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Volumn 39, Issue 1, 2001, Pages 27-41

Tetanus and botulinum neurotoxins: Turning bad guys into good by research

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCHOLINE; BOTULINUM TOXIN; BOTULINUM TOXIN A; BOTULINUM TOXIN B; BOTULINUM TOXIN C; BOTULINUM TOXIN D; BOTULINUM TOXIN E; BOTULINUM TOXIN F; BOTULINUM TOXIN G; METALLOPROTEINASE; NERVE PROTEIN; NEUROTOXIN; SYNAPTOBREVIN; SYNAPTOSOME ASSOCIATED PROTEIN; TETANUS TOXIN; UNCLASSIFIED DRUG;

EID: 0035239239     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0041-0101(00)00163-X     Document Type: Short Survey
Times cited : (153)

References (168)
  • 1
    • 0025151085 scopus 로고
    • Terminal sprouting in mouse neuromuscular junctions poisoned with botulinum type A toxin: Morphological and electrophysiological features
    • Angaut-Petit D., Molgo J., Comella J.X., Faille L., Tabti N. Terminal sprouting in mouse neuromuscular junctions poisoned with botulinum type A toxin: morphological and electrophysiological features. Neuroscience. 37:1990;799-808.
    • (1990) Neuroscience , vol.37 , pp. 799-808
    • Angaut-Petit, D.1    Molgo, J.2    Comella, J.X.3    Faille, L.4    Tabti, N.5
  • 2
    • 0025936145 scopus 로고
    • Tetanus toxin and neuronal membranes: The relationship between binding and neurotoxicity
    • Bakry N., Kamata Y., Sorensen R., Simson L.L. Tetanus toxin and neuronal membranes: the relationship between binding and neurotoxicity. J. Pharmacol. Exp. Ther. 258:1991;613-619.
    • (1991) J. Pharmacol. Exp. Ther. , vol.258 , pp. 613-619
    • Bakry, N.1    Kamata, Y.2    Sorensen, R.3    Simson, L.L.4
  • 4
    • 0028176426 scopus 로고
    • 2+-binding domain of clostridial neurotoxins restore exocytosis in chromaffin cells treated with tetanus or botulinum A neurotoxin
    • 2+-binding domain of clostridial neurotoxins restore exocytosis in chromaffin cells treated with tetanus or botulinum A neurotoxin. J. Biol. Chem. 269:1994;8122-8127.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8122-8127
    • Bartels, F.1    Bergel, H.2    Bigalke, H.3    Frevert, J.4    Halpern, J.5    Middlebrook, J.6
  • 5
    • 0028040137 scopus 로고
    • Pore formation by tetanus toxin, its chain and fragments in neuronal membranes and evaluation of the underlying motifs in the structure of the toxin molecule
    • Beise J., Hahnen J., Andersen-Beckh B., Dreyer F. Pore formation by tetanus toxin, its chain and fragments in neuronal membranes and evaluation of the underlying motifs in the structure of the toxin molecule. Naunyn Schemiedebergs Arch. Pharmacol. 349:1994;66-73.
    • (1994) Naunyn Schemiedebergs Arch. Pharmacol. , vol.349 , pp. 66-73
    • Beise, J.1    Hahnen, J.2    Andersen-Beckh, B.3    Dreyer, F.4
  • 8
    • 0022556315 scopus 로고
    • 125I -labeled botulinum neurotoxins with nerve terminals. Part II: Autoradiographic evidence for its uptake into motor nerves by acceptor-mediated endocytosis
    • 125I -labeled botulinum neurotoxins with nerve terminals. Part II: Autoradiographic evidence for its uptake into motor nerves by acceptor-mediated endocytosis. J. Cell Biol. 103:1986;535-544.
    • (1986) J. Cell Biol. , vol.103 , pp. 535-544
    • Black, J.D.1    Dolly, J.O.2
  • 10
    • 0027432376 scopus 로고
    • Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC-1/syntaxin
    • Blasi J., Chapman E.R., Yamasaki S., Binz T., Niemann H., Jahn R. Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC-1/syntaxin. EMBO J. 12:1993;4821-4828.
    • (1993) EMBO J. , vol.12 , pp. 4821-4828
    • Blasi, J.1    Chapman, E.R.2    Yamasaki, S.3    Binz, T.4    Niemann, H.5    Jahn, R.6
  • 11
    • 0023662110 scopus 로고
    • The N-terminal half of the heavy chain of botulinum type A neurotoxin forms channels in planar phospholipid bilayers
    • Blaustein R.O., Germann W.J., Finkelstein A., DasGupta B.R. The N-terminal half of the heavy chain of botulinum type A neurotoxin forms channels in planar phospholipid bilayers. FEBS Lett. 226:1987;115-120.
    • (1987) FEBS Lett. , vol.226 , pp. 115-120
    • Blaustein, R.O.1    Germann, W.J.2    Finkelstein, A.3    Dasgupta, B.R.4
  • 12
    • 0343155399 scopus 로고
    • Mode of action of tetanus toxin
    • Brooks V.B., Curtis D.R., Eccles J.C. Mode of action of tetanus toxin. Nature. 175:1955;120-121.
    • (1955) Nature , vol.175 , pp. 120-121
    • Brooks, V.B.1    Curtis, D.R.2    Eccles, J.C.3
  • 13
    • 0033607288 scopus 로고    scopus 로고
    • SNARE proteins mediate lipid bilayer fusion
    • Bock J.B., Scheller R.H. SNARE proteins mediate lipid bilayer fusion. Proc. Natl. Acad. Sci. USA. 96:1999;12227-12229.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12227-12229
    • Bock, J.B.1    Scheller, R.H.2
  • 14
    • 0002929018 scopus 로고
    • Pharmacology and histology of the therapeutic application of botulinum toxin
    • J. Jankovic, & M. Hallett. New York: Marcel Dekker
    • Borodic G.E., Ferrante R.J., Perace L.B., Alderson K. Pharmacology and histology of the therapeutic application of botulinum toxin. Jankovic J., Hallett M. Therapy with Botulinum Toxin. 1994;119-157 Marcel Dekker, New York.
    • (1994) Therapy with Botulinum Toxin , pp. 119-157
    • Borodic, G.E.1    Ferrante, R.J.2    Perace, L.B.3    Alderson, K.4
  • 15
    • 0020368289 scopus 로고
    • Tetanus toxin fragment forms channels in lipid vesicles at low pH
    • Boquet P., Duflot E. Tetanus toxin fragment forms channels in lipid vesicles at low pH. Proc. Natl. Acad. Sci. USA. 79:1982;7614-7618.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 7614-7618
    • Boquet, P.1    Duflot, E.2
  • 16
    • 0002301979 scopus 로고
    • The action of botulinum toxin on the neuromuscular junction
    • Burgen A.S.V., Dickens F., Zatman L.J. The action of botulinum toxin on the neuromuscular junction. J. Phisiol. (Lond.). 109:1949;10-24.
    • (1949) J. Phisiol. (Lond.) , vol.109 , pp. 10-24
    • Burgen, A.S.V.1    Dickens, F.2    Zatman, L.J.3
  • 18
    • 0342285706 scopus 로고
    • Studio sperimentale sull'eziologia del tetano
    • Carle A., Rattone G. Studio sperimentale sull'eziologia del tetano. Giorn. Accad. Med. Torino. 32:1884;174-179.
    • (1884) Giorn. Accad. Med. Torino. , vol.32 , pp. 174-179
    • Carle, A.1    Rattone, G.2
  • 20
    • 0030740254 scopus 로고    scopus 로고
    • Construction of hybrid proteins that migrate retrogradely and transsynaptically into the central nervous system
    • Coen L., Osta R., Maury M., Brulet P. Construction of hybrid proteins that migrate retrogradely and transsynaptically into the central nervous system. Proc. Natl. Acad. Sci. USA. 94:1997;9400-9405.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9400-9405
    • Coen, L.1    Osta, R.2    Maury, M.3    Brulet, P.4
  • 21
    • 0032995728 scopus 로고    scopus 로고
    • Characterization of a vertebrate neuromuscular junction that demonstrates selective resistance to botulinum toxin
    • Coffield J.A., Bakry N.M., Maksymowych A.B., Simpson L.L. Characterization of a vertebrate neuromuscular junction that demonstrates selective resistance to botulinum toxin. J. Pharmacol. Exp. Ther. 289:1999;1509-1516.
