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Volumn 44, Issue , 2004, Pages 167-193

Identification of the Major Steps in Botulinum Toxin Action

Author keywords

Acetylcholine; Airway epithelia; Endoprotease; Gut epithelia; Neuromuscular junction

Indexed keywords

ACETYLCHOLINE; BOTULINUM TOXIN; PROTEINASE; VACCINE;

EID: 1342323663     PISSN: 03621642     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.pharmtox.44.101802.121554     Document Type: Review
Times cited : (482)

References (132)
  • 1
    • 37049232988 scopus 로고
    • The most poisonous poison
    • Lamanna C. 1959. The most poisonous poison. Science 130:763-72
    • (1959) Science , vol.130 , pp. 763-772
    • Lamanna, C.1
  • 2
    • 0029122024 scopus 로고
    • Botulism: The present status of the disease
    • Hatheway CL. 1995. Botulism: the present status of the disease. Curr. Top. Microbiol. Immunol. 195:55-75
    • (1995) Curr. Top. Microbiol. Immunol. , vol.195 , pp. 55-75
    • Hatheway, C.L.1
  • 3
    • 0032145932 scopus 로고    scopus 로고
    • Botulism in the United States: A clinical and epidemiologic review
    • Shapiro RL, Hatheway C, Swerdlow DL. 1998. Botulism in the United States: a clinical and epidemiologic review. Ann. Intern. Med. 129:221-28
    • (1998) Ann. Intern. Med. , vol.129 , pp. 221-228
    • Shapiro, R.L.1    Hatheway, C.2    Swerdlow, D.L.3
  • 4
    • 0030851442 scopus 로고    scopus 로고
    • Clinical recognition and management of patients exposed to biological warfare agents
    • Franz DR, Jahrling PB, Friedlander AM, McClaine DJ, Hoover DL, et al. 1997. Clinical recognition and management of patients exposed to biological warfare agents. JAMA 278:399-411
    • (1997) JAMA , vol.278 , pp. 399-411
    • Franz, D.R.1    Jahrling, P.B.2    Friedlander, A.M.3    McClaine, D.J.4    Hoover, D.L.5
  • 6
    • 0036053928 scopus 로고    scopus 로고
    • Bioterrorism: From threat to reality
    • Atlas RM. 2002. Bioterrorism: from threat to reality. Annu. Rev. Microbiol. 56:167-85
    • (2002) Annu. Rev. Microbiol. , vol.56 , pp. 167-185
    • Atlas, R.M.1
  • 7
    • 0025857556 scopus 로고
    • Therapeutic uses of botulinum toxin
    • Jankovic J, Brin MF. 1991. Therapeutic uses of botulinum toxin. N. Engl. J. Med. 324:1186-94
    • (1991) N. Engl. J. Med. , vol.324 , pp. 1186-1194
    • Jankovic, J.1    Brin, M.F.2
  • 9
    • 0031086319 scopus 로고    scopus 로고
    • Botulinum toxin: The story of its development for the treatment of human disease
    • Schantz EJ, Johnson EA. 1997. Botulinum toxin: the story of its development for the treatment of human disease. Perspect. Biol. Med. 40:317-27
    • (1997) Perspect. Biol. Med. , vol.40 , pp. 317-327
    • Schantz, E.J.1    Johnson, E.A.2
  • 10
    • 0033812990 scopus 로고    scopus 로고
    • Pharmacotherapy with botulinum toxin: Harnessing nature's most potent neurotoxin
    • Bell MS, Vermeulen LC, Sperling KB. 2000. Pharmacotherapy with botulinum toxin: harnessing nature's most potent neurotoxin. Rev. Ther. 20:1079-91
    • (2000) Rev. Ther. , vol.20 , pp. 1079-1091
    • Bell, M.S.1    Vermeulen, L.C.2    Sperling, K.B.3
  • 12
    • 0032555584 scopus 로고    scopus 로고
    • Binding and transcytosis of botulinum toxin by polarized human colon carcinoma, cells
    • Maksymowych AB, Simpson LL. 1998. Binding and transcytosis of botulinum toxin by polarized human colon carcinoma, cells. J. Biol. Chem. 273:21950-57
    • (1998) J. Biol. Chem. , vol.273 , pp. 21950-21957
    • Maksymowych, A.B.1    Simpson, L.L.2
  • 13
    • 0037373083 scopus 로고    scopus 로고
    • Inhalational poisoning by botulinum toxin and inhalation vaccination with its heavy-chain component
    • Park JB, Simpson LL. 2003. Inhalational poisoning by botulinum toxin and inhalation vaccination with its heavy-chain component. Infect. Immun. 71:1147-54
    • (2003) Infect. Immun. , vol.71 , pp. 1147-1154
    • Park, J.B.1    Simpson, L.L.2
  • 14
    • 0018853111 scopus 로고
    • Kinetic studies on the interaction between botulinum toxin type A and the cholinergic neuromuscular junction
    • Simpson LL. 1980. Kinetic studies on the interaction between botulinum toxin type A and the cholinergic neuromuscular junction. J. Pharmacol. Exp. Ther. 213: 504-8
    • (1980) J. Pharmacol. Exp. Ther. , vol.213 , pp. 504-508
    • Simpson, L.L.1
  • 15
    • 0019619833 scopus 로고
    • The origin, structure and pharmacological activity of botulinum toxin
    • Simpson LL. 1981. The origin, structure and pharmacological activity of botulinum toxin. Pharmacol. Rev. 33:155-88
    • (1981) Pharmacol. Rev. , vol.33 , pp. 155-188
    • Simpson, L.L.1
  • 17
    • 0034121745 scopus 로고    scopus 로고
    • How botulinum and tetanus neurotoxins block neurotransmitter release
    • Humeau Y, Doussau F, Grant NJ, Poulain B. 2000. How botulinum and tetanus neurotoxins block neurotransmitter release. Biochimie 82:427-46
    • (2000) Biochimie , vol.82 , pp. 427-446
    • Humeau, Y.1    Doussau, F.2    Grant, N.J.3    Poulain, B.4
  • 19
    • 0033731911 scopus 로고    scopus 로고
    • Identification of the characteristics that underlie botulinum toxin potency: Implications for designing novel drugs
    • Simpson LL. 2000. Identification of the characteristics that underlie botulinum toxin potency: implications for designing novel drugs. Biochimie 82:943-53
    • (2000) Biochimie , vol.82 , pp. 943-953
    • Simpson, L.L.1
  • 20
    • 0008901811 scopus 로고
    • Serological subtypes of botulinal neurotoxins
    • ed. BR DasGupta. New York: Plenum
    • Gimenez DF, Gimenez JA. 1993. Serological subtypes of botulinal neurotoxins. In Botulinum and Tetanus Neurotoxins, ed. BR DasGupta, pp. 421-31. New York: Plenum
    • (1993) Botulinum and Tetanus Neurotoxins , pp. 421-431
    • Gimenez, D.F.1    Gimenez, J.A.2
  • 21
    • 0020286209 scopus 로고
    • Clostridium botulinum toxins
    • Sakaguchi G. 1983. Clostridium botulinum toxins. Pharmacol. Ther. 19:165-94
    • (1983) Pharmacol. Ther. , vol.19 , pp. 165-194
    • Sakaguchi, G.1
  • 22
    • 0029080131 scopus 로고
