biochem J 1987, 247:363-368.
    • (1987) Biochem J , vol.247 , pp. 363-368
    • Aktories, K.1    Frevert, J.2
  • 3
    • 0024341897 scopus 로고
    • Botulinum ADP-ribosyltransferase C3: a new tool to study low molecular weight GTP-binding proteins
    • Aktories K, Hall A. Botulinum ADP-ribosyltransferase C3: a new tool to study low molecular weight GTP-binding proteins. Tips 1989, 10:415-418.
    • (1989) Tips , vol.10 , pp. 415-418
    • Aktories, K.1    Hall, A.2
  • 4
    • 0029100780 scopus 로고
    • Studies on the active site structure of C3-like exoenzymes: involvement of glutamic acid in catalysis of ADP-ribosylation
    • Aktories K, Jung M, Böhmer J, Fritz G, Vandekerckhove J, Just I. Studies on the active site structure of C3-like exoenzymes: involvement of glutamic acid in catalysis of ADP-ribosylation. Biochimie 1995, 77:326-332.
    • (1995) Biochimie , vol.77 , pp. 326-332
    • Aktories, K.1    Jung, M.2    Böhmer, J.3    Fritz, G.4    Vandekerckhove, J.5    Just, I.6
  • 6
    • 0036828872 scopus 로고    scopus 로고
    • PH-induced collapse of the extracellular loops closes Escherichia coli maltoporin and allows the study of asymmetric sugar binding
    • Andersen C, Schiffler B, Charbit A, Benz R. PH-induced collapse of the extracellular loops closes Escherichia coli maltoporin and allows the study of asymmetric sugar binding. J Biol Chem 2002, 277:41318-41325.
    • (2002) J Biol Chem , vol.277 , pp. 41318-41325
    • Andersen, C.1    Schiffler, B.2    Charbit, A.3    Benz, R.4
  • 7
    • 0027400947 scopus 로고
    • A chimeric toxin to study the role of the 21 kDa GTP binding protein rho in the control of actin microfilament assembly
    • Aullo P, Giry M, Olsnes S, Popoff MR, Kocks C, Boquet P. A chimeric toxin to study the role of the 21 kDa GTP binding protein rho in the control of actin microfilament assembly. EMBO J 1993, 12:921-931.
    • (1993) EMBO J , vol.12 , pp. 921-931
    • Aullo, P.1    Giry, M.2    Olsnes, S.3    Popoff, M.R.4    Kocks, C.5    Boquet, P.6
  • 8
    • 0032036388 scopus 로고    scopus 로고
    • The N-terminal part of the enzyme component (C2I) of the binary Clostridium botulinum C2 toxin interacts with the binding component C2II and functions as a carrier system for a Rho ADP-ribosylating C3-like fusion toxin
    • Barth H, Hofmann F, Olenik C, Just I, Aktories K. The N-terminal part of the enzyme component (C2I) of the binary Clostridium botulinum C2 toxin interacts with the binding component C2II and functions as a carrier system for a Rho ADP-ribosylating C3-like fusion toxin. Infect Immun 1998, 66:1364-1369.
    • (1998) Infect Immun , vol.66 , pp. 1364-1369
    • Barth, H.1    Hofmann, F.2    Olenik, C.3    Just, I.4    Aktories, K.5
  • 10
    • 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. Low pH-induced formation of ion channels by Clostridium difficile toxin B in target cells. J Biol Chem 2001, 276:10670-10676.
    • (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
  • 11
    • 0037085473 scopus 로고    scopus 로고
    • The binary Clostridium botulinum C2 toxin as a protein delivery system: identification of the minimal protein region necessary for interaction of toxin components
    • Barth H, Roebling R, Fritz M, Aktories K. The binary Clostridium botulinum C2 toxin as a protein delivery system: identification of the minimal protein region necessary for interaction of toxin components. J Biol Chem 2002, 277:5074-5081.