    • (1999) J. Pharmacol. Exp. Ther. , vol.289 , pp. 1509-1516
    • Coffield, J.A.1    Bakry, N.M.2    Maksymowych, A.B.3    Simpson, L.L.4
  • 22
    • 0027298449 scopus 로고
    • Sprouting of mammalian motor nerve terminals induced by in vivo injection of botulinum type-D toxin and the functional recovery of paralysed neuromuscular junctions
    • Comella J.X., Molgo J., Faille L. Sprouting of mammalian motor nerve terminals induced by in vivo injection of botulinum type-D toxin and the functional recovery of paralysed neuromuscular junctions. Neurosci. Lett. 153:1993;61-64.
    • (1993) Neurosci. Lett. , vol.153 , pp. 61-64
    • Comella, J.X.1    Molgo, J.2    Faille, L.3
  • 23
    • 0028359504 scopus 로고
    • Solid-phase synthesis, conformational analysis and in vitro cleavage of synthetic human synaptobrevin II 1-93 by tetanus toxin L chain
    • Cornille F., Goudreau N., Ficheux D., Niemann H., Roques B.P. Solid-phase synthesis, conformational analysis and in vitro cleavage of synthetic human synaptobrevin II 1-93 by tetanus toxin L chain. Eur. J. Biochem. 222:1994;173-181.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 173-181
    • Cornille, F.1    Goudreau, N.2    Ficheux, D.3    Niemann, H.4    Roques, B.P.5
  • 24
    • 0029041786 scopus 로고
    • Inhibition of neurotransmitter release by synthetic proline-rich peptides shows that the N-terminal domain of vesicle-associated membrane protein/synaptobrevin is critical for neuroexocytosis
    • Cornille F., Deloye F., Fournie-Zaluski M.C., Roques B.P., Poulain B. Inhibition of neurotransmitter release by synthetic proline-rich peptides shows that the N-terminal domain of vesicle-associated membrane protein/synaptobrevin is critical for neuroexocytosis. J. Biol. Chem. 270:1995;16826-16832.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16826-16832
    • Cornille, F.1    Deloye, F.2    Fournie-Zaluski, M.C.3    Roques, B.P.4    Poulain, B.5
  • 27
    • 0033594949 scopus 로고    scopus 로고
    • A single amino acid near the C terminus of the synaptosome associated protein of 25 kDa (SNAP-25) is essential for exocytosis in chromaffin cells
    • Criado M., Gil A., Viniegra S., Gutierrez L.M. A single amino acid near the C terminus of the synaptosome associated protein of 25 kDa (SNAP-25) is essential for exocytosis in chromaffin cells. Proc. Natl. Acad. Sci. USA. 96:1999;7256-7261.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7256-7261
    • Criado, M.1    Gil, A.2    Viniegra, S.3    Gutierrez, L.M.4
  • 28
    • 0021912250 scopus 로고
    • Fate of tetanus toxin bound to the surface of primary neurons in culture: Evidence for rapid internalization
    • Critchley D.R., Nelson P.G., Habig W.H., Fishman P.H. Fate of tetanus toxin bound to the surface of primary neurons in culture: evidence for rapid internalization. J. Cell. Biol. 100:1985;1499-1507.
    • (1985) J. Cell. Biol. , vol.100 , pp. 1499-1507
    • Critchley, D.R.1    Nelson, P.G.2    Habig, W.H.3    Fishman, P.H.4
  • 29
    • 0002592605 scopus 로고
    • Structures of botulinum neurotoxin, its functional domains, and perspectives on the cristalline type A toxin
    • J. Jankovic, & M. Hallett. New York: Marcel Dekker
    • Das Gupta B.R. Structures of botulinum neurotoxin, its functional domains, and perspectives on the cristalline type A toxin. Jankovic J., Hallett M. Therapy with Botulinum Toxin. 1994;15-39 Marcel Dekker, New York.
    • (1994) Therapy with Botulinum Toxin , pp. 15-39
    • Das Gupta, B.R.1
  • 31
    • 0027434988 scopus 로고
    • Botulinum A like type B and tetanus toxins fulfils criteria for being a zinc-dependent protease
    • de Paiva A., Ashton A.C., Foran P., Schiavo G., Montecucco C., Dolly J.O. Botulinum A like type B and tetanus toxins fulfils criteria for being a zinc-dependent protease. J. Neurochem. 61:1993;2338-2341.
    • (1993) J. Neurochem. , vol.61 , pp. 2338-2341
    • De Paiva, A.1    Ashton, A.C.2    Foran, P.3    Schiavo, G.4    Montecucco, C.5    Dolly, J.O.6
  • 32
    • 0033055065 scopus 로고    scopus 로고
    • Functional repair of motor endplates after botulinum neurotoxin type A poisoning: Biphasic switch of synaptic activity between nerve sprouts and their parents terminals
    • de Paiva A., Meunier F.A., Molgo J., Aoki K.R., Dolly J.O. Functional repair of motor endplates after botulinum neurotoxin type A poisoning: biphasic switch of synaptic activity between nerve sprouts and their parents terminals. Proc. Natl. Acad. Sci. USA. 96:1999;3200-3205.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3200-3205
    • De Paiva, A.1    Meunier, F.A.2    Molgo, J.3    Aoki, K.R.4    Dolly, J.O.5
  • 33
    • 0021243873 scopus 로고
    • Acceptors for botulinum neurotoxin reside on motor nerve terminals and mediate its internalization
    • Dolly J.O., Black J., Williams R.S., Melling J. Acceptors for botulinum neurotoxin reside on motor nerve terminals and mediate its internalization. Nature. 307:1984;457-460.
    • (1984) Nature , vol.307 , pp. 457-460
    • Dolly, J.O.1    Black, J.2    Williams, R.S.3    Melling, J.4
  • 34
    • 0027201146 scopus 로고
    • Tetanus toxin light chain expression in Sertoli cells of transgenic mice causes alterations of the actin cytoskeleton and disrupts spermatogenesis
    • Eisel U., Reynolds K., Riddick M., Zimmer A., Niemann H., Zimmer A. Tetanus toxin light chain expression in Sertoli cells of transgenic mice causes alterations of the actin cytoskeleton and disrupts spermatogenesis. EMBO. J. 12:1993;3365-3372.
    • (1993) EMBO. J. , vol.12 , pp. 3365-3372
    • Eisel, U.1    Reynolds, K.2    Riddick, M.3    Zimmer, A.4    Niemann, H.5    Zimmer, A.6
  • 35
    • 0030901704 scopus 로고    scopus 로고
    • Botulinum neurotoxin serotype C: A novel effective botulinum toxin therapy in human
    • Eleopra R., Tugnoli V., Rossetto O., Montecucco C., De Grandis D. Botulinum neurotoxin serotype C: a novel effective botulinum toxin therapy in human. Neurosci. Lett. 224:1997;91-94.
    • (1997) Neurosci. Lett. , vol.224 , pp. 91-94
    • Eleopra, R.1    Tugnoli, V.2    Rossetto, O.3    Montecucco, C.4    De Grandis, D.5
  • 36
    • 85080380648 scopus 로고    scopus 로고
    • Botulinum neurotoxin serotype A and E in human: Evidence of a different temporal profile in the neuromuscular block induced
    • Eleopra R., Tugnoli V., Rossetto O., De Grandis D., Montecucco C. Botulinum neurotoxin serotype A and E in human: evidence of a different temporal profile in the neuromuscular block induced. Neurosci. Lett. 224:1998;91-94.
    • (1998) Neurosci. Lett. , vol.224 , pp. 91-94
    • Eleopra, R.1    Tugnoli, V.2    Rossetto, O.3    De Grandis, D.4    Montecucco, C.5
  • 37
    • 0010281124 scopus 로고
    • Die Pathogenie des Tetanus
    • Faber K. Die Pathogenie des Tetanus. Berl. klin. Wochenschr. 27:1890;717-720.
    • (1890) Berl. Klin. Wochenschr. , vol.27 , pp. 717-720
    • Faber, K.1
  • 39
    • 0028558884 scopus 로고
    • Differences in the protease activities of tetanus and botulinum B toxins revealed by the cleavage of vesicle-associated membrane protein and various sized fragments
    • Foran P., Shone C.C., Dolly J.O. Differences in the protease activities of tetanus and botulinum B toxins revealed by the cleavage of vesicle-associated membrane protein and various sized fragments. Biochemistry. 33:1994;15365-15374.
    • (1994) Biochemistry , vol.33 , pp. 15365-15374
    • Foran, P.1    Shone, C.C.2    Dolly, J.O.3
  • 40
    • 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 G.W., Shone C.C., Foster K.A., Dolly J.O. Botulinum neurotoxin C1 cleaves both syntaxin and SNAP-25 in intact and permeabilized chromaffin cells: correlation with its blockade of catecholamine release. Biochemistry. 35:1996;2630-2636.
