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Volumn 19, Issue 3, 1999, Pages 219-260

Structure, activity, and immune (T and B cell) recognition of botulinum neurotoxins

Author keywords

Antibodies; Botulinum neurotoxin; Epitopes; Synthetic peptides; T cells

Indexed keywords

BOTULINUM TOXIN A; EPITOPE; INACTIVATED VACCINE; NEUROTRANSMITTER;

EID: 0033023671     PISSN: 10408401     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (101)

References (271)
  • 1
    • 0002837246 scopus 로고
    • Uber einen neuen anaeroben Bacillus und seine Beziehungen zum Botulismus
    • Van Ermengem, E., Uber einen neuen anaeroben Bacillus und seine Beziehungen zum Botulismus, Z. Hyg. Infektionskr., 26, 1-56, 1897.
    • (1897) Z. Hyg. Infektionskr. , vol.26 , pp. 1-56
    • Van Ermengem, E.1
  • 2
    • 0042492045 scopus 로고
    • Contributions a l'etude des intoxications alimentaires
    • Van Ermengem, E., Contributions a l'etude des intoxications alimentaires, Arch. Int. Pharmacodyn., 3, 213-350, 499-601, 1897.
    • (1897) Arch. Int. Pharmacodyn. , vol.3 , pp. 213-350
    • Van Ermengem, E.1
  • 4
    • 0041883019 scopus 로고
    • An intracellular study of the action of repetitive nerve volleys and of botulinum toxin on miniature end-plate potentials
    • Brooks, V. B., An intracellular study of the action of repetitive nerve volleys and of botulinum toxin on miniature end-plate potentials, J. Physiol., 134, 264-277, 1956.
    • (1956) J. Physiol. , vol.134 , pp. 264-277
    • Brooks, V.B.1
  • 5
    • 0000038294 scopus 로고
    • Botulism-structure and chemistry of botulinum
    • Hardgree, M. C. and Tu, A. T., Eds., Marcel Dekker, New York
    • Sakaguchi, G., Ohishi, I., and Kozaki, S., Botulism-structure and chemistry of botulinum, in Handbook of Natural Toxins, Hardgree, M. C. and Tu, A. T., Eds., vol. 4, Marcel Dekker, New York, 1988, 191-216.
    • (1988) Handbook of Natural Toxins , vol.4 , pp. 191-216
    • Sakaguchi, G.1    Ohishi, I.2    Kozaki, S.3
  • 6
    • 0031839302 scopus 로고    scopus 로고
    • Clinical spectrum of botulism
    • Cherington, M., Clinical spectrum of botulism, Muscle Nerve, 6, 701-710, 1998.
    • (1998) Muscle Nerve , vol.6 , pp. 701-710
    • Cherington, M.1
  • 7
    • 0001994620 scopus 로고
    • The disease and the treatment of botulism
    • Simpson, L. L., Ed., Academic Press, New York
    • Tacket, C. O. and Rogawski, M. A., The disease and the treatment of botulism, in Botulinum Neurotoxin and Tetanus Toxin, Simpson, L. L., Ed., Academic Press, New York, 1989, 351-373.
    • (1989) Botulinum Neurotoxin and Tetanus Toxin , pp. 351-373
    • Tacket, C.O.1    Rogawski, M.A.2
  • 9
    • 37049232988 scopus 로고
    • The most poisonous poison
    • Llamana, C., The most poisonous poison, Science, 130, 763-772, 1959.
    • (1959) Science , vol.130 , pp. 763-772
    • Llamana, C.1
  • 10
    • 0002951890 scopus 로고
    • Cell surface receptors for protein toxins
    • Simpson, L. L., Ed., Academic Press, New York
    • Middlebrook, J. L., Cell surface receptors for protein toxins, in Botulinum Neurotoxin and Tetanus Toxin, Simpson, L. L., Ed., Academic Press, New York, 1989, 95-119.
