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Volumn 82, Issue 5, 2000, Pages 427-446

How botulinum and tetanus neurotoxins block neurotransmitter release

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCHOLINE; BOTULINUM TOXIN; METALLOPROTEINASE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; PROTEIN KINASE C; SNARE PROTEIN; SYNAPTOBREVIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNTAXIN; TETANUS TOXIN;

EID: 0034121745     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(00)00216-9     Document Type: Article
Times cited : (401)

References (221)
  • 1
    • 0342285706 scopus 로고
    • Studio esperimentale sull'eziologia del tetano
    • Carle A., Rattone G. Studio esperimentale sull'eziologia del tetano. Giorn. Accad. Mede. Torino. 32:1884;174-179.
    • (1884) Giorn. Accad. Mede. Torino , vol.32 , pp. 174-179
    • Carle, A.1    Rattone, G.2
  • 2
    • 0002837246 scopus 로고
    • Über einem neuen anaeroben Bacillus und seine Beziehungen zum Botulisms
    • Van Ermengen E. Über einem neuen anaeroben Bacillus und seine Beziehungen zum Botulisms. Z. Hyg. Infeckt. Krankh. 26:1897;1-56.
    • (1897) Z. Hyg. Infeckt. Krankh. , vol.26 , pp. 1-56
    • Van Ermengen, E.1
  • 3
    • 85031579963 scopus 로고
    • The history of tetanus
    • G. Nistico, B. Bizzini, B. Bytchneko, & R. Triau. Rome-Milan: Pyrthagora Press
    • Pitzura M. The history of tetanus. Nistico G, Bizzini B, Bytchneko B, Triau R. Eight International Conference on Tetanus. 1989;1-15 Pyrthagora Press, Rome-Milan.
    • (1989) Eight International Conference on Tetanus , pp. 1-15
    • Pitzura, M.1
  • 5
    • 0000712596 scopus 로고
    • Molecular Biology of Clostridial neurotoxins
    • J.E. Alouf, & J.H. Freer. San Diego: Academic Press
    • Niemann H. Molecular Biology of Clostridial neurotoxins. Alouf J.E, Freer J.H. Sourcebook of bacterial protein toxins. 1991;303-348 Academic Press, San Diego.
    • (1991) Sourcebook of Bacterial Protein Toxins , pp. 303-348
    • Niemann, H.1
  • 7
    • 0002301979 scopus 로고
    • The action of botulinum toxin on neuromuscular junction
    • Burgen A.S.V., Dickens F., Zatman L.J. The action of botulinum toxin on neuromuscular junction. J. Physiol. (Lond.). 109:1949;10-24.
    • (1949) J. Physiol. (Lond.) , vol.109 , pp. 10-24
    • Burgen, A.S.V.1    Dickens, F.2    Zatman, L.J.3
  • 8
    • 0019619833 scopus 로고
    • The origin, structure, and pharmacological activity of botulinum toxin
    • Simpson L.L. The origin, structure, and pharmacological activity of botulinum toxin. Pharmacol. Rev. 33:1981;155-188.
    • (1981) Pharmacol. Rev. , vol.33 , pp. 155-188
    • Simpson, L.L.1
  • 10
    • 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., Niemann H. The complete sequence of botulinum neurotoxin type A and comparison with other clostridial neurotoxins. J. Biol. Chem. 265:1990;9153-9158.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9153-9158
    • Binz, T.1    Kurazono, H.2    Wille, M.3    Frevert, J.4    Wernars, K.5    Niemann, H.6
  • 12
    • 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
  • 13
    • 0028268948 scopus 로고
    • Clostridial neurotoxins: New tools for dissecting exocytosis
    • Niemann H., Blasi J., Jahn R. Clostridial neurotoxins: new tools for dissecting exocytosis. Trends Cell Biol. 4:1994;179-185.
    • (1994) Trends Cell Biol. , vol.4 , pp. 179-185
    • Niemann, H.1    Blasi, J.2    Jahn, R.3
  • 14
    • 0029613765 scopus 로고
    • Structure and function of tetanus and botulinum neurotoxins
    • Montecucco C., Schiavo G. Structure and function of tetanus and botulinum neurotoxins. Q. Rev. Biophys. 28:1995;423-472.
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 423-472
    • Montecucco, C.1    Schiavo, G.2
  • 15
    • 0031712779 scopus 로고    scopus 로고
    • Crystal structure of botulinum neurotoxin type A and implications for toxicity
    • Lacy D.B., Tepp W., Cohen A.C., DasGupta B.R., Stevens R.C. Crystal structure of botulinum neurotoxin type A and implications for toxicity. Nat. Struct. Biol. 5:1998;898-902.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 898-902
    • Lacy, D.B.1    Tepp, W.2    Cohen, A.C.3    Dasgupta, B.R.4    Stevens, R.C.5
  • 16
    • 0026548114 scopus 로고
    • Properties and use of botulinum toxin and other microbial neurotoxins in medicine
    • Schantz E.J., Johnson E.A. Properties and use of botulinum toxin and other microbial neurotoxins in medicine. Microbiol. Rev. 56:1992;80-99.
    • (1992) Microbiol. Rev. , vol.56 , pp. 80-99
    • Schantz, E.J.1    Johnson, E.A.2
  • 17
    • 0029160109 scopus 로고
    • Ecology of neurotoxigenic strains of clostridia
    • Popoff M.R. Ecology of neurotoxigenic strains of clostridia. Curr. Top. Microbiol. Immunol. 195:1995;1-29.
    • (1995) Curr. Top. Microbiol. Immunol. , vol.195 , pp. 1-29
    • Popoff, M.R.1
  • 19
    • 0030802038 scopus 로고    scopus 로고
    • Rho proteins: Targets for bacterial toxins
    • Aktories K. Rho proteins: targets for bacterial toxins. Trends Microbiol. 5:1997;282-288.
    • (1997) Trends Microbiol. , vol.5 , pp. 282-288
    • Aktories, K.1
  • 20
    • 0032496097 scopus 로고    scopus 로고
    • Interactions between bacterial toxins and intestinal cells
    • Popoff M.R. Interactions between bacterial toxins and intestinal cells. Toxicon. 36:1998;665-685.
    • (1998) Toxicon , vol.36 , pp. 665-685
    • Popoff, M.R.1
  • 21
    • 0002891522 scopus 로고
    • The Structure of Botulinum Neurotoxin
    • L.L. Simpson. San Diego: Academic Press Inc
    • DasGupta B.R. The Structure of Botulinum Neurotoxin. Simpson L.L. Botulinum neurotoxin and tetanus toxin. 1989;53-67 Academic Press Inc, San Diego.
    • (1989) Botulinum Neurotoxin and Tetanus Toxin , pp. 53-67
    • Dasgupta, B.R.1
  • 23
    • 0024964619 scopus 로고
    • Reductive chain separation of botulinum A toxin - A prerequisite to its inhibitory action on exocytosis in chromaffin cells
    • Stecher B., Gratzl M., Ahnert-Hilger G. Reductive chain separation of botulinum A toxin - a prerequisite to its inhibitory action on exocytosis in chromaffin cells. FEBS Lett. 248:1989;23-27.
    • (1989) FEBS Lett. , vol.248 , pp. 23-27
    • Stecher, B.1    Gratzl, M.2    Ahnert-Hilger, G.3
  • 24
    • 0002750164 scopus 로고    scopus 로고
    • Structural and genomic features of clostridial neurotoxins
    • J.H. Freer, & J.E. Alouf. London: Academic Press
    • Popoff M.R., Marvaud J.C. Structural and genomic features of clostridial neurotoxins. Freer J.H, Alouf J.E. The Comprehensive Sourcebook of Bacterial Protein Toxins. 1999;202-228 Academic Press, London.
    • (1999) The Comprehensive Sourcebook of Bacterial Protein Toxins , pp. 202-228
    • Popoff, M.R.1    Marvaud, J.C.2
  • 26
    • 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 G.M., Stevens R.C. Biophysical characterization of the stability of the 150-kilodalton botulinum toxin, the nontoxic component, and the 900-kilodalton botulinum toxin complex species. Infect. Immun. 1998;2420-2425.
    • (1998) Infect. Immun. , pp. 2420-2425
    • Chen, F.1    Kuziemko, G.M.2    Stevens, R.C.3
  • 27
    • 0022555430 scopus 로고
    • Molecular pharmacology of botulinum toxin and tetanus toxin
    • Simpson L.L. Molecular pharmacology of botulinum toxin and tetanus toxin. Annu. Rev. Pharmacol. Toxicol. 26:1986;427-453.
    • (1986) Annu. Rev. Pharmacol. Toxicol. , vol.26 , pp. 427-453
    • Simpson, L.L.1
  • 29
    • 0029122024 scopus 로고
    • Botulism: The present status of the disease
    • Hatheway C.L. Botulism: the present status of the disease. Curr. Top. Microbiol. Immunol. 195:1995;55-75.
    • (1995) Curr. Top. Microbiol. Immunol. , vol.195 , pp. 55-75
    • Hatheway, C.L.1
  • 30
    • 0013602913 scopus 로고
    • Botulinus toxin: Effect on the central nervous system of man
    • Tyler H.R. Botulinus toxin: effect on the central nervous system of man. Science. 139:1963;847-848.
    • (1963) Science , vol.139 , pp. 847-848
    • Tyler, H.R.1
  • 31
    • 0017701735 scopus 로고
    • The action of botulinum A neurotoxin on the inhibition by antidromic stimulation of the lumbar monosynaptic reflex
    • Wiegand H., Wellhoner H.H. The action of botulinum A neurotoxin on the inhibition by antidromic stimulation of the lumbar monosynaptic reflex. Naunyn Schmiedebergs Arch. Pharmacol. 298:1977;235-238.
