메뉴 건너뛰기




Volumn 68, Issue 2, 1997, Pages 649-658

Microtubules and microfilaments participate in the inhibition of synaptosomal noradrenaline release by tetanus toxin

Author keywords

Cytoskeleton; Divalent cations; Endoprotease; Neurotransmitter release; Tetanus toxin; Transglutaminase

Indexed keywords

BARIUM; CALCIUM; COLCHICINE; CYTOCHALASIN D; DANSYLCADAVERINE; NOCODAZOLE; NORADRENALIN; PACLITAXEL; SYNAPTOBREVIN; TETANUS TOXIN; ZINC;

EID: 0031012623     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1997.68020649.x     Document Type: Article
Times cited : (16)

References (58)
  • 2
    • 0023944855 scopus 로고
    • Characterization of the inhibitory action of botulinum neurotoxin type A on the release of several transmitters from rat cerebrocortical synaptosomes
    • Ashton A. C. and Dolly J. O. (1988) Characterization of the inhibitory action of botulinum neurotoxin type A on the release of several transmitters from rat cerebrocortical synaptosomes. J. Neurochem. 50, 1808-1816.
    • (1988) J. Neurochem. , vol.50 , pp. 1808-1816
    • Ashton, A.C.1    Dolly, J.O.2
  • 3
    • 0026032612 scopus 로고
    • Microtubule-dissociatmg drugs and A23187 reveal differences in the inhibition of synaptosomal transmitter release by botulinum neurotoxins type A and B
    • Ashton A. C. and Dolly J. O. (1991) Microtubule-dissociatmg drugs and A23187 reveal differences in the inhibition of synaptosomal transmitter release by botulinum neurotoxins type A and B. J. Neurochem. 56, 827-835.
    • (1991) J. Neurochem. , vol.56 , pp. 827-835
    • Ashton, A.C.1    Dolly, J.O.2
  • 4
    • 0038381241 scopus 로고
    • Factors underlying the characteristic inhibition of the neuronal release of transmitters by tetanus and various botulinum toxins
    • DasGupta B. R., ed. Plenum Press, New York
    • Ashton A. C., de Paiva A., Poulain B., Taue L., and Dolly J. O. (1993) Factors underlying the characteristic inhibition of the neuronal release of transmitters by tetanus and various botulinum toxins, in Botulinum, Tetanus Neurotoxins: Neurotransmission and Biomedical Aspects (DasGupta B. R., ed), pp. 191-213. Plenum Press, New York.
    • (1993) Botulinum, Tetanus Neurotoxins: Neurotransmission and Biomedical Aspects , pp. 191-213
    • Ashton, A.C.1    De Paiva, A.2    Poulain, B.3    Taue, L.4    Dolly, J.O.5
  • 6
    • 0027311070 scopus 로고
    • + and glutamate activates different neurotransmitter release mechanisms in GABAergic neurons: Vesicular versus non-vesicular release of GABA
    • + and glutamate activates different neurotransmitter release mechanisms in GABAergic neurons: vesicular versus non-vesicular release of GABA. Neuroscience 54, 1019-1034.
    • (1993) Neuroscience , vol.54 , pp. 1019-1034
    • Belhage, B.1    Hansen, G.H.2    Schousboe, A.3
  • 7
    • 0026528613 scopus 로고
    • Interaction of free and synaptic vesicle-bound synapsin I with F-actin
    • Benfenati F., Valtorta F., Chieregatti E., and Greengard P. (1992) Interaction of free and synaptic vesicle-bound synapsin I with F-actin. Neuron 8, 377-386.
    • (1992) Neuron , vol.8 , pp. 377-386
    • Benfenati, F.1    Valtorta, F.2    Chieregatti, E.3    Greengard, P.4
  • 9
    • 0028175219 scopus 로고
    • Okadaic acid disrupts clusters of synaptic vesicles in frog motor nerve terminals
    • Betz W. J. and Henkel A. W. (1994) Okadaic acid disrupts clusters of synaptic vesicles in frog motor nerve terminals. J. Cell Biol. 124, 843-854.