    • (1989) Botulinum Neurotoxin and Tetanus Toxin , pp. 95-119
    • Middlebrook, J.L.1
  • 11
    • 0014690770 scopus 로고
    • Isolation and characterization of Clostridium botulinum type B toxin
    • Beers, W. H. and Reich, E., Isolation and characterization of Clostridium botulinum type B toxin, J. Biol. Chem., 244, 4473-4479, 1969.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4473-4479
    • Beers, W.H.1    Reich, E.2
  • 12
    • 0016641006 scopus 로고
    • Molecular construction of Clostridium botulinum type F progenitor toxin
    • Ohishi, I. and Sakaguchi, G., Molecular construction of Clostridium botulinum type F progenitor toxin, Appl. Microbiol., 29, 444-447, 1975.
    • (1975) Appl. Microbiol. , vol.29 , pp. 444-447
    • Ohishi, I.1    Sakaguchi, G.2
  • 13
    • 0015502845 scopus 로고
    • A common subunit structure in Clostridium botulinum type A, B and E toxins
    • Das Gupta, B. R. and Sugiyama, H., A common subunit structure in Clostridium botulinum type A, B and E toxins, Biochem. Biophys. Res. Commun., 48, 108-112, 1972.
    • (1972) Biochem. Biophys. Res. Commun. , vol.48 , pp. 108-112
    • Das Gupta, B.R.1    Sugiyama, H.2
  • 14
    • 0018906584 scopus 로고
    • Kinetic studies on the interaction between botulinum toxin type A and the cholinergic neuromuscular junction
    • Simpson, L. L., Kinetic studies on the interaction between botulinum toxin type A and the cholinergic neuromuscular junction, J. Pharmacol. Exp. Ther., 212, 16-21, 1980.
    • (1980) J. Pharmacol. Exp. Ther. , vol.212 , pp. 16-21
    • Simpson, L.L.1
  • 15
    • 0016678458 scopus 로고
    • Molecular construction of Clostridium botulinum type A toxins
    • Sugui, S. and Sakaguchi, G., Molecular construction of Clostridium botulinum type A toxins, Infec. Immun., 12, 1262-1270, 1975.
    • (1975) Infec. Immun. , vol.12 , pp. 1262-1270
    • Sugui, S.1    Sakaguchi, G.2
  • 16
    • 0016769651 scopus 로고
    • Purification and properties of Clostridium botulinum type F toxin
    • Yang, K. H. and Sugiyama, H., Purification and properties of Clostridium botulinum type F toxin, Appl. Microbiol., 29, 598-603, 1975.
    • (1975) Appl. Microbiol. , vol.29 , pp. 598-603
    • Yang, K.H.1    Sugiyama, H.2
  • 17
    • 0017756527 scopus 로고
    • Clostridium botulinum type D toxin: Purification, molecular structure and some immunological properties
    • Miyazaki, S., Iwasaki, M., and Sakaguchi, G., Clostridium botulinum type D toxin: purification, molecular structure and some immunological properties, Infect. Immun., 17, 395-401, 1977.
    • (1977) Infect. Immun. , vol.17 , pp. 395-401
    • Miyazaki, S.1    Iwasaki, M.2    Sakaguchi, G.3
  • 18
    • 0018454061 scopus 로고
    • Structure and toxicity of Clostridium botulinum type C toxin
    • Syuto, B. and Kubo, S., Structure and toxicity of Clostridium botulinum type C toxin, Japan. J. Med. Sci. Biol., 32132-32133, 1979.
    • (1979) Japan. J. Med. Sci. Biol. , pp. 32132-32133
    • Syuto, B.1    Kubo, S.2
  • 19
    • 0018911425 scopus 로고
    • Evidence that botulinum C2 toxin has two dissimilar components
    • Iwasaki, M., Ohishi, I., and Sakaguchi, G., Evidence that botulinum C2 toxin has two dissimilar components, Infect. Immun., 29, 390-394, 1980.