    • (1977) Naunyn Schmiedebergs Arch. Pharmacol. , vol.298 , pp. 235-238
    • Wiegand, H.1    Wellhoner, H.H.2
  • 32
    • 0028134740 scopus 로고
    • Botulinum neurotoxin alters the discharge characteristics of abducens motoneurons in the alert cat
    • Moreno-Lopez B., De La Cruz R.R., Pastor A.M., Delgado-Garcia J.M. Botulinum neurotoxin alters the discharge characteristics of abducens motoneurons in the alert cat. J. Neurophysiol. 72:1994;2041-2044.
    • (1994) J. Neurophysiol. , vol.72 , pp. 2041-2044
    • Moreno-Lopez, B.1    De La Cruz, R.R.2    Pastor, A.M.3    Delgado-Garcia, J.M.4
  • 34
    • 0014431104 scopus 로고
    • Tetanus toxin and spinal inhibition
    • Curtis D.R., De Groat W.C. Tetanus toxin and spinal inhibition. Brain Res. 10:1968;208-212.
    • (1968) Brain Res. , vol.10 , pp. 208-212
    • Curtis, D.R.1    De Groat, W.C.2
  • 35
    • 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 Schmiedebergs Arch. Pharmacol. 311:1980;33-40.
    • (1980) Naunyn Schmiedebergs Arch. Pharmacol. , vol.311 , pp. 33-40
    • Habermann, E.1    Dreyer, F.2    Bigalke, H.3
  • 36
    • 0021287337 scopus 로고
    • A study of the action of tetanus toxin at rat soleus neuromuscular junctions
    • Bevan S., Wendon L.M. A study of the action of tetanus toxin at rat soleus neuromuscular junctions. J. Physiol. (Lond.). 348:1984;1-17.
    • (1984) J. Physiol. (Lond.) , vol.348 , pp. 1-17
    • Bevan, S.1    Wendon, L.M.2
  • 37
    • 0016210779 scopus 로고
    • Observations on the action of type A botulinum toxin on frog neuromuscular junctions
    • Boroff D.A., Del Castillo J., Evoy W.H., Steinhardt R.A. Observations on the action of type A botulinum toxin on frog neuromuscular junctions. J. Physiol. (Lond.). 240:1974;227-253.
    • (1974) J. Physiol. (Lond.) , vol.240 , pp. 227-253
    • Boroff, D.A.1    Del Castillo, J.2    Evoy, W.H.3    Steinhardt, R.A.4
  • 38
    • 0017141174 scopus 로고
    • Botulinum toxin: Mechanism of presynaptic blockade
    • Kao I., Drachman D.B., Price D.L. Botulinum toxin: mechanism of presynaptic blockade. Science. 193:1976;1256-1258.
    • (1976) Science , vol.193 , pp. 1256-1258
    • Kao, I.1    Drachman, D.B.2    Price, D.L.3
  • 39
    • 0017157878 scopus 로고
    • Effects of botulinum toxin on neuromuscular transmission in the rat
    • Cull-Candy S.G., Lundh H., Thesleff S. Effects of botulinum toxin on neuromuscular transmission in the rat. J. Physiol. (Lond.). 260:1976;177-203.
    • (1976) J. Physiol. (Lond.) , vol.260 , pp. 177-203
    • Cull-Candy, S.G.1    Lundh, H.2    Thesleff, S.3
  • 40
    • 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. Transmitter release in tetanus and botulinum A toxin-poisoned mammalian motor endplates and its dependence on nerve stimulation and temperature. Pflugers. Arch. 399:1983;228-234.
    • (1983) Pflugers. Arch. , vol.399 , pp. 228-234
    • Dreyer, F.1    Schmitt, A.2
  • 41
    • 0023161962 scopus 로고
    • Acetylcholine receptors and sodium channels in denervated and botulinum-toxin-treated adult rat muscle
    • Bambrick L., Gordon T. Acetylcholine receptors and sodium channels in denervated and botulinum-toxin-treated adult rat muscle. J. Physiol. (Lond.). 382:1987;69-86.
    • (1987) J. Physiol. (Lond.) , vol.382 , pp. 69-86
    • Bambrick, L.1    Gordon, T.2
  • 42
    • 0028279433 scopus 로고
    • Botulinum toxin converts muscle acetylcholine receptors from adult to embryonic type
    • Koltgen D., Ceballos-Baumann A.O., Franke C. Botulinum toxin converts muscle acetylcholine receptors from adult to embryonic type. Muscle Nerve. 17:1994;779-784.
    • (1994) Muscle Nerve , vol.17 , pp. 779-784
    • Koltgen, D.1    Ceballos-Baumann, A.O.2    Franke, C.3
  • 43
    • 85031579268 scopus 로고    scopus 로고
    • Neurotoxins affecting the quantal acetylcholine release from vertebrate motor nerve terminals
    • Molgó J., Van der Kloot W., Poulain B. Neurotoxins affecting the quantal acetylcholine release from vertebrate motor nerve terminals. Int. Rev. Cytol. 00:2000.
    • (2000) Int. Rev. Cytol. , vol.0
    • Molgó, J.1    Van Der Kloot, W.2    Poulain, B.3
  • 44
    • 0028110103 scopus 로고
    • Quantal acetylcholine release at the vertebrate neuromuscular junction
    • Van der Kloot W, Molgó J. Quantal acetylcholine release at the vertebrate neuromuscular junction. Physiol. Rev. 74:1994;915-926.
    • (1994) Physiol. Rev. , vol.74 , pp. 915-926
    • Van Der Kloot, W.1    Molgó, J.2
  • 47
    • 0028284526 scopus 로고
    • Molecular mechanisms of action of bacterial protein toxins
    • Menestrina G., Schiavo G., Montecucco C. Molecular mechanisms of action of bacterial protein toxins. Mol. Aspects M. 15:1994;79-193.
    • (1994) Mol. Aspects M , vol.15 , pp. 79-193
    • Menestrina, G.1    Schiavo, G.2    Montecucco, C.3
  • 48
    • 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
  • 49
    • 0024356962 scopus 로고
    • Light chain of tetanus toxin intracellularly inhibits acetylcholine release at neuro-neuronal synapses, and its internalization is mediated by heavy chain
    • Mochida S., Poulain B., Weller U., Habermann E., Tauc L. Light chain of tetanus toxin intracellularly inhibits acetylcholine release at neuro-neuronal synapses, and its internalization is mediated by heavy chain. FEBS Lett. 253:1989;47-51.
    • (1989) FEBS Lett. , vol.253 , pp. 47-51
    • Mochida, S.1    Poulain, B.2    Weller, U.3    Habermann, E.4    Tauc, L.5
  • 50
    • 0024353830 scopus 로고
    • Isolated light chains of botulinum neurotoxins inhibit exocytosis. Studies in digitonin-permeabilized chromaffin cells
    • Bittner M.A., DasGupta B.R., Holz R.W. Isolated light chains of botulinum neurotoxins inhibit exocytosis. Studies in digitonin-permeabilized chromaffin cells. J. Biol. Chem. 264:1989;10354-10360.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10354-10360
    • Bittner, M.A.1    Dasgupta, B.R.2    Holz, R.W.3
  • 51
    • 0025676110 scopus 로고
    • Light chain of botulinum neurotoxin is active in mammalian motor nerve terminals when delivered via liposomes
    • De Paiva A., Dolly J.O. Light chain of botulinum neurotoxin is active in mammalian motor nerve terminals when delivered via liposomes. FEBS Lett. 277:1990;171-174.
    • (1990) FEBS Lett. , vol.277 , pp. 171-174
    • De Paiva, A.1    Dolly, J.O.2
  • 52
    • 0023888382 scopus 로고
    • Neurotransmitter release is blocked intracellularly by botulinum neurotoxin, and this requires uptake of both toxin polypeptides by a process mediated by the larger chain
    • Poulain B., Tauc L., Maisey E.A., Wadsworth J.D., Mohan P.M., Dolly J.O. Neurotransmitter release is blocked intracellularly by botulinum neurotoxin, and this requires uptake of both toxin polypeptides by a process mediated by the larger chain. Proc. Natl. Acad. Sci. USA. 85:1988;4090-4094.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 4090-4094
    • Poulain, B.1    Tauc, L.2    Maisey, E.A.3    Wadsworth, J.D.4    Mohan, P.M.5    Dolly, J.O.6
  • 54
    • 0024559146 scopus 로고
    • A unique signature identifies a family of zinc-dependent metallopeptidases
    • Jongeneel C.V., Bouvier J., Bairoch A. A unique signature identifies a family of zinc-dependent metallopeptidases. FEBS Lett. 242:1989;211-214.
    • (1989) FEBS Lett. , vol.242 , pp. 211-214
    • Jongeneel, C.V.1    Bouvier, J.2    Bairoch, A.3
  • 55
    • 0026795607 scopus 로고
    • Identification and partial characterization of a low affinity metal-binding site in the light chain of tetanus toxin
    • Wright J.F., Pernollet M., Reboul A., Aude C., Colomb M.G. Identification and partial characterization of a low affinity metal-binding site in the light chain of tetanus toxin. J. Biol. Chem. 267:1992;9053-9058.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9053-9058
    • Wright, J.F.1    Pernollet, M.2    Reboul, A.3    Aude, C.4    Colomb, M.G.5
  • 57
    • 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
  • 58
    • 0027442891 scopus 로고
    • Chelation of zinc antagonizes the neuromuscular blocking properties of the seven serotypes of botulinum neurotoxin as well as tetanus toxin
    • Simpson L.L., Coffield J.A., Bakry N. Chelation of zinc antagonizes the neuromuscular blocking properties of the seven serotypes of botulinum neurotoxin as well as tetanus toxin. J. Pharmacol. Exp. Ther. 267:1993;720-727.
