메뉴 건너뛰기




Volumn 67, Issue , 2013, Pages 31-36

Botulinum neurotoxins

Author keywords

Botulinum neurotoxins; Botulism; Neuromuscular junction; SNARE proteins

Indexed keywords

BOTULINUM TOXIN; BOTULINUM TOXIN A; BOTULINUM TOXIN B; BOTULINUM TOXIN C; BOTULINUM TOXIN D; BOTULINUM TOXIN E; SNARE PROTEIN; SYNAPTOBREVIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNTAXIN; TETANUS TOXIN; UNCLASSIFIED DRUG;

EID: 84875262150     PISSN: 00410101     EISSN: 18793150     Source Type: Journal    
DOI: 10.1016/j.toxicon.2013.01.017     Document Type: Review
Times cited : (42)

References (93)
  • 2
    • 42149103800 scopus 로고    scopus 로고
    • Future aspects of botulinum neurotoxins
    • Aoki K.R. Future aspects of botulinum neurotoxins. J. Neural Transm. 2008, 115:567-573.
    • (2008) J. Neural Transm. , vol.115 , pp. 567-573
    • Aoki, K.R.1
  • 4
    • 0019731010 scopus 로고
    • Infant botulism: epidemiology and relation to sudden infant death syndrome
    • Arnon S.S., Damus K., Chin J. Infant botulism: epidemiology and relation to sudden infant death syndrome. Epidemiol. Rev. 1981, 3:45-66.
    • (1981) Epidemiol. Rev. , vol.3 , pp. 45-66
    • Arnon, S.S.1    Damus, K.2    Chin, J.3
  • 6
    • 65949090949 scopus 로고    scopus 로고
    • Cell entry strategy of clostridial neurotoxins
    • Binz T., Rummel A. Cell entry strategy of clostridial neurotoxins. J. Neurochem. 2009, 109:1584-1595.
    • (2009) J. Neurochem. , vol.109 , pp. 1584-1595
    • Binz, T.1    Rummel, A.2
  • 7
    • 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. 1990, 265:9153-9158.
    • (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
  • 9
    • 0037065664 scopus 로고    scopus 로고
    • Arg(362) and Tyr(365) of the botulinum neurotoxin type a light chain are involved in transition state stabilization
    • Binz T., Bade S., Rummel A., Kollewe A., Alves J. Arg(362) and Tyr(365) of the botulinum neurotoxin type a light chain are involved in transition state stabilization. Biochemistry 2002, 41:1717-1723.
    • (2002) Biochemistry , vol.41 , pp. 1717-1723
    • Binz, T.1    Bade, S.2    Rummel, A.3    Kollewe, A.4    Alves, J.5
  • 11
    • 0027432376 scopus 로고
    • Botulinum neurotoxin C blocks neurotransmitter release by means of cleaving HPC-I/syntaxin
    • Blasi J., Chapman E.R., Yamasaki S., Binz T., Nieman H., Jahn R. Botulinum neurotoxin C blocks neurotransmitter release by means of cleaving HPC-I/syntaxin. EMBO J. 1993, 12:4821-4828.
    • (1993) EMBO J. , vol.12 , pp. 4821-4828
    • Blasi, J.1    Chapman, E.R.2    Yamasaki, S.3    Binz, T.4    Nieman, H.5    Jahn, R.6
  • 12
    • 11144341950 scopus 로고    scopus 로고
    • Substrate recognition strategy for botulinum neurotoxin serotype A
    • Breidenbach M.A., Brunger A.T. Substrate recognition strategy for botulinum neurotoxin serotype A. Nature 2004, 432:925-929.
    • (2004) Nature , vol.432 , pp. 925-929
    • Breidenbach, M.A.1    Brunger, A.T.2
  • 13
    • 68949179783 scopus 로고    scopus 로고
    • Receptor and substrate interactions of clostridial neurotoxins
    • Brunger A.T., Rummel A. Receptor and substrate interactions of clostridial neurotoxins. Toxicon 2009, 54:550-560.
    • (2009) Toxicon , vol.54 , pp. 550-560
    • Brunger, A.T.1    Rummel, A.2
  • 14
    • 0002301979 scopus 로고
    • The action of botulinum toxin at the neuro-muscular junction
    • Burgen A.S.V., Dickens F., Zatman L.J. The action of botulinum toxin at the neuro-muscular junction. J. Physiol. (London) 1949, 109:10-24.