    • Molecular genetics of clostridial neurotoxins
    • Minton NP. 1995. Molecular genetics of clostridial neurotoxins. Curr. Top. Microbiol. Immunol. 195:161-94
    • (1995) Curr. Top. Microbiol. Immunol. , vol.195 , pp. 161-194
    • Minton, N.P.1
  • 23
    • 0028903373 scopus 로고
    • Structure and function of Clostridium botulinum toxins
    • Oguma K, Fujinaga Y, Inoue K. 1995. Structure and function of Clostridium botulinum toxins. Microbiol. Immunol. 39: 161-68
    • (1995) Microbiol. Immunol. , vol.39 , pp. 161-168
    • Oguma, K.1    Fujinaga, Y.2    Inoue, K.3
  • 24
    • 0033520494 scopus 로고    scopus 로고
    • Sequence homology and structural analysis of the clostridial neurotoxins
    • Lacy BD, Stevens RC. 1999. Sequence homology and structural analysis of the clostridial neurotoxins. J. Mol. Biol. 291: 1091-104
    • (1999) J. Mol. Biol. , vol.291 , pp. 1091-1104
    • Lacy, B.D.1    Stevens, R.C.2
  • 26
    • 1342339428 scopus 로고
    • Botulism: The present status of the disease
    • ed. C Montecucco. Berlin: Springer-Verlag
    • Hatheway CL. 1988. Botulism: the present status of the disease. In Clostridial Neurotoxins, ed. C Montecucco, pp. 55-75. Berlin: Springer-Verlag
    • (1988) Clostridial Neurotoxins , pp. 55-75
    • Hatheway, C.L.1
  • 27
    • 0022463687 scopus 로고
    • Clostridial neurotoxins: Handling and action at the cellular and molecular level
    • Habermann E, Dreyer F. 1986. Clostridial neurotoxins: handling and action at the cellular and molecular level. Curr. Top. Microbiol. Immunol. 129:94-179
    • (1986) Curr. Top. Microbiol. Immunol. , vol.129 , pp. 94-179
    • Habermann, E.1    Dreyer, F.2
  • 28
    • 0029074299 scopus 로고
    • Molecular aspects of tetanus and botulinum neurotoxin poisoning
    • Ahnert-Hilger G, Bigalke H. 1995. Molecular aspects of tetanus and botulinum neurotoxin poisoning. Prog. Neurobiol. 46:83-96
    • (1995) Prog. Neurobiol. , vol.46 , pp. 83-96
    • Ahnert-Hilger, G.1    Bigalke, H.2
  • 29
    • 0032692933 scopus 로고    scopus 로고
    • Retention of cleaved synaptosome-associated protein of 25 kDa (SNAP-25) in neuromuscular junctions: A new hypothesis to explain persistence of botulinum A poisoning
    • Raciborska DA, Charlton MP. 1999. Retention of cleaved synaptosome-associated protein of 25 kDa (SNAP-25) in neuromuscular junctions: a new hypothesis to explain persistence of botulinum A poisoning. Can. J. Pharmacol. 77:679-88
    • (1999) Can. J. Pharmacol. , vol.77 , pp. 679-688
    • Raciborska, D.A.1    Charlton, M.P.2
  • 30
    • 0035918270 scopus 로고    scopus 로고
    • The role of the synaptic protein SNAP-25 in the potency of botulinum neurotoxin type A
    • Keller JE, Neale EA. 2001. The role of the synaptic protein SNAP-25 in the potency of botulinum neurotoxin type A. J. Biol. Chem. 276:13476-82
    • (2001) J. Biol. Chem. , vol.276 , pp. 13476-13482
    • Keller, J.E.1    Neale, E.A.2
  • 31
    • 0037428398 scopus 로고    scopus 로고
    • Evaluation of the therapeutic usefulness of botulinum neurotoxin B, Cl, E, and F compared with the long lasting type A
    • Foran PG, Mohammed N, Lisk GO, Nagwaney S, Lawrence GW, et al. 2003. Evaluation of the therapeutic usefulness of botulinum neurotoxin B, Cl, E, and F compared with the long lasting type A. J. Biol. Chem. 278:1363-71
    • (2003) J. Biol. Chem. , vol.278 , pp. 1363-1371
    • Foran, P.G.1    Mohammed, N.2    Lisk, G.O.3    Nagwaney, S.4    Lawrence, G.W.5
  • 32
    • 0018881662 scopus 로고
    • Infant botulism
    • Amon SS. 1980. Infant botulism. Annu. Rev. Med. 31:541-60
    • (1980) Annu. Rev. Med. , vol.31 , pp. 541-560
    • Amon, S.S.1
  • 33
    • 0018871257 scopus 로고
    • Quantitative evidence of intestinal colonization by Clostridium botulinum in four cases of infant botulism
    • Wilcke BW, Midura TF, Amon SS. 1980. Quantitative evidence of intestinal colonization by Clostridium botulinum in four cases of infant botulism. J. Infect. Dis. 141:419-23
    • (1980) J. Infect. Dis. , vol.141 , pp. 419-423
    • Wilcke, B.W.1    Midura, T.F.2    Amon, S.S.3
  • 35
    • 0029958814 scopus 로고    scopus 로고
    • Update: Infant botulism
    • Midura TF. 1996. Update: infant botulism. Clin. Microbiol. Rev. 9:119-25
    • (1996) Clin. Microbiol. Rev. , vol.9 , pp. 119-125
    • Midura, T.F.1
  • 36
    • 0022632851 scopus 로고
    • Botulism in an adult associated with food-borne intestinal infection with Clostridium botulinum
    • Chia JK, Clark JB, Ryan CA, Pollack M. 1986. Botulism in an adult associated with food-borne intestinal infection with Clostridium botulinum. N. Engl. J. Med. 315:239-41
    • (1986) N. Engl. J. Med. , vol.315 , pp. 239-241
    • Chia, J.K.1    Clark, J.B.2    Ryan, C.A.3    Pollack, M.4
  • 37
    • 0031435919 scopus 로고    scopus 로고
    • The haemagglutinin of Clostridium botulinum type C progenitor toxin plays an essential role in binding of toxin to the epithelial cells of guinea pig small intestine, leading to the efficient absorption of the toxin
    • Fujinaga Y, Inoue K, Watanabe S, Yokota K, Hirai Y, et al. 1997. The haemagglutinin of Clostridium botulinum type C progenitor toxin plays an essential role in binding of toxin to the epithelial cells of guinea pig small intestine, leading to the efficient absorption of the toxin. Microbiology 143:3841-47
    • (1997) Microbiology , vol.143 , pp. 3841-3847
    • Fujinaga, Y.1    Inoue, K.2    Watanabe, S.3    Yokota, K.4    Hirai, Y.5
  • 38
    • 0033952269 scopus 로고    scopus 로고
    • Identification and characterization of functional subunits of Clostridium botulinum type A progenitor toxin involved in binding to intestinal microvilli and erythocytes
    • Fujinaga Y, Inoue K, Nomura T, Sasaki J, Marvaud JC, et al. 2000. Identification and characterization of functional subunits of Clostridium botulinum type A progenitor toxin involved in binding to intestinal microvilli and erythocytes. FEBS Lett. 467: 179-83
    • (2000) FEBS Lett. , vol.467 , pp. 179-183
    • Fujinaga, Y.1    Inoue, K.2    Nomura, T.3    Sasaki, J.4    Marvaud, J.C.5