    • (1993) J. Pharmacol. Exp. Ther. , vol.267 , pp. 720-727
    • Simpson, L.L.1    Coffield, J.A.2    Bakry, N.3
  • 59
    • 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
  • 61
    • 0029076502 scopus 로고
    • Interactions between heavy metal chelators and botulinum neurotoxins at the mouse neuromuscular junction
    • Sheridan R.E., Deshpande S.S. Interactions between heavy metal chelators and botulinum neurotoxins at the mouse neuromuscular junction. Toxicon. 33:1995;539-549.
    • (1995) Toxicon , vol.33 , pp. 539-549
    • Sheridan, R.E.1    Deshpande, S.S.2
  • 62
    • 0032515962 scopus 로고    scopus 로고
    • Role of zinc in the structure and toxic activity of botulinum neurotoxin
    • Fu F.N., Lomneth R.B., Cai S., Singh B.R. Role of zinc in the structure and toxic activity of botulinum neurotoxin. Biochemistry. 37:1998;5267-5278.
    • (1998) Biochemistry , vol.37 , pp. 5267-5278
    • Fu, F.N.1    Lomneth, R.B.2    Cai, S.3    Singh, B.R.4
  • 64
    • 0029074183 scopus 로고
    • A study of zinc-dependent metalloendopeptidase inhibitors as pharmacological antagonists in botulinum neurotoxin poisoning
    • Deshpande S.S., Sheridan R.E., Adler M. A study of zinc-dependent metalloendopeptidase inhibitors as pharmacological antagonists in botulinum neurotoxin poisoning. Toxicon. 33:1995;551-557.
    • (1995) Toxicon , vol.33 , pp. 551-557
    • Deshpande, S.S.1    Sheridan, R.E.2    Adler, M.3
  • 65
    • 0032537562 scopus 로고    scopus 로고
    • Efficacy of a novel metalloprotease inhibitor on botulinum neurotoxin B activity
    • Adler M., Nicholson J.D., Cornille F., Hackley B.E. Jr. Efficacy of a novel metalloprotease inhibitor on botulinum neurotoxin B activity. FEBS Lett. 429:1998;234-238.
    • (1998) FEBS Lett. , vol.429 , pp. 234-238
    • Adler, M.1    Nicholson, J.D.2    Cornille, F.3    Hackley B.E., Jr.4
  • 67
    • 0031691573 scopus 로고    scopus 로고
    • The active site structure of tetanus neurotoxin resolved by multiple scattering analysis in X-ray absorption spectroscopy
    • Meneghini C., Morante S. The active site structure of tetanus neurotoxin resolved by multiple scattering analysis in X-ray absorption spectroscopy. Biophys. J. 75:1998;1953-1963.
    • (1998) Biophys. J. , vol.75 , pp. 1953-1963
    • Meneghini, C.1    Morante, S.2
  • 69
    • 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
  • 70
    • 0028216482 scopus 로고
    • A single mutation in the recombinant light chain of tetanus toxin abolishes its proteolytic activity and removes the toxicity seen after reconstitution with native heavy chain
    • Li Y., Foran P., Fairweather N.F., de Paiva A., Weller U., Dougan G., Dolly J.O. A single mutation in the recombinant light chain of tetanus toxin abolishes its proteolytic activity and removes the toxicity seen after reconstitution with native heavy chain. Biochemistry. 33:1994;7014-7020.
    • (1994) Biochemistry , vol.33 , pp. 7014-7020
    • Li, Y.1    Foran, P.2    Fairweather, N.F.3    De Paiva, A.4    Weller, U.5    Dougan, G.6    Dolly, J.O.7
  • 71
    • 0028268948 scopus 로고
    • Clostridial neurotoxins: New tools for dissecting exocytosis
    • Niemann H., Blasi J., Jahn R. Clostridial neurotoxins: new tools for dissecting exocytosis. Trends Cell Biol. 4:1994;179-185.
    • (1994) Trends Cell Biol. , vol.4 , pp. 179-185
    • Niemann, H.1    Blasi, J.2    Jahn, R.3
  • 72
    • 0030732413 scopus 로고    scopus 로고
    • Botulinum neurotoxin types A and E require the SNARE motif in SNAP-25 for proteolysis
    • Washbourne P., Pellizzari R., Baldini G., Wilson M.C., Montecucco C. Botulinum neurotoxin types A and 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
  • 73
    • 0032953048 scopus 로고    scopus 로고
    • Proteolysis of SNAP-25 isoforms by botulinum neurotoxin types A, C, and E: Domains and 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., Binz T. Proteolysis of SNAP-25 isoforms by botulinum neurotoxin types A, C, and E: domains and 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    Binz, T.8
  • 74
    • 0033529593 scopus 로고    scopus 로고
    • Identification of SNAREs involved in regulated exocytosis in the pancreatic acinar cell
    • Hansen N.J., Antonin W., Edwardson J.M. Identification of SNAREs involved in regulated exocytosis in the pancreatic acinar cell. J. Biol. Chem. 274:1999;22871-22876.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22871-22876
    • Hansen, N.J.1    Antonin, W.2    Edwardson, J.M.3
  • 75
    • 0030897432 scopus 로고    scopus 로고
    • In vitro characterization of botulinum toxin types A, C and D action on human tissues: Combined electrophysiologic, pharmacologic and molecular biologic approaches
    • Coffield J.A., Bakry N., Zhang R.D., Carlson J., Gomella L.G., Simpson L.L. In vitro characterization of botulinum toxin types A, C and D action on human tissues: combined electrophysiologic, pharmacologic and molecular biologic approaches. J. Pharmacol. Exp. Ther. 280:1997;1489-1498.
    • (1997) J. Pharmacol. Exp. Ther. , vol.280 , pp. 1489-1498
    • Coffield, J.A.1    Bakry, N.2    Zhang, R.D.3    Carlson, J.4    Gomella, L.G.5    Simpson, L.L.6
  • 77
    • 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
  • 78
    • 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
  • 80
    • 0033491695 scopus 로고    scopus 로고
    • Activity-dependent changes in partial VAMP complexes during neurotransmitter release
    • Hua S.Y., Charlton M.P. Activity-dependent changes in partial VAMP complexes during neurotransmitter release. Nat. Neurosci. 2:1999;1078-1083.
    • (1999) Nat. Neurosci. , vol.2 , pp. 1078-1083
    • Hua, S.Y.1    Charlton, M.P.2
  • 81
    • 0028130728 scopus 로고
    • Synaptic vesicle membrane fusion complex: Action of clostridial neurotoxins on assembly
    • Hayashi T., Mc Mahon H., Yamasaki S., Binz T., Hata Y., Südhof 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    Mc Mahon, H.2    Yamasaki, S.3    Binz, T.4    Hata, Y.5    Südhof, T.C.6    Niemann, H.7
  • 82
    • 0027946206 scopus 로고
    • Fusion complex formation protects synaptobrevin against proteolysis by tetanus toxin light chain
    • Pellegrini L.L., O' Connor V., Betz H. Fusion complex formation protects synaptobrevin against proteolysis by tetanus toxin light chain. FEBS Lett. 353:1994;319-323.
    • (1994) FEBS Lett. , vol.353 , pp. 319-323
    • Pellegrini, L.L.1    O.'. Connor, V.2    Betz, H.3
  • 83
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution
    • Sutton R.B., Fasshauer D., Jahn R., Brunger A.T. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A 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
  • 84
    • 0030607217 scopus 로고    scopus 로고
    • Adrenal chromaffin cells contain functionally different SNAP-25 monomers and SNAP-25/syntaxin heterodimers
    • Hohne-Zell B., Gratzl M. Adrenal chromaffin cells contain functionally different SNAP-25 monomers and SNAP-25/syntaxin heterodimers. FEBS Lett. 394:1996;109-116.
    • (1996) FEBS Lett. , vol.394 , pp. 109-116
    • Hohne-Zell, B.1    Gratzl, M.2
  • 85
    • 0033057030 scopus 로고    scopus 로고
    • A stable interaction between syntaxin 1a and synaptobrevin 2 mediated by their transmembrane domains
    • Margittai M., Otto H., Jahn R. A stable interaction between syntaxin 1a and synaptobrevin 2 mediated by their transmembrane domains. FEBS Lett. 446:1999;40-44.
    • (1999) FEBS Lett. , vol.446 , pp. 40-44
    • Margittai, M.1    Otto, H.2    Jahn, R.3
  • 86
    • 0031019926 scopus 로고    scopus 로고
    • Binding of the synaptic vesicle v-SNARE, synaptotagmin, to the plasma membrane t-SNARE, SNAP-25, can explain docked vesicles at neurotoxin-treated synapses
    • Schiavo G., Stenbeck G., Rothman J.E., Söllner T.H. Binding of the synaptic vesicle v-SNARE, synaptotagmin, to the plasma membrane t-SNARE, SNAP-25, can explain docked vesicles at neurotoxin-treated synapses. Proc. Natl. Acad. Sci. USA. 94:1997;997-1001.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 997-1001
    • Schiavo, G.1    Stenbeck, G.2    Rothman, J.E.3    Söllner, T.H.4
  • 87
    • 0027971368 scopus 로고
    • Vesicle-associated membrane protein and synaptophysin are associated on the synaptic vesicle
    • Calakos N., Scheller R.H. Vesicle-associated membrane protein and synaptophysin are associated on the synaptic vesicle. J. Biol. Chem. 269:1994;24534-24537.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24534-24537
    • Calakos, N.1    Scheller, R.H.2
  • 88
    • 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
  • 90
    • 0027198568 scopus 로고
    • Antibodies against rat brain vesicle-associated membrane protein (synaptobrevin) prevent inhibition of acetylcholine release by tetanus toxin or botulinum neurotoxin type B
    • Poulain B., Rossetto O., Deloye F., Schiavo G., Tauc L., Montecucco C. Antibodies against rat brain vesicle-associated membrane protein (synaptobrevin) prevent inhibition of acetylcholine release by tetanus toxin or botulinum neurotoxin type B. J. Neurochem. 61:1993;1175-1178.