    • (1980) Infect. Immun. , vol.29 , pp. 390-394
    • Iwasaki, M.1    Ohishi, I.2    Sakaguchi, G.3
  • 20
    • 0019158135 scopus 로고
    • Purification and characterization of two components of botulinum C2 toxin
    • Ohishi, I., Iwasaka, M., and Sakaguchi, G., Purification and characterization of two components of botulinum C2 toxin, Infect. Immun., 30, 668-673, 1980.
    • (1980) Infect. Immun. , vol.30 , pp. 668-673
    • Ohishi, I.1    Iwasaka, M.2    Sakaguchi, G.3
  • 21
    • 0019857932 scopus 로고
    • Separation of Clostridium botulinum type A derivative toxin into two fragments
    • Kozaki, S., Togashi, S., and Sakaguchi, G., Separation of Clostridium botulinum type A derivative toxin into two fragments, Japan. J. Med. Sci. Biol., 34, 61-68, 1981.
    • (1981) Japan. J. Med. Sci. Biol. , vol.34 , pp. 61-68
    • Kozaki, S.1    Togashi, S.2    Sakaguchi, G.3
  • 22
    • 0020345357 scopus 로고
    • A comparison of the pharmacological properties of Clostridium botulinum type C and type C2
    • Simpson, L. L., A comparison of the pharmacological properties of Clostridium botulinum type C and type C2, J. Pharmacol. Exp. Ther., 223, 695-701, 1982.
    • (1982) J. Pharmacol. Exp. Ther. , vol.223 , pp. 695-701
    • Simpson, L.L.1
  • 23
    • 0028886648 scopus 로고
    • Molecular characterization of two forms of nontoxic-nonhemagglutinin components of Clostridium botulinum type A progenitor toxins
    • Fujita, R., Fujinaga, Y., Inoue, K., Nakajima, H., Kumon, H., and Oguma, K., Molecular characterization of two forms of nontoxic-nonhemagglutinin components of Clostridium botulinum type A progenitor toxins, FEBS Lett., 376, 41-44, 1995.
    • (1995) FEBS Lett. , vol.376 , pp. 41-44
    • Fujita, R.1    Fujinaga, Y.2    Inoue, K.3    Nakajima, H.4    Kumon, H.5    Oguma, K.6
  • 25
    • 0029814724 scopus 로고    scopus 로고
    • Organization and nucleotide sequence of genes for hemagglutinin components of Clostridium botulinum type B progenitor toxin
    • Yang, G. H., Rhee, S. D., Jung, H. H., and Yang K. H., Organization and nucleotide sequence of genes for hemagglutinin components of Clostridium botulinum type B progenitor toxin, Biochem. Mol. Biol. Int., 39, 1141-1146, 1996.
    • (1996) Biochem. Mol. Biol. Int. , vol.39 , pp. 1141-1146
    • Yang, G.H.1    Rhee, S.D.2    Jung, H.H.3    Yang, K.H.4
  • 26
    • 2642651881 scopus 로고    scopus 로고
    • Gene organization and sequence determination of the two botulinum neurotoxin gene clusters in Clostridium botulinum type A(B) strain NCTC 2916
    • Rodriguez, J. M., Collins, M. D., and East, A. K., Gene organization and sequence determination of the two botulinum neurotoxin gene clusters in Clostridium botulinum type A(B) strain NCTC 2916, Curr. Microbiol., 36, 226-231, 1998.
    • (1998) Curr. Microbiol. , vol.36 , pp. 226-231
    • Rodriguez, J.M.1    Collins, M.D.2    East, A.K.3
  • 27
    • 0030200501 scopus 로고    scopus 로고
    • Genetic characterization of the botulinum toxin complex of Clostridium botulinum strain NCTC 2916
    • Henderson, I., Whelan, S. M., Davis, T. O., and Minton, N. P., Genetic characterization of the botulinum toxin complex of Clostridium botulinum strain NCTC 2916, FEMS Microbiol. Lett., 140, 151-158, 1996.
