메뉴 건너뛰기




Volumn 392, Issue 3, 2009, Pages 614-629

The Protective Antigen Component of Anthrax Toxin Forms Functional Octameric Complexes

Author keywords

anthrax toxin; cell surface assembly; lethal toxin; oligomerization; translocation

Indexed keywords

ANTHRAX TOXIN; BACTERIAL ANTIGEN;

EID: 69349098830     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.07.037     Document Type: Article
Times cited : (191)

References (70)
  • 1
    • 34447291354 scopus 로고    scopus 로고
    • Anthrax toxin: receptor binding, internalization, pore formation, and translocation
    • Young J.A., and Collier R.J. Anthrax toxin: receptor binding, internalization, pore formation, and translocation. Annu. Rev. Biochem. 76 (2007) 243-265
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 243-265
    • Young, J.A.1    Collier, R.J.2
  • 3
    • 0038303163 scopus 로고    scopus 로고
    • Human capillary morphogenesis protein 2 functions as an anthrax toxin receptor
    • Scobie H.M., Rainey G.J.A., Bradley K.A., and Young J.A. Human capillary morphogenesis protein 2 functions as an anthrax toxin receptor. Proc. Natl Acad. Sci. USA 100 (2003) 5170-5174
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 5170-5174
    • Scobie, H.M.1    Rainey, G.J.A.2    Bradley, K.A.3    Young, J.A.4
  • 4
    • 0028018856 scopus 로고
    • Anthrax protective antigen forms oligomers during intoxication of mammalian cells
    • Milne J.C., Furlong D., Hanna P.C., Wall J.S., and Collier R.J. Anthrax protective antigen forms oligomers during intoxication of mammalian cells. J. Biol. Chem. 269 (1994) 20607-20612
    • (1994) J. Biol. Chem. , vol.269 , pp. 20607-20612
    • Milne, J.C.1    Furlong, D.2    Hanna, P.C.3    Wall, J.S.4    Collier, R.J.5
  • 6
  • 7
    • 4444267311 scopus 로고    scopus 로고
    • Structure of heptameric protective antigen bound to an anthrax toxin receptor: a role for receptor in pH-dependent pore formation
    • Lacy D.B., Wigelsworth D.J., Melnyk R.A., Harrison S.C., and Collier R.J. Structure of heptameric protective antigen bound to an anthrax toxin receptor: a role for receptor in pH-dependent pore formation. Proc. Natl Acad. Sci. USA 101 (2004) 13147-13151
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 13147-13151
    • Lacy, D.B.1    Wigelsworth, D.J.2    Melnyk, R.A.3    Harrison, S.C.4    Collier, R.J.5
  • 9
    • 0022891493 scopus 로고
    • Macrophages are sensitive to anthrax lethal toxin through an acid-dependent process
    • Friedlander A.M. Macrophages are sensitive to anthrax lethal toxin through an acid-dependent process. J. Biol. Chem. 261 (1986) 7123-7126
    • (1986) J. Biol. Chem. , vol.261 , pp. 7123-7126
    • Friedlander, A.M.1
  • 10
    • 0024523836 scopus 로고
    • Anthrax toxin: channel-forming activity of protective antigen in planar phospholipid bilayers
    • Blaustein R.O., Koehler T.M., Collier R.J., and Finkelstein A. Anthrax toxin: channel-forming activity of protective antigen in planar phospholipid bilayers. Proc. Natl Acad. Sci. USA 86 (1989) 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
  • 11
    • 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. Protein translocation through the anthrax toxin transmembrane pore is driven by a proton gradient. J. Mol. Biol. 355 (2006) 968-979
    • (2006) J. Mol. Biol. , vol.355 , pp. 968-979
    • Krantz, B.A.1    Finkelstein, A.2    Collier, R.J.3
  • 12
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore
