메뉴 건너뛰기




Volumn 18, Issue 1, 1999, Pages 95-112

Structure-function relationship of clostridial neurotoxins

Author keywords

[No Author keywords available]

Indexed keywords

BOTULINUM TOXIN; CARRIER PROTEIN; CLOSTRIDIUM TOXIN; METALLOPROTEINASE; NEUROTOXIN; PROTEINASE;

EID: 0033065263     PISSN: 07313837     EISSN: None     Source Type: Journal    
DOI: 10.3109/15569549909036019     Document Type: Review
Times cited : (50)

References (83)
  • 1
    • 0024338084 scopus 로고
    • Nicking of single chain Clostridium botulinum type A neurotoxin by an endogenous protease
    • Dekleva, M. L. and DasGupta, B. R. (1989) Nicking of single chain Clostridium botulinum type A neurotoxin by an endogenous protease. Biochem Biophys. Res. Commun. 162, 767-772.
    • (1989) Biochem Biophys. Res. Commun. , vol.162 , pp. 767-772
    • Dekleva, M.L.1    DasGupta, B.R.2
  • 2
    • 0025992494 scopus 로고
    • Limited proteolysis of tetanus toxin. Relation to activity and identification of cleavage sites
    • Krieglstein, K. G., Henschen, A. H., Weller, U. and Habermann, E. (1991) Limited proteolysis of tetanus toxin. Relation to activity and identification of cleavage sites. Eur. J. Biochem. 202, 41-51.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 41-51
    • Krieglstein, K.G.1    Henschen, A.H.2    Weller, U.3    Habermann, E.4
  • 3
    • 0030461941 scopus 로고
    • Bacterial protein toxins and cell vesicle trafficking
    • Montecucco, C., Papini, E. and Schiavo, G. (1994) Bacterial protein toxins and cell vesicle trafficking. Experientia. 15, 1026-1032.
    • (1994) Experientia , vol.15 , pp. 1026-1032
    • Montecucco, C.1    Papini, E.2    Schiavo, G.3
  • 4
    • 0028491306 scopus 로고
    • Clostridial neurotoxins as tools to investigate the molecular events of neurotransmitter release
    • Schiavo, G., Rossetto, O. and Montecucco, C. (1994) Clostridial neurotoxins as tools to investigate the molecular events of neurotransmitter release. Semin. Cell Biol. 5, 221-229.
    • (1994) Semin. Cell Biol. , vol.5 , pp. 221-229
    • Schiavo, G.1    Rossetto, O.2    Montecucco, C.3
  • 6
    • 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. and Montecucco, C. (1992) Tetanus toxin is a zinc protein and its inhibition of neurotransmitter release and protease activity depend on zinc. EMBO J. 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
  • 9
    • 0023046224 scopus 로고
    • The complete nucleotide sequence of tetanus toxin
    • Fairweather, N. and Lyness, V. A. (1986) The complete nucleotide sequence of tetanus toxin. Nuclear Acids Res. 14, 7809-7812.
    • (1986) Nuclear Acids Res. , vol.14 , pp. 7809-7812
    • Fairweather, N.1    Lyness, V.A.2
  • 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. and Niemann, H. (1990) The complete sequence of botulinum neurotoxin type A and comparison with other clostridial neurotoxins. J. Biol. Chem. 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
  • 11
    • 0028268948 scopus 로고
    • Clostridial neurotoxins: New tools for dissecting exocytosis
    • Niemann, H., Blasi, J. and Jahn, R. (1994) Clostridial neurotoxins: new tools for dissecting exocytosis. Trends Cell Biol. 4, 179-185.