    • (1993) J. Neurochem. , vol.61 , pp. 1175-1178
    • Poulain, B.1    Rossetto, O.2    Deloye, F.3    Schiavo, G.4    Tauc, L.5    Montecucco, C.6
  • 91
    • 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
  • 92
    • 0032418273 scopus 로고    scopus 로고
    • Different VAMP/synaptobrevin complexes for spontaneous and evoked transmitter release at the crayfish neuromuscular junction
    • Hua S.Y., Raciborska D.A., Trimble W.S., Charlton M.P. Different VAMP/synaptobrevin complexes for spontaneous and evoked transmitter release at the crayfish neuromuscular junction. J. Neurophysiol. 80:1998;3233-3246.
    • (1998) J. Neurophysiol. , vol.80 , pp. 3233-3246
    • Hua, S.Y.1    Raciborska, D.A.2    Trimble, W.S.3    Charlton, M.P.4
  • 94
    • 0031016979 scopus 로고    scopus 로고
    • Inhibition of transmitter release correlates with the proteolytic activity of tetanus toxin and botulinus toxin A in individual cultured synapses of Hirudo medicinalis
    • Bruns D., Engers S., Yang C., Ossig R., Jeromin A., Jahn R. Inhibition of transmitter release correlates with the proteolytic activity of tetanus toxin and botulinus toxin A in individual cultured synapses of Hirudo medicinalis. J. Neurosci. 17:1997;1898-1910.
    • (1997) J. Neurosci. , vol.17 , pp. 1898-1910
    • Bruns, D.1    Engers, S.2    Yang, C.3    Ossig, R.4    Jeromin, A.5    Jahn, R.6
  • 96
    • 0023162290 scopus 로고
    • Botulinum toxin inhibits quantal acetylcholine release and energy metabolism in the Torpedo electric organ
    • Dunant Y., Esquerda J.E., Loctin F., Marsal J., Muller D. Botulinum toxin inhibits quantal acetylcholine release and energy metabolism in the Torpedo electric organ. J. Physiol. (Lond.). 385:1987;677-692.
    • (1987) J. Physiol. (Lond.) , vol.385 , pp. 677-692
    • Dunant, Y.1    Esquerda, J.E.2    Loctin, F.3    Marsal, J.4    Muller, D.5
  • 97
    • 0023877985 scopus 로고
    • Tetanus and botulinum toxins block the release of acetylcholine from slices of rat striatum and from the isolated electric organ of Torpedo at different concentrations
    • Rabasseda X., Blasi J., Marsal J., Dunant Y., Casanova A., Bizzini B. Tetanus and botulinum toxins block the release of acetylcholine from slices of rat striatum and from the isolated electric organ of Torpedo at different concentrations. Toxicon. 26:1988;329-336.
    • (1988) Toxicon , vol.26 , pp. 329-336
    • Rabasseda, X.1    Blasi, J.2    Marsal, J.3    Dunant, Y.4    Casanova, A.5    Bizzini, B.6
  • 98
    • 0023101807 scopus 로고
    • Differential effects of various secretagogues on quantal transmitter release from mouse motor nerve terminals treated with botulinum A and tetanus toxin
    • Dreyer F., Rosenberg F., Becker C., Bigalke H., Penner R. Differential effects of various secretagogues on quantal transmitter release from mouse motor nerve terminals treated with botulinum A and tetanus toxin. Naunyn Schmiedebergs Arch. Pharmacol. 335:1987;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
  • 99
    • 0023180498 scopus 로고
    • Distinct sites of action of clostridial neurotoxins revealed by double-poisoning of mouse motor nerve terminals
    • Gansel M., Penner R., Dreyer F. Distinct sites of action of clostridial neurotoxins revealed by double-poisoning of mouse motor nerve terminals. Pflugers Arch. 409:1987;533-539.
    • (1987) Pflugers Arch. , vol.409 , pp. 533-539
    • Gansel, M.1    Penner, R.2    Dreyer, F.3
  • 100
    • 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
  • 101
    • 0024535487 scopus 로고
    • A study of synchronization of quantal transmitter release from mammalian motor endings by the use of botulinal toxins type A and D
    • Molgó J., Siegel L.S., Tabti N., Thesleff S. A study of synchronization of quantal transmitter release from mammalian motor endings by the use of botulinal toxins type A and D. J. Physiol. (Lond.). 411:1989;195-205.
    • (1989) J. Physiol. (Lond.) , vol.411 , pp. 195-205
    • Molgó, J.1    Siegel, L.S.2    Tabti, N.3    Thesleff, S.4
  • 103
    • 0030050917 scopus 로고    scopus 로고
    • Axonal transport and distribution of synaptobrevin I and II in the rat peripheral nervous system
    • Li J.Y., Edelmann L., Jahn R., Dahlstrom A. Axonal transport and distribution of synaptobrevin I and II in the rat peripheral nervous system. J. Neurosci. 16:1996;137-147.
    • (1996) J. Neurosci. , vol.16 , pp. 137-147
    • Li, J.Y.1    Edelmann, L.2    Jahn, R.3    Dahlstrom, A.4
  • 104
    • 0030612655 scopus 로고    scopus 로고
    • 2+ partially rescues synaptic transmission in hippocampal cultures treated with botulinum toxin A and C, but not tetanus toxin
    • 2+ partially rescues synaptic transmission in hippocampal cultures treated with botulinum toxin A and C, but not tetanus toxin. J. Neurosci. 17:1997;7190-7202.
    • (1997) J. Neurosci. , vol.17 , pp. 7190-7202
    • Capogna, M.1    Mc Kinney, R.A.2    O.'. Connor, V.3    Gahwiler, B.H.4    Thompson, S.M.5
  • 105
    • 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
  • 107
    • 0032521343 scopus 로고    scopus 로고
    • Distinct requirements for evoked and spontaneous release of neurotransmitter are revealed by mutations in the Drosophila gene neuronal-synaptobrevin
    • Deitcher D.L., Ueda A., Stewart B.A., Burgess R.W., Kidokoro Y., Schwarz T.L. Distinct requirements for evoked and spontaneous release of neurotransmitter are revealed by mutations in the Drosophila gene neuronal-synaptobrevin. J. Neurosci. 18:1998;2028-2039.
    • (1998) J. Neurosci. , vol.18 , pp. 2028-2039
    • Deitcher, D.L.1    Ueda, A.2    Stewart, B.A.3    Burgess, R.W.4    Kidokoro, Y.5    Schwarz, T.L.6
  • 109
    • 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
  • 110
    • 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
  • 111
    • 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
  • 114
    • 0029004741 scopus 로고
    • Disassembly of the reconstituded synaptic vesicle membrane fusion complex in vitro
    • Hayashi T., Yamasaki S., Nauenburg S., Binz T., Niemann H. Disassembly of the reconstituded synaptic vesicle membrane fusion complex in vitro. EMBO J. 14:1995;2317-2325.
    • (1995) EMBO J. , vol.14 , pp. 2317-2325
    • Hayashi, T.1    Yamasaki, S.2    Nauenburg, S.3    Binz, T.4    Niemann, H.5
  • 115
    • 0027973132 scopus 로고
    • SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin via domains that may form coiled coils
    • Chapman E.R., An S., Barton N., Jahn R. SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin via domains that may form coiled coils. J. Biol. Chem. 269:1994;27427-27432.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27427-27432
    • Chapman, E.R.1    An, S.2    Barton, N.3    Jahn, R.4
  • 116
    • 0029118637 scopus 로고
    • Clostridial neurotoxins compromise the stability of a low energy SNARE complex mediating NSF activation of synaptic vesicle fusion
    • Pellegrini L.L., O'Connor V., Lottspeich F., Betz H. Clostridial neurotoxins compromise the stability of a low energy SNARE complex mediating NSF activation of synaptic vesicle fusion. EMBO J. 14:1995;4705-4713.
    • (1995) EMBO J. , vol.14 , pp. 4705-4713
    • Pellegrini, L.L.1    O'Connor, V.2    Lottspeich, F.3    Betz, H.4
  • 117
    • 0031051382 scopus 로고    scopus 로고
    • Effect of mutations in vesicle-associated membrane protein (VAMP) on the assembly of multimeric protein complexes
    • Hao J.C., Salem N., Peng X.R., Kelly R.B., Bennett M.K. Effect of mutations in vesicle-associated membrane protein (VAMP) on the assembly of multimeric protein complexes. J. Neurosci. 17:1997;1596-1603.
    • (1997) J. Neurosci. , vol.17 , pp. 1596-1603
    • Hao, J.C.1    Salem, N.2    Peng, X.R.3    Kelly, R.B.4    Bennett, M.K.5
  • 119
    • 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., DasGupta 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    Dasgupta, B.R.4    Dolly, J.O.5
  • 120
    • 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. Nat. Neurosci. 1:1998;192-200.
    • (1998) Nat. Neurosci. , vol.1 , pp. 192-200
    • Xu, T.1    Binz, T.2    Niemann, H.3    Neher, E.4
  • 121
    • 0032509210 scopus 로고    scopus 로고
    • Calcium can disrupt the SNARE protein complex on sea urchin egg secretory vesicles without irreversibly blocking fusion
    • Tahara M., Coorssen J.R., Timmers K., Blank P.S., Whalley T., Scheller R., Zimmerberg J. Calcium can disrupt the SNARE protein complex on sea urchin egg secretory vesicles without irreversibly blocking fusion. J. Biol. Chem. 273:1998;33667-33673.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33667-33673
    • Tahara, M.1    Coorssen, J.R.2    Timmers, K.3    Blank, P.S.4    Whalley, T.5    Scheller, R.6    Zimmerberg, J.7
  • 122
    • 0033366466 scopus 로고    scopus 로고
    • Snapin: A SNARE-associated protein implicated in synaptic transmission
    • Ilardi J.M., Mochida S., Sheng Z.H. Snapin: a SNARE-associated protein implicated in synaptic transmission. Nat. Neurosci. 2:1999;119-124.