    • Song L., Hobaugh M.R., Shustak C., Cheley S., Bayley H., and Gouaux J.E. Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore. Science 274 (1996) 1859-1866
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 13
    • 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. Identification of residues lining the anthrax protective antigen channel. Biochemistry 37 (1998) 3941-3948
    • (1998) Biochemistry , vol.37 , pp. 3941-3948
    • Benson, E.L.1    Huynh, P.D.2    Finkelstein, A.3    Collier, R.J.4
  • 15
    • 0025244287 scopus 로고
    • Diffusion limitation in the block by symmetric tetraalkylammonium ions of anthrax toxin channels in planar phospholipid bilayer membranes
    • Blaustein R.O., and Finkelstein A. Diffusion limitation in the block by symmetric tetraalkylammonium ions of anthrax toxin channels in planar phospholipid bilayer membranes. J. Gen. Physiol. 96 (1990) 943-957
    • (1990) J. Gen. Physiol. , vol.96 , pp. 943-957
    • Blaustein, R.O.1    Finkelstein, A.2
  • 16
    • 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. Characterization of membrane translocation by anthrax protective antigen. Biochemistry 37 (1998) 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
  • 17
    • 10044281903 scopus 로고    scopus 로고
    • Protein translocation through anthrax toxin channels formed in planar lipid bilayers
    • Zhang S., Udho E., Wu Z., Collier R.J., and Finkelstein A. Protein translocation through anthrax toxin channels formed in planar lipid bilayers. Biophys. J. 87 (2004) 3842-3849
    • (2004) Biophys. J. , vol.87 , pp. 3842-3849
    • Zhang, S.1    Udho, E.2    Wu, Z.3    Collier, R.J.4    Finkelstein, A.5
  • 18
    • 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. Acid-induced unfolding of the amino-terminal domains of the lethal and edema factors of anthrax toxin. J. Mol. Biol. 344 (2004) 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
  • 19
    • 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., et al. A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore. Science 309 (2005) 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
  • 20
    • 0035097284 scopus 로고    scopus 로고
    • Involvement of domain 3 in oligomerization by the protective antigen moiety of anthrax toxin
    • Mogridge J., Mourez M., and Collier R.J. Involvement of domain 3 in oligomerization by the protective antigen moiety of anthrax toxin. J. Bacteriol. 183 (2001) 2111-2116
    • (2001) J. Bacteriol. , vol.183 , pp. 2111-2116
    • Mogridge, J.1    Mourez, M.2    Collier, R.J.3
  • 21
    • 0037076304 scopus 로고    scopus 로고
    • Mapping the lethal factor and edema factor binding sites on oligomeric anthrax protective antigen
    • Cunningham K., Lacy D.B., Mogridge J., and Collier R.J. Mapping the lethal factor and edema factor binding sites on oligomeric anthrax protective antigen. Proc. Natl Acad. Sci. USA 99 (2002) 7049-7053
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 7049-7053
    • Cunningham, K.1    Lacy, D.B.2    Mogridge, J.3    Collier, R.J.4
  • 22
    • 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. Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process. J. Cell Biol. 160 (2003) 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
  • 23
    • 58449092971 scopus 로고    scopus 로고
    • The cytoplasmic domain of anthrax toxin receptor 1 affects binding of the protective antigen
    • Go M.Y., Chow E.M., and Mogridge J. The cytoplasmic domain of anthrax toxin receptor 1 affects binding of the protective antigen. Infect. Immun. 77 (2009) 52-59
    • (2009) Infect. Immun. , vol.77 , pp. 52-59