    • (1994) Trends Cell Biol. , vol.4 , pp. 179-185
    • Niemann, H.1    Blasi, J.2    Jahn, R.3
  • 14
    • 0026721240 scopus 로고
    • Molecular cloning of the Clostridium botulinum structural gene encoding the type B neurotoxin and determination of its entire nucleotide sequence
    • Whelan, S. M., Elmore, M. J., Bodsworth, N. J., Brehm, J. K., Atkinson, T., and Minton, N. P. (1992) Molecular cloning of the Clostridium botulinum structural gene encoding the type B neurotoxin and determination of its entire nucleotide sequence. Appl. Environ. Microbiol. 58, 2345-2354.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 2345-2354
    • Whelan, S.M.1    Elmore, M.J.2    Bodsworth, N.J.3    Brehm, J.K.4    Atkinson, T.5    Minton, N.P.6
  • 16
    • 0027248876 scopus 로고
    • Tetanus and botulinsm neurotoxins: A new group of zinc protease
    • Montecucco, C. and Schiavo, G. (1993) Tetanus and botulinsm neurotoxins: a new group of zinc protease. Trends Biochem. Sci. 18, 324-327.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 324-327
    • Montecucco, C.1    Schiavo, G.2
  • 18
    • 0024353830 scopus 로고
    • Isolated light chains of botulinum neurotoxins inhibit exocytosis. Studies in digitonin-permeabilized chromaffin cells
    • Bittner, M. A., DasGupta, B. R. and Holz, R. W. (1989) Isolated light chains of botulinum neurotoxins inhibit exocytosis. Studies in digitonin-permeabilized chromaffin cells. J. Biol. Chem. 264, 10354-10360.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10354-10360
    • Bittner, M.A.1    DasGupta, B.R.2    Holz, R.W.3
  • 19
    • 0026000571 scopus 로고
    • Botulinum neurotoxin light chain inhibits norepinephrine secretion in PC12 cells at an intracellular membranous or cytoskeletal site
    • Lomneth, R., Martin, T. F. and DasGupta, B. R. (1991) Botulinum neurotoxin light chain inhibits norepinephrine secretion in PC12 cells at an intracellular membranous or cytoskeletal site. J. Neurochem. 57, 1413-1421.
    • (1991) J. Neurochem. , vol.57 , pp. 1413-1421
    • Lomneth, R.1    Martin, T.F.2    DasGupta, B.R.3
  • 20
    • 0020663105 scopus 로고
    • Botulinum neurotoxin type E: Studies on mechanism of action and on structure-activity relationships
    • Simpson, L. L. and DasGupta, B. R. (1983) Botulinum neurotoxin type E: studies on mechanism of action and on structure-activity relationships. J. Pharmacol. Exp. Ther. 224, 135-140.
    • (1983) J. Pharmacol. Exp. Ther. , vol.224 , pp. 135-140
    • Simpson, L.L.1    DasGupta, B.R.2
  • 21
    • 0030866129 scopus 로고    scopus 로고
    • Botulinum neurotoxin type A: Limited proteolysis by endoproteinase Glu-C and alpha-chymotrypsin enhanced following reduction; identification of the cleaved sites and fragments
    • Beecher, D. J. and DasGupta, B. R. (1997) Botulinum neurotoxin type A: limited proteolysis by endoproteinase Glu-C and alpha-chymotrypsin enhanced following reduction; identification of the cleaved sites and fragments. J. Protein Chem. 16, 701-712.
    • (1997) J. Protein Chem. , vol.16 , pp. 701-712
    • Beecher, D.J.1    DasGupta, B.R.2
  • 22
    • 0030853242 scopus 로고    scopus 로고
    • Covalent structure of botulinum neurotoxin type E: Location of sulfhydryl groups, and disulfide bridges and identification of C-termini of light and heavy chain
    • Antharavally, B. S. and DasGupta, B. R. (1997) Covalent structure of botulinum neurotoxin type E: location of sulfhydryl groups, and disulfide bridges and identification of C-termini of light and heavy chain. J. Protein Chem. 16, 787-799.