    • (1949) J. Physiol. (London) , vol.109 , pp. 10-24
    • Burgen, A.S.V.1    Dickens, F.2    Zatman, L.J.3
  • 15
    • 68849129297 scopus 로고    scopus 로고
    • Central effects of tetanus and botulinum neurotoxins
    • Caleo M., Schiavo G. Central effects of tetanus and botulinum neurotoxins. Toxicon 2009, 54:593-599.
    • (2009) Toxicon , vol.54 , pp. 593-599
    • Caleo, M.1    Schiavo, G.2
  • 16
    • 69749107105 scopus 로고    scopus 로고
    • Assay of diffusion of different botulinum neurotoxin type a formulations injected in the mouse leg
    • Carli L., Montecucco C., Rossetto O. Assay of diffusion of different botulinum neurotoxin type a formulations injected in the mouse leg. Muscle Nerve 2009, 40:374-380.
    • (2009) Muscle Nerve , vol.40 , pp. 374-380
    • Carli, L.1    Montecucco, C.2    Rossetto, O.3
  • 19
    • 0026710446 scopus 로고
    • Serum IgG antibody to ganglioside GQ1b is a possible marker of Miller Fisher syndrome
    • Chiba A., Kusunoki S., Shimizu T., Kanazawa I. Serum IgG antibody to ganglioside GQ1b is a possible marker of Miller Fisher syndrome. Ann. Neurol. 1992, 31:677-679.
    • (1992) Ann. Neurol. , vol.31 , pp. 677-679
    • Chiba, A.1    Kusunoki, S.2    Shimizu, T.3    Kanazawa, I.4
  • 20
    • 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. 1997, 280:1489-1498.
    • (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
  • 23
    • 58549094719 scopus 로고    scopus 로고
    • Glycosylated SV2A and SV2B mediate the entry of botulinum neurotoxin E into neurons
    • Dong M., Liu H., Tepp W.H., Johnson E.A., Janz R., Chapman E.R. Glycosylated SV2A and SV2B mediate the entry of botulinum neurotoxin E into neurons. Mol. Biol. Cell. 2008, 19:5226-5237.
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 5226-5237
    • Dong, M.1    Liu, H.2    Tepp, W.H.3    Johnson, E.A.4    Janz, R.5    Chapman, E.R.6
  • 24
    • 3242755055 scopus 로고    scopus 로고
    • Historical notes on botulism, Clostridium botulinum, botulinum toxin, and the idea of the therapeutic use of the toxin
    • Erbguth F.J. Historical notes on botulism, Clostridium botulinum, botulinum toxin, and the idea of the therapeutic use of the toxin. Mov. Disord. 2004, 19(Suppl. 8):S2-S6.
    • (2004) Mov. Disord. , vol.19 , Issue.SUPPL. 8
    • Erbguth, F.J.1
  • 25
    • 34547509346 scopus 로고    scopus 로고
    • Single molecule detection of intermediates during botulinum neurotoxin translocation across membranes
    • Fischer A., Montal M. Single molecule detection of intermediates during botulinum neurotoxin translocation across membranes. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:10447-10452.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 10447-10452
    • Fischer, A.1    Montal, M.2
  • 27
    • 77950858619 scopus 로고    scopus 로고
    • Gaining ground: assays for therapeutics against botulinum neurotoxin
    • Hakami R.M., Ruthel G., Stahl A.M., Bavari S. Gaining ground: assays for therapeutics against botulinum neurotoxin. Trends Microbiol. 2010, 18:164-172.
    • (2010) Trends Microbiol. , vol.18 , pp. 164-172
    • Hakami, R.M.1    Ruthel, G.2    Stahl, A.M.3    Bavari, S.4
  • 29
    • 0034121745 scopus 로고    scopus 로고
    • How botulinum and tetanus neurotoxins block neurotransmitter release
    • Humeau Y., Doussau F., Grant N.J., Poulain B. How botulinum and tetanus neurotoxins block neurotransmitter release. Biochimie 2000, 82:427-446.
    • (2000) Biochimie , vol.82 , pp. 427-446
    • Humeau, Y.1    Doussau, F.2    Grant, N.J.3    Poulain, B.4
  • 31
  • 32
    • 33845871995 scopus 로고    scopus 로고
    • Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity
    • Jin R., Rummel A., Binz T., Brunger A.T. Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity. Nature 2006, 444:1092-1095.