    • Go, M.Y.1    Chow, E.M.2    Mogridge, J.3
  • 25
    • 22744450986 scopus 로고    scopus 로고
    • Anthrax toxin receptor 2 mediates Bacillus anthracis killing of macrophages following spore challenge
    • Banks D.J., Barnajian M., Maldonado-Arocho F.J., Sanchez A.M., and Bradley K.A. Anthrax toxin receptor 2 mediates Bacillus anthracis killing of macrophages following spore challenge. Cell Microbiol. 7 (2005) 1173-1185
    • (2005) Cell Microbiol. , vol.7 , pp. 1173-1185
    • Banks, D.J.1    Barnajian, M.2    Maldonado-Arocho, F.J.3    Sanchez, A.M.4    Bradley, K.A.5
  • 26
    • 0008658305 scopus 로고
    • Observations on the cause of death in experimental anthrax
    • Smith H., Keppie J., and Stanley J.L. Observations on the cause of death in experimental anthrax. Lancet 267 (1954) 474-476
    • (1954) Lancet , vol.267 , pp. 474-476
    • Smith, H.1    Keppie, J.2    Stanley, J.L.3
  • 28
    • 33745856268 scopus 로고    scopus 로고
    • Detection of anthrax toxin in the serum of animals infected with Bacillus anthracis by using engineered immunoassays
    • Mabry R., Brasky K., Geiger R., Carrion Jr. R., Hubbard G.B., Leppla S., et al. Detection of anthrax toxin in the serum of animals infected with Bacillus anthracis by using engineered immunoassays. Clin. Vaccine Immunol. 13 (2006) 671-677
    • (2006) Clin. Vaccine Immunol. , vol.13 , pp. 671-677
    • Mabry, R.1    Brasky, K.2    Geiger, R.3    Carrion Jr., R.4    Hubbard, G.B.5    Leppla, S.6
  • 29
    • 0014264785 scopus 로고
    • In vivo-produced anthrax toxin
    • Fish D.C., and Lincoln R.E. In vivo-produced anthrax toxin. J. Bacteriol. 95 (1968) 919-924
    • (1968) J. Bacteriol. , vol.95 , pp. 919-924
    • Fish, D.C.1    Lincoln, R.E.2
  • 30
    • 0025225339 scopus 로고
    • Voltage-dependent block of anthrax toxin channels in planar phospholipid bilayer membranes by symmetric tetraalkylammonium ions. Single-channel analysis
    • Blaustein R.O., Lea E.J., and Finkelstein A. Voltage-dependent block of anthrax toxin channels in planar phospholipid bilayer membranes by symmetric tetraalkylammonium ions. Single-channel analysis. J. Gen. Physiol. 96 (1990) 921-942
    • (1990) J. Gen. Physiol. , vol.96 , pp. 921-942
    • Blaustein, R.O.1    Lea, E.J.2    Finkelstein, A.3
  • 31
    • 0014254250 scopus 로고
    • Pharmacological modifications of the sodium channels of frog nerve
    • Hille B. Pharmacological modifications of the sodium channels of frog nerve. J. Gen. Physiol. 51 (1968) 199-219
    • (1968) J. Gen. Physiol. , vol.51 , pp. 199-219
    • Hille, B.1
  • 32
    • 34047224102 scopus 로고    scopus 로고
    • LRP5 and LRP6 are not required for protective antigen-mediated internalization or lethality of anthrax lethal toxin
    • Young J.J., Bromberg-White J.L., Zylstra C., Church J.T., Boguslawski E., and Resau J.H. LRP5 and LRP6 are not required for protective antigen-mediated internalization or lethality of anthrax lethal toxin. PLoS Pathogen 3 (2007) e27
    • (2007) PLoS Pathogen , vol.3
    • Young, J.J.1    Bromberg-White, J.L.2    Zylstra, C.3    Church, J.T.4    Boguslawski, E.5    Resau, J.H.6
  • 33
    • 0033543208 scopus 로고    scopus 로고
    • Anthrax protective antigen: prepore-to-pore conversion
    • Miller C.J., Elliott J.L., and Collier R.J. Anthrax protective antigen: prepore-to-pore conversion. Biochemistry 38 (1999) 10432-10441
    • (1999) Biochemistry , vol.38 , pp. 10432-10441
    • Miller, C.J.1    Elliott, J.L.2    Collier, R.J.3
  • 34
    • 3542993051 scopus 로고    scopus 로고