    • (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
  • 41
    • 0029034875 scopus 로고
    • CuZn superoxide dismutase (SOD-1): Tetanus toxin fragment C hybrid protein for targeted delivery of SOD-1 to neuronal cells
    • Francis J.W., Hosler B.A., Brown H.R. Jr, Fishman P.S. CuZn superoxide dismutase (SOD-1): tetanus toxin fragment C hybrid protein for targeted delivery of SOD-1 to neuronal cells. J. Bio. Chem. 270:1995;15434-15442.
    • (1995) J. Bio. Chem. , vol.270 , pp. 15434-15442
    • Francis, J.W.1    Hosler, B.A.2    Brown H.R., Jr.3    Fishman, P.S.4
  • 42
    • 0029114846 scopus 로고
    • The present status of tetanus and tetanus vaccination
    • Galazka A., Gasse F. The present status of tetanus and tetanus vaccination. Curr. Top. Microbiol. Immunol. 195:1995;31-53.
    • (1995) Curr. Top. Microbiol. Immunol. , vol.195 , pp. 31-53
    • Galazka, A.1    Gasse, F.2
  • 43
    • 0023903076 scopus 로고
    • Characterization of the channel properties of tetanus toxin in planar lipid bilayers
    • Gambale F., Montal M. Characterization of the channel properties of tetanus toxin in planar lipid bilayers. Biophys. J. 53:1988;771-783.
    • (1988) Biophys. J. , vol.53 , pp. 771-783
    • Gambale, F.1    Montal, M.2
  • 45
    • 0031030099 scopus 로고    scopus 로고
    • A peptide that mimics the C-terminal sequence of SNAP-25 inhibits secretory vesicle docking in chromaffin cells
    • Gutierrez L.M., Viniegra S., Rueda J., Ferrier Montiel A.V., Canaves J.M., Montal M. A peptide that mimics the C-terminal sequence of SNAP-25 inhibits secretory vesicle docking in chromaffin cells. J. Biol. Chem. 272:1997;2634-2639.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2634-2639
    • Gutierrez, L.M.1    Viniegra, S.2    Rueda, J.3    Ferrier Montiel, A.V.4    Canaves, J.M.5    Montal, M.6
  • 46
    • 0018838743 scopus 로고
    • Tetanus toxin blocks the neuromuscular transmission in vitro like botulinum A toxin
    • Habermann E., Dreyer F., Bigalke H. Tetanus toxin blocks the neuromuscular transmission in vitro like botulinum A toxin. Naunyn Schemiedebergs. Arch. Pharmacol. 311:1980;33-40.
    • (1980) Naunyn Schemiedebergs. Arch. Pharmacol. , vol.311 , pp. 33-40
    • Habermann, E.1    Dreyer, F.2    Bigalke, H.3
  • 47
    • 0022463687 scopus 로고
    • Clostridial neurotoxins: Handling and action at the cellular and molecular level
    • Habermann E., Dreyer F. Clostridial neurotoxins: handling and action at the cellular and molecular level. Curr. Top. Microbiol. Immunol. 129:1986;93-179.
    • (1986) Curr. Top. Microbiol. Immunol. , vol.129 , pp. 93-179
    • Habermann, E.1    Dreyer, F.2
  • 48
    • 0022510860 scopus 로고
    • Tetanus toxin in dissociated spinal cord cultures: Long-term characterization of form and action
    • Habig W.H., Bigalke H., Bergey G.K., Neale E.A., Hardegree M.C., Nelson P.G. Tetanus toxin in dissociated spinal cord cultures: long-term characterization of form and action. J. Neurochem. 47:1986;930-937.
    • (1986) J. Neurochem. , vol.47 , pp. 930-937
    • Habig, W.H.1    Bigalke, H.2    Bergey, G.K.3    Neale, E.A.4    Hardegree, M.C.5    Nelson, P.G.6
  • 49
    • 0027265079 scopus 로고
    • Characterization of the receptor-binding domain of tetanus toxin
    • Halpern J.L., Loftus A. Characterization of the receptor-binding domain of tetanus toxin. J. Biol. Chem. 268:1993;11188-11192.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11188-11192
    • Halpern, J.L.1    Loftus, A.2
  • 50
    • 0029115155 scopus 로고
    • Neurospecific binding, internalization, and retrograde axonal transport
    • Halpern J.L., Neale E.A. Neurospecific binding, internalization, and retrograde axonal transport. Curr. Top. Microbiol. Immunol. 195:1995;221-241.
    • (1995) Curr. Top. Microbiol. Immunol. , vol.195 , pp. 221-241
    • Halpern, J.L.1    Neale, E.A.2
  • 51
    • 0028130728 scopus 로고
    • Synaptic vesicle membrane fusion complex: Action of clostridial neurotoxins on assembly
    • Hayashi T., McMahon H., Yamasaki S., Binz T., Hata Y., Sudhof T.C., Niemann H. Synaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assembly. EMBO J. 13:1994;5051-5061.
    • (1994) EMBO J. , vol.13 , pp. 5051-5061
    • Hayashi, T.1    McMahon, H.2    Yamasaki, S.3    Binz, T.4    Hata, Y.5    Sudhof, T.C.6    Niemann, H.7
  • 52
    • 0031411460 scopus 로고    scopus 로고
    • Localization of putative receptors for tetanus toxin and botulinum neurotoxin type A in rat central nervous system
    • Herreros J., Marti E., Ruiz-Montasell B., Casanova A., Niemann H., Blasi J. Localization of putative receptors for tetanus toxin and botulinum neurotoxin type A in rat central nervous system. Eur. J. Neurosci. 9:1997;2677-2686.
    • (1997) Eur. J. Neurosci. , vol.9 , pp. 2677-2686
    • Herreros, J.1    Marti, E.2    Ruiz-Montasell, B.3    Casanova, A.4    Niemann, H.5    Blasi, J.6
  • 53
    • 0034177056 scopus 로고    scopus 로고
    • C-terminal half of tetanus toxin fragment C is sufficient for neuronal binding and interaction with a putative protein receptor
    • Herreros, J., Lalli, G., Schiavo, G., 2000. C-terminal half of tetanus toxin fragment C is sufficient for neuronal binding and interaction with a putative protein receptor. Biochem. J. 347, 199-204.
    • (2000) Biochem. J. , vol.347 , pp. 199-204
    • Herreros, J.1    Lalli, G.2    Schiavo, G.3
  • 54
    • 0345570658 scopus 로고
    • Channels formed by botulinum, tetanus, and diphtheria toxins in planar lipid bilayers: Relevance to translocation of proteins across membranes
    • Hoch D.H., Romero-Mira M., Ehrlich B.E., Finkelstein A., Das gupta B.R., Simpson L.L. Channels formed by botulinum, tetanus, and diphtheria toxins in planar lipid bilayers: relevance to translocation of proteins across membranes. Proc. Natl. Acad. Sci. USA. 82:1985;1692-1696.
    • (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    Das Gupta, B.R.5    Simpson, L.L.6
  • 55
    • 0028072443 scopus 로고
    • Synaptobrevin cleavage by the tetanus toxin light chain is linked to the inhibition of exocytosis in chromaffin cells
    • Hohne-Zell B., Ecker A., Weller U., Gratzl M. Synaptobrevin cleavage by the tetanus toxin light chain is linked to the inhibition of exocytosis in chromaffin cells. FEBS Lett. 355:1994;131-134.
    • (1994) FEBS Lett. , vol.355 , pp. 131-134
    • Hohne-Zell, B.1    Ecker, A.2    Weller, U.3    Gratzl, M.4
  • 56
    • 0033491695 scopus 로고    scopus 로고
    • Activity dependent changes in partial-VAMP complexes during neurotransmitter release
    • Hua S.Y., Charlton M. Activity dependent changes in partial-VAMP complexes during neurotransmitter release. Nature Neurosci. 2:1999;1078-1083.
    • (1999) Nature Neurosci. , vol.2 , pp. 1078-1083
    • Hua, S.Y.1    Charlton, M.2
  • 57
    • 0001718582 scopus 로고
    • Influence of nerve-endings activity and of drugs on the rate of paralysis of rat diaphragm preparations by Clostridium botulinum type A toxin
    • Hughes R., Whaler B.C. Influence of nerve-endings activity and of drugs on the rate of paralysis of rat diaphragm preparations by Clostridium botulinum type A toxin. J. Physiol. (Lond.). 160:1962;221-233.