  • 39
    • 0035043484 scopus 로고    scopus 로고
    • Clostridium botulinum type A haemagglutinin-positive progenitor toxin (HA+-PTX) binds to oligosaccharides containing Galβ1-4GlcNAc through one subcomponent of haemagglutinin (HA1)
    • Inoue K, Fujinaga Y, Honke K, Arimitsu H, Mahmut N, et al. 2001. Clostridium botulinum type A haemagglutinin-positive progenitor toxin (HA+-PTX) binds to oligosaccharides containing Galβ1-4GlcNAc through one subcomponent of haemagglutinin (HA1). Microbiology 147:811-19
    • (2001) Microbiology , vol.147 , pp. 811-819
    • Inoue, K.1    Fujinaga, Y.2    Honke, K.3    Arimitsu, H.4    Mahmut, N.5
  • 40
    • 0032767291 scopus 로고    scopus 로고
    • Pure botulinum neurotoxin is absorbed from the stomach and small intestine and produces peripheral neuromuscular blockade
    • Maksymowych AB, Reinhard M, Malizio CJ, Goodnough MC, Johnson EA, et al. 1999. Pure botulinum neurotoxin is absorbed from the stomach and small intestine and produces peripheral neuromuscular blockade. Infect. Immun. 67:4708-12
    • (1999) Infect. Immun. , vol.67 , pp. 4708-4712
    • Maksymowych, A.B.1    Reinhard, M.2    Malizio, C.J.3    Goodnough, M.C.4    Johnson, E.A.5
  • 44
    • 0038946003 scopus 로고    scopus 로고
    • Conversion by Peyer's Patch lymphocytes of human enterocytes into M Cells that transport bacteria
    • Kerneis S, Bogdanova A, Kraehenbuhl J-P, Pringault E. 1997. Conversion by Peyer's Patch lymphocytes of human enterocytes into M Cells that transport bacteria. Science 277:949-52
    • (1997) Science , vol.277 , pp. 949-952
    • Kerneis, S.1    Bogdanova, A.2    Kraehenbuhl, J.-P.3    Pringault, E.4
  • 45
    • 0029126079 scopus 로고
    • Immunodiagnosis and immunotherapy of tetanus and botulinum neurotoxins
    • Middlebrook JL, Brown JE. 1995. Immunodiagnosis and immunotherapy of tetanus and botulinum neurotoxins. Curr. Top. Microbiol. Immunol. 195:89-122
    • (1995) Curr. Top. Microbiol. Immunol. , vol.195 , pp. 89-122
    • Middlebrook, J.L.1    Brown, J.E.2
  • 46
    • 0033023671 scopus 로고    scopus 로고
    • Structure, activity, and immune (T and B cell) recognition of botulinum neurotoxins
    • Atassi MZ, Oshima M. 1999. Structure, activity, and immune (T and B cell) recognition of botulinum neurotoxins. Crit. Rev. Immunol. 19:219-60
    • (1999) Crit. Rev. Immunol. , vol.19 , pp. 219-260
    • Atassi, M.Z.1    Oshima, M.2
  • 47
    • 0033748727 scopus 로고    scopus 로고
    • Development of vaccines for prevention of botulism
    • Byrne MP, Smith LA. 2000. Development of vaccines for prevention of botulism. Biochimie 82:955-66
    • (2000) Biochimie , vol.82 , pp. 955-966
    • Byrne, M.P.1    Smith, L.A.2
  • 48
    • 0030734570 scopus 로고    scopus 로고
    • Induction of an immune response by oral administration of recombinant botulinum toxin
    • Kiyatkin N, Maksymowych AB, Simpson LL. 1997. Induction of an immune response by oral administration of recombinant botulinum toxin. Infect. Immun. 65:4586-91
    • (1997) Infect. Immun. , vol.65 , pp. 4586-4591
    • Kiyatkin, N.1    Maksymowych, A.B.2    Simpson, L.L.3
  • 49
    • 73849176950 scopus 로고
    • Botulisimus durch inhalation
    • Holzer VE. 1962. Botulisimus durch inhalation. Med. Klin. 57:1735-38
    • (1962) Med. Klin. , vol.57 , pp. 1735-1738
    • Holzer, V.E.1
  • 50
    • 0009666734 scopus 로고
    • The action of proteolytic enzymes on Clostridium botulinum type A toxin
    • Halliwell G. 1954. The action of proteolytic enzymes on Clostridium botulinum type A toxin. Biochem. J. 58:4-8
    • (1954) Biochem. J. , vol.58 , pp. 4-8
    • Halliwell, G.1
  • 51
    • 0021359806 scopus 로고
    • Oral toxicities of Clostridium botulinum type A and B toxins from different strains
    • Ohishi I. 1984. Oral toxicities of Clostridium botulinum type A and B toxins from different strains. Infect. Immun. 43:487-90
    • (1984) Infect. Immun. , vol.43 , pp. 487-490
    • Ohishi, I.1
  • 52
    • 0018861922 scopus 로고
    • Oral toxicities of Clostridium botulinum type C and D toxins of different molecular size
    • Ohishi I, Sakaguchi G. 1980. Oral toxicities of Clostridium botulinum type C and D toxins of different molecular size. Infect. Immun. 28:303-9
    • (1980) Infect. Immun. , vol.28 , pp. 303-309
    • Ohishi, I.1    Sakaguchi, G.2
  • 53
    • 0017579106 scopus 로고
    • Oral toxicities of Clostridium botulinum toxins in response to molecular size
    • Ohishi I, Sugii S, Sakaguchi G. 1977. Oral toxicities of Clostridium botulinum toxins in response to molecular size. Infect. Immun. 16:107-9
    • (1977) Infect. Immun. , vol.16 , pp. 107-109
    • Ohishi, I.1    Sugii, S.2    Sakaguchi, G.3
  • 54
    • 0017378439 scopus 로고
    • Intestinal absorption of botulinum toxins of different molecular sizes in rats
    • Sugii S, Ohishi I, Sakaguchi G. 1977. Intestinal absorption of botulinum toxins of different molecular sizes in rats. Infect. Immun. 17:491-96
    • (1977) Infect. Immun. , vol.17 , pp. 491-496
    • Sugii, S.1    Ohishi, I.2    Sakaguchi, G.3
  • 55
    • 0031866118 scopus 로고    scopus 로고
    • Biophysical characterization of the stability of the 150-kilodalton botulinum toxin, the nontoxic component, and the 900-kilodalton botulinum toxin complex species
    • Chen F, Kuziemko GM, Stevens RC. 1998. Biophysical characterization of the stability of the 150-kilodalton botulinum toxin, the nontoxic component, and the 900-kilodalton botulinum toxin complex species. Infect. Immun. 66:2420-25
    • (1998) Infect. Immun. , vol.66 , pp. 2420-2425
    • Chen, F.1    Kuziemko, G.M.2    Stevens, R.C.3
  • 56
    • 0002301979 scopus 로고
    • The action of botulinum toxin on the neuromuscular junction
    • Burgen ASV, Dickens F, Zatman LJ. 1949. The action of botulinum toxin on the neuromuscular junction. J. Physiol. 109:10-24
    • (1949) J. Physiol. , vol.109 , pp. 10-24
    • Burgen, A.S.V.1    Dickens, F.2    Zatman, L.J.3
  • 57
    • 0022556314 scopus 로고