    • Crystal structure of a complex between anthrax toxin and its host cell receptor
    • Santelli E., Bankston L.A., Leppla S.H., and Liddington R.C. Crystal structure of a complex between anthrax toxin and its host cell receptor. Nature 430 (2004) 905-908
    • (2004) Nature , vol.430 , pp. 905-908
    • Santelli, E.1    Bankston, L.A.2    Leppla, S.H.3    Liddington, R.C.4
  • 35
    • 2542445481 scopus 로고    scopus 로고
    • Binding stoichiometry and kinetics of the interaction of a human anthrax toxin receptor, CMG2, with protective antigen
    • Wigelsworth D.J., Krantz B.A., Christensen K.A., Lacy D.B., Juris S.J., and Collier R.J. Binding stoichiometry and kinetics of the interaction of a human anthrax toxin receptor, CMG2, with protective antigen. J. Biol. Chem. 279 (2004) 23349-23356
    • (2004) J. Biol. Chem. , vol.279 , pp. 23349-23356
    • Wigelsworth, D.J.1    Krantz, B.A.2    Christensen, K.A.3    Lacy, D.B.4    Juris, S.J.5    Collier, R.J.6
  • 36
    • 0026794750 scopus 로고
    • Functional characterization of protease-treated Bacillus anthracis protective antigen
    • Novak J.M., Stein M.P., Little S.F., Leppla S.H., and Friedlander A.M. Functional characterization of protease-treated Bacillus anthracis protective antigen. J. Biol. Chem. 267 (1992) 17186-17193
    • (1992) J. Biol. Chem. , vol.267 , pp. 17186-17193
    • Novak, J.M.1    Stein, M.P.2    Little, S.F.3    Leppla, S.H.4    Friedlander, A.M.5
  • 37
    • 0002661972 scopus 로고
    • The anthrax toxin complex
    • Alouf J.E., and Freer J.H. (Eds), Academic Press, London
    • Leppla S.H. The anthrax toxin complex. In: Alouf J.E., and Freer J.H. (Eds). Sourcebook of Bacterial Protein Toxins (1991), Academic Press, London 277-302
    • (1991) Sourcebook of Bacterial Protein Toxins , pp. 277-302
    • Leppla, S.H.1
  • 38
    • 0029916264 scopus 로고    scopus 로고
    • Staphylococcal alpha-toxin, streptolysin-O, and Escherichia coli hemolysin: prototypes of pore-forming bacterial cytolysins
    • Bhakdi S., Bayley H., Valeva A., Walev I., Walker B., Kehoe M., and Palmer M. Staphylococcal alpha-toxin, streptolysin-O, and Escherichia coli hemolysin: prototypes of pore-forming bacterial cytolysins. Arch. Microbio. 165 (1996) 73-79
    • (1996) Arch. Microbio. , vol.165 , pp. 73-79
    • Bhakdi, S.1    Bayley, H.2    Valeva, A.3    Walev, I.4    Walker, B.5    Kehoe, M.6    Palmer, M.7
  • 40
    • 0026457115 scopus 로고
    • The Staphylococcus aureus alpha-toxin channel complex and the effect of Ca2+ ions on its interaction with lipid layers
    • Ward R.J., and Leonard K. The Staphylococcus aureus alpha-toxin channel complex and the effect of Ca2+ ions on its interaction with lipid layers. J. Struct. Biol. 109 (1992) 129-141
    • (1992) J. Struct. Biol. , vol.109 , pp. 129-141
    • Ward, R.J.1    Leonard, K.2
  • 41
    • 0024204145 scopus 로고
    • The projection structure of alpha-toxin from Staphylococcus aureus in human platelet membranes as analyzed by electron microscopy and image processing
    • Olofsson A., Kaveus U., Thelestam M., and Hebert H. The projection structure of alpha-toxin from Staphylococcus aureus in human platelet membranes as analyzed by electron microscopy and image processing. J. Ultrastruct. Mol. Struct. Res. 100 (1988) 194-200
    • (1988) J. Ultrastruct. Mol. Struct. Res. , vol.100 , pp. 194-200
    • Olofsson, A.1    Kaveus, U.2    Thelestam, M.3    Hebert, H.4
  • 42
    • 0032548897 scopus 로고    scopus 로고
    • Staphylococcal alpha-hemolysin can form hexamers in phospholipid bilayers
