메뉴 건너뛰기




Volumn 47, Issue 2, 2004, Pages 304-314

β-bungarotoxin-induced depletion of synaptic vesicles at the mammalian neuromuscular junction

Author keywords

Bungarotoxin; Botulinum toxin C; Conotoxin MVIIC; Exocytosis

Indexed keywords

BETA BUNGAROTOXIN; BOTULINUM TOXIN; BOTULINUM TOXIN C; CONOTOXIN; SNARE PROTEIN; SYNAPTOPHYSIN; UNCLASSIFIED DRUG; VOLTAGE GATED CALCIUM CHANNEL;

EID: 3042511715     PISSN: 00283908     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuropharm.2004.04.012     Document Type: Article
Times cited : (54)

References (42)
  • 3
    • 84956848860 scopus 로고
    • Observations on the isolated phrenic nerve diaphragm preparation of the rat
    • Bülbring E. Observations on the isolated phrenic nerve diaphragm preparation of the rat. British Journal of Pharmacology. 1:1946;38-61
    • (1946) British Journal of Pharmacology , vol.1 , pp. 38-61
    • Bülbring, E.1
  • 5
    • 84883837027 scopus 로고
    • Isolation of toxins from the venom of Bungarus multicinctus and their modes of neuromuscular blocking action
    • Chang C.C., Lee C.Y. Isolation of toxins from the venom of Bungarus multicinctus and their modes of neuromuscular blocking action. Archives Internationale de Pharmacodynamique. 144:1963;241-257
    • (1963) Archives Internationale de Pharmacodynamique , vol.144 , pp. 241-257
    • Chang, C.C.1    Lee, C.Y.2
  • 7
    • 0014897979 scopus 로고
    • Ultrastructural changes in the motor nerve terminals caused by β-bungarotoxin
    • Chen I.L., Lee C.Y. Ultrastructural changes in the motor nerve terminals caused by β-bungarotoxin. Virchows Archiv. 6:1970;318-325
    • (1970) Virchows Archiv , vol.6 , pp. 318-325
    • Chen, I.L.1    Lee, C.Y.2
  • 8
    • 0032912951 scopus 로고    scopus 로고
    • Nerve terminal damage by β-bungarotoxin. Its clinical significance
    • Dixon R.W., Harris J.B. Nerve terminal damage by β-bungarotoxin. Its clinical significance. American Journal of Pathology. 154:1999;447-455
    • (1999) American Journal of Pathology , vol.154 , pp. 447-455
    • Dixon, R.W.1    Harris, J.B.2
  • 10
    • 0020078313 scopus 로고
    • Binding of β-bungarotoxin to Torpedo electric organ synaptosomes. A high resolution autoradiographic study
    • Esquadera J.E., Solsona C., Marsal J. Binding of β-bungarotoxin to Torpedo electric organ synaptosomes. A high resolution autoradiographic study. Neuroscience. 7:1982;751-758
    • (1982) Neuroscience , vol.7 , pp. 751-758
    • Esquadera, J.E.1    Solsona, C.2    Marsal, J.3
  • 12
    • 0029874232 scopus 로고    scopus 로고
    • Botulinum neurotoxin C1 cleaves both syntaxin and SNAP-25 in intact and permeabilised chromaffin cells; Correlation with its blockade of catecholamine release
    • Foran P., Lawrence G.L., Shone C.C., Foster K.A., Dolly J.O. Botulinum neurotoxin C1 cleaves both syntaxin and SNAP-25 in intact and permeabilised 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.L.2    Shone, C.C.3    Foster, K.A.4    Dolly, J.O.5
  • 15
    • 0002677718 scopus 로고
    • Phospholipases in snake venoms and their effects on nerve and muscle
    • A.L. Harvey. New York: Pergammon Press
    • Harris J.B. Phospholipases in snake venoms and their effects on nerve and muscle. Harvey A.L. Snake Toxins. 1991;91-129 Pergammon Press, New York