    • 125I-labeled botulinum neurotoxins with nerve terminals. I. Ultrastructural autoradiograpic localization and quatitation of distinct membrane acceptors for types A and B on motor nerves
    • 125I-labeled botulinum neurotoxins with nerve terminals. I. Ultrastructural autoradiograpic localization and quatitation of distinct membrane acceptors for types A and B on motor nerves. J. Cell Biol. 103: 521-34
    • (1986) J. Cell Biol. , vol.103 , pp. 521-534
    • Black, J.D.1    Dolly, J.O.2
  • 58
    • 0022556315 scopus 로고
    • 125I-labeled botulinum neurotoxins with nerve terminals. II. Autoradiographic evidence for its uptake into motor nerves by acceptor-mediated endocytosis
    • 125I-labeled botulinum neurotoxins with nerve terminals. II. Autoradiographic evidence for its uptake into motor nerves by acceptor-mediated endocytosis. J. Cell Biol. 103:535-44
    • (1986) J. Cell Biol. , vol.103 , pp. 535-544
    • Black, J.D.1    Dolly, J.O.2
  • 59
    • 0015084187 scopus 로고
    • Ganglioside inactivation of botulinum toxin
    • Simpson LL, Rapport MM. 1971. Ganglioside inactivation of botulinum toxin. J. Neurochem. 18:1341-43
    • (1971) J. Neurochem. , vol.18 , pp. 1341-1343
    • Simpson, L.L.1    Rapport, M.M.2
  • 60
    • 0015126099 scopus 로고
    • The binding of botulinum toxin to membrane lipids: Sphingolipids, steroids, and fatty acids
    • Simpson LL, Rapport MM. 1971. The binding of botulinum toxin to membrane lipids: sphingolipids, steroids, and fatty acids. J. Neurochem. 18:1751-59
    • (1971) J. Neurochem. , vol.18 , pp. 1751-1759
    • Simpson, L.L.1    Rapport, M.M.2
  • 61
    • 0018867612 scopus 로고
    • Interaction between Clostridium botulinum neurotoxin and gangliosides
    • Kitamura M, Iwamori M, Nagai Y. 1980. Interaction between Clostridium botulinum neurotoxin and gangliosides. Biochim. Biophys. Acta 628:328-35
    • (1980) Biochim. Biophys. Acta , vol.628 , pp. 328-335
    • Kitamura, M.1    Iwamori, M.2    Nagai, Y.3
  • 64
  • 65
    • 0026337092 scopus 로고
    • Binding of botulinum and tetanus neurotoxins to gangliosides GT1b and derivatives thereof
    • Schengrund C-L, DasGupta BR, Ringler NJ. 1991. Binding of botulinum and tetanus neurotoxins to gangliosides GT1b and derivatives thereof. J. Neurochem. 57:1024-32
    • (1991) J. Neurochem. , vol.57 , pp. 1024-1032
    • Schengrund, C.-L.1    DasGupta, B.R.2    Ringler, N.J.3
  • 66
    • 0027516462 scopus 로고
    • Purification and characterization of the ganglioside-binding fragment of Clostridium botulinum type E neurotoxin
    • Kamata Y, Kimura Y, Hiroi T, Sakaguchi G, Kozaki S. 1993. Purification and characterization of the ganglioside-binding fragment of Clostridium botulinum type E neurotoxin. Biochim. Biophys. Acta 1156:213-18
    • (1993) Biochim. Biophys. Acta , vol.1156 , pp. 213-218
    • Kamata, Y.1    Kimura, Y.2    Hiroi, T.3    Sakaguchi, G.4    Kozaki, S.5
  • 67
    • 0030742486 scopus 로고    scopus 로고
    • Interaction between botulinum neurotoxin type A and ganglioside: Ganglioside inactivates the neurotoxin and quenches its tryptophan fluorescence
    • Kamata Y, Yoshimoto M, Kozaki S. 1997. Interaction between botulinum neurotoxin type A and ganglioside: ganglioside inactivates the neurotoxin and quenches its tryptophan fluorescence. Toxicon 35:1337-40
    • (1997) Toxicon , vol.35 , pp. 1337-1340
    • Kamata, Y.1    Yoshimoto, M.2    Kozaki, S.3
  • 68
    • 0031663156 scopus 로고    scopus 로고
    • Ganglioside GT1b as a complementary receptor component for Clostridium botulinum neurotoxins
    • Kozaki S, Kamata Y, Watarai S, Nishiki T, Mochida S. 1998. Ganglioside GT1b as a complementary receptor component for Clostridium botulinum neurotoxins. Microb. Pathog. 25:91-99
    • (1998) Microb. Pathog. , vol.25 , pp. 91-99
    • Kozaki, S.1    Kamata, Y.2    Watarai, S.3    Nishiki, T.4    Mochida, S.5
  • 69
    • 0025943451 scopus 로고
    • Lectins from triticum vulgaris and limax flavus are universal antagonists of botulinum neurotoxin and tetanus toxin
    • Bakry N, Kamata Y, Simpson LL. 1991. Lectins from triticum vulgaris and limax flavus are universal antagonists of botulinum neurotoxin and tetanus toxin . J. Pharmacol. Exp. Ther. 258:830-36
    • (1991) J. Pharmacol. Exp. Ther. , vol.258 , pp. 830-836
    • Bakry, N.1    Kamata, Y.2    Simpson, L.L.3
  • 70
    • 0032872478 scopus 로고    scopus 로고
    • Gangliosides are the binding substances in neural cells for tetanus and botulinum toxins in mice
    • Kitamura M, Takamiya K, Aizawa S, Furukawa K, Furukawa K. 1999. Gangliosides are the binding substances in neural cells for tetanus and botulinum toxins in mice. Biochim. Biophys. Acta 1441:1-3
    • (1999) Biochim. Biophys. Acta , vol.1441 , pp. 1-3
    • Kitamura, M.1    Takamiya, K.2    Aizawa, S.3    Furukawa, K.4    Furukawa, K.5
  • 71
    • 0037104801 scopus 로고    scopus 로고
    • Complex gangliosides at the neuromuscular junction are membrane receptors for autoantibodies and botulinum neurotoxin but redundant for normal synaptic function
    • Bullens RWM, O'Hanlon GM, Wagner E, Molenaar PC, Furukawa K, et al. 2002. Complex gangliosides at the neuromuscular junction are membrane receptors for autoantibodies and botulinum neurotoxin but redundant for normal synaptic function. J. Neurosci. 22:6876-84
    • (2002) J. Neurosci. , vol.22 , pp. 6876-6884
    • Bullens, R.W.M.1    O'Hanlon, G.M.2    Wagner, E.3    Molenaar, P.C.4    Furukawa, K.5
  • 72
    • 0037031826 scopus 로고    scopus 로고
    • Botulinum neurotoxin A activity is dependent upon the presence of specific gangliosides in neuroblastoma cells expressing synaptotagmin I
    • Yowler BC, Kensinger RD, Schengrund C-L. 2002. Botulinum neurotoxin A activity is dependent upon the presence of specific gangliosides in neuroblastoma cells expressing synaptotagmin I. J. Biol. Chem. 227:32815-19
    • (2002) J. Biol. Chem. , vol.227 , pp. 32815-32819
    • Yowler, B.C.1    Kensinger, R.D.2    Schengrund, C.-L.3
  • 73
    • 46149134882 scopus 로고
    • How do tetanus and botulinum toxins bind to neuronal membranes?