    • (1994) J. Cell Biol. , vol.124 , pp. 843-854
    • Betz, W.J.1    Henkel, A.W.2
  • 10
    • 0021046016 scopus 로고
    • Taxol stabilizes synaptosomal microtubules without inhibiting acetylcholine release
    • Burgoyne R. D. and Cumming R. (1983) Taxol stabilizes synaptosomal microtubules without inhibiting acetylcholine release. Brain Res. 280, 190-193.
    • (1983) Brain Res. , vol.280 , pp. 190-193
    • Burgoyne, R.D.1    Cumming, R.2
  • 11
    • 0021185585 scopus 로고
    • Activation of calmodulin by various metal cations as a function of ionic radius
    • Chao S.-H., Suzuki Y., Zysk J. R., and Cheung W. Y. (1984) Activation of calmodulin by various metal cations as a function of ionic radius. Mol. Pharmacol. 26, 75-82.
    • (1984) Mol. Pharmacol. , vol.26 , pp. 75-82
    • Chao, S.-H.1    Suzuki, Y.2    Zysk, J.R.3    Cheung, W.Y.4
  • 14
    • 0026655015 scopus 로고
    • Tetanus toxin potently stimulates tissue transglutaminase - A possible mechanism of neurotoxicity
    • Facchiano F. and Luini A. (1992) Tetanus toxin potently stimulates tissue transglutaminase - a possible mechanism of neurotoxicity. J. Biol. Chem. 267, 13267-13271.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13267-13271
    • Facchiano, F.1    Luini, A.2
  • 15
    • 0027480066 scopus 로고
    • Covalent modification of synapsin I by a tetanus toxin-activated transglutaminase
    • Facchiano F., Benfenati F., Valtorta F., and Luini A. (1993) Covalent modification of synapsin I by a tetanus toxin-activated transglutaminase. J. Biol. Chem. 268, 4588-4591.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4588-4591
    • Facchiano, F.1    Benfenati, F.2    Valtorta, F.3    Luini, A.4
  • 16
    • 0028558884 scopus 로고
    • Differences in the protease activities of tetanus and botulinum B toxins revealed by cleavage of vesicle-associated-membrane protein and various sized fragments
    • Foran P., Shone C. C., and Dolly J. O. (1994) Differences in the protease activities of tetanus and botulinum B toxins revealed by cleavage of vesicle-associated-membrane protein and various sized fragments. Biochemistry 33, 15365-15374.
    • (1994) Biochemistry , vol.33 , pp. 15365-15374
    • Foran, P.1    Shone, C.C.2    Dolly, J.O.3
  • 17
    • 0024095187 scopus 로고
    • Action of cytochalasins on the organization of actin filaments and microtubules in a neuronal growth cone
    • Forscher P. and Smith S. J. (1988) Action of cytochalasins on the organization of actin filaments and microtubules in a neuronal growth cone. J. Cell Biol. 107, 1505-1516.
    • (1988) J. Cell Biol. , vol.107 , pp. 1505-1516
    • Forscher, P.1    Smith, S.J.2
  • 18
    • 0023180498 scopus 로고
    • Distinct sites of action of clostridial neurotoxins revealed by double-poisoning of mouse motor nerve terminals
    • Gansel M., Penner R., and Dreyer F. (1987) Distinct sites of action of clostridial neurotoxins revealed by double-poisoning of mouse motor nerve terminals. Pflugers Arch. 409, 533-539.
    • (1987) Pflugers Arch. , vol.409 , pp. 533-539
    • Gansel, M.1    Penner, R.2    Dreyer, F.3
  • 19
    • 0028923383 scopus 로고
    • 2+/calmodulin and phosphorylation: Inhibition of actin binding and bundling
    • 2+/calmodulin and phosphorylation: inhibition of actin binding and bundling. Biochemistry 34, 1912-1920.
    • (1995) Biochemistry , vol.34 , pp. 1912-1920
    • Goold, R.1    Chan, K.-M.2    Baines, A.J.3
  • 20
    • 0020084419 scopus 로고
    • Presynaptic microtubules: Organization and assembly/disassembly
    • Gordon-Weeks P. R., Burgoyne R. D., and Gray E. G. (1982) Presynaptic microtubules: organization and assembly/disassembly. Neuroscience 7, 739-749.