    • (2002) J Biol Chem , vol.277 , pp. 5074-5081
    • Barth, H.1    Roebling, R.2    Fritz, M.3    Aktories, K.4
  • 12
    • 4544264417 scopus 로고    scopus 로고
    • Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteins
    • table.
    • Barth H, Aktories K, Popoff MR, Stiles BG. Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteins. Microbiol Mol Biol Rev 2004, 68:373-402. table.
    • (2004) Microbiol Mol Biol Rev , vol.68 , pp. 373-402
    • Barth, H.1    Aktories, K.2    Popoff, M.R.3    Stiles, B.G.4
  • 13
    • 0018139740 scopus 로고
    • Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli
    • Benz R, Janko K, Boos W, Lauger P. Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli. Biochim Biophys Acta 1978, 511:305-319.
    • (1978) Biochim Biophys Acta , vol.511 , pp. 305-319
    • Benz, R.1    Janko, K.2    Boos, W.3    Lauger, P.4
  • 14
    • 0035063194 scopus 로고    scopus 로고
    • Cellular uptake of the binary Clostridium perfringens iota-toxin
    • Blöcker D, Behlke J, Aktories K, Barth H. Cellular uptake of the binary Clostridium perfringens iota-toxin. Infect Immun 2001, 69:2980-2987.
    • (2001) Infect Immun , vol.69 , pp. 2980-2987
    • Blöcker, D.1    Behlke, J.2    Aktories, K.3    Barth, H.4
  • 15
    • 0037881855 scopus 로고    scopus 로고
    • Channel foramtion by the binding component of Clostridium botulinum C2 toxin: glutamate 307 of C2II affects channel properties in vitro and pH-dependent C2I translocation in vivo
    • Blöcker D, Bachmeyer C, Benz R, Aktories K, Barth H. Channel foramtion by the binding component of Clostridium botulinum C2 toxin: glutamate 307 of C2II affects channel properties in vitro and pH-dependent C2I translocation in vivo. Biochemistry 2003, 42:5368-5377.
    • (2003) Biochemistry , vol.42 , pp. 5368-5377
    • Blöcker, D.1    Bachmeyer, C.2    Benz, R.3    Aktories, K.4    Barth, H.5
  • 16
    • 0032573378 scopus 로고    scopus 로고
    • Identification of two distinct mechanisms of phagocytosis controlled by different Rho GTPases
    • Caron E, Hall A. Identification of two distinct mechanisms of phagocytosis controlled by different Rho GTPases. Science 1998, 282:1717-1721.
    • (1998) Science , vol.282 , pp. 1717-1721
    • Caron, E.1    Hall, A.2
  • 17
    • 0024449589 scopus 로고
    • The mammalian G protein rho C is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects actin microfilament in Vero cells
    • Chardin P, Boquet P, Madaule P, Popoff MR, Rubin EJ, Gill DM. The mammalian G protein rho C is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects actin microfilament in Vero cells. EMBO J 1989, 8:1087-1092.
    • (1989) EMBO J , vol.8 , pp. 1087-1092
    • Chardin, P.1    Boquet, P.2    Madaule, P.3    Popoff, M.R.4    Rubin, E.J.5    Gill, D.M.6
  • 18
    • 0019287379 scopus 로고
    • The entry of diphtheria toxin into the mammalian cell cytoplasm: evidence for lysosomal involvement
    • Draper RK, Simon MI. The entry of diphtheria toxin into the mammalian cell cytoplasm: evidence for lysosomal involvement. J Cell Biol 1980, 87:849-854.
    • (1980) J Cell Biol , vol.87 , pp. 849-854
    • Draper, R.K.1    Simon, M.I.2
  • 19
    • 0028281986 scopus 로고
    • The channel formed in planar lipid bilayers by the protective antigen component of anthrax toxin
    • Finkelstein A. The channel formed in planar lipid bilayers by the protective antigen component of anthrax toxin. Toxicology 1994, 87:29-41.