    • Montecucco C. 1986. How do tetanus and botulinum toxins bind to neuronal membranes? Trends Biochem. Sci. 11:315-17
    • (1986) Trends Biochem. Sci. , vol.11 , pp. 315-317
    • Montecucco, C.1
  • 74
    • 0002951890 scopus 로고
    • Cell surface receptors for protein toxins
    • ed. LL Simpson. San Diego: Academic
    • Middlebrook JL. 1989. Cell surface receptors for protein toxins. In Botulinum Neurotoxin and Tetanus Toxin, ed. LL Simpson, pp. 95-119. San Diego: Academic
    • (1989) Botulinum Neurotoxin and Tetanus Toxin , pp. 95-119
    • Middlebrook, J.L.1
  • 75
    • 0029863395 scopus 로고    scopus 로고
    • Productive and non-productive binding of botulinum neurotoxin A to motor nerve endings are distinguished by its heavy chain
    • Daniels-Holgate PU, Dolly JO. 1996. Productive and non-productive binding of botulinum neurotoxin A to motor nerve endings are distinguished by its heavy chain. J. Neurosci. Res. 44:263-71
    • (1996) J. Neurosci. Res. , vol.44 , pp. 263-271
    • Daniels-Holgate, P.U.1    Dolly, J.O.2
  • 76
    • 0032842847 scopus 로고    scopus 로고
    • Functional characterization of tetanus and botulinum neurotoxins binding domains
    • Lalli G, Herreros J, Osborne SL, Montecucco C, Rossetto O, et al. 1999. Functional characterization of tetanus and botulinum neurotoxins binding domains. J. Cell Sci. 112:2715-24
    • (1999) J. Cell Sci. , vol.112 , pp. 2715-2724
    • Lalli, G.1    Herreros, J.2    Osborne, S.L.3    Montecucco, C.4    Rossetto, O.5
  • 77
    • 0027486425 scopus 로고
    • Solubilization and characterization of the acceptor for Clostridum botulinum type B neurotoxin from rat brain synaptic membranes
    • Nishiki T, Ogasawara J, Kamata Y, Kozaki S. 1993. Solubilization and characterization of the acceptor for Clostridum botulinum type B neurotoxin from rat brain synaptic membranes. Biochim. Biophys. Acta 1158:333-38
    • (1993) Biochim. Biophys. Acta , vol.1158 , pp. 333-338
    • Nishiki, T.1    Ogasawara, J.2    Kamata, Y.3    Kozaki, S.4
  • 78
    • 0028341442 scopus 로고
    • Identification of protein receptor for Clostridium botulinum type B neurotoxin in rat brain synaptosomes
    • Nishiki T, Kamata Y, Nemoto Y, Omori A, Ito T, et al. 1994. Identification of protein receptor for Clostridium botulinum type B neurotoxin in rat brain synaptosomes. J. Biol. Chem. 269:10498-503
    • (1994) J. Biol. Chem. , vol.269 , pp. 10498-10503
    • Nishiki, T.1    Kamata, Y.2    Nemoto, Y.3    Omori, A.4    Ito, T.5
  • 79
    • 0029912989 scopus 로고    scopus 로고
    • Binding of botulinum type B neurotoxin to Chinese hamster ovary cells transfected with rat synaptotagmin II cDNA
    • Nishiki T, Tokuyama Y, Kamata Y, Nemoto Y, Yoshida A, et al. 1996. Binding of botulinum type B neurotoxin to Chinese hamster ovary cells transfected with rat synaptotagmin II cDNA. Neurosci. Lett. 208:105-8
    • (1996) Neurosci. Lett. , vol.208 , pp. 105-108
    • Nishiki, T.1    Tokuyama, Y.2    Kamata, Y.3    Nemoto, Y.4    Yoshida, A.5
  • 80
    • 0030064241 scopus 로고    scopus 로고
    • The high-affinity binding of Clostridium botulinum type B neurotoxin to synaptotagmin II associated with gangliosides GT1b/GD1a
    • 996
    • Nishiki T, Tokuyama Y, Kamata Y, Nemoto Y, Yoshida A, et al. 996. The high-affinity binding of Clostridium botulinum type B neurotoxin to synaptotagmin II associated with gangliosides GT1b/GD1a. FEBS Lett. 378:253-57
    • FEBS Lett. , vol.378 , pp. 253-257
    • Nishiki, T.1    Tokuyama, Y.2    Kamata, Y.3    Nemoto, Y.4    Yoshida, A.5
  • 81
    • 0031663156 scopus 로고    scopus 로고
    • Ganglioside GT1b as a complementary receptor component for Clostridium botulinum neurotoxins
    • Kozaki S, Kamata Y, Watarai S, Nishiki T, Mochida S. 1998. Ganglioside GT1b as a complementary receptor component for Clostridium botulinum neurotoxins Microb. Pathog. 25:91-99
    • (1998) Microb. Pathog. , vol.25 , pp. 91-99
    • Kozaki, S.1    Kamata, Y.2    Watarai, S.3    Nishiki, T.4    Mochida, S.5
  • 83
    • 0033884053 scopus 로고    scopus 로고
    • Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B
    • Swaminathan S, Eswaramoorthy S. 2000. Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B. Nat. Struct. Biol. 7:693-99
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 693-699
    • Swaminathan, S.1    Eswaramoorthy, S.2
  • 84
    • 0023717355 scopus 로고
    • Effects of pH on the binding of Clostridium botulinum type E derivative toxin to gangliosides and phospholipids
    • Kamata Y, Kozaki S, Sakaguchi G. 1988. Effects of pH on the binding of Clostridium botulinum type E derivative toxin to gangliosides and phospholipids. FEMS Microbiol. Lett. 55:71-76
    • (1988) FEMS Microbiol. Lett. , vol.55 , pp. 71-76
    • Kamata, Y.1    Kozaki, S.2    Sakaguchi, G.3
  • 86
    • 0034730834 scopus 로고    scopus 로고
    • Structure-based sequence alignment for the β-trefoil subdomain of the clostridial neurotoxin family provides residue level information about the putative ganglioside binding site
    • Ginalski K, Venclovas C, Lesyng B, Fidelis K. 2000. Structure-based sequence alignment for the β-trefoil subdomain of the clostridial neurotoxin family provides residue level information about the putative ganglioside binding site. FEBS Lett. 482:119-24
    • (2000) FEBS Lett. , vol.482 , pp. 119-124
    • Ginalski, K.1    Venclovas, C.2    Lesyng, B.3    Fidelis, K.4
  • 87
    • 0035937477 scopus 로고    scopus 로고
    • Tyrosine-1290 of tetanus neurotoxin plays a key role in its binding to gangliosides and functional binding to neurons