    • (1962) J. Physiol. (Lond.) , vol.160 , pp. 221-233
    • Hughes, R.1    Whaler, B.C.2
  • 60
    • 0022271661 scopus 로고
    • Comparison of the action of types A and F botulinum toxin at the rat neuromuscular junction
    • Kauffman J.A., Way J.F. Jr, Siegel L.S., Sellin L.C. Comparison of the action of types A and F botulinum toxin at the rat neuromuscular junction. Toxicol. Appl. Pharmacol. 79:1985;211-217.
    • (1985) Toxicol. Appl. Pharmacol. , vol.79 , pp. 211-217
    • Kauffman, J.A.1    Way J.F., Jr.2    Siegel, L.S.3    Sellin, L.C.4
  • 61
    • 0032776446 scopus 로고    scopus 로고
    • Persistence of botulinum neurotoxin action in cultured spinal cord cells
    • Keller J.E., Neale E.A., Oyler G., Adler M. Persistence of botulinum neurotoxin action in cultured spinal cord cells. FEBS Lett. 456:1999;137-142.
    • (1999) FEBS Lett. , vol.456 , pp. 137-142
    • Keller, J.E.1    Neale, E.A.2    Oyler, G.3    Adler, M.4
  • 62
    • 0342720789 scopus 로고
    • Central nervous changes in experimental tetanus and the mode of action of the tetanus toxin. Communication I: Irradiation of the excitation on stimulating the tetanized limb
    • Kryzhanovsky G.N. Central nervous changes in experimental tetanus and the mode of action of the tetanus toxin. Communication I: Irradiation of the excitation on stimulating the tetanized limb. Bull. Exp. Biol. Med. 44:1958;1456-1464.
    • (1958) Bull. Exp. Biol. Med. , vol.44 , pp. 1456-1464
    • Kryzhanovsky, G.N.1
  • 64
    • 0031712779 scopus 로고    scopus 로고
    • Crystal structure of botulinum neurotoxin type A and implications for toxicity
    • Lacy B.D., Tepp W., Das Gupta B.R., Stevens R.C. Crystal structure of botulinum neurotoxin type A and implications for toxicity. Nature Struct. Biology. 5:1998;898-902.
    • (1998) Nature Struct. Biology , vol.5 , pp. 898-902
    • Lacy, B.D.1    Tepp, W.2    Das Gupta, B.R.3    Stevens, R.C.4
  • 65
    • 0033520494 scopus 로고    scopus 로고
    • Crystal structure of botulinum neurotoxin type A and implications for toxicity
    • Lacy B.D., Stevens R.C. Crystal structure of botulinum neurotoxin type A and implications for toxicity. J. Mol. Biol. 291:1999;1091-1104.
    • (1999) J. Mol. Biol. , vol.291 , pp. 1091-1104
    • Lacy, B.D.1    Stevens, R.C.2
  • 67
    • 84954214582 scopus 로고    scopus 로고
    • Clostridial toxins and endocrine secretion: Their use in insuline secreting cells
    • K. Aktories. London: Chapman and Hall
    • Lang J., Regazzi R., Wollheim C.B. Clostridial toxins and endocrine secretion: their use in insuline secreting cells. Aktories K. Bacterial Toxins. Tools in Cell Biology and Pharmacology. 1997;217-237 Chapman and Hall, London.
    • (1997) Bacterial Toxins. Tools in Cell Biology and Pharmacology , pp. 217-237
    • Lang, J.1    Regazzi, R.2    Wollheim, C.B.3
  • 68
    • 0030900523 scopus 로고    scopus 로고
    • Importance of two adjacent C-terminal sequences of SNAP-25 in exocytosis from intact and permeabilized chromaffin cells revealed by inhibition with botulinum neurotoxins A and E
    • Lawrence G.W., Foran P., Mohammed N., Das gupta B.R., Dolly J.O. Importance of two adjacent C-terminal sequences of SNAP-25 in exocytosis from intact and permeabilized chromaffin cells revealed by inhibition with botulinum neurotoxins A and E. Biochemistry. 36:1997;3061-3067.
    • (1997) Biochemistry , vol.36 , pp. 3061-3067
    • Lawrence, G.W.1    Foran, P.2    Mohammed, N.3    Das Gupta, B.R.4    Dolly, J.O.5
  • 69
    • 0029047219 scopus 로고
    • Structural predictions of the channel-forming region of botulinum neurotoxin heavy chain
    • Lebeda F.J., Olson M.A. Structural predictions of the channel-forming region of botulinum neurotoxin heavy chain. Toxicon. 33:1995;559-567.
    • (1995) Toxicon , vol.33 , pp. 559-567
    • Lebeda, F.J.1    Olson, M.A.2
  • 70
    • 0034008947 scopus 로고    scopus 로고
    • Probing the mechanistic role of glutamate residue in the zinc binding motif of type A botulinum neurotoxin light chain
    • Li L., Binz T., Niemann H., Singh B.R. Probing the mechanistic role of glutamate residue in the zinc binding motif of type A botulinum neurotoxin light chain. Biochemistry. 39:2000;2399-2405.
    • (2000) Biochemistry , vol.39 , pp. 2399-2405
    • Li, L.1    Binz, T.2    Niemann, H.3    Singh, B.R.4
  • 72
    • 0017656115 scopus 로고
    • Antagonism of the paralysis produced by botulinum toxin in the rat. The effects of tetraethylammonium, guanidine and 4-aminopyridine
    • Lundh H., Leander S., Thesleff S. Antagonism of the paralysis produced by botulinum toxin in the rat. The effects of tetraethylammonium, guanidine and 4-aminopyridine. J. Neurol. Sci. 32:1977;29-43.
    • (1977) J. Neurol. Sci. , vol.32 , pp. 29-43
    • Lundh, H.1    Leander, S.2    Thesleff, S.3
  • 74
    • 0029002962 scopus 로고
    • The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer
    • Martoglio B., Hofmann M.W., Brunner J., Dobberstein B. The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer. Cell 1995. 81:1995;207-214.
    • (1995) Cell 1995 , vol.81 , pp. 207-214
    • Martoglio, B.1    Hofmann, M.W.2    Brunner, J.3    Dobberstein, B.4
  • 75
    • 0343155346 scopus 로고
    • The chromaffin cell: A suitable model for investigating the actions and the metabolism of tetanus and botulinum A neurotoxin
    • Marxen P., Bigalke H. The chromaffin cell: a suitable model for investigating the actions and the metabolism of tetanus and botulinum A neurotoxin. Naunyn Schemiedebergs Arch. Pharmacol. 343:1991;12-29.
    • (1991) Naunyn Schemiedebergs Arch. Pharmacol. , vol.343 , pp. 12-29
    • Marxen, P.1    Bigalke, H.2
  • 77
    • 0023919946 scopus 로고
    • The effect of lanthanum on nerve terminals in goldfish muscle after paralysis with tetanus toxin
    • Mellanby J., Beaumont M.A., Thompson P.A. The effect of lanthanum on nerve terminals in goldfish muscle after paralysis with tetanus toxin. Neuroscience. 25:1988;1095-1106.
    • (1988) Neuroscience , vol.25 , pp. 1095-1106
    • Mellanby, J.1    Beaumont, M.A.2    Thompson, P.A.3
  • 78
    • 0024599014 scopus 로고
    • Interaction of tetanus toxin with lipid vesicles. Effects of pH, surface charge, and transmembrane potential on the kinetics of channel formation
    • Menestrina G., Forti S., Gambale F. Interaction of tetanus toxin with lipid vesicles. Effects of pH, surface charge, and transmembrane potential on the kinetics of channel formation. Biophys. J. 55:1989;393-405.
    • (1989) Biophys. J. , vol.55 , pp. 393-405
    • Menestrina, G.1    Forti, S.2    Gambale, F.3
  • 79
    • 0029080131 scopus 로고
    • Molecular genetics of clostridial neurotoxins
    • Minton N.P. Molecular genetics of clostridial neurotoxins. Curr. Top. Microbiol. Immunol. 195:1995;161-194.
    • (1995) Curr. Top. Microbiol. Immunol. , vol.195 , pp. 161-194
    • Minton, N.P.1
  • 80
    • 0024306217 scopus 로고
    • Characterization of the actions of botulinum neurotoxin type E at the rat neuromuscular junction
    • Molgo J., Das gupta B.R., Thesleff S. Characterization of the actions of botulinum neurotoxin type E at the rat neuromuscular junction. Acta. Physiol. Scan. 137:1989;497-501.