    • (1994) Toxicology , vol.87 , pp. 29-41
    • Finkelstein, A.1
  • 21
    • 0035808303 scopus 로고    scopus 로고
    • Crystal structure and novel recognition motif of Rho ADP-ribosylating C3 exoenzyme from Clostridium botulinum: structural insights for recognition specificity and catalysis
    • Han S, Arvai AS, Clancy SB, Tainer JA. Crystal structure and novel recognition motif of Rho ADP-ribosylating C3 exoenzyme from Clostridium botulinum: structural insights for recognition specificity and catalysis. J Mol Biol 2001, 305:95-107.
    • (2001) J Mol Biol , vol.305 , pp. 95-107
    • Han, S.1    Arvai, A.S.2    Clancy, S.B.3    Tainer, J.A.4
  • 22
    • 0041856090 scopus 로고    scopus 로고
    • The host cell chaperone Hsp90 is essential for translocation of the binary Clostridium botulinum C2 toxin into the cytosol
    • Haug G, Leemhuis J, Tiemann D, Meyer DK, Aktories K, Barth H. The host cell chaperone Hsp90 is essential for translocation of the binary Clostridium botulinum C2 toxin into the cytosol. J Biol Chem 2003, 278:32266-32274.
    • (2003) J Biol Chem , vol.278 , pp. 32266-32274
    • Haug, G.1    Leemhuis, J.2    Tiemann, D.3    Meyer, D.K.4    Aktories, K.5    Barth, H.6
  • 23
    • 2142662149 scopus 로고    scopus 로고
    • The host cell chaperone Hsp90 is necessary for cytotoxic action of the binary iota-like toxins
    • Haug G, Aktories K, Barth H. The host cell chaperone Hsp90 is necessary for cytotoxic action of the binary iota-like toxins. Infect Immun 2004, 72:3066-3068.
    • (2004) Infect Immun , vol.72 , pp. 3066-3068
    • Haug, G.1    Aktories, K.2    Barth, H.3
  • 24
    • 28844479772 scopus 로고    scopus 로고
    • Role of Rho GTPase in astrocyte morphology and migratory response during in vitro wound healing
    • Holtje M, Hoffmann A, Hofmann F, Mucke C, Grosse G, Van Rooijen N. Role of Rho GTPase in astrocyte morphology and migratory response during in vitro wound healing. J Neurochem 2005, 95:1237-1248.
    • (2005) J Neurochem , vol.95 , pp. 1237-1248
    • Holtje, M.1    Hoffmann, A.2    Hofmann, F.3    Mucke, C.4    Grosse, G.5    Van Rooijen, N.6
  • 25
    • 0026706241 scopus 로고
    • Purification and characterization of an ADP-ribosyltransferase produced by Clostridium limosum
    • Just I, Mohr C, Schallehn G, Menard L, Didsbury JR, Vandekerckhove J. Purification and characterization of an ADP-ribosyltransferase produced by Clostridium limosum. J Biol Chem 1992a, 267:10274-10280.
    • (1992) J Biol Chem , vol.267 , pp. 10274-10280
    • Just, I.1    Mohr, C.2    Schallehn, G.3    Menard, L.4    Didsbury, J.R.5    Vandekerckhove, J.6
  • 26
    • 77950620475 scopus 로고
    • A novel C3-like ADP-ribosyltransferase produced by Clostridium limosum
    • Poirier GG, Moreau P. New York, Berlin, Springer-Verlag.
    • Just I, Schallehn G, Aktories K. A novel C3-like ADP-ribosyltransferase produced by Clostridium limosum. ADP-Ribosylation Reactions 1992b, 373-376. Poirier GG, Moreau P, In, New York, Berlin, Springer-Verlag, pp.