    • (1997) J. Protein Chem. , vol.16 , pp. 787-799
    • Antharavally, B.S.1    DasGupta, B.R.2
  • 23
    • 0025347889 scopus 로고
    • Botulinum neurotoxin type E fragmented with endoproteinase Lys-C reveals the site trypsin nicks and homology with tetanus neurotoxin
    • Gimenez, J. A. and DasGupta, B. R. (1990) Botulinum neurotoxin type E fragmented with endoproteinase Lys-C reveals the site trypsin nicks and homology with tetanus neurotoxin. Biochimie. 72, 213-217.
    • (1990) Biochimie. , vol.72 , pp. 213-217
    • Gimenez, J.A.1    DasGupta, B.R.2
  • 24
    • 0023711730 scopus 로고
    • Tetanus toxin: Biochemical and pharmacological comparison between its protoxin and some isotoxins obtained by limited proteolysis
    • Weller, U., Mauler, F. and Habermann E. (1988) Tetanus toxin: biochemical and pharmacological comparison between its protoxin and some isotoxins obtained by limited proteolysis. Naunyn Schmiedebergs Arch Pharmacol 338, 99-106.
    • (1988) Naunyn Schmiedebergs Arch Pharmacol , vol.338 , pp. 99-106
    • Weller, U.1    Mauler, F.2    Habermann, E.3
  • 25
    • 0020398466 scopus 로고
    • Binding to mouse brain synaptosomes of Clostridium botulinum type E derivative toxin before and after tryptic activation
    • Kozaki, S. and Sakaguchi, G. (1982) Binding to mouse brain synaptosomes of Clostridium botulinum type E derivative toxin before and after tryptic activation. Toxicon 20, 841-846.
    • (1982) Toxicon , vol.20 , pp. 841-846
    • Kozaki, S.1    Sakaguchi, G.2
  • 26
    • 0023048904 scopus 로고
    • Botulinum neurotoxin type B. Its purification, radioiodination and interaction with rat-brain synaptosomal membranes
    • Evans, D. M., Williams, R. S., Shone, C. C., Hambleton, P., Melling, J. and Dolly, J. O. (1986) Botulinum neurotoxin type B. Its purification, radioiodination and interaction with rat-brain synaptosomal membranes. Eur. J. Biochem. 154, 409-416.
    • (1986) Eur. J. Biochem. , vol.154 , pp. 409-416
    • Evans, D.M.1    Williams, R.S.2    Shone, C.C.3    Hambleton, P.4    Melling, J.5    Dolly, J.O.6
  • 27
    • 0024506750 scopus 로고
    • Effect of pH on the interaction of botulinum neurotoxins A, B and E with liposomes
    • Montecucco, C., Schiavo, G. and DasGupta, B. R. (1989) Effect of pH on the interaction of botulinum neurotoxins A, B and E with liposomes. Biochem J. 259, 47-53.
    • (1989) Biochem J. , vol.259 , pp. 47-53
    • Montecucco, C.1    Schiavo, G.2    DasGupta, B.R.3
  • 28
    • 0023958306 scopus 로고
    • Circular dichroic and fluorescence spectroscopic study of the conformation of botulinum neurotoxin types A and E
    • Datta, A. and DasGupta, B. R. (1988) Circular dichroic and fluorescence spectroscopic study of the conformation of botulinum neurotoxin types A and E. Mol. Cell Biochem. 79, 153-159.
    • (1988) Mol. Cell Biochem. , vol.79 , pp. 153-159
    • Datta, A.1    DasGupta, B.R.2
  • 29
    • 0025103812 scopus 로고
    • Conformational changes associated with the nicking and activation of botulinum neurotoxin type E
    • Singh, B. R. and DasGupta, B. R. (1990) Conformational changes associated with the nicking and activation of botulinum neurotoxin type E. Biophys. Chem. 38, 123-130.