    • (1989) Acta. Physiol. Scan. , vol.137 , pp. 497-501
    • Molgo, J.1    Das Gupta, B.R.2    Thesleff, S.3
  • 81
    • 46149134882 scopus 로고
    • How do tetanus and botulinum toxins bind to neuronal membranes?
    • Montecucco C. How do tetanus and botulinum toxins bind to neuronal membranes? Trends Biochem. Sci. 11:1986;315-317.
    • (1986) Trends Biochem. Sci. , vol.11 , pp. 315-317
    • Montecucco, C.1
  • 83
    • 0024506750 scopus 로고
    • Effect of pH on the interaction of botulinum neurotoxins A, B and E with liposomes
    • Montecucco C., Schiavo G., Das gupta B.R. Effect of pH on the interaction of botulinum neurotoxins A, B and E with liposomes. Biochem. J. 259:1989;47-53.
    • (1989) Biochem. J. , vol.259 , pp. 47-53
    • Montecucco, C.1    Schiavo, G.2    Das Gupta, B.R.3
  • 85
    • 0027248876 scopus 로고
    • Tetanus and botulism neurotoxins: A new group of zinc proteases
    • Montecucco C., Schiavo G. Tetanus and botulism neurotoxins: a new group of zinc proteases. Trends Biochem. Sci. 18:1993;324-327.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 324-327
    • Montecucco, C.1    Schiavo, G.2
  • 86
    • 0028236333 scopus 로고
    • Bacterial protein toxins penetrate cells via a four-step mechanism
    • Montecucco C., Papini E., Schiavo G. Bacterial protein toxins penetrate cells via a four-step mechanism. FEBS Lett. 346:1994;92-98.
    • (1994) FEBS Lett. , vol.346 , pp. 92-98
    • Montecucco, C.1    Papini, E.2    Schiavo, G.3
  • 87
    • 0030045128 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy study of zinc coordination in tetanus neurotoxin, astacin, alkaline protease and thermolysin
    • Morante S., Furenlid L., Schiavo G., Tonello F., Zwilling R., Montecucco C. X-ray absorption spectroscopy study of zinc coordination in tetanus neurotoxin, astacin, alkaline protease and thermolysin. Eur. J. Biochem. 235:1996;606-612.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 606-612
    • Morante, S.1    Furenlid, L.2    Schiavo, G.3    Tonello, F.4    Zwilling, R.5    Montecucco, C.6
  • 88
    • 0032839760 scopus 로고    scopus 로고
    • Botulinum toxin in the treatment of neurological disorders of the autonomic nervous system
    • Naumann M., Jost W.H., Toyka K.V. Botulinum toxin in the treatment of neurological disorders of the autonomic nervous system. Arch. Neurol. 56:1999;914-916.
    • (1999) Arch. Neurol. , vol.56 , pp. 914-916
    • Naumann, M.1    Jost, W.H.2    Toyka, K.V.3
  • 89
    • 0342871818 scopus 로고
    • Application of tetanus toxin for structure-function studies in neuronal cell cultures
    • G. Nistico', B. Bizzini, B. Bytchencko, & R. Triau. Rome: Pythagora Press
    • Neale E.A., Habig W.H., Schrier B.K., Bergey G.K., Bowers L.M., Koh J. Application of tetanus toxin for structure-function studies in neuronal cell cultures. Nistico' G., Bizzini B., Bytchencko B., Triau R. Eight International Conference on Tetanus. 1989;66-70 Pythagora Press, Rome.
    • (1989) Eight International Conference on Tetanus , pp. 66-70
    • Neale, E.A.1    Habig, W.H.2    Schrier, B.K.3    Bergey, G.K.4    Bowers, L.M.5    Koh, J.6
  • 90
    • 0033552583 scopus 로고    scopus 로고
    • Botulinum neurotoxin A blocks synaptic vesicle exocytosis but not endocytosis at the nerve terminal
    • Neale E.A., Bowers L.M., Jia M., Bateman K.E., Williamson L.C. Botulinum neurotoxin A blocks synaptic vesicle exocytosis but not endocytosis at the nerve terminal. J. Cell. Biol. 147:1999;1249-1260.
    • (1999) J. Cell. Biol. , vol.147 , pp. 1249-1260
    • Neale, E.A.1    Bowers, L.M.2    Jia, M.3    Bateman, K.E.4    Williamson, L.C.5
  • 91
    • 0000712596 scopus 로고
    • Molecular biology of clostridial neurotoxins
    • J.E. Alouf, & J.J. Freer. London: Academic Press
    • Niemann H. Molecular biology of clostridial neurotoxins. Alouf J.E., Freer J.J. A Sourcebook of Bacterial Protein Toxins. 1991;303-348 Academic Press, London.
    • (1991) A Sourcebook of Bacterial Protein Toxins , pp. 303-348
    • Niemann, H.1
  • 92
    • 0030064241 scopus 로고    scopus 로고
    • The high-affinity binding of Clostridium botulinum type B neurotoxin to synaptotagmin II associated with gangliosides GT1b/GD1a
    • Nishiki T., Tokuyama Y., Kamata Y., Nemoto Y., Yoshida A., Sato K., Sekiguchi M., Takahashi M., Kozaki S. The high-affinity binding of Clostridium botulinum type B neurotoxin to synaptotagmin II associated with gangliosides GT1b/GD1a. FEBS Lett. 378:1996;253-257.
    • (1996) FEBS Lett. , vol.378 , pp. 253-257
    • Nishiki, T.1    Tokuyama, Y.2    Kamata, Y.3    Nemoto, Y.4    Yoshida, A.5    Sato, K.6    Sekiguchi, M.7    Takahashi, M.8    Kozaki, S.9
  • 94
    • 0033601298 scopus 로고    scopus 로고
    • Rescue of exocytosis in botulinum toxin A-poisoned chromaffin cells by expression of cleavage-resistant SNAP-25. Identification of the minimal essential C-terminal residues
    • O'Sullivan G.A., Mohammed N., Foran P.G., Lawrence G.W., Oliver Dolly J.O. Rescue of exocytosis in botulinum toxin A-poisoned chromaffin cells by expression of cleavage-resistant SNAP-25. Identification of the minimal essential C-terminal residues. J. Biol. Chem. 274:1999;36897-36904.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36897-36904
    • O'Sullivan, G.A.1    Mohammed, N.2    Foran, P.G.3    Lawrence, G.W.4    Oliver Dolly, J.O.5
  • 96
    • 0023196480 scopus 로고
    • A study of the mechanism of internalisation of tetanus toxin by primary mouse spinal cord cultures
    • Parton R.G., Ockleford C.D., Critchley D.R. A study of the mechanism of internalisation of tetanus toxin by primary mouse spinal cord cultures. J. Neurochem. 49:1987;1057-1068.
    • (1987) J. Neurochem. , vol.49 , pp. 1057-1068
    • Parton, R.G.1    Ockleford, C.D.2    Critchley, D.R.3
  • 97
    • 0023781370 scopus 로고
    • Tetanus toxin binding to mouse spinal cord cells: An evaluation of the role of gangliosides in toxin internalization
    • Parton R.G., Ockleford C.D., Critchley D.R. Tetanus toxin binding to mouse spinal cord cells: an evaluation of the role of gangliosides in toxin internalization. Brain Res. 475:1988;118-127.
    • (1988) Brain Res. , vol.475 , pp. 118-127
    • Parton, R.G.1    Ockleford, C.D.2    Critchley, D.R.3
  • 98
    • 0029811998 scopus 로고    scopus 로고
    • Structural determinants of the specificity for synaptic vesicle-associated membrane protein/synaptobrevin of tetanus and botulinum type B and G neurotoxins
    • Pellizzari R., Rossetto O., Lozzi L., Giovedi S., Johnson E., Shone C.C., Montecucco C. Structural determinants of the specificity for synaptic vesicle-associated membrane protein/synaptobrevin of tetanus and botulinum type B and G neurotoxins. J. Biol. Chem. 271:1996;20353-20358.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20353-20358
    • Pellizzari, R.1    Rossetto, O.2    Lozzi, L.3    Giovedi, S.4    Johnson, E.5    Shone, C.C.6    Montecucco, C.7
  • 99
    • 0030787389 scopus 로고    scopus 로고
    • The interaction of synaptic vesicle-associated membrane protein/synaptobrevin with botulinum neurotoxins D and F
    • Pellizzari R., Mason S., Shone C.C., Montecucco C. The interaction of synaptic vesicle-associated membrane protein/synaptobrevin with botulinum neurotoxins D and F. FEBS Lett. 409:1997;339-342.