    • (1992) ADP-Ribosylation Reactions , pp. 373-376
    • Just, I.1    Schallehn, G.2    Aktories, K.3
  • 27
    • 0026773213 scopus 로고
    • ADP-ribosylation of small GTP-binding proteins by Bacillus cereus
    • Just I, Schallehn G, Aktories K. ADP-ribosylation of small GTP-binding proteins by Bacillus cereus. Biochem Biophys Res Commun 1992c, 183:931-936.
    • (1992) Biochem Biophys Res Commun , vol.183 , pp. 931-936
    • Just, I.1    Schallehn, G.2    Aktories, K.3
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0030059222 scopus 로고    scopus 로고
    • Role of Rho in chemoattractant-activated leukocyte adhesion through integrins
    • Laudanna C, Campbell JJ, Butcher EC. Role of Rho in chemoattractant-activated leukocyte adhesion through integrins. Science 1996, 271:981-983.
    • (1996) Science , vol.271 , pp. 981-983
    • Laudanna, C.1    Campbell, J.J.2    Butcher, E.C.3
  • 30
    • 0036721793 scopus 로고    scopus 로고
    • Requirement for RhoA kinase activation in leukocyte de-adhesion
    • Liu L, Schwartz BR, Lin N, Winn RK, Harlan JM. Requirement for RhoA kinase activation in leukocyte de-adhesion. J Immunol 2002, 169:2330-2336.
    • (2002) J Immunol , vol.169 , pp. 2330-2336
    • Liu, L.1    Schwartz, B.R.2    Lin, N.3    Winn, R.K.4    Harlan, J.M.5
  • 31
    • 12844261651 scopus 로고    scopus 로고
    • Rho GTPases and leucocyte-induced endothelial remodelling
    • Millan J, Ridley AJ. Rho GTPases and leucocyte-induced endothelial remodelling. Biochem J 2005, 385:329-337.
    • (2005) Biochem J , vol.385 , pp. 329-337
    • Millan, J.1    Ridley, A.J.2
  • 32
    • 33646905907 scopus 로고    scopus 로고
    • Localization of the C3-Like ADP-ribosyltransferase from Staphylococcus aureus during bacterial invasion of mammalian cells
    • Molinari G, Rohde M, Wilde C, Just I, Aktories K, Chhatwal GS. Localization of the C3-Like ADP-ribosyltransferase from Staphylococcus aureus during bacterial invasion of mammalian cells. Infect Immun 2006, 74:3673-3677.
    • (2006) Infect Immun , vol.74 , pp. 3673-3677
    • Molinari, G.1    Rohde, M.2    Wilde, C.3    Just, I.4    Aktories, K.5    Chhatwal, G.S.6
  • 33
    • 0032145173 scopus 로고    scopus 로고
    • Protein toxins and membrane transport
    • Montecucco C. Protein toxins and membrane transport. Curr Opin Cell Biol 1998, 10:530-536.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 530-536
    • Montecucco, C.1
  • 34
    • 0029147540 scopus 로고
    • Preparation of native and recombinant Clostridium botulinum C3 ADP-ribosyltransferase and identification of Rho proteins by ADP-ribosylation
    • Balch WE, Der CJ, Hall A. San Diego, CA, Academic Press.
    • Morii N, Narumiya S. Preparation of native and recombinant Clostridium botulinum C3 ADP-ribosyltransferase and identification of Rho proteins by ADP-ribosylation. Methods in Enzymology 1995, 196-206. Balch WE, Der CJHall A. In, San Diego, CA, Academic Press, pp.
    • (1995) Methods in Enzymology , pp. 196-206
    • Morii, N.1    Narumiya, S.2
  • 35
    • 0025737882 scopus 로고
    • Insertion of diphtheria toxin B-fragment into the plasma membrane at low pH
    • Moskaug JO, Stenmark H, Olsnes S. Insertion of diphtheria toxin B-fragment into the plasma membrane at low pH. J Biol Chem 1991, 266:2652-2659.