    • Sutton JM, Chow-Worn O, Spaven L, Silman NJ, Hallis B, et al. 2001. Tyrosine-1290 of tetanus neurotoxin plays a key role in its binding to gangliosides and functional binding to neurons. FEBS Lett. 493:45-49
    • (2001) FEBS Lett. , vol.493 , pp. 45-49
    • Sutton, J.M.1    Chow-Worn, O.2    Spaven, L.3    Silman, N.J.4    Hallis, B.5
  • 88
    • 0035943672 scopus 로고    scopus 로고
    • The crystal structure of tetanus toxin Hc fragment complexed with a synthetic GT1b analogue suggests cross-linking between ganglioside receptors and the toxin
    • Fotinou C, Emsley P, Black I, Andos H, Ishida H, et al. 2001. The crystal structure of tetanus toxin Hc fragment complexed with a synthetic GT1b analogue suggests cross-linking between ganglioside receptors and the toxin. J. Biol. Chem. 276:32274-81
    • (2001) J. Biol. Chem. , vol.276 , pp. 32274-32281
    • Fotinou, C.1    Emsley, P.2    Black, I.3    Andos, H.4    Ishida, H.5
  • 90
    • 0029925681 scopus 로고    scopus 로고
    • Neurotransmitter release
    • Matthews G. 1996. Neurotransmitter release. Annu. Rev. Neurosci. 19:219-33
    • (1996) Annu. Rev. Neurosci. , vol.19 , pp. 219-233
    • Matthews, G.1
  • 92
    • 0026719481 scopus 로고
    • Exo-endocytotic recycling of synaptic vesicles in developing processes of cultured hippocampal neurons
    • Matteoli M, Takei K, Perin MS, Sudhof TC, De Camilli P. 1992. Exo-endocytotic recycling of synaptic vesicles in developing processes of cultured hippocampal neurons. J. Cell Biol. 177:849-61
    • (1992) J. Cell Biol. , vol.177 , pp. 849-861
    • Matteoli, M.1    Takei, K.2    Perin, M.S.3    Sudhof, T.C.4    De Camilli, P.5
  • 93
    • 1342296932 scopus 로고    scopus 로고
    • Transport of toxins across intracellular membranes
    • ed. DL Burns, JT Barbier, BH Iglewski. Washington, DC: ASM
    • Sandvig K. 2003. Transport of toxins across intracellular membranes. In Bacterial Protein Toxins, ed. DL Burns, JT Barbier, BH Iglewski, pp. 157-72. Washington, DC: ASM
    • (2003) Bacterial Protein Toxins , pp. 157-172
    • Sandvig, K.1
  • 94
    • 0019956937 scopus 로고
    • The interaction between aminoquinolines and presynaptically acting neurotoxins
    • Simpson LL. 1982. The interaction between aminoquinolines and presynaptically acting neurotoxins. J. Pharmacol. Exp. Ther. 222:43-48
    • (1982) J. Pharmacol. Exp. Ther. , vol.222 , pp. 43-48
    • Simpson, L.L.1
  • 95
    • 0020522175 scopus 로고
    • Ammonium chloride and methylamine hydrochloride antagonize clostridial neurotoxins
    • Simpson LL. 1983. Ammonium chloride and methylamine hydrochloride antagonize clostridial neurotoxins. J. Pharmacol. Exp. Ther. 225:546-52
    • (1983) J. Pharmacol. Exp. Ther. , vol.225 , pp. 546-552
    • Simpson, L.L.1
  • 96
    • 0028293577 scopus 로고
    • Inhibition of vacuolar adenosine triphosphatase anatagonizes the effects of clostridial neurotoxins but not phospholipase A2 neurotoxins
    • Simpson LL, Coffield JA, Bakry N. 1994. Inhibition of vacuolar adenosine triphosphatase anatagonizes the effects of clostridial neurotoxins but not phospholipase A2 neurotoxins. J. Pharmacol. Exp. Ther. 269:256-62
    • (1994) J. Pharmacol. Exp. Ther. , vol.269 , pp. 256-262
    • Simpson, L.L.1    Coffield, J.A.2    Bakry, N.3
  • 97
    • 0345570658 scopus 로고
    • Channels formed by botulinum, tetanus, and diphtheria toxins in planar lipid bilayers: Relevance to translocation of proteins across membranes
    • Hoch DH, Romero-Mira M, Ehrlich BE, Finkelstein A, DasGupta BR, et al. 1985. Channels formed by botulinum, tetanus, and diphtheria toxins in planar lipid bilayers: relevance to translocation of proteins across membranes. Proc. Natl. Acad. Sci. USA 82:1692-96
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1692-1696
    • Hoch, D.H.1    Romero-Mira, M.2    Ehrlich, B.E.3    Finkelstein, A.4    DasGupta, B.R.5
  • 98
    • 0037222077 scopus 로고    scopus 로고
    • Translocation of botulinum neurotoxin light chain protease through the heavy chain channel
    • Koriazova LK, Montal M. 2003. Translocation of botulinum neurotoxin light chain protease through the heavy chain channel. Nat. Struct. Biol. 10:13-18
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 13-18
    • Koriazova, L.K.1    Montal, M.2
  • 99
    • 0035920221 scopus 로고    scopus 로고
    • The role of zinc binding in the biological activity of botulinum toxin
    • Simpson LL, Maksymowych AB, Hao S. 2001. The role of zinc binding in the biological activity of botulinum toxin. J. Biol. Chem. 276:27034-41
    • (2001) J. Biol. Chem. , vol.276 , pp. 27034-27041
    • Simpson, L.L.1    Maksymowych, A.B.2    Hao, S.3
  • 100
    • 0019191156 scopus 로고
    • The effects of botulinum toxin on the synthesis, storage and release of acetylcholine
    • Gundersen CB. 1980. The effects of botulinum toxin on the synthesis, storage and release of acetylcholine. Prog. Neurobiol. 14:99-119
    • (1980) Prog. Neurobiol. , vol.14 , pp. 99-119
    • Gundersen, C.B.1
  • 101
    • 0018884424 scopus 로고
    • Effects and mechanisms of polypeptide neurotoxins that act presynaptically
    • Howard BD, Gundersen CB Jr. 1980. Effects and mechanisms of polypeptide neurotoxins that act presynaptically. Annu. Rev. Pharmacol. Toxicol. 20:307-36
    • (1980) Annu. Rev. Pharmacol. Toxicol. , vol.20 , pp. 307-336
    • Howard, B.D.1    Gundersen Jr., C.B.2
  • 103
    • 0021209479 scopus 로고
    • Miniature end-plate potentials in rat skeletal muscle poisoned with botulinum toxin