    • (1997) FEBS Lett. , vol.409 , pp. 339-342
    • Pellizzari, R.1    Mason, S.2    Shone, C.C.3    Montecucco, C.4
  • 100
    • 0022539795 scopus 로고
    • Characterization of tetanus toxin binding to rat brain membranes. Evidence for a high-affinity proteinase-sensitive receptor
    • Pierce E.J., Davison M.D., Parton R.G., Habig W.H., Critchley D.R. Characterization of tetanus toxin binding to rat brain membranes. Evidence for a high-affinity proteinase-sensitive receptor. Biochem. J. 236:1986;845-852.
    • (1986) Biochem. J. , vol.236 , pp. 845-852
    • Pierce, E.J.1    Davison, M.D.2    Parton, R.G.3    Habig, W.H.4    Critchley, D.R.5
  • 101
    • 0029864604 scopus 로고    scopus 로고
    • Tetanus toxin-sensitive VAMP-related proteins are present in murine macrophages
    • Pitzurra L., Rossetto O., Chimienti A.R., Blasi E., Bistoni F. Tetanus toxin-sensitive VAMP-related proteins are present in murine macrophages. Cell. Immun. 169:1996;113-116.
    • (1996) Cell. Immun. , vol.169 , pp. 113-116
    • Pitzurra, L.1    Rossetto, O.2    Chimienti, A.R.3    Blasi, E.4    Bistoni, F.5
  • 103
    • 51249161407 scopus 로고
    • Zur Frage der Pathogenese des Tetanus und des Fortbewegungsmechanismus des Tetanustoxin entlang der Nerven
    • Ponomarev A.W. Zur Frage der Pathogenese des Tetanus und des Fortbewegungsmechanismus des Tetanustoxin entlang der Nerven. Z. Ges. Exp. Med. 61:1928;93-106.
    • (1928) Z. Ges. Exp. Med. , vol.61 , pp. 93-106
    • Ponomarev, A.W.1
  • 104
    • 0031901958 scopus 로고    scopus 로고
    • Presynaptic protein interactions in vivo: Evidence from botulinum A, C, D and E action at frog neuromuscular junction
    • Raciborska D.A., Trimble W.S., Charlton M.P. Presynaptic protein interactions in vivo: evidence from botulinum A, C, D and E action at frog neuromuscular junction. Eur. J. Neurosci. 10:1998;2617-2628.
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 2617-2628
    • Raciborska, D.A.1    Trimble, W.S.2    Charlton, M.P.3
  • 105
    • 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 D.A., Charlton M.P. 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. Physiol. Pharmacol. 77:1999;679-688.
    • (1999) Can. J. Physiol. Pharmacol. , vol.77 , pp. 679-688
    • Raciborska, D.A.1    Charlton, M.P.2
  • 107
    • 0025300655 scopus 로고
    • Tetanus toxin channel in phosphatidylserine planar bilayers: Conductance states and pH dependence
    • Rauch G., Gambale F., Montal M. Tetanus toxin channel in phosphatidylserine planar bilayers: conductance states and pH dependence. Eur. J. Biochem. 18:1990;79-83.
    • (1990) Eur. J. Biochem. , vol.18 , pp. 79-83
    • Rauch, G.1    Gambale, F.2    Montal, M.3
  • 108
    • 0029004315 scopus 로고
    • Families of aspartic peptidases, and those of unknown catalytic mechanism
    • Rawlings N.D., Barrett A.J. Families of aspartic peptidases, and those of unknown catalytic mechanism. Methods Enzymol. 248:1995;105-120.
    • (1995) Methods Enzymol , vol.248 , pp. 105-120
    • Rawlings, N.D.1    Barrett, A.J.2
  • 109
    • 0021802697 scopus 로고
    • Interaction of tetanus toxin with lipid vesicles at low pH. Protection of specific polypeptides against proteolysis
    • Roa M., Boquet P. Interaction of tetanus toxin with lipid vesicles at low pH. Protection of specific polypeptides against proteolysis. J. Biol. Chem. 260:1985;6827-6835.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6827-6835
    • Roa, M.1    Boquet, P.2
  • 111
    • 0031086319 scopus 로고    scopus 로고
    • Botulinum toxin: The story of its development for the treatment of human disease
    • Schantz E.J., Johnson E.A. Botulinum toxin: the story of its development for the treatment of human disease. Perspect. Biol. Med. 40:1997;317-327.
    • (1997) Perspect. Biol. Med. , vol.40 , pp. 317-327
    • Schantz, E.J.1    Johnson, E.A.2
  • 112
    • 0025648954 scopus 로고
    • An intact interchain disulfide bond is required for the neurotoxicity of tetanus toxin
    • Schiavo G., Papini E., Genna G., Montecucco C. An intact interchain disulfide bond is required for the neurotoxicity of tetanus toxin. Infect. Immun. 58:1990;4136-4141.
    • (1990) Infect. Immun. , vol.58 , pp. 4136-4141
    • Schiavo, G.1    Papini, E.2    Genna, G.3    Montecucco, C.4
  • 113
    • 0025771193 scopus 로고
    • Tetanus toxin receptor. Specific cross-linking of tetanus toxin to a protein of NGF-differentiated PC12 cells
    • Schiavo G., Ferrari G., Rossetto O., Montecucco C. Tetanus toxin receptor. Specific cross-linking of tetanus toxin to a protein of NGF-differentiated PC12 cells. FEBS Lett. 290:1991;227-230.
    • (1991) FEBS Lett. , vol.290 , pp. 227-230
    • Schiavo, G.1    Ferrari, G.2    Rossetto, O.3    Montecucco, C.4
  • 114
    • 0025879549 scopus 로고
    • On the role of polysialoglycosphingolipids as tetanus toxin receptor. A study with lipid monolayers
    • Schiavo G., Demel R., Montecucco C. On the role of polysialoglycosphingolipids as tetanus toxin receptor. A study with lipid monolayers. Eur. J. Biochem. 199:1991;705-711.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 705-711
    • Schiavo, G.1    Demel, R.2    Montecucco, C.3
  • 115
    • 0026673922 scopus 로고
    • Tetanus toxin is a zinc protein and its inhibition of neurotransmitter release and protease activity depend on zinc
    • Schiavo G., Poulain B., Rossetto O., Benfenati F., Tauc L., Montecucco C. Tetanus toxin is a zinc protein and its inhibition of neurotransmitter release and protease activity depend on zinc. EMBO J. 11:1992;3577-3583.
    • (1992) EMBO J. , vol.11 , pp. 3577-3583
    • Schiavo, G.1    Poulain, B.2    Rossetto, O.3    Benfenati, F.4    Tauc, L.5    Montecucco, C.6
  • 120
    • 0027241009 scopus 로고
    • Botulinum neurotoxin serotype F is a zinc endopeptidase specific for VAMP/synaptobrevin
    • Schiavo G., Shone C.C., Rossetto O., Alexander F.C., Montecucco C. Botulinum neurotoxin serotype F is a zinc endopeptidase specific for VAMP/synaptobrevin. J. Biol. Chem. 268:1993;11516-11519.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11516-11519
    • Schiavo, G.1    Shone, C.C.2    Rossetto, O.3    Alexander, F.C.4    Montecucco, C.5
  • 122
    • 0029061475 scopus 로고
    • Tetanus and botulism neurotoxins: Isolation and assay
    • Schiavo G., Montecucco C. Tetanus and botulism neurotoxins: isolation and assay. Methods Enzymol. 248:1995;643-652.
    • (1995) Methods Enzymol. , vol.248 , pp. 643-652
    • Schiavo, G.1    Montecucco, C.2
  • 123
    • 0028922592 scopus 로고
    • Botulinum neurotoxin type C cleaves a single Lys-Ala bond within the carboxyl-terminal region of syntaxins
    • Schiavo G., Shone C.C., Bennett M.K., Scheller R.H., Montecucco C. Botulinum neurotoxin type C cleaves a single Lys-Ala bond within the carboxyl-terminal region of syntaxins. J. Biol. Chem. 270:1995;10566-10570.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10566-10570
    • Schiavo, G.1    Shone, C.C.2    Bennett, M.K.3    Scheller, R.H.4    Montecucco, C.5
  • 125
    • 0027282605 scopus 로고
    • Direct visualization of botulinum neurotoxin-induced channels in phospholipid vesicles
    • Schmid M.F., Robinson J.P., dasgupta B.R. Direct visualization of botulinum neurotoxin-induced channels in phospholipid vesicles. Nature. 364:1993;827-830.