    • (1991) J Biol Chem , vol.266 , pp. 2652-2659
    • Moskaug, J.O.1    Stenmark, H.2    Olsnes, S.3
  • 37
    • 84954218790 scopus 로고    scopus 로고
    • Clostridium botulinum C3 exoenzyme and studies on Rho proteins
    • Aktories K. (ed.)., Weinheim, Chapman&Hall.
    • Nobes CD, Hall A. Clostridium botulinum C3 exoenzyme and studies on Rho proteins. Bacterial Toxins - Tools in Cell Biology and Pharmacology 1997, 71-83. Aktories K, In, (ed.)., Weinheim, Chapman&Hall, pp.
    • (1997) Bacterial Toxins - Tools in Cell Biology and Pharmacology , pp. 71-83
    • Nobes, C.D.1    Hall, A.2
  • 38
    • 0024115012 scopus 로고
    • On the membrane translocation of diphtheria toxin: at low pH the toxin induces ion channels on cells
    • Papini E, Sandona D, Rappuoli R, Montecucco P. On the membrane translocation of diphtheria toxin: at low pH the toxin induces ion channels on cells. EMBO J 1988, 7:3353-3359.
    • (1988) EMBO J , vol.7 , pp. 3353-3359
    • Papini, E.1    Sandona, D.2    Rappuoli, R.3    Montecucco, P.4
  • 39
    • 0027510933 scopus 로고
    • Cell penetration of diphtheria toxin. Reduction of the interchain disulfide bridge is the rate-limiting step of translocation in the cytosol
    • Papini E, Rappuoli R, Murgia M, Montecucco C. Cell penetration of diphtheria toxin. Reduction of the interchain disulfide bridge is the rate-limiting step of translocation in the cytosol. J Biol Chem 1993, 268:1567-1574.
    • (1993) J Biol Chem , vol.268 , pp. 1567-1574
    • Papini, E.1    Rappuoli, R.2    Murgia, M.3    Montecucco, C.4
  • 40
    • 2442691145 scopus 로고    scopus 로고
    • Exoenzyme Tat-C3 inhibits association of zymosan particles, phagocytosis, adhesion, and complement binding in macrophage cells
    • Park J, Kim JS, Jung KC, Lee HJ, Kim JI, Kim J. Exoenzyme Tat-C3 inhibits association of zymosan particles, phagocytosis, adhesion, and complement binding in macrophage cells. Mol Cells 2003, 16:216-223.
    • (2003) Mol Cells , vol.16 , pp. 216-223
    • Park, J.1    Kim, J.S.2    Jung, K.C.3    Lee, H.J.4    Kim, J.I.5    Kim, J.6
  • 42
    • 27144457720 scopus 로고    scopus 로고
    • Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme
    • Pautsch A, Vogelsgesang M, Trankle J, Herrmann C, Aktories K. Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme. EMBO J 2005, 24:3670-3680.
    • (2005) EMBO J , vol.24 , pp. 3670-3680
    • Pautsch, A.1    Vogelsgesang, M.2    Trankle, J.3    Herrmann, C.4    Aktories, K.5
  • 43
    • 0242414631 scopus 로고    scopus 로고
    • Cellular uptake of Clostridium difficile toxin B: translocation of the N-terminal catalytic domain into the cytosol of eukaryotic cells
    • Pfeifer G, Schirmer J, Leemhuis J, Busch C, Meyer DK, Aktories K, Barth H. Cellular uptake of Clostridium difficile toxin B: translocation of the N-terminal catalytic domain into the cytosol of eukaryotic cells. J Biol Chem 2003, 278:44535-44541.