    • (1990) Biophys. Chem. , vol.38 , pp. 123-130
    • Singh, B.R.1    DasGupta, B.R.2
  • 30
    • 0343281721 scopus 로고
    • Channels formed by botulinum type E neurotoxin in planar lipid bilayers
    • Blaustein, R. O., Hoch, D. H. and DasGupta, B. R. (1988) Channels formed by botulinum type E neurotoxin in planar lipid bilayers. FASEB J. 2, A1750.
    • (1988) FASEB J. , vol.2
    • Blaustein, R.O.1    Hoch, D.H.2    DasGupta, B.R.3
  • 31
    • 0024424934 scopus 로고
    • Inhibition of transmitter release by botulinum neurotoxin A. Contribution of various fragments to the intoxication process
    • Poulain, B., Wadsworth, J. D., Maisey, E. A., Shone, C. C., Melling, J., Tauc, L. and Dolly, J. O. (1989) Inhibition of transmitter release by botulinum neurotoxin A. Contribution of various fragments to the intoxication process. Eur. J. Biochem. 185, 197-203.
    • (1989) Eur. J. Biochem. , vol.185 , pp. 197-203
    • Poulain, B.1    Wadsworth, J.D.2    Maisey, E.A.3    Shone, C.C.4    Melling, J.5    Tauc, L.6    Dolly, J.O.7
  • 34
    • 0019619833 scopus 로고
    • The origin, structure, and pharmacological activity of botulinum toxin
    • Simpson, L. L. (1981) The origin, structure, and pharmacological activity of botulinum toxin. Pharmacol. Rev. 33, 155-188.
    • (1981) Pharmacol. Rev. , vol.33 , pp. 155-188
    • Simpson, L.L.1
  • 35
    • 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. and DasGupta, B. R. (1983) Comparison of the effects of botulinum neurotoxin types A and E at the rat neuromuscular junction. Med. Biol. 61, 120-125.
    • (1983) Med. Biol. , vol.61 , pp. 120-125
    • Sellin, L.C.1    Kauffman, J.A.2    DasGupta, B.R.3
  • 36
    • 0028204552 scopus 로고
    • Covalent structure of botulinum neurotoxin type A: Location of sulfhydryl groups, and disulfide bridges and identification of C-termini of light and heavy chains
    • Krieglstein, K. G., DasGupta, B. R. and Henschen, A. H. (1994) Covalent structure of botulinum neurotoxin type A: location of sulfhydryl groups, and disulfide bridges and identification of C-termini of light and heavy chains. J. Protein Chem. 13, 49-57.
    • (1994) J. Protein Chem. , vol.13 , pp. 49-57
    • Krieglstein, K.G.1    DasGupta, B.R.2    Henschen, A.H.3
  • 37
    • 0019856815 scopus 로고
    • Role of amino groups in the structure and biological activity of botulinum neurotoxin types A and E
    • DasGupta, B. R. and Rasmussen, S. (1981) Role of amino groups in the structure and biological activity of botulinum neurotoxin types A and E. Biochem. Biophys. Res. Commun. 101, 1209-1215.
    • (1981) Biochem. Biophys. Res. Commun. , vol.101 , pp. 1209-1215
    • DasGupta, B.R.1    Rasmussen, S.2
  • 38
    • 0022416338 scopus 로고
    • Inactivation of Clostridium botulinum type a neurotoxin by trypsin and purification of two tryptic fragments. Proteolytic action near the COOH-terminus of the heavy subunit destroys toxin-binding activity
    • Shone, C. C., Hambleton, P. and Melling, J. (1985) Inactivation of Clostridium botulinum type A neurotoxin by trypsin and purification of two tryptic fragments. Proteolytic action near the COOH-terminus of the heavy subunit destroys toxin-binding activity. Eur. J. Biochem. 151, 75-82.