    • (2006) Nature , vol.444 , pp. 1092-1095
    • Jin, R.1    Rummel, A.2    Binz, T.3    Brunger, A.T.4
  • 33
    • 34548688418 scopus 로고    scopus 로고
    • Structural and biochemical studies of botulinum neurotoxin serotype C1 light chain protease: implications for dual substrate specificity
    • Jin R., Sikorra S., Stegmann C.M., Pich A., Binz T., Brunger A.T. Structural and biochemical studies of botulinum neurotoxin serotype C1 light chain protease: implications for dual substrate specificity. Biochemistry 2007, 46:10685-10693.
    • (2007) Biochemistry , vol.46 , pp. 10685-10693
    • Jin, R.1    Sikorra, S.2    Stegmann, C.M.3    Pich, A.4    Binz, T.5    Brunger, A.T.6
  • 34
    • 59649122964 scopus 로고    scopus 로고
    • Botulism
    • Elsevier B.V. A.G. Engel (Ed.) Neuromuscular Junction Disorders (3rd series)
    • Johnson E.A., Montecucco C. Botulism. Handbook of Clinical Neurology 2008, vol. 91 (3rd series):333-368. Elsevier B.V. A.G. Engel (Ed.).
    • (2008) Handbook of Clinical Neurology , vol.91 , pp. 333-368
    • Johnson, E.A.1    Montecucco, C.2
  • 37
    • 77956591091 scopus 로고    scopus 로고
    • Identification of a unique ganglioside binding loop within botulinum neurotoxins C and D-SA
    • Karalewitz A.P., Kroken A.R., Fu Z., Baldwin M.R., Kim J.J., Barbieri J.T. Identification of a unique ganglioside binding loop within botulinum neurotoxins C and D-SA. Biochemistry 2010, 49:8117-8126.
    • (2010) Biochemistry , vol.49 , pp. 8117-8126
    • Karalewitz, A.P.1    Kroken, A.R.2    Fu, Z.3    Baldwin, M.R.4    Kim, J.J.5    Barbieri, J.T.6
  • 38
    • 79960680902 scopus 로고    scopus 로고
    • Novel ganglioside-mediated entry of botulinum neurotoxin serotype D into neurons
    • Kroken A.R., Karalewitz A.P., Fu Z., Kim J.J., Barbieri J.T. Novel ganglioside-mediated entry of botulinum neurotoxin serotype D into neurons. J. Biol. Chem. 2011, 286:26828-26837.
    • (2011) J. Biol. Chem. , vol.286 , pp. 26828-26837
    • Kroken, A.R.1    Karalewitz, A.P.2    Fu, Z.3    Kim, J.J.4    Barbieri, J.T.5
  • 39
    • 58549116147 scopus 로고    scopus 로고
    • Domain organization in Clostridium botulinum neurotoxin type E is unique: its implication in faster translocation
    • Kumaran D., Eswaramoorthy S., Furey W., Navaza J., Sax M., Swaminathan S. Domain organization in Clostridium botulinum neurotoxin type E is unique: its implication in faster translocation. J. Mol. Biol. 2009, 386:233-245.
    • (2009) J. Mol. Biol. , vol.386 , pp. 233-245
    • Kumaran, D.1    Eswaramoorthy, S.2    Furey, W.3    Navaza, J.4    Sax, M.5    Swaminathan, S.6
  • 40
    • 0033520494 scopus 로고    scopus 로고
    • Sequence homology and structural analysis of the clostridial neurotoxins
    • Lacy D.B., Stevens R.C. Sequence homology and structural analysis of the clostridial neurotoxins. J. Mol. Biol. 1999, 291:1091-1104.
    • (1999) J. Mol. Biol. , vol.291 , pp. 1091-1104
    • Lacy, D.B.1    Stevens, R.C.2
  • 41
    • 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. 1998, 5:898-902.
    • (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
  • 42
    • 0037376585 scopus 로고    scopus 로고
    • Toxicity of botulinum neurotoxins in central nervous system of mice
    • Luvisetto S., Rossetto O., Montecucco C., Pavone F. Toxicity of botulinum neurotoxins in central nervous system of mice. Toxicon 2003, 41:475-481.