    • Czajkowsky D.M., Sheng S., and Shao Z. Staphylococcal alpha-hemolysin can form hexamers in phospholipid bilayers. J. Mol. Biol. 276 (1998) 325-330
    • (1998) J. Mol. Biol. , vol.276 , pp. 325-330
    • Czajkowsky, D.M.1    Sheng, S.2    Shao, Z.3
  • 43
    • 51649089665 scopus 로고    scopus 로고
    • Model-based prediction of the alpha-hemolysin structure in the hexameric state
    • Furini S., Domene C., Rossi M., Tartagni M., and Cavalcanti S. Model-based prediction of the alpha-hemolysin structure in the hexameric state. Biophys. J. 95 (2008) 2265-2274
    • (2008) Biophys. J. , vol.95 , pp. 2265-2274
    • Furini, S.1    Domene, C.2    Rossi, M.3    Tartagni, M.4    Cavalcanti, S.5
  • 44
    • 0028567173 scopus 로고
    • Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore
    • Gouaux J.E., Braha O., Hobaugh M.R., Song L., Cheley S., Shustak C., and Bayley H. Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore. Proc. Natl Acad. Sci. USA 91 (1994) 12828-12831
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 12828-12831
    • Gouaux, J.E.1    Braha, O.2    Hobaugh, M.R.3    Song, L.4    Cheley, S.5    Shustak, C.6    Bayley, H.7
  • 45
    • 34547510914 scopus 로고    scopus 로고
    • Membrane protein stoichiometry determined from the step-wise photobleaching of dye-labelled subunits
    • Das S.K., Darshi M., Cheley S., Wallace M.I., and Bayley H. Membrane protein stoichiometry determined from the step-wise photobleaching of dye-labelled subunits. Chembiochem 8 (2007) 994-999
    • (2007) Chembiochem , vol.8 , pp. 994-999
    • Das, S.K.1    Darshi, M.2    Cheley, S.3    Wallace, M.I.4    Bayley, H.5
  • 46
    • 33847705768 scopus 로고    scopus 로고
    • Insertion of anthrax protective antigen into liposomal membranes: effects of a receptor
    • Sun J., Vernier G., Wigelsworth D.J., and Collier R.J. Insertion of anthrax protective antigen into liposomal membranes: effects of a receptor. J. Biol. Chem. 282 (2007) 1059-1065
    • (2007) J. Biol. Chem. , vol.282 , pp. 1059-1065
    • Sun, J.1    Vernier, G.2    Wigelsworth, D.J.3    Collier, R.J.4
  • 47
    • 3843146246 scopus 로고    scopus 로고
    • An efficient one-step site-directed and site-saturation mutagenesis protocol
    • Zheng L., Baumann U., and Reymond J.L. An efficient one-step site-directed and site-saturation mutagenesis protocol. Nucleic Acids Res. 32 (2004) e115
    • (2004) Nucleic Acids Res. , vol.32
    • Zheng, L.1    Baumann, U.2    Reymond, J.L.3
  • 48
    • 0037169549 scopus 로고    scopus 로고
    • Mapping the anthrax protective antigen binding site on the lethal and edema factors
    • Lacy D.B., Mourez M., Fouassier A., and Collier R.J. Mapping the anthrax protective antigen binding site on the lethal and edema factors. J. Biol. Chem. 277 (2002) 3006-3010
    • (2002) J. Biol. Chem. , vol.277 , pp. 3006-3010
    • Lacy, D.B.1    Mourez, M.2    Fouassier, A.3    Collier, R.J.4
  • 49
    • 33947480633 scopus 로고
    • Methods for the formation of single bimolecular lipid membranes in aqueous solution
    • Mueller P., Rudin D.O., Tien H.T., and Westcott W.C. Methods for the formation of single bimolecular lipid membranes in aqueous solution. J. Phys. Chem. 67 (1963) 534-535
    • (1963) J. Phys. Chem. , vol.67 , pp. 534-535
    • Mueller, P.1    Rudin, D.O.2    Tien, H.T.3    Westcott, W.C.4
  • 50
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Ludtke S.J., Baldwin P.R., and Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128 (1999) 82-97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 51