    • (1996) FEMS Microbiol. Lett. , vol.140 , pp. 151-158
    • Henderson, I.1    Whelan, S.M.2    Davis, T.O.3    Minton, N.P.4
  • 28
    • 0029087238 scopus 로고
    • Characterization of nontoxic-nonhemagglutinin component of the two types of progenitor toxin (M and L) produced by Clostridium botulinum type D CB-16
    • Ohyama, T., Watanabe, T., Fujinaga, Y., Inoue, K., Sunagawa, H., Fujii, N., Inoue, K., and Oguma, K., Characterization of nontoxic-nonhemagglutinin component of the two types of progenitor toxin (M and L) produced by Clostridium botulinum type D CB-16, Microbiol. Immunol., 39, 457-465, 1995.
    • (1995) Microbiol. Immunol. , vol.39 , pp. 457-465
    • Ohyama, T.1    Watanabe, T.2    Fujinaga, Y.3    Inoue, K.4    Sunagawa, H.5    Fujii, N.6    Inoue, K.7    Oguma, K.8
  • 29
    • 0032518928 scopus 로고    scopus 로고
    • Gene arrangement in the upstream region of Clostridium botulinum type E and Clostridium butyricum BL6340 progenitor toxin genes is different from that of other types
    • Kubota, T., Yonekura, N., Hariya, Y., Isogai, E., Isogai, H., Amano, K., and Fujii, N., Gene arrangement in the upstream region of Clostridium botulinum type E and Clostridium butyricum BL6340 progenitor toxin genes is different from that of other types, FEMS Microbiol. Lett., 158, 215-221, 1998.
    • (1998) FEMS Microbiol. Lett. , vol.158 , pp. 215-221
    • Kubota, T.1    Yonekura, N.2    Hariya, Y.3    Isogai, E.4    Isogai, H.5    Amano, K.6    Fujii, N.7
  • 30
    • 0030794919 scopus 로고    scopus 로고
    • Molecular characterization of the clusters of genes encoding the botulinum neurotoxin complex in Clostridium botulinum (Clostridium argentinense) type G and nonproteolytic Clostridium botulinum type B
    • Bhandari, M., Campbell, K. D., Collins, M. D., and East A. K., Molecular characterization of the clusters of genes encoding the botulinum neurotoxin complex in Clostridium botulinum (Clostridium argentinense) type G and nonproteolytic Clostridium botulinum type B, Current Microbiol., 35, 207-214, 1997.
    • (1997) Current Microbiol. , vol.35 , pp. 207-214
    • Bhandari, M.1    Campbell, K.D.2    Collins, M.D.3    East, A.K.4
  • 31
    • 15844377448 scopus 로고    scopus 로고
    • Genetic characterization of Clostridium botulinum type A containing silent type B neurotoxin gene sequences
    • Hutson, R. A., Zhou, Y., Collins, M. D., Johnson, E. A., Hatheway, C. L., and Sugiyama, H., Genetic characterization of Clostridium botulinum type A containing silent type B neurotoxin gene sequences, J. Biol. Chem., 271, 10786-10792, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10786-10792
    • Hutson, R.A.1    Zhou, Y.2    Collins, M.D.3    Johnson, E.A.4    Hatheway, C.L.5    Sugiyama, H.6
  • 32
    • 0029074299 scopus 로고
    • Molecular aspects of tetanus and botulinum neurotoxin poisoning
    • Ahnert-Hilger, G. and Bigalke, H., Molecular aspects of tetanus and botulinum neurotoxin poisoning, Prog. Neurobiol., 46, 83-96, 1995.
    • (1995) Prog. Neurobiol. , vol.46 , pp. 83-96
    • Ahnert-Hilger, G.1    Bigalke, H.2
  • 33
    • 0029597914 scopus 로고
    • Botulinum versus tetanus neurotoxins: Why is botulinum neurotoxin but not tetanus neurotoxin a food poison?