    • (1993) Nature , vol.364 , pp. 827-830
    • Schmid, M.F.1    Robinson, J.P.2    Dasgupta, B.R.3
  • 126
    • 0018716059 scopus 로고
    • Selective retrograde transsynaptic transfer of a protein, tetanus toxin, subsequent to its retrograde axonal transport
    • Schwab M.E., Suda K., Thoenen H. Selective retrograde transsynaptic transfer of a protein, tetanus toxin, subsequent to its retrograde axonal transport. J. Cell. Biol. 82:1979;798-810.
    • (1979) J. Cell. Biol. , vol.82 , pp. 798-810
    • Schwab, M.E.1    Suda, K.2    Thoenen, H.3
  • 127
    • 0001339033 scopus 로고
    • Clostridial neurotoxins as therapeutic agents
    • L.L. Simpson. San Diego: Academic Press
    • Scott A.B. Clostridial neurotoxins as therapeutic agents. Simpson L.L. Botulinum Neurotoxin and Tetanus Toxin. 1989;399-412 Academic Press, San Diego.
    • (1989) Botulinum Neurotoxin and Tetanus Toxin , pp. 399-412
    • Scott, A.B.1
  • 128
    • 0020515818 scopus 로고
    • Different effects of types A and B botulinum toxin on transmitter release at the rat neuromuscular junction
    • Sellin L.C., Thesleff S., Dasgupta B.R. Different effects of types A and B botulinum toxin on transmitter release at the rat neuromuscular junction. Acta Physiol. Scan. 119:1983;127-133.
    • (1983) Acta Physiol. Scan. , vol.119 , pp. 127-133
    • Sellin, L.C.1    Thesleff, S.2    Dasgupta, B.R.3
  • 129
    • 0023658427 scopus 로고
    • 2-terminus of the heavy subunit of Clostridium botulinum type A neurotoxin forms channels in lipid vesicles
    • 2-terminus of the heavy subunit of Clostridium botulinum type A neurotoxin forms channels in lipid vesicles. Eur. J. Biochem. 167:1987;175-180.
    • (1987) Eur. J. Biochem. , vol.167 , pp. 175-180
    • Shone, C.C.1    Hambleton, P.2    Melling, J.3
  • 130
    • 0027376762 scopus 로고
    • Proteolytic cleavage of synthetic fragments of vesicle-associated membrane protein, isoform-2 by botulinum type B neurotoxin
    • Shone C.C., Quinn C.P., Wait R., Hallis B., Fooks S.G., Hambleton P. Proteolytic cleavage of synthetic fragments of vesicle-associated membrane protein, isoform-2 by botulinum type B neurotoxin. Eur. J. Biochem. 217:1993;965-971.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 965-971
    • Shone, C.C.1    Quinn, C.P.2    Wait, R.3    Hallis, B.4    Fooks, S.G.5    Hambleton, P.6
  • 131
    • 0028065415 scopus 로고
    • Peptide substrate specificity and properties of the zinc-endopeptidase activity of botulinum type B neurotoxin
    • Shone C.C., Roberts A.K. Peptide substrate specificity and properties of the zinc-endopeptidase activity of botulinum type B neurotoxin. Eur. J. Biochem. 225:1994;263-270.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 263-270
    • Shone, C.C.1    Roberts, A.K.2
  • 132
    • 0040416564 scopus 로고
    • The reaction of 'tetanus sensitive' and 'tetanus resistant' animals to the injection of tetanal toxin into the spinal cord
    • Shumaker H.B., Lamont A., Firor W.M. The reaction of 'tetanus sensitive' and 'tetanus resistant' animals to the injection of tetanal toxin into the spinal cord. J. Immunol. 37:1939;425-433.
    • (1939) J. Immunol. , vol.37 , pp. 425-433
    • Shumaker, H.B.1    Lamont, A.2    Firor, W.M.3
  • 133
    • 0019956937 scopus 로고
    • The interaction between aminoquinolines and presynaptically acting neurotoxins
    • Simpson L.L. The interaction between aminoquinolines and presynaptically acting neurotoxins. J. Pharmacol. Exp. Ther. 222:1982;43-48.
    • (1982) J. Pharmacol. Exp. Ther. , vol.222 , pp. 43-48
    • Simpson, L.L.1
  • 134
    • 0020522175 scopus 로고
    • Ammonium chloride and methylamine hydrochloride antagonize clostridial neurotoxins
    • Simpson L.L. Ammonium chloride and methylamine hydrochloride antagonize clostridial neurotoxins. J. Pharmacol. Exp. Ther. 225:1983;546-552.
    • (1983) J. Pharmacol. Exp. Ther. , vol.225 , pp. 546-552
    • Simpson, L.L.1
  • 136
    • 0028293577 scopus 로고
    • Inhibition of vacuolar adenosine triphosphatase antagonizes the effects of clostridial neurotoxins but not phospholipase A2 neurotoxins
    • Simpson L.L., Coffield J.L., Bakry N. Inhibition of vacuolar adenosine triphosphatase antagonizes the effects of clostridial neurotoxins but not phospholipase A2 neurotoxins. J. Pharmacol. Exp. Ther. 269:1994;256-269.
    • (1994) J. Pharmacol. Exp. Ther. , vol.269 , pp. 256-269
    • Simpson, L.L.1    Coffield, J.L.2    Bakry, N.3
  • 137
    • 0030842423 scopus 로고    scopus 로고
    • Human response to botulinum toxin injection: Type B compared with type A
    • Sloop R.R., Cole B.A., Escutin R.O. Human response to botulinum toxin injection: type B compared with type A. Neurology. 49:1997;189-194.
    • (1997) Neurology , vol.49 , pp. 189-194
    • Sloop, R.R.1    Cole, B.A.2    Escutin, R.O.3
  • 139
  • 140
    • 3543096759 scopus 로고    scopus 로고
    • Crystal-structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
    • Sutton R.B., Fasshauer D., Jahn R., Brunger A.T. Crystal-structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution. Nature. 395:1998;347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 142
    • 0028815501 scopus 로고
    • Targeted expression of tetanus toxin light chain in Drosophila specifically eliminates synaptic transmission and causes behavioral defects
    • Sweeney S.T., Broadie K., Keane J., Niemann H., O'Kane C.J. Targeted expression of tetanus toxin light chain in Drosophila specifically eliminates synaptic transmission and causes behavioral defects. Neuron. 14:1995;341-351.
    • (1995) Neuron , vol.14 , pp. 341-351
    • Sweeney, S.T.1    Broadie, K.2    Keane, J.3    Niemann, H.4    O'Kane, C.J.5
  • 143
    • 0024533408 scopus 로고
    • Blocking effects of tetanus toxin and its fragment [A-B] on the excitatory and inhibitory synapses of the spinal motoneurons of the cat
    • Takano K., Kirchner F., Gremmelt A., Matsuda M., Ozutsumi N., Sugimoto N. Blocking effects of tetanus toxin and its fragment [A-B] on the excitatory and inhibitory synapses of the spinal motoneurons of the cat. Toxicon. 27:1989;385-392.
    • (1989) Toxicon , vol.27 , pp. 385-392
    • Takano, K.1    Kirchner, F.2    Gremmelt, A.3    Matsuda, M.4    Ozutsumi, N.5    Sugimoto, N.6
  • 146
    • 0033102461 scopus 로고    scopus 로고
    • Recombinant and truncated tetanus neurotoxin light chain: Cloning, expansion, purification and proteolytic activity
    • Tonello F., Pellizzar R., Pasqualeto S., Graudi G., Peggion E., Montecucco C. Recombinant and truncated tetanus neurotoxin light chain: cloning, expansion, purification and proteolytic activity. Protein. Exp. Purif. 15:1999;221-227.
    • (1999) Protein. Exp. Purif. , vol.15 , pp. 221-227
    • Tonello, F.1    Pellizzar, R.2    Pasqualeto, S.3    Graudi, G.4    Peggion, E.5    Montecucco, C.6
  • 147
    • 0031052777 scopus 로고    scopus 로고
    • Metal substitution of tetanus neurotoxin
    • Tonello F., Schiavo G., Montecucco C. Metal substitution of tetanus neurotoxin. Biochem. J. 322:1997;507-510.
    • (1997) Biochem. J. , vol.322 , pp. 507-510
    • Tonello, F.1    Schiavo, G.2    Montecucco, C.3
  • 149
    • 0002837246 scopus 로고
    • Uber ein neuenanaeroben Bacillus und seine Beziehungen zum Botulismus
    • van Ermengem E. Uber ein neuenanaeroben Bacillus und seine Beziehungen zum Botulismus. Ztschr. Hyg. Infektkr. 26:1897;1-56.