    • (1999) Nat. Neurosci. , vol.2 , pp. 119-124
    • Ilardi, J.M.1    Mochida, S.2    Sheng, Z.H.3
  • 123
    • 0032079715 scopus 로고    scopus 로고
    • Protease resistance of syntaxin. SNAP-25. VAMP complexes. Implications for assembly and structure
    • Poirier M.A., Hao J.C., Malkus P.N., Chan C., Moore M.F., King D.S., Bennett M.K. Protease resistance of syntaxin. SNAP-25. VAMP complexes. Implications for assembly and structure. J. Biol. Chem. 273:1998;11370-11377.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11370-11377
    • Poirier, M.A.1    Hao, J.C.2    Malkus, P.N.3    Chan, C.4    Moore, M.F.5    King, D.S.6    Bennett, M.K.7
  • 124
    • 0032944111 scopus 로고    scopus 로고
    • Evidence for calcium-dependent vesicular transmitter release insensitive to tetanus toxin and botulinum toxin type F
    • Fassio A., Sala R., Bonanno G., Marchi M., Raiteri M. Evidence for calcium-dependent vesicular transmitter release insensitive to tetanus toxin and botulinum toxin type F. Neuroscience. 90:1999;893-902.
    • (1999) Neuroscience , vol.90 , pp. 893-902
    • Fassio, A.1    Sala, R.2    Bonanno, G.3    Marchi, M.4    Raiteri, M.5
  • 125
    • 0033567076 scopus 로고    scopus 로고
    • Tetanus toxin blocks the exocytosis of synaptic vesicles clustered at synapses but not of synaptic vesicles in isolated axons
    • Verderio C., Coco S., Bacci A., Rossetto O., De Camilli P., Montecucco C., Matteoli M. Tetanus toxin blocks the exocytosis of synaptic vesicles clustered at synapses but not of synaptic vesicles in isolated axons. J. Neurosci. 19:1999;6723-6732.
    • (1999) J. Neurosci. , vol.19 , pp. 6723-6732
    • Verderio, C.1    Coco, S.2    Bacci, A.3    Rossetto, O.4    De Camilli, P.5    Montecucco, C.6    Matteoli, M.7
  • 126
    • 0032198135 scopus 로고    scopus 로고
    • A v-SNARE participates in synaptic vesicle formation mediated by the AP3 adaptor complex
    • Salem N., Faundez V., Horng J.T., Kelly R.B. A v-SNARE participates in synaptic vesicle formation mediated by the AP3 adaptor complex. Nat. Neurosci. 1:1998;551-556.
    • (1998) Nat. Neurosci. , vol.1 , pp. 551-556
    • Salem, N.1    Faundez, V.2    Horng, J.T.3    Kelly, R.B.4
  • 127
    • 0029041786 scopus 로고
    • Inhibition of neurotransmitter release by synthetic prolin-rich peptides shows that the N-terminal domain of vesicle associated membrane protein/synaptobrevin is critical for neuro-exocytosis
    • Cornille F., Deloye F., Fournié-Zaluski M.C., Roques B.P., Poulain B. Inhibition of neurotransmitter release by synthetic prolin-rich peptides shows that the N-terminal domain of vesicle associated membrane protein/synaptobrevin is critical for neuro-exocytosis. J. Biol. Chem. 270:1995;16826-16832.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16826-16832
    • Cornille, F.1    Deloye, F.2    Fournié-Zaluski, M.C.3    Roques, B.P.4    Poulain, B.5
  • 128
    • 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., Ferrer-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    Ferrer-Montiel, A.V.4    Canaves, J.M.5    Montal, M.6
  • 130
    • 0020960846 scopus 로고
    • Comparison of the effects of botulinum neurotoxin types A and E at the rat neuromuscular junction
    • Sellin L.C., Kauffman J.A., DasGupta B.R. Comparison of the effects of botulinum neurotoxin types A and E at the rat neuromuscular junction. Med. Biol. 61:1983;120-125.
    • (1983) Med. Biol. , vol.61 , pp. 120-125
    • Sellin, L.C.1    Kauffman, J.A.2    Dasgupta, B.R.3
  • 131
    • 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 parent terminals
    • De Paiva A., Meunier F.A., Molgó 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 parent 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    Molgó, J.3    Aoki, K.R.4    Dolly, J.O.5
  • 132
    • 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. Scand. 119:1983;127-133.
    • (1983) Acta Physiol. Scand. , vol.119 , pp. 127-133
    • Sellin, L.C.1    Thesleff, S.2    Dasgupta, B.R.3
  • 133
    • 0032515187 scopus 로고    scopus 로고
    • Different time courses of recovery after poisoning with botulinum neurotoxin serotypes A and E in humans
    • Eleopra R., Tugnoli V., Rossetto O., De Grandis D., Montecucco C. Different time courses of recovery after poisoning with botulinum neurotoxin serotypes A and E in humans. Neurosci. Lett. 256:1998;135-138.
    • (1998) Neurosci. Lett. , vol.256 , pp. 135-138
    • Eleopra, R.1    Tugnoli, V.2    Rossetto, O.3    De Grandis, D.4    Montecucco, C.5
  • 134
    • 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
  • 135
    • 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
  • 136
    • 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., 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    Dolly, J.O.5
  • 138
    • 0026655015 scopus 로고
    • Tetanus toxin potently stimulates tissue transglutaminase. A possible mechanism of neurotoxicity
    • Facchiano F., Luini A. Tetanus toxin potently stimulates tissue transglutaminase. A possible mechanism of neurotoxicity. J. Biol. Chem. 267:1992;13267-13271.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13267-13271
    • Facchiano, F.1    Luini, A.2
  • 139
    • 0027480066 scopus 로고
    • Covalent modification of synapsin I by a tetanus toxin-activated transglutaminase
    • Facchiano F., Benfenati F., Valtorta F., Luini A. Covalent modification of synapsin I by a tetanus toxin-activated transglutaminase. J. Biol. Chem. 268:1993;4588-4591.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4588-4591
    • Facchiano, F.1    Benfenati, F.2    Valtorta, F.3    Luini, A.4
  • 140
    • 0343082127 scopus 로고    scopus 로고
    • Intraneuronal transglutaminases are required for blockade of neurotransmitter release by tetanus toxin
    • Deloye F., Poulain B., Luini A., Facchiano F. Intraneuronal transglutaminases are required for blockade of neurotransmitter release by tetanus toxin. Toxicon. 34:1996;1086-1087.
    • (1996) Toxicon , vol.34 , pp. 1086-1087
    • Deloye, F.1    Poulain, B.2    Luini, A.3    Facchiano, F.4
  • 141
    • 0025959348 scopus 로고
    • Tetanus and botulinum A toxins inhibit stimulated F-actin rearrangement in chromaffin cells
    • Marxen P., Bigalke H. Tetanus and botulinum A toxins inhibit stimulated F-actin rearrangement in chromaffin cells. NeuroReport. 2:1991;33-36.
    • (1991) NeuroReport , vol.2 , pp. 33-36
    • Marxen, P.1    Bigalke, H.2
  • 142
    • 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
  • 143
    • 0026738405 scopus 로고
    • Tetanus toxin inhibits depolarization-stimulated protein phosphorylation in rat cortical synaptosomes: Effect on synapsin I phosphorylation and translocation
    • Presek P., Jessen S., Dreyer F., Jarvie P.E., Findik D., Dunkley P.R. Tetanus toxin inhibits depolarization-stimulated protein phosphorylation in rat cortical synaptosomes: effect on synapsin I phosphorylation and translocation. J. Neurochem. 59:1992;1336-1343.
    • (1992) J. Neurochem. , vol.59 , pp. 1336-1343
    • Presek, P.1    Jessen, S.2    Dreyer, F.3    Jarvie, P.E.4    Findik, D.5    Dunkley, P.R.6
  • 144
    • 0027317119 scopus 로고
    • Protease activity of botulinum neurotoxin type E and its light chain: Cleavage of actin
    • DasGupta B.R., Tepp W. Protease activity of botulinum neurotoxin type E and its light chain: cleavage of actin. Biochem. Biophys. Res. Commun. 190:1993;470-474.
    • (1993) Biochem. Biophys. Res. Commun. , vol.190 , pp. 470-474
    • Dasgupta, B.R.1    Tepp, W.2
  • 145
    • 0025055306 scopus 로고
    • In vivo translocation and down-regulation of protein kinase C following intraventricular administration of tetanus toxin
    • Aguilera J., Yavin E. In vivo translocation and down-regulation of protein kinase C following intraventricular administration of tetanus toxin. J. Neurochem. 54:1990;339-342.
    • (1990) J. Neurochem. , vol.54 , pp. 339-342
    • Aguilera, J.1    Yavin, E.2
  • 146
    • 0027392831 scopus 로고
    • GT1b ganglioside prevents tetanus toxin-induced protein kinase C activation and down-regulation in the neonatal brain in vivo
    • Aguilera J., Padros-Giralt C., Habig W.H., Yavin E. GT1b ganglioside prevents tetanus toxin-induced protein kinase C activation and down-regulation in the neonatal brain in vivo. J. Neurochem. 60:1993;709-713.
    • (1993) J. Neurochem. , vol.60 , pp. 709-713
    • Aguilera, J.1    Padros-Giralt, C.2    Habig, W.H.3    Yavin, E.4
  • 147
    • 0031882564 scopus 로고    scopus 로고
    • Tetanus toxin enhances protein kinase C activity translocation and increases polyphosphoinositide hydrolysis in rat cerebral cortex preparations
    • Gil C., Ruiz-Meana M., Alava M., Yavin E., Aguilera J. Tetanus toxin enhances protein kinase C activity translocation and increases polyphosphoinositide hydrolysis in rat cerebral cortex preparations. J. Neurochem. 70:1998;1636-1643.