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields
    • Frank J., Radermacher M., Penczek P., Zhu J., Li Y., Ladjadj M., and Leith A. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116 (1996) 190-199
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 54
    • 0742272143 scopus 로고    scopus 로고
    • Recognition and separation of single particles with size variation by statistical analysis of their images
    • White H.E., Saibil H.R., Ignatiou A., and Orlova E.V. Recognition and separation of single particles with size variation by statistical analysis of their images. J. Mol. Biol. 336 (2004) 453-460
    • (2004) J. Mol. Biol. , vol.336 , pp. 453-460
    • White, H.E.1    Saibil, H.R.2    Ignatiou, A.3    Orlova, E.V.4
  • 55
    • 0013159236 scopus 로고    scopus 로고
    • Cell surface tumor endothelium marker 8 cytoplasmic tail-independent anthrax toxin binding, proteolytic processing, oligomer formation, and internalization
    • Liu S., and Leppla S.H. Cell surface tumor endothelium marker 8 cytoplasmic tail-independent anthrax toxin binding, proteolytic processing, oligomer formation, and internalization. J. Biol. Chem. 278 (2003) 5227-5234
    • (2003) J. Biol. Chem. , vol.278 , pp. 5227-5234
    • Liu, S.1    Leppla, S.H.2
  • 57
    • 0026206788 scopus 로고
    • Sparse matrix sampling: A screening method for crystallization of proteins
    • Jancarik J., and Kim S.H. Sparse matrix sampling: A screening method for crystallization of proteins. J. Appl. Cryst. 24 (1991) 409-411
    • (1991) J. Appl. Cryst. , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.H.2
  • 58
    • 0017219062 scopus 로고
    • The growth and preliminary investigation of protein and nucleic acid crystals for X-ray diffraction analysis
    • McPherson Jr. A. The growth and preliminary investigation of protein and nucleic acid crystals for X-ray diffraction analysis. Methods Biochem. Anal. 23 (1976) 249-345
    • (1976) Methods Biochem. Anal. , vol.23 , pp. 249-345
    • McPherson Jr., A.1
  • 60
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Carter C.W., and Sweet R.M. (Eds), Academic Press, Inc., New York Macromolecular Crystallography, part A
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. In: Carter C.W., and Sweet R.M. (Eds). Methods in Enzymology Vol. 276 (1997), Academic Press, Inc., New York 307-326 Macromolecular Crystallography, part A
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 61
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 67
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26 (1993) 283-291
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 68
    • 0001528720 scopus 로고    scopus 로고
    • Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules
    • Fraczkiewicz R., and Braun W. Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules. J. Comp. Chem. 19 (1998) 319-333
    • (1998) J. Comp. Chem. , vol.19 , pp. 319-333
    • Fraczkiewicz, R.1    Braun, W.2
  • 69
    • 33748368713 scopus 로고    scopus 로고
    • Mass measurements of increased accuracy resolve heterogeneous populations of intact ribosomes
    • McKay A.R., Ruotolo B.T., Ilag L.L., and Robinson C.V. Mass measurements of increased accuracy resolve heterogeneous populations of intact ribosomes. J. Am. Chem. Soc. 128 (2006) 11433-11442
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 11433-11442
    • McKay, A.R.1    Ruotolo, B.T.2    Ilag, L.L.3    Robinson, C.V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.