    • (1985) Eur. J. Biochem. , vol.151 , pp. 75-82
    • Shone, C.C.1    Hambleton, P.2    Melling, J.3
  • 39
    • 0027209170 scopus 로고
    • Botulinum type A neurotoxin digested with pepsin yields 132, 97, 72, 45, 42, and 18 kD fragments
    • Gimenez, J. A. and DasGupta, B. R. (1993) Botulinum type A neurotoxin digested with pepsin yields 132, 97, 72, 45, 42, and 18 kD fragments. J. Protein Chem. 12, 351-363.
    • (1993) J. Protein Chem. , vol.12 , pp. 351-363
    • Gimenez, J.A.1    DasGupta, B.R.2
  • 40
    • 0027442858 scopus 로고
    • A role for the interchain disulfide or its participating thiols in the internalization of botulinum neurotoxin A revealed by a toxin derivative that binds to ecto-acceptors and inhibits transmitter release intracellularly
    • de Paiva, A., Poulain, B., Lawrence, G. W., Shone, C. C., Tauc, L. and Dolly, J. (1993) A role for the interchain disulfide or its participating thiols in the internalization of botulinum neurotoxin A revealed by a toxin derivative that binds to ecto-acceptors and inhibits transmitter release intracellularly. J. Biol. Chem. 268, 20838-20844.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20838-20844
    • De Paiva, A.1    Poulain, B.2    Lawrence, G.W.3    Shone, C.C.4    Tauc, L.5    Dolly, J.6
  • 41
    • 0021369619 scopus 로고
    • A functional role for cysteine disulfides in the transmembrane transport of diphtheria toxin
    • Wright, H. T., Marston, A. W. and Goldstein, D. J. (1984) A functional role for cysteine disulfides in the transmembrane transport of diphtheria toxin. J. Biol. Chem. 259, 1649-1654.
    • (1984) J. Biol. Chem. , vol.259 , pp. 1649-1654
    • Wright, H.T.1    Marston, A.W.2    Goldstein, D.J.3
  • 42
    • 0031954673 scopus 로고    scopus 로고
    • Status of cys residues in the covalent structure of botulinum neurotoxin types A, B, and E
    • Antharavally, B., Tepp, W. and DasGupta, B. R. (1998) Status of Cys residues in the covalent structure of botulinum neurotoxin types A, B, and E. J. Protein Chem. 17, 187-196.
    • (1998) J. Protein Chem. , vol.17 , pp. 187-196
    • Antharavally, B.1    Tepp, W.2    DasGupta, B.R.3
  • 43
    • 0025681434 scopus 로고
    • Structure and biological activity of botulinum neurotoxin
    • DasGupta, B. R. (1990) Structure and biological activity of botulinum neurotoxin. J. Physiol. (Paris) 84, 220-228.
    • (1990) J. Physiol. (Paris) , vol.84 , pp. 220-228
    • DasGupta, B.R.1
  • 44
    • 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. and Ahnert-Hilger, G. (1989) Reductive chain separation of botulinum A toxin - a prerequisite to its inhibitory action on exocytosis in chromaffin cells. FEBS Lett. 248, 23-27.
    • (1989) FEBS Lett. , vol.248 , pp. 23-27
    • Stecher, B.1    Gratzl, M.2    Ahnert-Hilger, G.3
  • 45
    • 0014027285 scopus 로고
    • Study of the toxin of Clostridium botulinum. Effects of 2-hydroxy-5-nitrobenzyl bromide on the biological activity of botulinum toxin
    • Boroff, D. A. and DasGupta, B. R. (1966) Study of the toxin of Clostridium botulinum. Effects of 2-hydroxy-5-nitrobenzyl bromide on the biological activity of botulinum toxin. Biochim. Biophys. Acta 117, 289-296.
    • (1966) Biochim. Biophys. Acta , vol.117 , pp. 289-296
    • Boroff, D.A.1    DasGupta, B.R.2
  • 46
    • 0018904312 scopus 로고
    • Role of arginine residues in the structure and biological activity of botulinum neurotoxin types A and E
    • DasGupta, B. R. and Sugiyama, H. (1980) Role of arginine residues in the structure and biological activity of botulinum neurotoxin types A and E. Biochem. Biophys. Res. Commun. 93, 369-375.