    • (1998) J. Neurochem. , vol.70 , pp. 1636-1643
    • Gil, C.1    Ruiz-Meana, M.2    Alava, M.3    Yavin, E.4    Aguilera, J.5
  • 148
    • 0023890087 scopus 로고
    • Diminished activity of protein kinase C in tetanus toxin-treated macrophages and in the spinal cord of mice manifesting generalized tetanus intoxication
    • Ho J.L., Klempner M.S. Diminished activity of protein kinase C in tetanus toxin-treated macrophages and in the spinal cord of mice manifesting generalized tetanus intoxication. J. Infect. Dis. 157:1988;925-933.
    • (1988) J. Infect. Dis. , vol.157 , pp. 925-933
    • Ho, J.L.1    Klempner, M.S.2
  • 149
    • 0024314117 scopus 로고
    • A role for cGMP during tetanus toxin blockade of acetylcholine release in the rat pheochromocytoma (PC12) cell line
    • Sandberg K., Berry C.J., Eugster E., Rogers T.B. A role for cGMP during tetanus toxin blockade of acetylcholine release in the rat pheochromocytoma (PC12) cell line. J. Neurosci. 9:1989;3946-3954.
    • (1989) J. Neurosci. , vol.9 , pp. 3946-3954
    • Sandberg, K.1    Berry, C.J.2    Eugster, E.3    Rogers, T.B.4
  • 151
    • 0033048096 scopus 로고    scopus 로고
    • Clostridium neurotoxins influence serotonin uptake and release differently in rat brain synaptosomes
    • Najib A., Pelliccioni P., Gil C., Aguilera J. Clostridium neurotoxins influence serotonin uptake and release differently in rat brain synaptosomes. J. Neurochem. 72:1999;1991-1998.
    • (1999) J. Neurochem. , vol.72 , pp. 1991-1998
    • Najib, A.1    Pelliccioni, P.2    Gil, C.3    Aguilera, J.4
  • 152
    • 0018951535 scopus 로고
    • Botulinum toxin injection into extraocular muscles as an alternative to strabismus surgery
    • Scott A.B. Botulinum toxin injection into extraocular muscles as an alternative to strabismus surgery. Ophthalmology. 87:1980;1044-1049.
    • (1980) Ophthalmology , vol.87 , pp. 1044-1049
    • Scott, A.B.1
  • 155
    • 0029114846 scopus 로고
    • The present status of tetanus and tetanus vaccination
    • Galazka A., Gasse F. The present status of tetanus and tetanus vaccination. Curr. Topic Microbiol. Immunol. 195:1995;31-53.
    • (1995) Curr. Topic Microbiol. Immunol. , vol.195 , pp. 31-53
    • Galazka, A.1    Gasse, F.2
  • 156
    • 0020663105 scopus 로고
    • Botulinum neurotoxin type E: Studies on mechanism of action and on structure-activity relationships
    • Simpson L.L., DasGupta B.R. Botulinum neurotoxin type E: studies on mechanism of action and on structure-activity relationships. J. Pharmacol. Exp. Ther. 224:1983;135-140.
    • (1983) J. Pharmacol. Exp. Ther. , vol.224 , pp. 135-140
    • Simpson, L.L.1    Dasgupta, B.R.2
  • 157
    • 0024306217 scopus 로고
    • Characterization of the actions of botulinum neurotoxin type E at the rat neuromuscular junction
    • Molgó J., DasGupta B.R., Thesleff S. Characterization of the actions of botulinum neurotoxin type E at the rat neuromuscular junction. Acta. Physiol. Scand. 137:1989;497-501.
    • (1989) Acta. Physiol. Scand. , vol.137 , pp. 497-501
    • Molgó, J.1    Dasgupta, B.R.2    Thesleff, S.3
  • 158
    • 0021209479 scopus 로고
    • Miniature end-plate potentials in rat skeletal muscle poisoned with botulinum toxin
    • Kim Y.I., Lomo T., Lupa M.T., Thesleff S. Miniature end-plate potentials in rat skeletal muscle poisoned with botulinum toxin. J. Physiol. (Lond.). 356:1984;587-599.
    • (1984) J. Physiol. (Lond.) , vol.356 , pp. 587-599
    • Kim, Y.I.1    Lomo, T.2    Lupa, M.T.3    Thesleff, S.4
  • 159
    • 0030027138 scopus 로고    scopus 로고
    • Effect of 3,4-diaminopyridine on rat extensor digitorum longus muscle paralyzed by local injection of botulinum neurotoxin
    • Adler M., Macdonald D.A., Sellin L.C., Parker G.W. Effect of 3,4-diaminopyridine on rat extensor digitorum longus muscle paralyzed by local injection of botulinum neurotoxin. Toxicon. 34:1996;237-249.
    • (1996) Toxicon , vol.34 , pp. 237-249
    • Adler, M.1    MacDonald, D.A.2    Sellin, L.C.3    Parker, G.W.4
  • 160
    • 0007957382 scopus 로고
    • Mode of action of botulinum toxin E on the transmitter release process at the mouse neuromuscular junction
    • Wieszt L., Dreyer F. Mode of action of botulinum toxin E on the transmitter release process at the mouse neuromuscular junction. Naunyn Schmiedeberg Arch. Pharmacol. 344:1991;R74.
    • (1991) Naunyn Schmiedeberg Arch. Pharmacol. , vol.344 , pp. 74
    • Wieszt, L.1    Dreyer, F.2
  • 161
    • 0025331378 scopus 로고
    • Response of the chick ciliary ganglion-iris neuromuscular preparation to botulinum neurotoxin
    • Lomneth R., Suszkiw J.B., DasGupta B.R. Response of the chick ciliary ganglion-iris neuromuscular preparation to botulinum neurotoxin. Neurosci. Lett. 113:1990;211-216.
    • (1990) Neurosci. Lett. , vol.113 , pp. 211-216
    • Lomneth, R.1    Suszkiw, J.B.2    Dasgupta, B.R.3
  • 162
    • 0018187764 scopus 로고
    • Experimental botulism in chickens: The cecum as the site of production and absorption of botulinum toxin
    • Miyazaki S., Sakaguchi G. Experimental botulism in chickens: the cecum as the site of production and absorption of botulinum toxin. Jpn. J. Med. Sci. Biol. 31:1978;1-15.
    • (1978) Jpn. J. Med. Sci. Biol. , vol.31 , pp. 1-15
    • Miyazaki, S.1    Sakaguchi, G.2
  • 163
    • 0021279206 scopus 로고
    • Studies on the mode of action of botulinum toxin type A at the frog neuromuscular junction
    • Molgó J., Thesleff S. Studies on the mode of action of botulinum toxin type A at the frog neuromuscular junction. Brain Res. 297:1984;309-316.
    • (1984) Brain Res. , vol.297 , pp. 309-316
    • Molgó, J.1    Thesleff, S.2
  • 164
    • 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
  • 165
    • 0015123666 scopus 로고
    • The effect of type D botulinum toxin on frog neuromuscular junctions
    • Harris A.J., Miledi R. The effect of type D botulinum toxin on frog neuromuscular junctions. J. Physiol. (Lond.). 217:1971;497-515.
    • (1971) J. Physiol. (Lond.) , vol.217 , pp. 497-515
    • Harris, A.J.1    Miledi, R.2
  • 166
    • 0015369160 scopus 로고
    • The effect of tetanus toxin at the neuromuscular junction in the goldfish
    • Mellanby J., Thompson P.A. The effect of tetanus toxin at the neuromuscular junction in the goldfish. J. Physiol. (Lond.). 224:1972;407-419.
    • (1972) J. Physiol. (Lond.) , vol.224 , pp. 407-419
    • Mellanby, J.1    Thompson, P.A.2
  • 167
    • 0028818658 scopus 로고
    • Tetanus toxin inhibits spontaneous quantal release and cleaves VAMP/synaptobrevin
    • Herreros J., Miralles F.X., Solsona C., Bizzini B., Blasi J., Marsal J. Tetanus toxin inhibits spontaneous quantal release and cleaves VAMP/synaptobrevin. Brain Res. 699:1995;165-170.
    • (1995) Brain Res. , vol.699 , pp. 165-170
    • Herreros, J.1    Miralles, F.X.2    Solsona, C.3    Bizzini, B.4    Blasi, J.5    Marsal, J.6
  • 169
    • 0024829325 scopus 로고
    • Multiple domains of botulinum neurotoxin contribute to its inhibition of transmitter release in Aplysia neurons
    • Poulain B., Wadsworth J.D., Shone C.C., Mochida S., Lande S., Melling J., Dolly O., Tauc L. Multiple domains of botulinum neurotoxin contribute to its inhibition of transmitter release in Aplysia neurons. J. Biol. Chem. 264:1989;21928-21933.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21928-21933
    • Poulain, B.1    Wadsworth, J.D.2    Shone, C.C.3    Mochida, S.4    Lande, S.5    Melling, J.6    Dolly, O.7    Tauc, L.8
  • 170
    • 0028241680 scopus 로고
    • Transmission at the squid giant synapse was blocked by tetanus toxin by affecting synaptobrevin, a vesicle-bound protein
    • Llinas R., Sugimori M., Chu D., Morita M., Blasi J., Herreros J., Jahn R., Marsal J. Transmission at the squid giant synapse was blocked by tetanus toxin by affecting synaptobrevin, a vesicle-bound protein. J. Physiol. (Lond.). 477:1994;129-133.