    • (1982) Neuroscience , vol.7 , pp. 739-749
    • Gordon-Weeks, P.R.1    Burgoyne, R.D.2    Gray, E.G.3
  • 21
    • 0016783881 scopus 로고
    • Presynaptic microtubules and their association with synaptic vesicles
    • Gray E. G. (1975) Presynaptic microtubules and their association with synaptic vesicles. Proc. R. Soc. Lond. [Biol.] 190, 369-372.
    • (1975) Proc. R. Soc. Lond. [Biol.] , vol.190 , pp. 369-372
    • Gray, E.G.1
  • 22
    • 0027402975 scopus 로고
    • Synaptic vesicle phosphoproteins and regulation of synaptic function
    • Greengard P., Valtorta F., Czernik A. J., and Benfenati F. (1993) Synaptic vesicle phosphoproteins and regulation of synaptic function. Science 259, 780-785.
    • (1993) Science , vol.259 , pp. 780-785
    • Greengard, P.1    Valtorta, F.2    Czernik, A.J.3    Benfenati, F.4
  • 23
    • 0029885396 scopus 로고    scopus 로고
    • Synaptic vesicle movements monitored by fluorescence recovery after photobleaching in nerve terminals stained with FMI-43
    • Henkel A. W., Simpson L. L., Ridge R. M. A. P., and Betz W. J. (1996) Synaptic vesicle movements monitored by fluorescence recovery after photobleaching in nerve terminals stained with FMI-43. J. Neurosci. 16, 3960-3967.
    • (1996) J. Neurosci. , vol.16 , pp. 3960-3967
    • Henkel, A.W.1    Simpson, L.L.2    Ridge, R.M.A.P.3    Betz, W.J.4
  • 24
    • 0002671681 scopus 로고
    • Molecular architecture and dynamics of the neuronal cytoskeleton
    • Burgoyne R. D., eds. Wiley-Liss, New York
    • Hirokawa N. (1991) Molecular architecture and dynamics of the neuronal cytoskeleton, in The Neuronal Cytoskeleton (Burgoyne R. D., eds), pp. 5-74. Wiley-Liss, New York.
    • (1991) The Neuronal Cytoskeleton , pp. 5-74
    • Hirokawa, N.1
  • 25
    • 0026516994 scopus 로고
    • Mechanism of action of taxol
    • Horwitz S. B. (1992) Mechanism of action of taxol. Trends Pharmacol. Sci. 13, 134-136.
    • (1992) Trends Pharmacol. Sci. , vol.13 , pp. 134-136
    • Horwitz, S.B.1
  • 26
    • 0028541012 scopus 로고
    • 2+-dependent inactivation in a mammalian central neuron involves the cytoskeleton
    • 2+-dependent inactivation in a mammalian central neuron involves the cytoskeleton. Pflugers Arch. 429, 14-21.
    • (1994) Pflugers Arch. , vol.429 , pp. 14-21
    • Johnson, B.D.1    Byerly, L.2
  • 27
    • 0022476828 scopus 로고
    • Synaptosomal bioenergetics. The role of glycolysis, pyruvate oxidation and responses to hypoglycaemia
    • Kauppinen R. A. and Nicholls D. G. (1986) Synaptosomal bioenergetics. The role of glycolysis, pyruvate oxidation and responses to hypoglycaemia. Eur. J. Biochem. 158, 159-165.
    • (1986) Eur. J. Biochem. , vol.158 , pp. 159-165
    • Kauppinen, R.A.1    Nicholls, D.G.2
  • 29
    • 0023375957 scopus 로고
    • Hindered diffusion of inert tracer particles in the cytoplasm of mouse 3T3 cells
    • Luby-Phelps K., Castle P. E., Taylor D. L., and Lanni F. (1987) Hindered diffusion of inert tracer particles in the cytoplasm of mouse 3T3 cells. Proc. Natl. Acad. Sci. USA 84, 4910-4913.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4910-4913
    • Luby-Phelps, K.1    Castle, P.E.2    Taylor, D.L.3    Lanni, F.4
  • 30
    • 0025773634 scopus 로고
    • The biochemistry of the neuron. Neurosecretory habituation to repetitive depolarizations in PC12 cells
    • Martin P. T. and Koshland D. E. Jr. (1991) The biochemistry of the neuron. Neurosecretory habituation to repetitive depolarizations in PC12 cells. J. Biol. Chem. 266, 7388-7392.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7388-7392
    • Martin, P.T.1    Koshland Jr., D.E.2
  • 32
    • 0027298283 scopus 로고
    • Barium-evoked glutamate release from guinea-pig cerebrocortical synaptosomes
    • McMahon H. T. and Nicholls D. G. (1993) Barium-evoked glutamate release from guinea-pig cerebrocortical synaptosomes. J. Neurochem. 61, 110-115.