    • (1980) Biochem. Biophys. Res. Commun. , vol.93 , pp. 369-375
    • DasGupta, B.R.1    Sugiyama, H.2
  • 47
    • 0019856815 scopus 로고
    • Role of amino groups in the structure and biological activity of botulinum neurotoxin types A and E
    • DasGupta, B. R. and Rasmussen, S. (1981) Role of amino groups in the structure and biological activity of botulinum neurotoxin types A and E. Biochem. Biophys. Res. Commun. 101, 1209-1215.
    • (1981) Biochem. Biophys. Res. Commun. , vol.101 , pp. 1209-1215
    • DasGupta, B.R.1    Rasmussen, S.2
  • 48
    • 0023751965 scopus 로고
    • Reductive methylation of lysine residues of botulinum neurotoxin types A and B
    • Sathyamoorthy, V. and DasGupta, B. R. (1988) Reductive methylation of lysine residues of botulinum neurotoxin types A and B. Mol. Cell Biochem. 83, 65-72.
    • (1988) Mol. Cell Biochem. , vol.83 , pp. 65-72
    • Sathyamoorthy, V.1    DasGupta, B.R.2
  • 49
    • 0021146063 scopus 로고
    • Effect of diethylpyrocarbonate on the biological activities of botulinum neurotoxin types A and E
    • DasGupta, B. R. and Rasmussen, S. (1984) Effect of diethylpyrocarbonate on the biological activities of botulinum neurotoxin types A and E. Arch Biochem. Biophys. 232, 172-817.
    • (1984) Arch Biochem. Biophys. , vol.232 , pp. 172-817
    • Dasgupta, B.R.1    Rasmussen, S.2
  • 50
    • 0024564405 scopus 로고
    • Effect of tetranitromethane on the biological activities of botulinum neurotoxin types A, B and E
    • Woody, M. and DasGupta, B. R. (1989) Effect of tetranitromethane on the biological activities of botulinum neurotoxin types A, B and E. Mol. Cell Biochem. 85, 159-169.
    • (1989) Mol. Cell Biochem. , vol.85 , pp. 159-169
    • Woody, M.1    DasGupta, B.R.2
  • 51
    • 0024446098 scopus 로고
    • Modification of carboxyl groups in botulinum neurotoxin types A and E
    • Woody, M. A. Herian, A. and DasGupta, B. R. (1989) Modification of carboxyl groups in botulinum neurotoxin types A and E. Toxicon 27, 1143-1150.
    • (1989) Toxicon , vol.27 , pp. 1143-1150
    • Woody, M.A.1    Herian, A.2    DasGupta, B.R.3
  • 52
    • 0022220030 scopus 로고
    • Separation, purification, partial characterization and comparison of the heavy and light chains of botulinum neurotoxin types A, B, and E
    • Sathyamoorthy, V. and DasGupta, B. R. (1985) Separation, purification, partial characterization and comparison of the heavy and light chains of botulinum neurotoxin types A, B, and E. J. Biol. Chem. 260, 10461-10466.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10461-10466
    • Sathyamoorthy, V.1    DasGupta, B.R.2
  • 53
    • 0023664001 scopus 로고
    • Role of the heavy and light chains of botulinum neurotoxin in neuromuscular paralysis
    • Bandyopadhyay, S., Clark, A. W., DasGupta, B. R. and Sathyamoorthy, V. (1987) Role of the heavy and light chains of botulinum neurotoxin in neuromuscular paralysis. J. Biol. Chem. 262, 2660-2663.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2660-2663
    • Bandyopadhyay, S.1    Clark, A.W.2    DasGupta, B.R.3    Sathyamoorthy, V.4
  • 54
    • 0024565663 scopus 로고
    • Structure of heavy and light chain subunits of type A botulinum neurotoxin analyzed by circular dichroism and fluorescence measurements
    • Singh, B. R. and DasGupta, B. R. (1989) Structure of heavy and light chain subunits of type A botulinum neurotoxin analyzed by circular dichroism and fluorescence measurements. Mol. Cell Biochem. 85, 67-73.