    • (1991) Snake Toxins , pp. 91-129
    • Harris, J.B.1
  • 16
    • 85053947236 scopus 로고
    • Snake venom presynaptic toxins
    • A.T. Tu. New York: Marcel Decker
    • Hawgood B., Bon C. Snake venom presynaptic toxins. Tu A.T. Natural Toxins. Reptile Venoms and Toxins. vol. 5:1991;3-52 Marcel Decker, New York
    • (1991) Natural Toxins Reptile Venoms and Toxins , vol.5 , pp. 3-52
    • Hawgood, B.1    Bon, C.2
  • 17
    • 0028807364 scopus 로고
    • Monitoring of black widow spider venom (BWSV) induced exo- and endocytosis in living frog nerve terminals with FMI-43
    • Henkel A.W., Betz W.J. Monitoring of black widow spider venom (BWSV) induced exo- and endocytosis in living frog nerve terminals with FMI-43. Neuropharmacology. 34:1995;1397-1406
    • (1995) Neuropharmacology , vol.34 , pp. 1397-1406
    • Henkel, A.W.1    Betz, W.J.2
  • 18
    • 0036417225 scopus 로고    scopus 로고
    • β-Bungarotoxin is a potent inducer of apoptosis in cultured rat neurons by receptor-mediated internalisation
    • Herkert M., Shakhman O., Schweins E., Becker G.M. β-Bungarotoxin is a potent inducer of apoptosis in cultured rat neurons by receptor-mediated internalisation. European Journal of Neuroscience. 14:2001;821-828
    • (2001) European Journal of Neuroscience , vol.14 , pp. 821-828
    • Herkert, M.1    Shakhman, O.2    Schweins, E.3    Becker, G.M.4
  • 20
    • 0017232429 scopus 로고
    • Evidence that β-bungarotoxin acts at the exterior of nerve terminals
    • Howard B.D., Wu W. Evidence that β-bungarotoxin acts at the exterior of nerve terminals. Brain Research. 103:1976;190-192
    • (1976) Brain Research , vol.103 , pp. 190-192
    • Howard, B.D.1    Wu, W.2
  • 22
    • 0035119874 scopus 로고    scopus 로고
    • Cleavage of intracellular substrates of botulinum toxin A, C and D in a mammalian target tissue
    • Kalandakanond S., Coffield J.A. Cleavage of intracellular substrates of botulinum toxin A, C and D in a mammalian target tissue. Journal of Pharmacology and Experimental Therapy. 296:2001;749-755
    • (2001) Journal of Pharmacology and Experimental Therapy , vol.296 , pp. 749-755
    • Kalandakanond, S.1    Coffield, J.A.2
  • 23
    • 0001166951 scopus 로고
    • A formaldehyde-glutaraldehyde fixative of high osmolarity for use in electron microscopy
    • Karnovsky M.J. A formaldehyde-glutaraldehyde fixative of high osmolarity for use in electron microscopy. Journal of Cell Biology. 27:1965;137A
    • (1965) Journal of Cell Biology , vol.27
    • Karnovsky, M.J.1
  • 28
    • 0344406175 scopus 로고    scopus 로고
    • Taipoxin induces F-actin fragmentation and enhances release of catecholamines in bovine chromaffin cells
    • Nico P., Rossetto O., Gil A., Montecucco S., Gutierrez L.M. Taipoxin induces F-actin fragmentation and enhances release of catecholamines in bovine chromaffin cells. Journal of Neurochemistry. 85:2003;329-337
    • (2003) Journal of Neurochemistry , vol.85 , pp. 329-337
    • Nico, P.1    Rossetto, O.2    Gil, A.3    Montecucco, S.4    Gutierrez, L.M.5
  • 30
    • 0022508383 scopus 로고
    • 2-mediated attack on cholinergic synaptic vesicles by β-bungarotoxin
