메뉴 건너뛰기




Volumn 13, Issue 3, 2011, Pages 359-373

Role of CypA and Hsp90 in membrane translocation mediated by anthrax protective antigen

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ANTHRAX TOXIN; BAFILOMYCIN A1; CYCLOPHILIN; CYCLOPHILIN A; CYCLOSPORIN A; DIPHTHERIA TOXIN; ELONGATION FACTOR; ELONGATION FACTOR 2; HEAT SHOCK PROTEIN 90; HYBRID PROTEIN; PEPTIDYLPROLYL ISOMERASE; PROTEIN RAD1; RADICICOL;

EID: 79951470779     PISSN: 14625814     EISSN: 14625822     Source Type: Journal    
DOI: 10.1111/j.1462-5822.2010.01539.x     Document Type: Article
Times cited : (55)

References (53)
  • 1
    • 0037415611 scopus 로고    scopus 로고
    • Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process
    • Abrami, L., Liu, S., Cosson, P., Leppla, S.H., and van der Goot, F.G. (2003) Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process. J Cell Biol 160: 321-328.
    • (2003) J Cell Biol , vol.160 , pp. 321-328
    • Abrami, L.1    Liu, S.2    Cosson, P.3    Leppla, S.H.4    van der Goot, F.G.5
  • 2
    • 4444224022 scopus 로고    scopus 로고
    • Membrane insertion of anthrax protective antigen and cytoplasmic delivery of lethal factor occur at different stages of the endocytic pathway
    • Abrami, L., Lindsay, M., Parton, R.G., Leppla, S.H., and van der Goot, F.G. (2004) Membrane insertion of anthrax protective antigen and cytoplasmic delivery of lethal factor occur at different stages of the endocytic pathway. J Cell Biol 166: 645-651.
    • (2004) J Cell Biol , vol.166 , pp. 645-651
    • Abrami, L.1    Lindsay, M.2    Parton, R.G.3    Leppla, S.H.4    van der Goot, F.G.5
  • 3
    • 77950407292 scopus 로고    scopus 로고
    • Endocytosis of the anthrax toxin is mediated by clathrin, actin and unconventional adaptors
    • Abrami, L., Bischofberger, M., Kunz, B., Groux, R., and van der Goot, F.G. (2010) Endocytosis of the anthrax toxin is mediated by clathrin, actin and unconventional adaptors. PLoS Pathog 6: e1000792.
    • (2010) PLoS Pathog , vol.6
    • Abrami, L.1    Bischofberger, M.2    Kunz, B.3    Groux, R.4    van der Goot, F.G.5
  • 4
    • 0026319518 scopus 로고
    • Slow conformational changes in protein folding can be accelerated by enzymes
    • Bang, H., and Fischer, G. (1991) Slow conformational changes in protein folding can be accelerated by enzymes. Biomed Biochim Acta 50: S137-S142.
    • (1991) Biomed Biochim Acta , vol.50
    • Bang, H.1    Fischer, G.2
  • 6
    • 0039003839 scopus 로고    scopus 로고
    • Cellular uptake of Clostridium botulinum C2 toxin requires oligomerization and acidification
    • Barth, H., Blöcker, D., Behlke, J., Bergsma-Schutter, W., Brisson, A., Benz, R., and Aktories, K. (2000) Cellular uptake of Clostridium botulinum C2 toxin requires oligomerization and acidification. J Biol Chem 275: 18704-18711.
    • (2000) J Biol Chem , vol.275 , pp. 18704-18711
    • Barth, H.1    Blöcker, D.2    Behlke, J.3    Bergsma-Schutter, W.4    Brisson, A.5    Benz, R.6    Aktories, K.7
  • 7
    • 4544264417 scopus 로고    scopus 로고
    • Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteins
    • Barth, H., Aktories, K., Popoff, M.R., and Stiles, B.G. (2004) Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteins. Microbiol Mol Biol Rev 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
  • 8
    • 0032539990 scopus 로고    scopus 로고
    • Identification of residues lining the anthrax protective antigen channel
    • Benson, E.L., Huynh, P.D., Finkelstein, A., and Collier, R.J. (1998) Identification of residues lining the anthrax protective antigen channel. Biochemistry 37: 3941-3948.