    • (2003) J Biol Chem , vol.278 , pp. 44535-44541
    • Pfeifer, G.1    Schirmer, J.2    Leemhuis, J.3    Busch, C.4    Meyer, D.K.5    Aktories, K.6    Barth, H.7
  • 44
    • 0034114105 scopus 로고    scopus 로고
    • PH-induced conformational changes in Clostridium difficile toxin B
    • Qa'Dan M, Spyres LM, Ballard JD. pH-induced conformational changes in Clostridium difficile toxin B. Infect Immun 2000, 68:2470-2474.
    • (2000) Infect Immun , vol.68 , pp. 2470-2474
    • Qa'Dan, M.1    Spyres, L.M.2    Ballard, J.D.3
  • 45
    • 0345668477 scopus 로고    scopus 로고
    • The cytosolic entry of diphtheria toxin catalytic domain requires a host cell cytosolic translocation factor complex
    • Ratts R, Zeng H, Berg EA, Blue C, McComb ME, Costello CE. The cytosolic entry of diphtheria toxin catalytic domain requires a host cell cytosolic translocation factor complex. J Cell Biol 2003, 160:1139-1150.
    • (2003) J Cell Biol , vol.160 , pp. 1139-1150
    • Ratts, R.1    Zeng, H.2    Berg, E.A.3    Blue, C.4    McComb, M.E.5    Costello, C.E.6
  • 46
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley AJ, Hall A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 1992, 70:389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 47
    • 0019271816 scopus 로고
    • Diphtheria toxin entry into cells is facilitated by low pH
    • Sandvig K, Olsnes S. Diphtheria toxin entry into cells is facilitated by low pH. J Cell Biol 1980, 87:828-832.
    • (1980) J Cell Biol , vol.87 , pp. 828-832
    • Sandvig, K.1    Olsnes, S.2
  • 49
  • 50
    • 0028286786 scopus 로고
    • Interaction of Clostridium botulinum C2 toxin with lipid bilayer membranes: formation of cation-selective channels and inhibition of channel function by chloroquine and peptides
    • Schmid A, Benz R, Just I, Aktories K. Interaction of Clostridium botulinum C2 toxin with lipid bilayer membranes: formation of cation-selective channels and inhibition of channel function by chloroquine and peptides. J Biol Chem 1994, 269:16706-16711.
    • (1994) J Biol Chem , vol.269 , pp. 16706-16711
    • Schmid, A.1    Benz, R.2    Just, I.3    Aktories, K.4
  • 51
    • 44949253112 scopus 로고    scopus 로고
    • Phosphorylation of fibroblast growth factor (FGF) receptor 1 at Ser777 by p38 mitogen-activated protein kinase regulates translocation of exogenous FGF1 to the cytosol and nucleus
    • Sorensen V, Zhen Y, Zakrzewska M, Haugsten EM, Walchli S, Nilsen T. Phosphorylation of fibroblast growth factor (FGF) receptor 1 at Ser777 by p38 mitogen-activated protein kinase regulates translocation of exogenous FGF1 to the cytosol and nucleus. Mol Cell Biol 2008, 28:4129-4141.
    • (2008) Mol Cell Biol , vol.28 , pp. 4129-4141
    • Sorensen, V.1    Zhen, Y.2    Zakrzewska, M.3    Haugsten, E.M.4    Walchli, S.5    Nilsen, T.6
  • 52
    • 0036438489 scopus 로고    scopus 로고
    • Azithromycin, a lysosomotropic antibiotic, has distinct effects on fluid-phase and receptor-mediated endocytosis, but does not impair phagocytosis in J774 macrophages
    • Tyteca D, Van Der Smissen P, Mettlen M, Van Bambeke F, Tulkens PM, Mingeot-Leclercq MP, Courtoy PJ. Azithromycin, a lysosomotropic antibiotic, has distinct effects on fluid-phase and receptor-mediated endocytosis, but does not impair phagocytosis in J774 macrophages. Exp Cell Res 2002, 281:86-100.