    • Kim YI, Lomo T, Lupa MT, Thesleff S. 1984. Miniature end-plate potentials in rat skeletal muscle poisoned with botulinum toxin. J. Physiol. 356:587-99
    • (1984) J. Physiol. , vol.356 , pp. 587-599
    • Kim, Y.I.1    Lomo, T.2    Lupa, M.T.3    Thesleff, S.4
  • 104
    • 0023159095 scopus 로고
    • The effects of in vitro applications of purified botulinum neurotoxin at mouse motor nerve terminals
    • Dolly JO, Lande S, Wray DW. 1987. The effects of in vitro applications of purified botulinum neurotoxin at mouse motor nerve terminals. J. Physiol. 386:475-84
    • (1987) J. Physiol. , vol.386 , pp. 475-484
    • Dolly, J.O.1    Lande, S.2    Wray, D.W.3
  • 105
    • 0015123666 scopus 로고
    • The effect of type D botulinum toxin on frog neuromuscular junctions
    • Harris AJ, Miledi R. 1971. The effect of type D botulinum toxin on frog neuromuscular junctions. J. Physiol. 217:497-515
    • (1971) J. Physiol. , vol.217 , pp. 497-515
    • Harris, A.J.1    Miledi, R.2
  • 106
    • 0021052568 scopus 로고
    • Transmitter release in tetanus and botulinum A toxin-poisoned mammalian motor endplates and its dependence on nerve stimulation and temperature
    • Dreyer F, Schmitt A. 1983. Transmitter release in tetanus and botulinum A toxin-poisoned mammalian motor endplates and its dependence on nerve stimulation and temperature. Pflugers Arch. 399: 228-34
    • (1983) Pflugers Arch. , vol.399 , pp. 228-234
    • Dreyer, F.1    Schmitt, A.2
  • 107
    • 0020515818 scopus 로고
    • Different effects of types A and B botulinum toxin on transmitter release at the rat neuromuscular junction
    • Sellin LC, Thesleff S, DasGupta BR. 1983. Different effects of types A and B botulinum toxin on transmitter release at the rat neuromuscular junction. Acta Physiol. Scand. 119:127-33
    • (1983) Acta Physiol. Scand. , vol.119 , pp. 127-133
    • Sellin, L.C.1    Thesleff, S.2    DasGupta, B.R.3
  • 108
    • 0023180498 scopus 로고
    • Distinct sites of action of clostridium neurotoxins revealed by double-poisoning of mouse motor nerve terminals
    • Gansel M, Penner R, Dreyer F. 1987. Distinct sites of action of clostridium neurotoxins revealed by double-poisoning of mouse motor nerve terminals. Pflugers Arch. 409:533-39
    • (1987) Pflugers Arch. , vol.409 , pp. 533-539
    • Gansel, M.1    Penner, R.2    Dreyer, F.3
  • 109
    • 0024306217 scopus 로고
    • Characterization of the actions of botulinum neurotoxin type E at the rat neuromuscular junction
    • Molgo J, DasGupta BR, Thesleff S. 1989. Characterization of the actions of botulinum neurotoxin type E at the rat neuromuscular junction. Acta Physiol. Scand. 137:497-501
    • (1989) Acta Physiol. Scand. , vol.137 , pp. 497-501
    • Molgo, J.1    DasGupta, B.R.2    Thesleff, S.3
  • 110
    • 0024535487 scopus 로고
    • A study of synchronization of quantal transmitter release from mammalian motor endings by the use of botulinum toxins type A and D
    • Molgo J, Siegel LS, Tabti N, Thesleff S. 1989. A study of synchronization of quantal transmitter release from mammalian motor endings by the use of botulinum toxins type A and D. J. Physiol. 411:195-205
    • (1989) J. Physiol. , vol.411 , pp. 195-205
    • Molgo, J.1    Siegel, L.S.2    Tabti, N.3    Thesleff, S.4
  • 111
    • 0017141174 scopus 로고
    • Botulinum toxin: Mechanism of presyanptic blockade
    • Kao I, Drachman DB, Price DL. 1976. Botulinum toxin: mechanism of presyanptic blockade. Science 193:1256-58
    • (1976) Science , vol.193 , pp. 1256-1258
    • Kao, I.1    Drachman, D.B.2    Price, D.L.3
  • 112
    • 0023101807 scopus 로고
    • Differential effects of various secretagogues on equantal transmitter release from mouse motor nerve terminals treated with botulinum A and tetanus toxin
    • Dreyer F, Rosenberg F, Becker C, Bigalke H, Penner R. 1987. Differential effects of various secretagogues on equantal transmitter release from mouse motor nerve terminals treated with botulinum A and tetanus toxin. Naunyn-Schmiedebergs Arch. Pharmacol. 335:1-7
    • (1987) Naunyn-Schmiedebergs Arch. Pharmacol. , vol.335 , pp. 1-7
    • Dreyer, F.1    Rosenberg, F.2    Becker, C.3    Bigalke, H.4    Penner, R.5
  • 113
    • 0025314995 scopus 로고
    • The complete sequence of botulinum neurotoxin type A and comparison with other clostridial neurotoxins
    • Binz T, Kurazono H, Wille M, Frevert J, Wernars K, et al. 1990. The complete sequence of botulinum neurotoxin type A and comparison with other clostridial neurotoxins. J. Biol. Chem. 265:9153-58
    • (1990) J. Biol. Chem. , vol.265 , pp. 9153-9158
    • Binz, T.1    Kurazono, H.2    Wille, M.3    Frevert, J.4    Wernars, K.5
  • 114
    • 0025319832 scopus 로고
    • The complete amino acid sequence of the Clostridium botulinum type A neurotoxin, deduced by nucleotide sequence analysis of the encoding gene
    • Thompson DE, Brehm JK, Oultram JD, Swinfield T-J, Shone CC, et al. 1990. The complete amino acid sequence of the Clostridium botulinum type A neurotoxin, deduced by nucleotide sequence analysis of the encoding gene. Eur. J. Biochem. 189:73-81
    • (1990) Eur. J. Biochem. , vol.189 , pp. 73-81
    • Thompson, D.E.1    Brehm, J.K.2    Oultram, J.D.3    Swinfield, T.-J.4    Shone, C.C.5
  • 115
    • 0026721240 scopus 로고
    • Molecular cloning of the Clostridum botulinum structural gene encoding the type B neurotoxin and determination of its entire nucleotide sequence