    • (1998) Biochemistry , vol.37 , pp. 3941-3948
    • Benson, E.L.1    Huynh, P.D.2    Finkelstein, A.3    Collier, R.J.4
  • 9
    • 0024523836 scopus 로고
    • Anthrax toxin: channel-forming activity of protective antigen in planar phopholipid bilayers
    • Blaustein, R.O., Koehler, T.M., Collier, R.J., and Finkelstein, A. (1989) Anthrax toxin: channel-forming activity of protective antigen in planar phopholipid bilayers. Proc Natl Acad Sci USA 86: 2209-2213.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 2209-2213
    • Blaustein, R.O.1    Koehler, T.M.2    Collier, R.J.3    Finkelstein, A.4
  • 10
    • 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., and Barth, H. (2003a) 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 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
  • 11
    • 18144441577 scopus 로고    scopus 로고
    • Clostridium botulinum C2 toxin: low pH-induced pore formation is required for translocation of the enzyme component C2I into the cytosol of host cells
    • Blöcker, D., Pohlmann, K., Haug, G., Bachmeyer, C., Benz, R., Aktories, K., and Barth, H. (2003b) Clostridium botulinum C2 toxin: low pH-induced pore formation is required for translocation of the enzyme component C2I into the cytosol of host cells. J Biol Chem 278: 37360-37367.
    • (2003) J Biol Chem , vol.278 , pp. 37360-37367
    • Blöcker, D.1    Pohlmann, K.2    Haug, G.3    Bachmeyer, C.4    Benz, R.5    Aktories, K.6    Barth, H.7
  • 12
    • 34848840291 scopus 로고    scopus 로고
    • Botulinum neurotoxin heavy chain belt as an intramolecular chaperone for the light chain
    • Brunger, A.T., Breidenbach, M.A., Jin, R., Fischer, A., Santos, J.S., and Montal, M. (2007) Botulinum neurotoxin heavy chain belt as an intramolecular chaperone for the light chain. PLoS Pathog 3: 1191-1194.
    • (2007) PLoS Pathog , vol.3 , pp. 1191-1194
    • Brunger, A.T.1    Breidenbach, M.A.2    Jin, R.3    Fischer, A.4    Santos, J.S.5    Montal, M.6
  • 13
    • 0346074091 scopus 로고
    • Bacterial Toxins and Virulence Factors in Disease
    • In Moss, J., Iglewski, B., Vaughan, M., and Tu, A.T. (eds). New York: Marcel Dekker.
    • Collier, R.J. (1995) Three-dimensional structure of diphtheria toxin. In Bacterial Toxins and Virulence Factors in Disease. Moss, J., Iglewski, B., Vaughan, M., and Tu, A.T. (eds). New York: Marcel Dekker, pp. 81-93.
    • (1995) Three-dimensional structure of diphtheria toxin , pp. 81-93
    • Collier, R.J.1
  • 14
    • 70350708307 scopus 로고    scopus 로고
    • Membrane translocation by anthrax toxin
    • Collier, R.J. (2009) Membrane translocation by anthrax toxin. Mol Aspects Med 30: 413-422.
    • (2009) Mol Aspects Med , vol.30 , pp. 413-422
    • Collier, R.J.1
  • 16
    • 0037438354 scopus 로고    scopus 로고
    • Thermodynamic characterization of the interaction of human cyclophilin 18 with cyclosporin A
    • Fanghänel, J., and Fischer, G. (2003) Thermodynamic characterization of the interaction of human cyclophilin 18 with cyclosporin A. Biophys Chem 100: 351-366.