    • (1897) Ztschr. Hyg. Infektkr. , vol.26 , pp. 1-56
    • Van Ermengem, E.1
  • 151
    • 0032953048 scopus 로고    scopus 로고
    • Proteolysis of SNAP-25 isoforms by botulinum neurotoxins type A, C and E: Domains of amino-acid residues controlling the formation of enzyme-substrate complexes and cleavage
    • Vaidyanathan V.V., Yoshino K., Jahnz M., Dorries C., Bade S., Nauenburg S., Niemann H. Proteolysis of SNAP-25 isoforms by botulinum neurotoxins type A, C and E: domains of amino-acid residues controlling the formation of enzyme-substrate complexes and cleavage. J. Neurochem. 72:1999;327-337.
    • (1999) J. Neurochem. , vol.72 , pp. 327-337
    • Vaidyanathan, V.V.1    Yoshino, K.2    Jahnz, M.3    Dorries, C.4    Bade, S.5    Nauenburg, S.6    Niemann, H.7
  • 152
    • 0033037446 scopus 로고    scopus 로고
    • Internalization and proteolytic action of botulinum toxins in CNS neurons and astrocytes
    • Verderio C., Coco S., Rossetto O., Montecucco C., Matteoli M. Internalization and proteolytic action of botulinum toxins in CNS neurons and astrocytes. J. Neurochem. 73:1999;372-379.
    • (1999) J. Neurochem. , vol.73 , pp. 372-379
    • Verderio, C.1    Coco, S.2    Rossetto, O.3    Montecucco, C.4    Matteoli, M.5
  • 153
    • 0030732413 scopus 로고    scopus 로고
    • Botulinum neurotoxin type-A and type-E require the SNARE motif in SNAP-25 for proteolysis
    • Washbourne P., Pellizzari R., Baldini G., Wilson M.C., Montecucco C. Botulinum neurotoxin type-A and type-E require the SNARE motif in SNAP-25 for proteolysis. FEBS Lett. 418:1997;1-5.
    • (1997) FEBS Lett. , vol.418 , pp. 1-5
    • Washbourne, P.1    Pellizzari, R.2    Baldini, G.3    Wilson, M.C.4    Montecucco, C.5
  • 155
    • 0342751280 scopus 로고    scopus 로고
    • Exocytotic mechanism studied by truncated and zero layer mutants of the C-terminus of SNAP-25
    • Wei S.H., Xu T., Ashery U., Kollewe A., Matti U., Antonin W., Rettig J., Neher E. Exocytotic mechanism studied by truncated and zero layer mutants of the C-terminus of SNAP-25. EMBO J. 19:2000;1279-1289.
    • (2000) EMBO J. , vol.19 , pp. 1279-1289
    • Wei, S.H.1    Xu, T.2    Ashery, U.3    Kollewe, A.4    Matti, U.5    Antonin, W.6    Rettig, J.7    Neher, E.8
  • 156
    • 0023028984 scopus 로고
    • Quantitative comparison between tetanus toxin, some fragments and toxoid for binding and axonal transport in the rat
    • Weller U., Taylor C.F., Habermann E. Quantitative comparison between tetanus toxin, some fragments and toxoid for binding and axonal transport in the rat. Toxicon. 24:1986;1055-1063.
    • (1986) Toxicon , vol.24 , pp. 1055-1063
    • Weller, U.1    Taylor, C.F.2    Habermann, E.3
  • 158
    • 0023630082 scopus 로고
    • Tetanus toxin binds with high affinity to neuroblastoma × glioma hybrid cells NG 108 15 and impairs their stimulated acetylcholine release
    • Wellhoner H.H., Neville D.M. Jr. Tetanus toxin binds with high affinity to neuroblastoma × glioma hybrid cells NG 108 15 and impairs their stimulated acetylcholine release. J. Biol. Chem. 262:1987;17374-17378.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17374-17378
    • Wellhoner, H.H.1    Neville D.M., Jr.2
  • 159
    • 0000354574 scopus 로고
    • Tetanus and botulinum neurotoxins
    • H. Herchen, Hucho F. Berlin: Springer-Verlag
    • Wellhoner H.H. Tetanus and botulinum neurotoxins. Herchen H., Hucho F. Handbook of Experimental Pharmacology. vol. 102:1992;357-417 Springer-Verlag, Berlin.
    • (1992) Handbook of Experimental Pharmacology , vol.102 , pp. 357-417
    • Wellhoner, H.H.1
  • 160
    • 0029891288 scopus 로고    scopus 로고
    • Substrate residues N-terminal to the cleavage site of botulinum type B neurotoxin play a role in determining the specificity of its endopeptidase activity
    • Witcome M., Rossetto O., Montecucco C., Shone C.C. Substrate residues N-terminal to the cleavage site of botulinum type B neurotoxin play a role in determining the specificity of its endopeptidase activity. FEBS Lett. 386:1996;133-136.
    • (1996) FEBS Lett. , vol.386 , pp. 133-136
    • Witcome, M.1    Rossetto, O.2    Montecucco, C.3    Shone, C.C.4
  • 161
    • 0027946632 scopus 로고
    • Bafilomycin A1 inhibits the action of tetanus toxin in spinal cord neurons in cell culture
    • Williamson L.C., Neale E.A. Bafilomycin A1 inhibits the action of tetanus toxin in spinal cord neurons in cell culture. J. Neurochem. 63:1994;2342-2345.
    • (1994) J. Neurochem. , vol.63 , pp. 2342-2345
    • Williamson, L.C.1    Neale, E.A.2
  • 162
    • 0029980484 scopus 로고    scopus 로고
    • Clostridial neurotoxins and substrate proteolysis in intact neurons: Botulinum neurotoxin C acts on synaptosomal-associated protein of 25 kDa
    • Williamson L.C., Halpern J.L., Montecucco C., Brown J.E., Neale E.A. Clostridial neurotoxins and substrate proteolysis in intact neurons: botulinum neurotoxin C acts on synaptosomal-associated protein of 25 kDa. J. Biol. Chem. 271:1996;7694-7699.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7694-7699
    • Williamson, L.C.1    Halpern, J.L.2    Montecucco, C.3    Brown, J.E.4    Neale, E.A.5
  • 163
    • 33644681150 scopus 로고    scopus 로고
    • Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity
    • Xu T., Binz T., Niemann H., Neher E. Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity. Nature Neurosci. 1:1998;192-200.
    • (1998) Nature Neurosci. , vol.1 , pp. 192-200
    • Xu, T.1    Binz, T.2    Niemann, H.3    Neher, E.4
  • 164
    • 0033598965 scopus 로고    scopus 로고
    • Inhibition of SNARE complex assembly differentially affects kinetic components of exocytosis
    • Xu T., Rammner B., Margittai M., Artalejo A.R., Neher E., Jahn R. Inhibition of SNARE complex assembly differentially affects kinetic components of exocytosis. Cell. 99:1999;713-722.
    • (1999) Cell , vol.99 , pp. 713-722
    • Xu, T.1    Rammner, B.2    Margittai, M.3    Artalejo, A.R.4    Neher, E.5    Jahn, R.6
  • 167
    • 0028234762 scopus 로고
    • Synaptobrevin/vesicle-associated membrane protein (VAMP) of Aplysia californica: Structure and proteolysis by tetanus toxin and botulinal neurotoxins type D and F
    • Yamasaki S., Hu Y., Binz T., Kalkuhl A., Kurazono H., Tamura T., Jahn R., Kandel E., Niemann H. Synaptobrevin/vesicle-associated membrane protein (VAMP) of Aplysia californica: structure and proteolysis by tetanus toxin and botulinal neurotoxins type D and F. Proc. Natl. Acad. Sci. USA. 91:1994;4688-4692.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4688-4692
    • Yamasaki, S.1    Hu, Y.2    Binz, T.3    Kalkuhl, A.4    Kurazono, H.5    Tamura, T.6    Jahn, R.7    Kandel, E.8    Niemann, H.9
  • 168
    • 0022452373 scopus 로고
    • Tetanus toxin receptors on nerve cells contain a trypsin-sensitive component
    • Yavin E., Nathan A. Tetanus toxin receptors on nerve cells contain a trypsin-sensitive component. Eur. J. Biochem. 154:1986;403-407.
    • (1986) Eur. J. Biochem. , vol.154 , pp. 403-407
    • Yavin, E.1    Nathan, A.2


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