    • (2002) Exp Cell Res , vol.281 , pp. 86-100
    • Tyteca, D.1    Van Der Smissen, P.2    Mettlen, M.3    Van Bambeke, F.4    Tulkens, P.M.5    Mingeot-Leclercq, M.P.6    Courtoy, P.J.7
  • 53
    • 0030993268 scopus 로고    scopus 로고
    • ADP-ribosylation of Rho-proteins with botulinum C3 exoenzyme inhibits invasion and shape changes of T-lymphoma cells
    • Verschueren H, De Baetselier P, De Braekeleer J, Dewit J, Aktories K, Just I. ADP-ribosylation of Rho-proteins with botulinum C3 exoenzyme inhibits invasion and shape changes of T-lymphoma cells. Eur J Cell Biol 1997, 73:182-187.
    • (1997) Eur J Cell Biol , vol.73 , pp. 182-187
    • Verschueren, H.1    De Baetselier, P.2    De Braekeleer, J.3    Dewit, J.4    Aktories, K.5    Just, I.6
  • 54
    • 33846814964 scopus 로고    scopus 로고
    • C3 exoenzymes, novel insights into structure and action of Rho-ADP-ribosylating toxins
    • Vogelsgesang M, Pautsch A, Aktories K. C3 exoenzymes, novel insights into structure and action of Rho-ADP-ribosylating toxins. Naunyn Schmiedebergs Arch Pharmacol 2007, 374:347-360.
    • (2007) Naunyn Schmiedebergs Arch Pharmacol , vol.374 , pp. 347-360
    • Vogelsgesang, M.1    Pautsch, A.2    Aktories, K.3
  • 55
    • 0025778012 scopus 로고
    • Alteration of the cytoskeleton of mammalian cells cultured in vitro by Clostridium botulinum C2 toxin and C3 ADP-ribosyltransferase
    • Wiegers W, Just I, Müller H, Hellwig A, Traub P, Aktories K. Alteration of the cytoskeleton of mammalian cells cultured in vitro by Clostridium botulinum C2 toxin and C3 ADP-ribosyltransferase. Eur J Cell Biol 1991, 54:237-245.
    • (1991) Eur J Cell Biol , vol.54 , pp. 237-245
    • Wiegers, W.1    Just, I.2    Müller, H.3    Hellwig, A.4    Traub, P.5    Aktories, K.6
  • 56
    • 0034875571 scopus 로고    scopus 로고
    • The Rho-ADP-ribosylating C3 exoenzyme from Clostridium botulinum and related C3-like transferases
    • Wilde C, Aktories K. The Rho-ADP-ribosylating C3 exoenzyme from Clostridium botulinum and related C3-like transferases. Toxicon 2001, 39:1647-1660.
    • (2001) Toxicon , vol.39 , pp. 1647-1660
    • Wilde, C.1    Aktories, K.2
  • 57
    • 0035937815 scopus 로고    scopus 로고
    • A novel C3-like ADP-ribosyltransferase from Staphylococcus aureus modifying RhoE and Rnd3
    • Wilde C, Chhatwal GS, Schmalzing G, Aktories K, Just I. A novel C3-like ADP-ribosyltransferase from Staphylococcus aureus modifying RhoE and Rnd3. J Biol Chem 2001, 276:9537-9542.
    • (2001) J Biol Chem , vol.276 , pp. 9537-9542
    • Wilde, C.1    Chhatwal, G.S.2    Schmalzing, G.3    Aktories, K.4    Just, I.5
  • 59
    • 0035833247 scopus 로고    scopus 로고
    • RhoA is required for monocyte tail retraction during transendothelial migration
    • Worthylake RA, Lemoine S, Watson JM, Burridge K. RhoA is required for monocyte tail retraction during transendothelial migration. J Cell Biol 2001, 154:147-160.
    • (2001) J Cell Biol , vol.154 , pp. 147-160
    • Worthylake, R.A.1    Lemoine, S.2    Watson, J.M.3    Burridge, K.4


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