    • (2003) Biophys Chem , vol.100 , pp. 351-366
    • Fanghänel, J.1    Fischer, G.2
  • 17
    • 0024959449 scopus 로고
    • Cyp and peptidyl-prolyl cis-trans isomerase are probably identical proteins
    • Fischer, G., Wittmann-Liebold, B., Lang, K., Kiefhaber, T., and Schmid, F.X. (1989) Cyp and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature 337: 476-478.
    • (1989) Nature , vol.337 , pp. 476-478
    • Fischer, G.1    Wittmann-Liebold, B.2    Lang, K.3    Kiefhaber, T.4    Schmid, F.X.5
  • 18
    • 0022891493 scopus 로고
    • Macrophages are sensitive to anthrax lethal toxin through an acid-dependent process
    • Friedlander, A.M. (1986) Macrophages are sensitive to anthrax lethal toxin through an acid-dependent process. J Biol Chem 261: 7123-7126.
    • (1986) J Biol Chem , vol.261 , pp. 7123-7126
    • Friedlander, A.M.1
  • 19
    • 0032564464 scopus 로고    scopus 로고
    • Interactions of Salmonella with host cells: encounters of the closest kind
    • Galan, J.E. (1998) Interactions of Salmonella with host cells: encounters of the closest kind. Proc Natl Acad Sci USA 95: 14006-14008.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14006-14008
    • Galan, J.E.1
  • 21
    • 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, D.K., Aktories, K., and Barth, H. (2003a) The host cell chaperone Hsp90 is essential for translocation of the binary Clostridium botulinum C2 toxin into the cytosol. J Biol Chem 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
  • 22
    • 0346333312 scopus 로고    scopus 로고
    • Cellular uptake of Clostridium botulinum C2 toxin: membrane translocation of a fusion toxin requires unfolding of its dihydrofolate reductase domain
    • Haug, G., Wilde, C., Leemhuis, J., Meyer, D.K., Aktories, K., and Barth, H. (2003b) Cellular uptake of Clostridium botulinum C2 toxin: membrane translocation of a fusion toxin requires unfolding of its dihydrofolate reductase domain. Biochemistry 42: 15284-15291.
    • (2003) Biochemistry , vol.42 , pp. 15284-15291
    • Haug, G.1    Wilde, C.2    Leemhuis, J.3    Meyer, D.K.4    Aktories, K.5    Barth, H.6
  • 23
    • 64049084122 scopus 로고    scopus 로고
    • Cyp A facilitates translocation of the Clostridium botulinum C2 toxin across membranes of acidified endosomes into the cytosol of mammalian cells
    • Kaiser, E., Pust, S., Kroll, C., and Barth, H. (2009) Cyp A facilitates translocation of the Clostridium botulinum C2 toxin across membranes of acidified endosomes into the cytosol of mammalian cells. Cell Microbiol 11: 780-795.
    • (2009) Cell Microbiol , vol.11 , pp. 780-795
    • Kaiser, E.1    Pust, S.2    Kroll, C.3    Barth, H.4
  • 24
    • 7944221639 scopus 로고    scopus 로고
    • Acid-induced unfolding of the amino-terminal domains of the lethal and edema factors of anthrax toxin
    • Krantz, B.A., Trivedi, A.D., Cunningham, K., Christensen, K.A., and Collier, R.J. (2004) Acid-induced unfolding of the amino-terminal domains of the lethal and edema factors of anthrax toxin. J Mol Biol 344: 739-756.
    • (2004) J Mol Biol , vol.344 , pp. 739-756
    • Krantz, B.A.1    Trivedi, A.D.2    Cunningham, K.3    Christensen, K.A.4    Collier, R.J.5
  • 25
    • 23044508996 scopus 로고    scopus 로고
    • A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore
    • Krantz, B.A., Melnyk, R.A., Zhang, S., Juris, S.J., Lacy, D.B., Wu, Z., etal. (2005) A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore. Science 309: 777-781.