    • (2003) Toxicon , vol.41 , pp. 475-481
    • Luvisetto, S.1    Rossetto, O.2    Montecucco, C.3    Pavone, F.4
  • 44
    • 33645212684 scopus 로고    scopus 로고
    • The synaptic vesicle protein 2C mediates the uptake of botulinum neurotoxin A into phrenic nerves
    • Mahrhold S., Rummel A., Bigalke H., Davletov B., Binz T. The synaptic vesicle protein 2C mediates the uptake of botulinum neurotoxin A into phrenic nerves. FEBS Lett. 2006, 580:2011-2014.
    • (2006) FEBS Lett. , vol.580 , pp. 2011-2014
    • Mahrhold, S.1    Rummel, A.2    Bigalke, H.3    Davletov, B.4    Binz, T.5
  • 45
    • 77953642001 scopus 로고    scopus 로고
    • Botulinum neurotoxin: a marvel of protein design
    • Montal M. Botulinum neurotoxin: a marvel of protein design. Annu. Rev. Biochem. 2010, 79:591-617.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 591-617
    • Montal, M.1
  • 46
    • 46149134882 scopus 로고
    • How do tetanus and botulinum toxins bind to neuronal membranes?
    • Montecucco C. How do tetanus and botulinum toxins bind to neuronal membranes?. Trends Biochem. Sci. 1986, 11:314-317.
    • (1986) Trends Biochem. Sci. , vol.11 , pp. 314-317
    • Montecucco, C.1
  • 47
    • 18744410709 scopus 로고    scopus 로고
    • Botulinal neurotoxins: revival of an old killer
    • Montecucco C., Molgó J. Botulinal neurotoxins: revival of an old killer. Curr. Opin. Pharmacol. 2005, 5:274-279.
    • (2005) Curr. Opin. Pharmacol. , vol.5 , pp. 274-279
    • Montecucco, C.1    Molgó, J.2
  • 48
    • 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. 1995, 28:423-472.
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 423-472
    • Montecucco, C.1    Schiavo, G.2
  • 49
    • 0028236333 scopus 로고
    • Bacterial protein toxins penetrate cells via a four-step mechanism
    • Montecucco C., Schiavo G., Papini E. Bacterial protein toxins penetrate cells via a four-step mechanism. FEBS Lett. 1994, 346:92-98.
    • (1994) FEBS Lett. , vol.346 , pp. 92-98
    • Montecucco, C.1    Schiavo, G.2    Papini, E.3
  • 50
    • 4644364793 scopus 로고    scopus 로고
    • Presynaptic receptor arrays for clostridial neurotoxins
    • Montecucco C., Rossetto O., Schiavo G. Presynaptic receptor arrays for clostridial neurotoxins. Trends Microbiol. 2004, 12:442-446.
    • (2004) Trends Microbiol. , vol.12 , pp. 442-446
    • Montecucco, C.1    Rossetto, O.2    Schiavo, G.3
  • 51
    • 21744457054 scopus 로고    scopus 로고
    • SNARE complexes and neuroexocytosis: how many, how close?
    • Montecucco C., Schiavo G., Pantano S. SNARE complexes and neuroexocytosis: how many, how close?. Trends Biochem. Sci. 2005, 30:367-372.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 367-372
    • Montecucco, C.1    Schiavo, G.2    Pantano, S.3
  • 52
    • 59649101806 scopus 로고    scopus 로고
    • The N-terminal half of the receptor domain of botulinum neurotoxin A binds to microdomains of the plasma membrane
    • Muraro L., Tosatto S., Motterlini L., Rossetto O., Montecucco C. The N-terminal half of the receptor domain of botulinum neurotoxin A binds to microdomains of the plasma membrane. Biochem. Biophys. Res. Commun. 2009, 380:76-80.
    • (2009) Biochem. Biophys. Res. Commun. , vol.380 , pp. 76-80
    • Muraro, L.1    Tosatto, S.2    Motterlini, L.3    Rossetto, O.4    Montecucco, C.5
  • 53
    • 43149084857 scopus 로고    scopus 로고
    • Assessment: botulinum neurotoxin in the treatment of autonomic disorders and pain (an evidence-based review): report of the Therapeutics and Technology Assessment Subcommittee of the American Academy of Neurology
    • Naumann M., So Y., Argoff C.E., Childers M.K., Dykstra D.D., Gronseth G.S., Jabbari B., Kaufmann H.C., Schurch B., Silberstein S.D., Simpson D.M. Assessment: botulinum neurotoxin in the treatment of autonomic disorders and pain (an evidence-based review): report of the Therapeutics and Technology Assessment Subcommittee of the American Academy of Neurology. Neurology 2008, 70:1707-1714.