    • (1993) J. Neurochem. , vol.61 , pp. 110-115
    • McMahon, H.T.1    Nicholls, D.G.2
  • 33
    • 0026795115 scopus 로고
    • Tetanus toxin and botulinum toxins type A and B inhibit glutamate, γ-aminobutyric acid, aspartate, and Met-enkephalin release from synaptosomes. Clues to the locus of action
    • McMahon H. T., Foran P., Dolly J. O., Verhage M., Wiegant V. M., and Nicholls D. G. (1992) Tetanus toxin and botulinum toxins type A and B inhibit glutamate, γ-aminobutyric acid, aspartate, and Met-enkephalin release from synaptosomes. Clues to the locus of action. J. Biol. Chem. 267, 21338-21343.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21338-21343
    • McMahon, H.T.1    Foran, P.2    Dolly, J.O.3    Verhage, M.4    Wiegant, V.M.5    Nicholls, D.G.6
  • 35
    • 0028353472 scopus 로고
    • The exocytotic fusion pore and neurotransmitter release
    • Monck J. R. and Fernandez J. M. (1994) The exocytotic fusion pore and neurotransmitter release. Neuron 12, 707-716.
    • (1994) Neuron , vol.12 , pp. 707-716
    • Monck, J.R.1    Fernandez, J.M.2
  • 36
    • 0028861992 scopus 로고
    • Axonal transport of mitochondria along microtubules and F-actin in living vertebrate neurons
    • Morris R. L. and Hollenbeck P. J. (1995) Axonal transport of mitochondria along microtubules and F-actin in living vertebrate neurons. J. Cell Biol. 131, 1315-1326.
    • (1995) J. Cell Biol. , vol.131 , pp. 1315-1326
    • Morris, R.L.1    Hollenbeck, P.J.2
  • 37
    • 0025189548 scopus 로고
    • 2+/calmodulin-dependent protein kinase II increases glutamate and noradrenaline release from synaptosomes
    • 2+/calmodulin-dependent protein kinase II increases glutamate and noradrenaline release from synaptosomes. Nature 343, 647-651.
    • (1990) Nature , vol.343 , pp. 647-651
    • Nichols, R.A.1    Sihra, T.S.2    Czernik, A.J.3    Nairn, A.C.4    Greengard, P.5
  • 38
    • 0026501150 scopus 로고
    • Synapsin I regulates glutamate release from rat brain synaptosomes
    • Nichols R. A., Chilcote T. J., Czernik A. J., and Greengard P. (1992) Synapsin I regulates glutamate release from rat brain synaptosomes. J. Neurochem. 58, 783-785.
    • (1992) J. Neurochem. , vol.58 , pp. 783-785
    • Nichols, R.A.1    Chilcote, T.J.2    Czernik, A.J.3    Greengard, P.4
  • 39
    • 0026093226 scopus 로고
    • Actin and tubulin binding domains of synapsin Ia and Ib
    • Petrucci T. C. and Morrow J. S. (1991) Actin and tubulin binding domains of synapsin Ia and Ib. Biochemistry 30, 413-422.
    • (1991) Biochemistry , vol.30 , pp. 413-422
    • Petrucci, T.C.1    Morrow, J.S.2
  • 41
    • 0030042104 scopus 로고    scopus 로고
    • Identification and localization of an actin-binding motif that is unique to the epsilon isoform of protein kinase C and participates in the regulation of synaptic function
    • Prekeris R., Mayhew M. W., Cooper J. B., and Terrian D. M. (1996) Identification and localization of an actin-binding motif that is unique to the epsilon isoform of protein kinase C and participates in the regulation of synaptic function. J. Cell Biol. 132, 77-90.