    • (2005) Science , vol.309 , pp. 777-781
    • Krantz, B.A.1    Melnyk, R.A.2    Zhang, S.3    Juris, S.J.4    Lacy, D.B.5    Wu, Z.6
  • 26
    • 29444456231 scopus 로고    scopus 로고
    • Protein translocation through the anthrax toxin transmembrane pore is driven by a proton gradient
    • Krantz, B.A., Finkelstein, A., and Collier, R.J. (2006) Protein translocation through the anthrax toxin transmembrane pore is driven by a proton gradient. J Mol Biol 355: 968-979.
    • (2006) J Mol Biol , vol.355 , pp. 968-979
    • Krantz, B.A.1    Finkelstein, A.2    Collier, R.J.3
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0031031848 scopus 로고    scopus 로고
    • Membrane translocation of diphtheria toxin fragment A exploits early to late endosome trafficking machinery
    • Lemichez, E., Bomsel, M., Devilliers, G., VanderSpek, J., Murphy, J.R., Lukianov, E.V., etal. (1997) Membrane translocation of diphtheria toxin fragment A exploits early to late endosome trafficking machinery. Mol Microbiol 23: 445-457.
    • (1997) Mol Microbiol , vol.23 , pp. 445-457
    • Lemichez, E.1    Bomsel, M.2    Devilliers, G.3    VanderSpek, J.4    Murphy, J.R.5    Lukianov, E.V.6
  • 29
    • 0000947082 scopus 로고
    • Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations in eukaryotic cells
    • Leppla, S. (1982) Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations in eukaryotic cells. Proc Natl Acad Sci USA 79: 3162-3166.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 3162-3166
    • Leppla, S.1
  • 31
    • 0034996586 scopus 로고    scopus 로고
    • The best defense is a good offense-Salmonella deploys an ADP-ribosylating toxin
    • Lesnick, M.L., and Guiney, D.G. (2001) The best defense is a good offense-Salmonella deploys an ADP-ribosylating toxin. Trends Microbiol 9: 2-4.
    • (2001) Trends Microbiol , vol.9 , pp. 2-4
    • Lesnick, M.L.1    Guiney, D.G.2
  • 32
    • 0029898287 scopus 로고    scopus 로고
    • Transport of an external Lys-Asp-Glu-Leu (KDEL) protein from the plasma membrane to the endoplasmic reticulum: studies with cholera toxin in Vero cells
    • Majoul, I.V., Bastiaens, P.I.H., and Söling, H.D. (1996) Transport of an external Lys-Asp-Glu-Leu (KDEL) protein from the plasma membrane to the endoplasmic reticulum: studies with cholera toxin in Vero cells. J Cell Biol 133: 777-789.
    • (1996) J Cell Biol , vol.133 , pp. 777-789
    • Majoul, I.V.1    Bastiaens, P.I.H.2    Söling, H.D.3
  • 33
    • 79951478290 scopus 로고    scopus 로고
    • Handbook of Experimental Pharmacology
    • In Born, G.V.R., Ganten, D., Herken, H., Starke, K., and Taylor, P. (eds). Berlin: Springer.
    • Masignani, V., Pizza, M., and Rappuoli, R. (2000) Common features of ADP-ribosyltransferases. In Handbook of Experimental Pharmacology. Born, G.V.R., Ganten, D., Herken, H., Starke, K., and Taylor, P. (eds). Berlin: Springer, pp. 21-44.
    • (2000) Common features of ADP-ribosyltransferases , pp. 21-44
    • Masignani, V.1    Pizza, M.2    Rappuoli, R.3
  • 34
    • 0033543208 scopus 로고    scopus 로고
    • Anthrax protective antigen: prepore-to-pore conversion
    • Miller, C.J., Elliott, J.L., and Collier, R.J. (1999) Anthrax protective antigen: prepore-to-pore conversion. Biochemistry 38: 10432-10441.