    • Singh, B. R., Li, B., and Read, D., Botulinum versus tetanus neurotoxins: why is botulinum neurotoxin but not tetanus neurotoxin a food poison? Toxicon, 33, 1541-1547, 1995.
    • (1995) Toxicon , vol.33 , pp. 1541-1547
    • Singh, B.R.1    Li, B.2    Read, D.3
  • 34
    • 0025314995 scopus 로고
    • The complete sequence of botulinum neurotoxin Type A and comparison with other clostridial neurotoxins
    • Binz, T., Kurazono, H., Micaela, W., Frevert, J., Wernars, K., and Niemann, H., The complete sequence of botulinum neurotoxin Type A and comparison with other clostridial neurotoxins, J. Biol. Chem., 265, 9153-9158, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9153-9158
    • Binz, T.1    Kurazono, H.2    Micaela, W.3    Frevert, J.4    Wernars, K.5    Niemann, H.6
  • 35
    • 0027379492 scopus 로고
    • Sequence of the gene coding for the neurotoxin of Clostridium botulinum type A associated with infant botulism: Comparison with other clostridial neurotoxins
    • Willems, A., East, A. K., Lawson, P. A., and Collins, M. D., Sequence of the gene coding for the neurotoxin of Clostridium botulinum type A associated with infant botulism: comparison with other clostridial neurotoxins, Res. Microbiol., 144, 547-556, 1993.
    • (1993) Res. Microbiol. , vol.144 , pp. 547-556
    • Willems, A.1    East, A.K.2    Lawson, P.A.3    Collins, M.D.4
  • 36
    • 0026816007 scopus 로고
    • Cloning of a Clostridium botulinum type B toxin gene fragment encoding the N-terminus of the heavy chain
    • Jung, H. H., Rhee, S. D., and Yang, K. H., Cloning of a Clostridium botulinum type B toxin gene fragment encoding the N-terminus of the heavy chain, FEMS Microbiol. Lett., 70, 69-72, 1992.
    • (1992) FEMS Microbiol. Lett. , vol.70 , pp. 69-72
    • Jung, H.H.1    Rhee, S.D.2    Yang, K.H.3
  • 37
    • 0027979777 scopus 로고
    • Nucleotide sequence of the gene coding for nonproteolytic Clostridium botulinum type B neurotoxin: Comparison with other clostridial neurotoxins
    • Hutson, R. A., Collins, M. D., East, A. K., and Thompson, D. E., Nucleotide sequence of the gene coding for nonproteolytic Clostridium botulinum type B neurotoxin: comparison with other clostridial neurotoxins, Curr. Microbiol., 28, 101-110, 1994.
    • (1994) Curr. Microbiol. , vol.28 , pp. 101-110
    • Hutson, R.A.1    Collins, M.D.2    East, A.K.3    Thompson, D.E.4
  • 39
    • 0029049105 scopus 로고
    • Botulinal neurotoxin C1 complex genes, clostridial neurotoxin homology and genetic transfer in Clostridium botulinum
    • Hauser, D., Gibert, M., Marvaud, J. C., Eklund, M. W., and Popoff, M. R., Botulinal neurotoxin C1 complex genes, clostridial neurotoxin homology and genetic transfer in Clostridium botulinum, Toxicon, 33, 515-26, 1995.
    • (1995) Toxicon , vol.33 , pp. 515-526
    • Hauser, D.1    Gibert, M.2    Marvaud, J.C.3    Eklund, M.W.4    Popoff, M.R.5
  • 41
    • 0026941186 scopus 로고
    • The complete amino acid sequence of the Clostridium botulinum type D neurotoxin, deduced by nucleotide sequence analysis of the encoding phage d-16 phi genome
    • Sunagawa, H., Ohyama, T., Watanabe, T., and Inoue, K., The complete amino acid sequence of the Clostridium botulinum type D neurotoxin, deduced by nucleotide sequence analysis of the encoding phage d-16 phi genome, J. Vet. Med. Sci., 54, 905-913, 1992.