    • (1996) J. Cell Biol. , vol.132 , pp. 77-90
    • Prekeris, R.1    Mayhew, M.W.2    Cooper, J.B.3    Terrian, D.M.4
  • 42
    • 0024314419 scopus 로고
    • Spatial segregation of the regulated and constitutive secretory pathways
    • Rivas R. J. and Moore H.-P. H. (1989) Spatial segregation of the regulated and constitutive secretory pathways. J. Cell Biol. 109, 51-60.
    • (1989) J. Cell Biol. , vol.109 , pp. 51-60
    • Rivas, R.J.1    Moore, H.-P.H.2
  • 44
    • 0026497466 scopus 로고
    • Tetanus and botulinum B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin
    • Schiavo G., Benfenati F., Poulain B., Rosetto O., de Lauretto P. P., DasGupta B. R., and Montecucco C. (1992) Tetanus and botulinum B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin. Nature 359, 832-835.
    • (1992) Nature , vol.359 , pp. 832-835
    • Schiavo, G.1    Benfenati, F.2    Poulain, B.3    Rosetto, O.4    De Lauretto, P.P.5    DasGupta, B.R.6    Montecucco, C.7
  • 45
    • 0017873116 scopus 로고
    • Influences of colchicine, vinblastine and cytochalasin on the release of 5-hydroxytryptamine from rat brain synaptosomes
    • Segawa T., Murakami H., Inouye A., and Tanaka Y. (1978) Influences of colchicine, vinblastine and cytochalasin on the release of 5-hydroxytryptamine from rat brain synaptosomes. J. Neurochem. 30, 175-180.
    • (1978) J. Neurochem. , vol.30 , pp. 175-180
    • Segawa, T.1    Murakami, H.2    Inouye, A.3    Tanaka, Y.4
  • 47
    • 0017904401 scopus 로고
    • On the role of barium in supporting the asynchronous release of acetylcholine quanta by motor nerve impulses
    • Silinsky E. M. (1978) On the role of barium in supporting the asynchronous release of acetylcholine quanta by motor nerve impulses. J. Physiol. (Lond.) 274, 157-171.
    • (1978) J. Physiol. (Lond.) , vol.274 , pp. 157-171
    • Silinsky, E.M.1
  • 48
    • 0029558545 scopus 로고
    • Synapsin I deficiency results in the structural change in the presynaptic terminals in the murine nervous system
    • Takei Y., Harada A., Takeda S., Kobayashi K., Terada S., Noda T., Takahashi T., and Hirokawa N. (1995) Synapsin I deficiency results in the structural change in the presynaptic terminals in the murine nervous system. J. Cell Biol. 131, 1789-1800.
    • (1995) J. Cell Biol. , vol.131 , pp. 1789-1800
    • Takei, Y.1    Harada, A.2    Takeda, S.3    Kobayashi, K.4    Terada, S.5    Noda, T.6    Takahashi, T.7    Hirokawa, N.8
  • 49
    • 0026584220 scopus 로고
    • Barium and calcium stimulate secretion from digitonin-permeabilized bovine adrenal chromaffin cells by similar pathways
    • TerBush D. R. and Holz R. W. (1992) Barium and calcium stimulate secretion from digitonin-permeabilized bovine adrenal chromaffin cells by similar pathways. J. Neurochem. 58, 680-687.
    • (1992) J. Neurochem. , vol.58 , pp. 680-687
    • TerBush, D.R.1    Holz, R.W.2
  • 50
    • 0028888558 scopus 로고
    • Persistent enhancement of sustained calcium-dependent glutamate release by phorbol esters: Role of calmodulin-independent serine/threonine phosphorylation and actin disassembly
    • Terrian D. M. and Ways D. K. (1995) Persistent enhancement of sustained calcium-dependent glutamate release by phorbol esters: role of calmodulin-independent serine/threonine phosphorylation and actin disassembly. J. Neurochem. 64, 181-190.
    • (1995) J. Neurochem. , vol.64 , pp. 181-190
    • Terrian, D.M.1    Ways, D.K.2
  • 51
    • 0027074332 scopus 로고
    • Disorganization of the Golgi complex and the cytoplasmic microtubule system in CHO cells exposed to okadaic acid
    • Thyberg J. and Moskalewski S. (1992) Disorganization of the Golgi complex and the cytoplasmic microtubule system in CHO cells exposed to okadaic acid. J. Cell Sci. 103, 1167-1175.