    • (1999) Biochemistry , vol.38 , pp. 10432-10441
    • Miller, C.J.1    Elliott, J.L.2    Collier, R.J.3
  • 35
    • 77953642001 scopus 로고    scopus 로고
    • Botulinum neurotoxin: a marvel of protein design
    • Montal, M. (2010) Botulinum neurotoxin: a marvel of protein design. Annu Rev Biochem 79: 591-617.
    • (2010) Annu Rev Biochem , vol.79 , pp. 591-617
    • Montal, M.1
  • 37
    • 34249854870 scopus 로고    scopus 로고
    • A cell-permeable fusion toxin as a tool to study the consequences of actin-ADP-ribosylation caused by the Salmonella enterica virulence factor SpvB in intact cells
    • Pust, S., Hochmann, H., Kaiser, E., von Figura, G., Heine, K., Aktories, K., and Barth, H. (2007) A cell-permeable fusion toxin as a tool to study the consequences of actin-ADP-ribosylation caused by the Salmonella enterica virulence factor SpvB in intact cells. J Biol Chem 282: 10272-10282.
    • (2007) J Biol Chem , vol.282 , pp. 10272-10282
    • Pust, S.1    Hochmann, H.2    Kaiser, E.3    von Figura, G.4    Heine, K.5    Aktories, K.6    Barth, H.7
  • 38
    • 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, E.A., Blue, C., McComb, M.E., Costello, C.E., etal. (2003) The cytosolic entry of diphtheria toxin catalytic domain requires a host cell cytosolic translocation factor complex. J Cell Biol 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
  • 39
    • 27344460405 scopus 로고    scopus 로고
    • A conserved motif in transmembrane helix 1 of diphtheria toxin mediates catalytic domain delivery to the cytosol
    • Ratts, R., Trujillo, C., Bharti, A., vanderSpek, J., Harrison, R., and Murphy, J.R. (2005) A conserved motif in transmembrane helix 1 of diphtheria toxin mediates catalytic domain delivery to the cytosol. Proc Natl Acad Sci USA 102: 15635-15640.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15635-15640
    • Ratts, R.1    Trujillo, C.2    Bharti, A.3    vanderSpek, J.4    Harrison, R.5    Murphy, J.R.6
  • 41
    • 33751070013 scopus 로고    scopus 로고
    • Structure and action of the binary C2 toxin from Clostridium botulinum
    • Schleberger, C., Hochmann, H., Barth, H., Aktories, K., and Schulz, G.E. (2006) Structure and action of the binary C2 toxin from Clostridium botulinum. J Mol Biol 364: 705-715.
    • (2006) J Mol Biol , vol.364 , pp. 705-715
    • Schleberger, C.1    Hochmann, H.2    Barth, H.3    Aktories, K.4    Schulz, G.E.5
  • 42
    • 0027256737 scopus 로고
    • Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions
    • Schmid, F.X. (1993) Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions. Annu Rev Biophys Biomol Struct 22: 123-142.
    • (1993) Annu Rev Biophys Biomol Struct , vol.22 , pp. 123-142
    • Schmid, F.X.1
  • 44
    • 56249144175 scopus 로고    scopus 로고
    • Cytosolic chaperones influence the fate of a toxin dislocated from the endoplasmic reticulum
    • Spooner, R.A., Hart, P.J., Cook, J.P., Pietroni, P., Rogon, C., Hohfeld, J., etal. (2008) Cytosolic chaperones influence the fate of a toxin dislocated from the endoplasmic reticulum. Proc Natl Acad Sci USA 105: 17408-17413.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 17408-17413
    • Spooner, R.A.1    Hart, P.J.2    Cook, J.P.3    Pietroni, P.4    Rogon, C.5    Hohfeld, J.6
  • 45
    • 42449105243 scopus 로고    scopus 로고
    • COPI coatomer complex proteins facilitate the translocation of anthrax lethal factor across vesicular membranes in vitro
    • Tamayo, A.G., Bharti, A., Trujillo, C., Harrison, R., and Murphy, J.R. (2008) COPI coatomer complex proteins facilitate the translocation of anthrax lethal factor across vesicular membranes in vitro. Proc Natl Acad Sci USA 105: 5254-5259.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 5254-5259
    • Tamayo, A.G.1    Bharti, A.2    Trujillo, C.3    Harrison, R.4    Murphy, J.R.5
  • 46
    • 70350733498 scopus 로고    scopus 로고
    • The anthrax lethal factor and its MAPK kinase-specific metalloprotease activity
    • Tonello, F., and Montecucco, C. (2009) The anthrax lethal factor and its MAPK kinase-specific metalloprotease activity. Mol Aspects Med 30: 431-438.