    • (2008) Neurology , vol.70 , pp. 1707-1714
    • Naumann, M.1    So, Y.2    Argoff, C.E.3    Childers, M.K.4    Dykstra, D.D.5    Gronseth, G.S.6    Jabbari, B.7    Kaufmann, H.C.8    Schurch, B.9    Silberstein, S.D.10    Simpson, D.M.11
  • 54
    • 0026572840 scopus 로고
    • Clostridial neurotoxins - proposal of a common nomenclature
    • Niemann H. Clostridial neurotoxins - proposal of a common nomenclature. Toxicon 1992, 30:223-225.
    • (1992) Toxicon , vol.30 , pp. 223-225
    • Niemann, H.1
  • 55
    • 0028341442 scopus 로고
    • Identification of protein receptor for Clostridium botulinum type B neurotoxin in rat brain synaptosomes
    • Nishiki T., Kamata Y., Nemoto Y., Omori A., Ito T., Takahashi M., Kozaki S. Identification of protein receptor for Clostridium botulinum type B neurotoxin in rat brain synaptosomes. J. Biol. Chem. 1994, 269:10498-10503.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10498-10503
    • Nishiki, T.1    Kamata, Y.2    Nemoto, Y.3    Omori, A.4    Ito, T.5    Takahashi, M.6    Kozaki, S.7
  • 56
    • 79651469055 scopus 로고    scopus 로고
    • Clostridium botulinum in the post-genomic era
    • Peck M.W., Stringer S.C., Carter A.T. Clostridium botulinum in the post-genomic era. Food Microbiol. 2011, 28:183-191.
    • (2011) Food Microbiol. , vol.28 , pp. 183-191
    • Peck, M.W.1    Stringer, S.C.2    Carter, A.T.3
  • 57
    • 0029811998 scopus 로고    scopus 로고
    • Structural determinants of the specificity for VAMP/synaptobrevin of tetanus and botulinum B and G neurotoxins
    • Pellizzari R., Rossetto O., Lozzi L., Giovedì S., Johonson E., Shone C.C., Montecucco C. Structural determinants of the specificity for VAMP/synaptobrevin of tetanus and botulinum B and G neurotoxins. J. Biol. Chem. 1996, 271:20353-20358.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20353-20358
    • Pellizzari, R.1    Rossetto, O.2    Lozzi, L.3    Giovedì, S.4    Johonson, E.5    Shone, C.C.6    Montecucco, C.7
  • 58
    • 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. 1997, 409:339-342.
    • (1997) FEBS Lett. , vol.409 , pp. 339-342
    • Pellizzari, R.1    Mason, S.2    Shone, C.C.3    Montecucco, C.4
  • 59
    • 79953289881 scopus 로고    scopus 로고
    • Botulinum neurotoxin D uses synaptic vesicle protein SV2 and gangliosides as receptors
    • Peng L., Tepp W.H., Johnson E.A., Dong M. Botulinum neurotoxin D uses synaptic vesicle protein SV2 and gangliosides as receptors. PLoS Pathog. 2011, 7:e1002008.
    • (2011) PLoS Pathog. , vol.7
    • Peng, L.1    Tepp, W.H.2    Johnson, E.A.3    Dong, M.4
  • 60
    • 80054105849 scopus 로고    scopus 로고
    • Double anchorage to the membrane and intact inter-chain disulfide bond are required for the low pH induced entry of tetanus and botulinum neurotoxins into neurons
    • Pirazzini M., Rossetto O., Bolognese P., Shone C.C., Montecucco C. Double anchorage to the membrane and intact inter-chain disulfide bond are required for the low pH induced entry of tetanus and botulinum neurotoxins into neurons. Cell. Microbiol. 2011, 13:1731-1743.
    • (2011) Cell. Microbiol. , vol.13 , pp. 1731-1743
    • Pirazzini, M.1    Rossetto, O.2    Bolognese, P.3    Shone, C.C.4    Montecucco, C.5
  • 61
    • 84875242690 scopus 로고    scopus 로고
    • Biological warfare agents
    • Birkháuser Verlag, Switzerland, A. Luch (Ed.) Molecular, Clinical and Environmental Toxicology
    • Pohanka M., Kuca K. Biological warfare agents. Clinical Toxicology 2010, vol. 2:559-578. Birkháuser Verlag, Switzerland. A. Luch (Ed.).