    • Whelan SM, Elmore MJ, Bodsworth NJ, Brehm JK, Atkinson T, et al. 1992. Molecular cloning of the Clostridum botulinum structural gene encoding the type B neurotoxin and determination of its entire nucleotide sequence. Appl. Environ. Microbiol. 58:2345-54
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 2345-2354
    • Whelan, S.M.1    Elmore, M.J.2    Bodsworth, N.J.3    Brehm, J.K.4    Atkinson, T.5
  • 116
    • 0026497466 scopus 로고
    • Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin
    • Schiavo G, Benfenati F, Poulain B, Rossetto O, Polverino de Laureto P, et al. 1992. Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin. Nature 359:832-35
    • (1992) Nature , vol.359 , pp. 832-835
    • Schiavo, G.1    Benfenati, F.2    Poulain, B.3    Rossetto, O.4    Polverino De Laureto, P.5
  • 117
    • 0027219725 scopus 로고
    • Botulinum neurotoxin A selectively cleaves the synaptic protein SNAP-25
    • Blasi J, Chapman ER, Link E, Binz T, Yamasaki S, et al. 1993. Botulinum neurotoxin A selectively cleaves the synaptic protein SNAP-25. Nature 365:160-63
    • (1993) Nature , vol.365 , pp. 160-163
    • Blasi, J.1    Chapman, E.R.2    Link, E.3    Binz, T.4    Yamasaki, S.5
  • 118
    • 0027432376 scopus 로고
    • Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC-1/syntaxin
    • Blasi J, Chapman ER, Yamasaki S, Binz T, Niemann H, et al. 1993. Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC-1/syntaxin. EMBO J. 12:4821-28
    • (1993) EMBO J. , vol.12 , pp. 4821-4828
    • Blasi, J.1    Chapman, E.R.2    Yamasaki, S.3    Binz, T.4    Niemann, H.5
  • 119
  • 120
    • 0028069674 scopus 로고
    • Proteolysis of SNAP-25 by types E and A botulinal neurotoxins
    • Binz T, Blasi J, Yamasaki S, Baumeister A, Link E, et al. 1993. Proteolysis of SNAP-25 by types E and A botulinal neurotoxins. J. Biol. Chem. 269:1617-20
    • (1993) J. Biol. Chem. , vol.269 , pp. 1617-1620
    • Binz, T.1    Blasi, J.2    Yamasaki, S.3    Baumeister, A.4    Link, E.5
  • 122
    • 0028199063 scopus 로고
    • Cleavage of members of the synaptobrevin/VAMP family by types D and F botulinal neurotoxins and tetanus toxin
    • Yamasaki S, Baumeister A, Binz T, Blasi J, Link E, et al. 1994. Cleavage of members of the synaptobrevin/VAMP family by types D and F botulinal neurotoxins and tetanus toxin. J. Biol. Chem. 269: 12764-72
    • (1994) J. Biol. Chem. , vol.269 , pp. 12764-12772
    • Yamasaki, S.1    Baumeister, A.2    Binz, T.3    Blasi, J.4    Link, E.5
  • 124
    • 0029874232 scopus 로고    scopus 로고
    • Botulinum neurotoxin C1 cleaves both syntaxin and SNAP-25 in intact and permeabilized chromaffin cells: Correlation with its blockade of catecholamine release
    • Foran P, Lawrence GW, Shone CC, Foster KA, Dolly JO. 1996. Botulinum neurotoxin C1 cleaves both syntaxin and SNAP-25 in intact and permeabilized chromaffin cells: correlation with its blockade of catecholamine release. Biochemistry 35:2630-36
    • (1996) Biochemistry , vol.35 , pp. 2630-2636
    • Foran, P.1    Lawrence, G.W.2    Shone, C.C.3    Foster, K.A.4    Dolly, J.O.5
  • 127
    • 0032515187 scopus 로고    scopus 로고
    • Different time courses of recovery after poisoning with botulinum neurotoxin serotypes A and E in humans
    • Eleopra R, Tungnoli V, Rossetto O, De Grandis D, Montecucco C. 1998. Different time courses of recovery after poisoning with botulinum neurotoxin serotypes A and E in humans. Neurosci. Lett. 256:135-38
    • (1998) Neurosci. Lett. , vol.256 , pp. 135-138
    • Eleopra, R.1    Tungnoli, V.2    Rossetto, O.3    De Grandis, D.4    Montecucco, C.5
  • 128
    • 0032776446 scopus 로고    scopus 로고
    • Persistence of botulinum neurotoxin action in cultured spinal cord cells
    • Keller JE, Neale EA, Oyler G, Adler M. 1999. Persistence of botulinum neurotoxin action in cultured spinal cord cells. FEBS Lett. 456:137-42
    • (1999) FEBS Lett. , vol.456 , pp. 137-142
    • Keller, J.E.1    Neale, E.A.2    Oyler, G.3    Adler, M.4
  • 129
    • 0034598654 scopus 로고    scopus 로고
    • Persistence of botulinum neurotoxin A demonstrated by sequential administration of serotypes A and E in rat EDL muscle
    • Adler M, Keller JE, Sheridan RE, Deshpande SS. 2001. Persistence of botulinum neurotoxin A demonstrated by sequential administration of serotypes A and E in rat EDL muscle. Toxicon 39:233-43
    • (2001) Toxicon , vol.39 , pp. 233-243
    • Adler, M.1    Keller, J.E.2    Sheridan, R.E.3    Deshpande, S.S.4
  • 130
    • 0037396608 scopus 로고    scopus 로고
    • Dynamics of motor nerve terminal remodeling unveiled using SNARE-cleaving botulinum toxins: The extent and duration are dictated by the sites of SNAP-25 truncation
    • Meunier FA, Lisk G, Sesardic D, Dolly JO. 2003. Dynamics of motor nerve terminal remodeling unveiled using SNARE-cleaving botulinum toxins: the extent and duration are dictated by the sites of SNAP-25 truncation. Mol. Cell. Neurosci. 22:1-13
    • (2003) Mol. Cell. Neurosci. , vol.22 , pp. 1-13
    • Meunier, F.A.1    Lisk, G.2    Sesardic, D.3    Dolly, J.O.4
  • 131
    • 0026769405 scopus 로고
    • Minimal essential domains specifying toxicity of the light chains of tetanus toxin and botulinum neurotoxin type A
    • Kuranzono H, Mochida S, Binz T, Eisel U, Quanz M, et al. 1992. Minimal essential domains specifying toxicity of the light chains of tetanus toxin and botulinum neurotoxin type A. J. Biol. Chem. 267:14721-29
    • (1992) J. Biol. Chem. , vol.267 , pp. 14721-14729
    • Kuranzono, H.1    Mochida, S.2    Binz, T.3    Eisel, U.4    Quanz, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.