    • (1989) Mol. Cell Biochem. , vol.85 , pp. 67-73
    • Singh, B.R.1    DasGupta, B.R.2
  • 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. and Colomb, M. G. (1992) Identification and partial characterization of a low affinity metal-binding site in the light chain of tetanus toxin. J. Biol. Chem. 267, 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
  • 56
    • 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., and Niemann, H., (1994) 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, 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
  • 57
    • 0027265710 scopus 로고
    • Cellubrevin is a ubiquitous tetanus-toxin substrate homologous to a putative synaptic vesicle fusion protein
    • McMahon, H. T., Ushkaryov, Y. A., Edelmann, L., Link, E., Binz, T., Niemann, H., Jahn, R. and Südhof, T. C. (1993) Cellubrevin is a ubiquitous tetanus-toxin substrate homologous to a putative synaptic vesicle fusion protein. Nature, 364, 346-349.
    • (1993) Nature , vol.364 , pp. 346-349
    • McMahon, 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
  • 58
    • 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. and Dolly, J. O. (1994) 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, 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
  • 61
    • 0026572840 scopus 로고
    • Clostridial neurotoxins-proposal of a common nomenclature
    • Niemann, H. (1992) Clostridial neurotoxins-proposal of a common nomenclature. Toxicon 30, 223-225.
    • (1992) Toxicon , vol.30 , pp. 223-225
    • Niemann, H.1
  • 63
    • 0028810969 scopus 로고
    • Expression and purification of the light chain of botulinum neurotoxin A: A single mutation abolishes its cleavage of SNAP-25 and neurotoxicity after reconstitution with the heavy chain
    • Zhou, L. de Paiva, A. Liu, D. Aoki, R. and Dolly, J. O. (1995) Expression and purification of the light chain of botulinum neurotoxin A: a single mutation abolishes its cleavage of SNAP-25 and neurotoxicity after reconstitution with the heavy chain. Biochemistry 34, 15175-15181.
    • (1995) Biochemistry , vol.34 , pp. 15175-15181
    • Zhou, L.1    De Paiva, A.2    Liu, D.3    Aoki, R.4    Dolly, J.O.5
  • 64
    • 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. and Jahn, R. (1993) Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC-1/syntaxin. EMBO J. 12, 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
  • 66
    • 0030045128 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy study of zinc coordination in tetanus neurotoxin, astacin, alkaline protease and thermolysin
    • Morante, S., Furenlid, L., Schiavo, G., Tonello, F., Zwilling, R. and Montecucco, C. (1996) X-ray absorption spectroscopy study of zinc coordination in tetanus neurotoxin, astacin, alkaline protease and thermolysin. Eur. J. Biochem. 235, 606-612.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 606-612
    • Morante, S.1    Furenlid, L.2    Schiavo, G.3    Tonello, F.4    Zwilling, R.5    Montecucco, C.6
  • 68
    • 0028310404 scopus 로고
    • Mechanism of action of tetanus and botulinum neurotoxins
    • Montecucco, C. and Schiavo, G. (1994) Mechanism of action of tetanus and botulinum neurotoxins. Microbiol. 13, 1-8.