    • (2010) Clinical Toxicology , vol.2 , pp. 559-578
    • Pohanka, M.1    Kuca, K.2
  • 62
    • 19344372277 scopus 로고    scopus 로고
    • Structural analysis of the catalytic domain of tetanus neurotoxin
    • Rao K.N., Kumaran D., Binz T., Swaminathan S. Structural analysis of the catalytic domain of tetanus neurotoxin. Toxicon 2005, 45:929-939.
    • (2005) Toxicon , vol.45 , pp. 929-939
    • Rao, K.N.1    Kumaran, D.2    Binz, T.3    Swaminathan, S.4
  • 63
    • 0035900618 scopus 로고    scopus 로고
    • Site-directed mutagenesis identifies active site residues of the light chain of botulinum neurotoxin type A
    • Rigoni M., Caccin P., Johnson E.A., Montecucco C., Rossetto O. Site-directed mutagenesis identifies active site residues of the light chain of botulinum neurotoxin type A. Biochem. Biophys. Res. Commun. 2001, 288:1231-1237.
    • (2001) Biochem. Biophys. Res. Commun. , vol.288 , pp. 1231-1237
    • Rigoni, M.1    Caccin, P.2    Johnson, E.A.3    Montecucco, C.4    Rossetto, O.5
  • 66
    • 69949182315 scopus 로고    scopus 로고
    • Botulinum neurotoxins C, E and F bind gangliosides via a conserved binding site prior to stimulation-dependent uptake with botulinum neurotoxin F utilising the three isoforms of SV2 as second receptor
    • Rummel A., Hafner K., Mahrhold S., Darashchonak N., Holt M., Jahn R., Beermann S., Karnath T., Bigalke H., Binz T. Botulinum neurotoxins C, E and F bind gangliosides via a conserved binding site prior to stimulation-dependent uptake with botulinum neurotoxin F utilising the three isoforms of SV2 as second receptor. J. Neurochem. 2009, 110:1942-1954.
    • (2009) J. Neurochem. , vol.110 , pp. 1942-1954
    • Rummel, A.1    Hafner, K.2    Mahrhold, S.3    Darashchonak, N.4    Holt, M.5    Jahn, R.6    Beermann, S.7    Karnath, T.8    Bigalke, H.9    Binz, T.10
  • 67
    • 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. 1992, 11:3577-3583.
    • (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
  • 71
    • 0027241009 scopus 로고
    • Botulinum neurotoxin serotype F is a zinc endopeptidase specific for VAMP/synaptobrevin
    • Schiavo G., Shone C.C., Rossetto O., Alexandre F.C.G., Montecucco C. Botulinum neurotoxin serotype F is a zinc endopeptidase specific for VAMP/synaptobrevin. J. Biol. Chem. 1993, 268:11516-11519.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11516-11519
    • Schiavo, G.1    Shone, C.C.2    Rossetto, O.3    Alexandre, F.C.G.4    Montecucco, C.5
  • 74
    • 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. 1995, 270:10566-10570.
    • (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
  • 76
    • 0001339033 scopus 로고
    • Clostridial toxin as therapeutic agents
    • Academic Press, New York, L.L. Simpson (Ed.)
    • Scott A.B. Clostridial toxin as therapeutic agents. Botulinum Neurotoxin and Tetanus Toxin 1989, 399-412. Academic Press, New York. L.L. Simpson (Ed.).
    • (1989) Botulinum Neurotoxin and Tetanus Toxin , pp. 399-412
    • Scott, A.B.1
  • 77
    • 0000517790 scopus 로고
    • Botulinum toxin and the blockade of transmitter release
    • Sellin L.C. Botulinum toxin and the blockade of transmitter release. Asia Pac. J. Pharmacol. 1987, 2:203-222.
    • (1987) Asia Pac. J. Pharmacol. , vol.2 , pp. 203-222
    • Sellin, L.C.1
  • 78
    • 0029161741 scopus 로고
    • Growth of clostridia and preparation of their Neurotoxins
    • Shone C.C., Tranter H.S. Growth of clostridia and preparation of their Neurotoxins. Curr. Top. Microbiol. Immunol. 1995, 195:143-160.