    • (2009) Mol Aspects Med , vol.30 , pp. 431-438
    • Tonello, F.1    Montecucco, C.2
  • 47
    • 0032581369 scopus 로고    scopus 로고
    • Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages
    • Vitale, G., Pellizzari, R., Recchi, C., Napolitani, G., Mock, M., and Montecucco, C. (1998) Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages. Biochem Biophys Res Commun 248: 706-711.
    • (1998) Biochem Biophys Res Commun , vol.248 , pp. 706-711
    • Vitale, G.1    Pellizzari, R.2    Recchi, C.3    Napolitani, G.4    Mock, M.5    Montecucco, C.6
  • 48
  • 49
    • 0032506245 scopus 로고    scopus 로고
    • Characterization of membrane translocation by anthrax protective antigen
    • Wesche, J., Elliott, J.L., Falnes, P.O., Olsnes, S., and Collier, R.J. (1998) Characterization of membrane translocation by anthrax protective antigen. Biochemistry 37: 15737-15746.
    • (1998) Biochemistry , vol.37 , pp. 15737-15746
    • Wesche, J.1    Elliott, J.L.2    Falnes, P.O.3    Olsnes, S.4    Collier, R.J.5
  • 50
    • 12844288569 scopus 로고    scopus 로고
    • Phosphorylation-regulated nucleocytoplasmic trafficking of internalized fibroblast growth factor-1
    • Wiedlocha, A., Nilsen, T., Wesche, J., Sorensen, V., Malecki, J., Marcinkowska, E., and Olsnes, S. (2005) Phosphorylation-regulated nucleocytoplasmic trafficking of internalized fibroblast growth factor-1. Mol Biol Cell 16: 794-810.
    • (2005) Mol Biol Cell , vol.16 , pp. 794-810
    • Wiedlocha, A.1    Nilsen, T.2    Wesche, J.3    Sorensen, V.4    Malecki, J.5    Marcinkowska, E.6    Olsnes, S.7
  • 51
    • 0025076421 scopus 로고
    • Active-site mutations of diptheria toxin: effects of repalcing glutamic acid-148 with aspartic acid, glutamine, or serine
    • Wilson, B.A., Reich, K.A., Weinstein, B.R., and Collier, R.J. (1990) Active-site mutations of diptheria toxin: effects of repalcing glutamic acid-148 with aspartic acid, glutamine, or serine. Biochemistry 29: 8643-8651.
    • (1990) Biochemistry , vol.29 , pp. 8643-8651
    • Wilson, B.A.1    Reich, K.A.2    Weinstein, B.R.3    Collier, R.J.4
  • 52
    • 34447291354 scopus 로고    scopus 로고
    • Anthrax toxin: receptor binding, internalization, pore formation, and translocation
    • Young, J.A., and Collier, R.J. (2007) Anthrax toxin: receptor binding, internalization, pore formation, and translocation. Annu Rev Biochem 76: 243-265.
    • (2007) Annu Rev Biochem , vol.76 , pp. 243-265
    • Young, J.A.1    Collier, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.