    • (1994) Microbiol. , vol.13 , pp. 1-8
    • Montecucco, C.1    Schiavo, G.2
  • 69
    • 0027248876 scopus 로고
    • Tetanus and botulism neurotoxins: A new group of zinc proteases
    • Montecucco, C. and Schiavo, G. (1993) Tetanus and botulism neurotoxins: a new group of zinc proteases. Trends Biochem. Sci. 18, 324-327.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 324-327
    • Montecucco, C.1    Schiavo, G.2
  • 70
    • 0029950893 scopus 로고    scopus 로고
    • Critical aspects of bacterial protein toxins
    • Singh, B. R. (1996) Critical aspects of bacterial protein toxins. Adv. Exp. Med. Biol. 391, 63-84.
    • (1996) Adv. Exp. Med. Biol. , vol.391 , pp. 63-84
    • Singh, B.R.1
  • 71
    • 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. and Singh, B. R. (1998) Role of zinc in the structure and toxic activity of botulinum neurotoxin. Biochemistry 37, 5267-5278.
    • (1998) Biochemistry , vol.37 , pp. 5267-5278
    • Fu, F.N.1    Lomneth, R.B.2    Cai, S.3    Singh, B.R.4
  • 72
    • 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. and Dolly, J. O. (1994) 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, 15365-15374.
    • (1994) Biochemistry , vol.33 , pp. 15365-15374
    • Foran, P.1    Shone, C.C.2    Dolly, J.O.3
  • 73
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Söllner, T., Bennett, M. K., Whiteheart, S. W., Scheller, R. H. and Rothman, J. E. (1993) A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 75, 409-418.
    • (1993) Cell , vol.75 , pp. 409-418
    • Söllner, T.1    Bennett, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 74
    • 0027228261 scopus 로고
    • Synaptic vesicle proteins in exocytosis: What do we know?
    • Walch-Solimena, C., Jahn, R. and Südhof, T. C. (1993) Synaptic vesicle proteins in exocytosis: what do we know? Curr. Opin. Neurobiol. 3, 329-336.
    • (1993) Curr. Opin. Neurobiol. , vol.3 , pp. 329-336
    • Walch-Solimena, C.1    Jahn, R.2    Südhof, T.C.3
  • 77
    • 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. and Dolly, J. O. (1996) Botulinum neurotoxin C1 cleaves both syntaxin and SNAP-25 in intact and permeabilized chromaffin cells: correlation with its blockade of catecholamine release. Biochemistry 35, 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
  • 78
    • 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. and Monteccuco, C. (1993b) Botulinum neurotoxin serotype F is a zinc endopeptidase specific for VAMP/synaptobrevin. J. Biol. Chem. 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    Monteccuco, C.5
  • 79
    • 0028156816 scopus 로고
    • Exploring the functional domain and the target of the tetanus toxin light chain in neurohypophysial terminals
    • Dayanithi, G., Stecher, B., Höhne-Zell, B., Yamasaki, S., Binz, T., Weller, U., Niemann, H. and Gratzl, M. (1994) Exploring the functional domain and the target of the tetanus toxin light chain in neurohypophysial terminals. Neuroscience 58, 423-431.
    • (1994) Neuroscience , vol.58 , pp. 423-431
    • Dayanithi, G.1    Stecher, B.2    Höhne-Zell, B.3    Yamasaki, S.4    Binz, T.5    Weller, U.6    Niemann, H.7    Gratzl, M.8
  • 80
    • 0027294626 scopus 로고
    • Production of biologically active light chain of tetanus toxin in Escherichia coli. Evidence for the importance of the C-terminal 16 amino acids for full biological activity
    • Fairweather, N. F., Sanders, D., Slater, D., Hudel, M., Habermann, E. and Weller, U. (1993) Production of biologically active light chain of tetanus toxin in Escherichia coli. Evidence for the importance of the C-terminal 16 amino acids for full biological activity. FEBS Lett. 323, 218-222.
    • (1993) FEBS Lett. , vol.323 , pp. 218-222
    • Fairweather, N.F.1    Sanders, D.2    Slater, D.3    Hudel, M.4    Habermann, E.5    Weller, U.6
  • 82
    • 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. and Montecucco, C. (1996) 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, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.