    • 2-mediated attack on cholinergic synaptic vesicles by β-bungarotoxin. Journal of Neurochemistry. 47:1986;1312-1317
    • (1986) Journal of Neurochemistry , vol.47 , pp. 1312-1317
    • Noremberg, K.1    Parsons, S.M.2
  • 31
    • 0028904492 scopus 로고
    • 2+ channel currents in rat cerebellar granule neurons
    • 2+ channel currents in rat cerebellar granule neurons. Journal of Neuroscience. 15:1995;2995-3012
    • (1995) Journal of Neuroscience , vol.15 , pp. 2995-3012
    • Randall, A.1    Tsien, R.W.2
  • 32
    • 0025092390 scopus 로고
    • β-bungarotoxin-mediated liposome fusion: Spectroscopic characterisation by fluorescence and ESR
    • Rufini S., Pedersen J.Z., Desideri A., Luly P. β-bungarotoxin- mediated liposome fusion: spectroscopic characterisation by fluorescence and ESR. Biochemistry. 29:1990;9644-9651
    • (1990) Biochemistry , vol.29 , pp. 9644-9651
    • Rufini, S.1    Pedersen, J.Z.2    Desideri, A.3    Luly, P.4
  • 33
    • 0022630108 scopus 로고
    • The mechanism of action of β-bungarotoxin at the presynaptic plasma membrane
    • Rugulo M., Dolly J.O., Nicholls D.G. The mechanism of action of β-bungarotoxin at the presynaptic plasma membrane. Biochemical Journal. 233:1986;519-523
    • (1986) Biochemical Journal , vol.233 , pp. 519-523
    • Rugulo, M.1    Dolly, J.O.2    Nicholls, D.G.3
  • 37
    • 0017694474 scopus 로고
    • Selective enzymatic hydrolysis of nerve terminal phospholipids by β-bungarotoxin: Biological and morphological studies
    • Z. Hall, R. Kelly, & C.F. Fox. New York: Alan Liss
    • Strong P.N., Heuser J.E., Kelly R.O. Selective enzymatic hydrolysis of nerve terminal phospholipids by β-bungarotoxin: biological and morphological studies. Hall Z., Kelly R., Fox C.F. Cellular Neurobiology. 1977;227-249 Alan Liss, New York
    • (1977) Cellular Neurobiology , pp. 227-249
    • Strong, P.N.1    Heuser, J.E.2    Kelly, R.O.3
  • 38
    • 0020396024 scopus 로고
    • A method demonstrating motor end-plates for light and electron microscopy
    • Strum J.M., Hall-Craggs E.C.B. A method demonstrating motor end-plates for light and electron microscopy. Journal of Neuroscience Methods. 6:1982;305-309
    • (1982) Journal of Neuroscience Methods , vol.6 , pp. 305-309
    • Strum, J.M.1    Hall-Craggs, E.C.B.2
  • 41
    • 0028258190 scopus 로고
    • 2+ channels in supporting hippocampal synaptic transmission
    • 2+ channels in supporting hippocampal synaptic transmission. Science. 264:1994;107-111
    • (1994) Science , vol.264 , pp. 107-111
    • Wheeler, D.B.1    Randall, A.D.2    Tsien, R.W.3
  • 42
    • 0029980484 scopus 로고    scopus 로고
    • Clostridial neurotoxins and substrate proteolysis in intact neurons: Botulinum C acts on synaptosomal-associated protein of 24 kDa
    • Williamson L.C., Halpern J.L., Montecucco C., Brown J.E., Neale E.A. Clostridial neurotoxins and substrate proteolysis in intact neurons: botulinum C acts on synaptosomal-associated protein of 24 kDa. Journal of Biological Chemistry. 271:1996;7694-7699
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 7694-7699
    • Williamson, L.C.1    Halpern, J.L.2    Montecucco, C.3    Brown, J.E.4    Neale, E.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.