    • (1992) J. Cell Sci. , vol.103 , pp. 1167-1175
    • Thyberg, J.1    Moskalewski, S.2
  • 52
    • 0027050487 scopus 로고
    • Synapsin I partially dissociates from synaptic vesicles during exocytosis induced by electrical stimulation
    • Tom Tarelli F., Bossi M., Fesce R., Greengard P., and Valtorta F. (1992) Synapsin I partially dissociates from synaptic vesicles during exocytosis induced by electrical stimulation. Neuron 9, 1143-1153.
    • (1992) Neuron , vol.9 , pp. 1143-1153
    • Tom Tarelli, F.1    Bossi, M.2    Fesce, R.3    Greengard, P.4    Valtorta, F.5
  • 53
    • 0027489573 scopus 로고
    • Cytoskeleton dynamics during neurotransmitter release
    • Trifaro J. M. and Vitale M. L. (1993) Cytoskeleton dynamics during neurotransmitter release. Trends Neurosci. 16, 466-472.
    • (1993) Trends Neurosci. , vol.16 , pp. 466-472
    • Trifaro, J.M.1    Vitale, M.L.2
  • 54
    • 0029993183 scopus 로고    scopus 로고
    • Destabilization of plasma membrane structure by prevention of actin polymerization. Microtubule-dependent tubulation of the plasma membrane
    • van Deurs B., von Bülow F., Vilhardt F., Holm P. K., and Sandvig K. (1996) Destabilization of plasma membrane structure by prevention of actin polymerization. Microtubule-dependent tubulation of the plasma membrane. J. Cell Sci. 109, 1655-1665.
    • (1996) J. Cell Sci. , vol.109 , pp. 1655-1665
    • Van Deurs, B.1    Von Bülow, F.2    Vilhardt, F.3    Holm, P.K.4    Sandvig, K.5
  • 55
    • 0026705498 scopus 로고
    • Endogenous noradrenaline and dopamine in nerve terminals of the hippocampus: Differences in levels and release kinetics
    • Verhage M., Ghijsen W. E. J. M., Boomsma F., and Lopes da Silva F. H. (1992) Endogenous noradrenaline and dopamine in nerve terminals of the hippocampus: differences in levels and release kinetics. J. Neurochem. 59, 881-887.
    • (1992) J. Neurochem. , vol.59 , pp. 881-887
    • Verhage, M.1    Ghijsen, W.E.J.M.2    Boomsma, F.3    Lopes Da Silva, F.H.4
  • 56
    • 0030042310 scopus 로고    scopus 로고
    • Effects of cytochalasin treatment on short-term synaptic plasticity at developing neuromuscular junctions in frogs
    • Wang X.-H., Zheng J. Q., and Poo M.-M. (1996) Effects of cytochalasin treatment on short-term synaptic plasticity at developing neuromuscular junctions in frogs. J. Physiol. (Lond.) 491, 187-195.
    • (1996) J. Physiol. (Lond.) , vol.491 , pp. 187-195
    • Wang, X.-H.1    Zheng, J.Q.2    Poo, M.-M.3
  • 57
    • 0024395212 scopus 로고
    • Chains and fragments of tetanus toxin: Separation, reassociation and pharmacological properties
    • Weller U., Dauzenroth M. E., Meyer Zu Heringdorf D., and Habermann E. (1989) Chains and fragments of tetanus toxin: separation, reassociation and pharmacological properties. Eur. J. Biochem. 182, 649-656.
    • (1989) Eur. J. Biochem. , vol.182 , pp. 649-656
    • Weller, U.1    Dauzenroth, M.E.2    Meyer Zu Heringdorf, D.3    Habermann, E.4
  • 58
    • 0029891288 scopus 로고    scopus 로고
    • Substrate residues N-terminal to the cleavage site of botulinum type B neurotoxin play a role in determining the specificity of its endoprotease activity
    • Wictome M., Rossetto O., Montecucco C., and Shone C. C. (1996) Substrate residues N-terminal to the cleavage site of botulinum type B neurotoxin play a role in determining the specificity of its endoprotease activity. FEBS Lett. 386, 133-136.
    • (1996) FEBS Lett. , vol.386 , pp. 133-136
    • Wictome, M.1    Rossetto, O.2    Montecucco, C.3    Shone, C.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.