    • (1995) Curr. Top. Microbiol. Immunol. , vol.195 , pp. 143-160
    • Shone, C.C.1    Tranter, H.S.2
  • 79
    • 0028293577 scopus 로고
    • Inhibition of vacuolar adenosine triphosphatase antagonizes the effects of clostridial neurotoxins but not phospholipase A2 neurotoxins
    • Simpson L.L., Coffield J.A., Bakry N. Inhibition of vacuolar adenosine triphosphatase antagonizes the effects of clostridial neurotoxins but not phospholipase A2 neurotoxins. J. Pharmacol. Exp. Ther. 1994, 269:256-262.
    • (1994) J. Pharmacol. Exp. Ther. , vol.269 , pp. 256-262
    • Simpson, L.L.1    Coffield, J.A.2    Bakry, N.3
  • 80
    • 77950859996 scopus 로고    scopus 로고
    • Botulism and vaccines for its prevention
    • Smith L.A. Botulism and vaccines for its prevention. Vaccine 2009, 27(Suppl. 4):D33-D39.
    • (2009) Vaccine , vol.27 , Issue.SUPPL. 4
    • Smith, L.A.1
  • 82
    • 81555214403 scopus 로고    scopus 로고
    • Molecular structures and functional relationships in clostridial neurotoxins
    • Swaminathan S. Molecular structures and functional relationships in clostridial neurotoxins. FEBS J. 2011, 278:4467-4485.
    • (2011) FEBS J. , vol.278 , pp. 4467-4485
    • Swaminathan, S.1
  • 83
    • 0033884053 scopus 로고    scopus 로고
    • Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B
    • Swaminathan S., Eswaramoorthy S. Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B. Nat. Struct. Biol. 2000, 7:693-699.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 693-699
    • Swaminathan, S.1    Eswaramoorthy, S.2
  • 84
    • 70350733498 scopus 로고    scopus 로고
    • The anthrax lethal factor and its MAPK kinase-specific metalloprotease activity
    • Tonello F., Montecucco C. The anthrax lethal factor and its MAPK kinase-specific metalloprotease activity. Mol. Aspects Med. 2009, 30:431-438.
    • (2009) Mol. Aspects Med. , vol.30 , pp. 431-438
    • Tonello, F.1    Montecucco, C.2
  • 86
    • 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., Dörries 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. 1999, 72:327-337.
    • (1999) J. Neurochem. , vol.72 , pp. 327-337
    • Vaidyanathan, V.V.1    Yoshino, K.2    Jahnz, M.3    Dörries, C.4    Bade, S.5    Nauenburg, S.6    Niemann, H.7    Binz, T.8
  • 87
    • 0002837246 scopus 로고
    • über ein neuen anaeroben Bacillus und seine Beziehungen zum Botulismus
    • van Ermengen E. über ein neuen anaeroben Bacillus und seine Beziehungen zum Botulismus. Z. Hyg. Infektkr. 1897, 26:1-56.
    • (1897) Z. Hyg. Infektkr. , vol.26 , pp. 1-56
    • van Ermengen, E.1
  • 89
    • 0028131847 scopus 로고
    • Acute ataxic neuropathy with cross-reactive antibodies to GD1b and GD3 gangliosides
    • Willison H.J., Almemar A., Veitch J., Thrush D. Acute ataxic neuropathy with cross-reactive antibodies to GD1b and GD3 gangliosides. Neurology 1994, 44:2395-2397.
    • (1994) Neurology , vol.44 , pp. 2395-2397
    • Willison, H.J.1    Almemar, A.2    Veitch, J.3    Thrush, D.4
  • 90
    • 0029891288 scopus 로고    scopus 로고
    • Substrate residues N-terminal to the cleavage site of botulinum type B neurotoxin play a role in determining the specificity of its endopeptidase activity
    • Witcome M., Rossetto O., Montecucco C., Shone C.C. Substrate residues N-terminal to the cleavage site of botulinum type B neurotoxin play a role in determining the specificity of its endopeptidase activity. FEBS Lett. 1996, 386:133-136.
    • (1996) FEBS Lett. , vol.386 , pp. 133-136
    • Witcome, M.1    Rossetto, O.2    Montecucco, C.3    Shone, C.C.4
  • 91
    • 0031111301 scopus 로고    scopus 로고
    • Avian botulism - another perspective
    • Wobeser G. Avian botulism - another perspective. J. Wildl. Dis. 1997, 33:181-186.
    • (1997) J. Wildl. Dis. , vol.33 , pp. 181-186
    • Wobeser, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.