    • (1994) J. Physiol. (Lond.) , vol.477 , pp. 129-133
    • Llinas, R.1    Sugimori, M.2    Chu, D.3    Morita, M.4    Blasi, J.5    Herreros, J.6    Jahn, R.7    Marsal, J.8
  • 171
    • 0028817584 scopus 로고
    • Genetic and electrophysiological studies of Drosophila syntaxin-1A demonstrate its role in non-neuronal secretion and neurotransmission
    • Schulze K.L., Broadie K., Perin M.S., Bellen H.J. Genetic and electrophysiological studies of Drosophila syntaxin-1A demonstrate its role in non-neuronal secretion and neurotransmission. Cell. 80:1995;311-320.
    • (1995) Cell , vol.80 , pp. 311-320
    • Schulze, K.L.1    Broadie, K.2    Perin, M.S.3    Bellen, H.J.4
  • 172
    • 0022544443 scopus 로고
    • Facilitation, augmentation and potentiation of transmitter release at frog neuromuscular junctions poisoned with botulinum toxin
    • Lupa M.T., Tabti N. Facilitation, augmentation and potentiation of transmitter release at frog neuromuscular junctions poisoned with botulinum toxin. Pflugers Arch. 406:1986;636-640.
    • (1986) Pflugers Arch. , vol.406 , pp. 636-640
    • Lupa, M.T.1    Tabti, N.2
  • 174
    • 0024495678 scopus 로고
    • Is the internal calcium regulation altered in type A botulinum toxin-poisoned motor endings?
    • Mallart A., Molgó J., Angaut-Petit D., Thesleff S. Is the internal calcium regulation altered in type A botulinum toxin-poisoned motor endings? Brain Res. 479:1989;167-171.
    • (1989) Brain Res. , vol.479 , pp. 167-171
    • Mallart, A.1    Molgó, J.2    Angaut-Petit, D.3    Thesleff, S.4
  • 175
    • 0030991439 scopus 로고    scopus 로고
    • 2+-free medium is associated with depletion of synaptic vesicles and swelling of motor nerve terminals in situ
    • 2+-free medium is associated with depletion of synaptic vesicles and swelling of motor nerve terminals in situ. Neuroscience. 78:1997;883-893.
    • (1997) Neuroscience , vol.78 , pp. 883-893
    • Meunier, F.A.1    Colasante, C.2    Molgó, J.3
  • 176
    • 0019858289 scopus 로고
    • Different effects of botulinum A toxin and tetanus toxin on the transmitter releasing process at the mammalian neuromuscular junction
    • Dreyer F., Schmitt A. Different effects of botulinum A toxin and tetanus toxin on the transmitter releasing process at the mammalian neuromuscular junction. Neurosci. Lett. 26:1981;307-311.
    • (1981) Neurosci. Lett. , vol.26 , pp. 307-311
    • Dreyer, F.1    Schmitt, A.2
  • 177
    • 0015550928 scopus 로고
    • The effects of tetanus toxin on neuromuscular transmission and on the morphology of motor end-plates in slow and fast skeletal muscle of the mouse
    • Duchen L.W., Tonge D.A. The effects of tetanus toxin on neuromuscular transmission and on the morphology of motor end-plates in slow and fast skeletal muscle of the mouse. J. Physiol. (Lond.). 228:1973;157-172.
    • (1973) J. Physiol. (Lond.) , vol.228 , pp. 157-172
    • Duchen, L.W.1    Tonge, D.A.2
  • 178
    • 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
  • 179
    • 0022570456 scopus 로고
    • A preclinical evaluation of aminopyridines as putative therapeutic agents in the treatment of botulism
    • Simpson L.L. A preclinical evaluation of aminopyridines as putative therapeutic agents in the treatment of botulism. Infect. Immun. 52:1986;858-862.
    • (1986) Infect. Immun. , vol.52 , pp. 858-862
    • Simpson, L.L.1
  • 180
    • 0023227635 scopus 로고
    • Aminoglycosides and 3,4-diaminopyridine on neuromuscular block caused by botulinum type A toxin
    • Molgó J., Lemeignan M., Thesleff S. Aminoglycosides and 3,4-diaminopyridine on neuromuscular block caused by botulinum type A toxin. Muscle Nerve. 10:1987;464-470.
    • (1987) Muscle Nerve , vol.10 , pp. 464-470
    • Molgó, J.1    Lemeignan, M.2    Thesleff, S.3
  • 181
    • 0023855380 scopus 로고
    • Zinc antagonizes the effect of botulinum type A toxin at the mouse neuromuscular junction
    • Nishimura M., Kozaki S., Sakaguchi G. Zinc antagonizes the effect of botulinum type A toxin at the mouse neuromuscular junction. Experientia. 44:1988;18-20.
    • (1988) Experientia , vol.44 , pp. 18-20
    • Nishimura, M.1    Kozaki, S.2    Sakaguchi, G.3
  • 182
    • 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
  • 183
    • 0017672831 scopus 로고
    • Action of brown widow spider venom and botulinum toxin on the frog neuromuscular junction examined with the freeze-fracture technique
    • Pumplin D.W., Reese T.S. Action of brown widow spider venom and botulinum toxin on the frog neuromuscular junction examined with the freeze-fracture technique. J. Physiol. (Lond.). 273:1977;443-457.
    • (1977) J. Physiol. (Lond.) , vol.273 , pp. 443-457
    • Pumplin, D.W.1    Reese, T.S.2
  • 184
    • 0029940351 scopus 로고    scopus 로고
    • Presynaptic inhibition of calcium-dependent and -independent release elicited with ionomycin, gadolinium, and alpha-latrotoxin in the hippocampus
    • Capogna M., Gahwiler B.H., Thompson S.M. Presynaptic inhibition of calcium-dependent and -independent release elicited with ionomycin, gadolinium, and alpha-latrotoxin in the hippocampus. J. Neurophysiol. 75:1996;2017-2028.
    • (1996) J. Neurophysiol. , vol.75 , pp. 2017-2028
    • Capogna, M.1    Gahwiler, B.H.2    Thompson, S.M.3
  • 185
    • 0025866734 scopus 로고
    • Ultrastructure of botulinum type-A poisoned frog motor nerve terminals after enhanced quantal transmitter release caused by carbonyl cyanide m-chlorophenylhydrazone
    • Pecot-Dechavassine M., Molgó J., Thesleff S. Ultrastructure of botulinum type-A poisoned frog motor nerve terminals after enhanced quantal transmitter release caused by carbonyl cyanide m-chlorophenylhydrazone. Neurosci. Lett. 130:1991;5-8.
    • (1991) Neurosci. Lett. , vol.130 , pp. 5-8
    • Pecot-Dechavassine, M.1    Molgó, J.2    Thesleff, S.3
  • 186
    • 0032944123 scopus 로고    scopus 로고
    • Endocytosis and exocytosis events regulate vesicle traffic in endothelial cells
    • Niles W.D., Malik A.B. Endocytosis and exocytosis events regulate vesicle traffic in endothelial cells. J. Membr. Biol. 167:1999;85-101.
    • (1999) J. Membr. Biol. , vol.167 , pp. 85-101
    • Niles, W.D.1    Malik, A.B.2
  • 187
    • 0342871818 scopus 로고
    • Applications of tetanus toxin for structure-function studies in neuronal cell cultures
    • G. Nistico, B. Bizzini, B. Bytchenko, & R. Triau. Rome, Milan: Pythogora Press
    • Neale E.A., Habig W.H., Schrier B.K., Bergey G.K., Bowers L.M., Koh J. Applications of tetanus toxin for structure-function studies in neuronal cell cultures. Nistico G, Bizzini B, Bytchenko B, Triau R. Eight International Conference on Tetanus. 1989;58-65 Pythogora Press, Rome, Milan.
    • (1989) Eight International Conference on Tetanus , pp. 58-65
    • Neale, E.A.1    Habig, W.H.2    Schrier, B.K.3    Bergey, G.K.4    Bowers, L.M.5    Koh, J.6
  • 188
    • 0020457736 scopus 로고
    • The antagonism between botulinum toxin and calcium in motor nerve terminals
    • Gundersen C.B., Katz B., Miledi R. The antagonism between botulinum toxin and calcium in motor nerve terminals. Proc. R. Soc. Lond. B. Biol. Sci. 216:1982;369-376.
    • (1982) Proc. R. Soc. Lond. B. Biol. Sci. , vol.216 , pp. 369-376
    • Gundersen, C.B.1    Katz, B.2    Miledi, R.3
  • 189
    • 0020524737 scopus 로고
    • Botulinum A toxin and tetanus toxin do not affect presynaptic membrane currents in mammalian motor nerve endings
    • Dreyer F., Mallart A., Brigant J.L. Botulinum A toxin and tetanus toxin do not affect presynaptic membrane currents in mammalian motor nerve endings. Brain Res. 270:1983;373-375.
    • (1983) Brain Res. , vol.270 , pp. 373-375
    • Dreyer, F.1    Mallart, A.2    Brigant, J.L.3
  • 191
    • 0032906479 scopus 로고    scopus 로고
    • The effect of transfection with Botulinum neurotoxin C1 light chain on exocytosis measured in cell populations and by single-cell amperometry in PC12 cells
    • Fisher R.J., Burgoyne R.D. The effect of transfection with Botulinum neurotoxin C1 light chain on exocytosis measured in cell populations and by single-cell amperometry in PC12 cells. Pflugers Arch. 437:1999;754-762.
    • (1999) Pflugers Arch. , vol.437 , pp. 754-762
    • Fisher, R.J.1    Burgoyne, R.D.2
  • 192
    • 0022454866 scopus 로고
    • Intracellularly injected tetanus toxin inhibits exocytosis in bovine adrenal chromaffin cells
    • Penner R., Neher E., Dreyer F. Intracellularly injected tetanus toxin inhibits exocytosis in bovine adrenal chromaffin cells. Nature. 324:1986;76-78.
    • (1986) Nature , vol.324 , pp. 76-78
    • Penner, R.1    Neher, E.2    Dreyer, F.3
  • 193
    • 0024370444 scopus 로고
    • Gangliosides mediate inhibitory effects of tetanus and botulinum A neurotoxins on exocytosis in chromaffin cells
    • Marxen P., Fuhrmann U., Bigalke H. Gangliosides mediate inhibitory effects of tetanus and botulinum A neurotoxins on exocytosis in chromaffin cells. Toxicon. 27:1989;849-859.
    • (1989) Toxicon , vol.27 , pp. 849-859
    • Marxen, P.1    Fuhrmann, U.2    Bigalke, H.3
  • 194
    • 0025193725 scopus 로고
    • 2+-dependent noradrenaline release from permeabilised PC12 cells is blocked by botulinum neurotoxin A or its light chain
    • 2+-dependent noradrenaline release from permeabilised PC12 cells is blocked by botulinum neurotoxin A or its light chain. FEBS Lett. 261:1990;323-326.
    • (1990) FEBS Lett. , vol.261 , pp. 323-326
    • McInnes, C.1    Dolly, J.O.2
  • 195
    • 0027416837 scopus 로고
    • Comparison of the intracellular effects of clostridial neurotoxins on exocytosis from streptolysin O-permeabilized rat pheochromocytoma (PC 12) and bovine adrenal chromaffin cells
    • Ahnert-Hilger G., Weller U. Comparison of the intracellular effects of clostridial neurotoxins on exocytosis from streptolysin O-permeabilized rat pheochromocytoma (PC 12) and bovine adrenal chromaffin cells. Neuroscience. 53:1993;547-552.
    • (1993) Neuroscience , vol.53 , pp. 547-552
    • Ahnert-Hilger, G.1    Weller, U.2
  • 197
    • 0031453767 scopus 로고    scopus 로고
    • Functional importance of synaptobrevin and SNAP-25 during exocytosis of histamine by rat gastric enterochromaffin-like cells
    • Hohne-Zell B., Galler A., Schepp W., Gratzl M., Prinz C. Functional importance of synaptobrevin and SNAP-25 during exocytosis of histamine by rat gastric enterochromaffin-like cells. Endocrinology. 138:1997;5518-5526.
    • (1997) Endocrinology , vol.138 , pp. 5518-5526
    • Hohne-Zell, B.1    Galler, A.2    Schepp, W.3    Gratzl, M.4    Prinz, C.5
  • 199
    • 0028241854 scopus 로고
    • Tetanus toxin light chain cleaves a vesicle-associated membrane protein (VAMP) isoform 2 in rat pancreatic zymogen granules and inhibits enzyme secretion
    • Gaisano H.Y., Sheu L., Foskett J.K., Trimble W.S. Tetanus toxin light chain cleaves a vesicle-associated membrane protein (VAMP) isoform 2 in rat pancreatic zymogen granules and inhibits enzyme secretion. J. Biol. Chem. 269:1994;17062-17066.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17062-17066
    • Gaisano, H.Y.1    Sheu, L.2    Foskett, J.K.3    Trimble, W.S.4
  • 200
    • 0029885364 scopus 로고    scopus 로고
    • Vesicle-associated membrane protein 2 is essential for cAMP-regulated exocytosis in rat parotid acinar cells. The inhibition of cAMP-dependent amylase release by botulinum neurotoxin B
    • Fujita-Yoshigaki J., Dohke Y., Hara-Yokoyama M., Kamata Y., Kozaki S., Furuyama S., Sugiya H. Vesicle-associated membrane protein 2 is essential for cAMP-regulated exocytosis in rat parotid acinar cells. The inhibition of cAMP-dependent amylase release by botulinum neurotoxin B. J. Biol. Chem. 271:1996;13130-13134.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13130-13134
    • Fujita-Yoshigaki, J.1    Dohke, Y.2    Hara-Yokoyama, M.3    Kamata, Y.4    Kozaki, S.5    Furuyama, S.6    Sugiya, H.7
  • 201
    • 0033593207 scopus 로고    scopus 로고
    • Proteins of the exocytotic core complex mediate platelet alpha-granule secretion. Roles of vesicle-associated membrane protein, SNAP-23, and syntaxin 4
    • Flaumenhaft R., Croce K., Chen E., Furie B., Furie B.C. Proteins of the exocytotic core complex mediate platelet alpha-granule secretion. Roles of vesicle-associated membrane protein, SNAP-23, and syntaxin 4. J. Biol. Chem. 274:1999;2492-2501.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2492-2501
    • Flaumenhaft, R.1    Croce, K.2    Chen, E.3    Furie, B.4    Furie, B.C.5
  • 202
    • 0028014529 scopus 로고
    • Cell membrane resealing by a vesicular mechanism similar to neurotransmitter release
    • Steinhardt R.A., Bi G., Alderton J.M. Cell membrane resealing by a vesicular mechanism similar to neurotransmitter release. Science. 263:1994;390-393.
    • (1994) Science , vol.263 , pp. 390-393
    • Steinhardt, R.A.1    Bi, G.2    Alderton, J.M.3
  • 203
    • 0030816723 scopus 로고    scopus 로고
    • In vitro exocytosis in sea urchin eggs requires a synaptobrevin-related protein
    • Avery J., Hodel A., Whitaker M. In vitro exocytosis in sea urchin eggs requires a synaptobrevin-related protein. J. Cell. Sci. 110:1997;1555-1561.
    • (1997) J. Cell. Sci. , vol.110 , pp. 1555-1561
    • Avery, J.1    Hodel, A.2    Whitaker, M.3
  • 206
    • 0031409695 scopus 로고    scopus 로고
    • + secretion is inhibited by clostridial toxins in an inner medullary collecting duct cell line
    • + secretion is inhibited by clostridial toxins in an inner medullary collecting duct cell line. Am. J. Physiol. 273:1997;1054-1057.
    • (1997) Am. J. Physiol. , vol.273 , pp. 1054-1057
    • Alexander, E.A.1    Shih, T.2    Schwartz, J.H.3
  • 207
    • 0033543660 scopus 로고    scopus 로고
    • SNARE proteins regulate H(+)-ATPase redistribution to the apical membrane in rat renal inner medullary collecting duct cells
    • Banerjee A., Shih T., Alexander E.A., Schwartz J.H. SNARE proteins regulate H(+)-ATPase redistribution to the apical membrane in rat renal inner medullary collecting duct cells. J. Biol. Chem. 274:1999;26518-26522.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26518-26522
    • Banerjee, A.1    Shih, T.2    Alexander, E.A.3    Schwartz, J.H.4
  • 208
    • 0028291894 scopus 로고
    • Tetanus toxin-mediated cleavage of cellubrevin impairs exocytosis of transferrin receptor-containing vesicles in CHO cells
    • Galli T., Chilcote T., Mundigl O., Binz T., Niemann H., De Camilli P. Tetanus toxin-mediated cleavage of cellubrevin impairs exocytosis of transferrin receptor-containing vesicles in CHO cells. J. Cell. Biol. 125:1994;1015-1024.
    • (1994) J. Cell. Biol. , vol.125 , pp. 1015-1024
    • Galli, T.1    Chilcote, T.2    Mundigl, O.3    Binz, T.4    Niemann, H.5    De Camilli, P.6
  • 210
    • 0031010616 scopus 로고    scopus 로고
    • Botulinum neurotoxin B inhibits insulin-stimulated glucose uptake into 3T3-Li adipocytes and cleaves cellubrevin unlike type A toxin which failed to proteolyse the SNAP-23 present
    • Chen F., Foran P., Shone C.C., Foster K.A., Melling J., Dolly J.O. Botulinum neurotoxin B inhibits insulin-stimulated glucose uptake into 3T3-Li adipocytes and cleaves cellubrevin unlike type A toxin which failed to proteolyse the SNAP-23 present. Biochemistry. 36:1997;5719-5728.
    • (1997) Biochemistry , vol.36 , pp. 5719-5728
    • Chen, F.1    Foran, P.2    Shone, C.C.3    Foster, K.A.4    Melling, J.5    Dolly, J.O.6
  • 211
    • 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
  • 212
    • 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
  • 213
    • 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
  • 217
    • 0027265710 scopus 로고
    • Cellubrevin is a ubiquitous tetanus-toxin substrate homologous to a putative synaptic vesicle fusion protein
    • Mc Mahon H.T., Ushkaryov Y.A., Edelmann L., Link E., Binz T., Niemann H., Jahn R., Südhof T.C. Cellubrevin is a ubiquitous tetanus-toxin substrate homologous to a putative synaptic vesicle fusion protein. Nature. 364:1993;346-349.
    • (1993) Nature , vol.364 , pp. 346-349
    • Mc Mahon, H.T.1    Ushkaryov, Y.A.2    Edelmann, L.3    Link, E.4    Binz, T.5    Niemann, H.6    Jahn, R.7    Südhof, T.C.8
  • 218
    • 0031814298 scopus 로고    scopus 로고
    • A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells
    • Galli T., Zahraoui A., Vaidyanathan V.V., Raposo G., Tian J.M., Karin M., Niemann H., Louvard D. A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells. Mol. Biol. Cell. 9:1998;1437-1448.
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 1437-1448
    • Galli, T.1    Zahraoui, A.2    Vaidyanathan, V.V.3    Raposo, G.4    Tian, J.M.5    Karin, M.6    Niemann, H.7    Louvard, D.8
  • 219
    • 0027363855 scopus 로고
    • Differential expression of transcripts from syb, a Drosophila melanogaster gene encoding VAMP (synaptobrevin) that is abundant in non-neuronal cells
    • Chin A.C., Burgess R.W., Wong B.R., Schwarz T.L., Scheller R.H. Differential expression of transcripts from syb, a Drosophila melanogaster gene encoding VAMP (synaptobrevin) that is abundant in non-neuronal cells. Gene. 131:1993;175-181.
    • (1993) Gene , vol.131 , pp. 175-181
    • Chin, A.C.1    Burgess, R.W.2    Wong, B.R.3    Schwarz, T.L.4    Scheller, R.H.5


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