    • (1992) J. Vet. Med. Sci. , vol.54 , pp. 905-913
    • Sunagawa, H.1    Ohyama, T.2    Watanabe, T.3    Inoue, K.4
  • 42
    • 0026517228 scopus 로고
    • Sequences of the botulinal neurotoxin E derived from Clostridium botulinum type E (strain Beluga) and Clostridium butyricum (strains ATCC 43181 and ATCC 43755)
    • Poulet, S., Hauser, D., Quanz, M., Niemann, H., and Popoff, M. R., Sequences of the botulinal neurotoxin E derived from Clostridium botulinum type E (strain Beluga) and Clostridium butyricum (strains ATCC 43181 and ATCC 43755), Biochem. Biophys. Res. Commun., 183, 107-113, 1992.
    • (1992) Biochem. Biophys. Res. Commun. , vol.183 , pp. 107-113
    • Poulet, S.1    Hauser, D.2    Quanz, M.3    Niemann, H.4    Popoff, M.R.5
  • 43
    • 0026601357 scopus 로고
    • The complete amino acid sequence of the Clostridium botulinum type-E neurotoxin derived by nucleotide-sequence analysis of the encoding gene
    • Whelan, S. M., Elmore, M. J., Bodsworth, N. J., Atkinson, T., and Minton, N. P., The complete amino acid sequence of the Clostridium botulinum type-E neurotoxin derived by nucleotide-sequence analysis of the encoding gene, Eur. J. Biochem., 204, 657-667, 1992.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 657-667
    • Whelan, S.M.1    Elmore, M.J.2    Bodsworth, N.J.3    Atkinson, T.4    Minton, N.P.5
  • 45
    • 0027769518 scopus 로고
    • Nucleotide sequence of the gene coding for Clostridium botulinum (Clostridium argentinense) type G neurotoxin: Genealogical comparison with other clostridial neurotoxins
    • Campbell, K., Collins, M. D., and East, A. K., Nucleotide sequence of the gene coding for Clostridium botulinum (Clostridium argentinense) type G neurotoxin: genealogical comparison with other clostridial neurotoxins, Biochim. Biophys. Acta, 1216, 487-491, 1993.
    • (1993) Biochim. Biophys. Acta , vol.1216 , pp. 487-491
    • Campbell, K.1    Collins, M.D.2    East, A.K.3
  • 46
    • 0027163418 scopus 로고
    • Gene probes for identification of the botulinal neurotoxin gene and specific identification of neurotoxin types B, E, and F. Also, B3: C. botulinum (strain nonproteolytic Eklund 2B) gene for neurotoxin type B. Accession # X70819. (Ref. same as B2); B4: C. botulinum (strain proteolytic B) gene for neurotoxin type B. Accession # X70817. (Ref. same as B2); B5: Clostridium botulinum neurotoxin type B
    • (botB) gene, complete cds. Accession # M81186
    • Campbell, K. D., Collins, M. D., and East, A. K., Gene probes for identification of the botulinal neurotoxin gene and specific identification of neurotoxin types B, E, and F. Also, B3: C. botulinum (strain nonproteolytic Eklund 2B) gene for neurotoxin type B. Accession # X70819. (Ref. same as B2); B4: C. botulinum (strain proteolytic B) gene for neurotoxin type B. Accession # X70817. (Ref. same as B2); B5: Clostridium botulinum neurotoxin type B (botB) gene, complete cds. Accession # M81186, J. Clin. Microbiol., 31, 2255-2262, 1993.
    • (1993) J. Clin. Microbiol. , vol.31 , pp. 2255-2262
    • Campbell, K.D.1    Collins, M.D.2    East, A.K.3
  • 47
    • 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., 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. Prot. Chem., 13, 49-57, 1994.
    • (1994) J. Prot. Chem. , vol.13 , pp. 49-57
    • Krieglstein, K.G.1    DasGupta, B.R.2    Henschen, A.H.3
  • 49
    • 0011712848 scopus 로고
    • Molecular biology of clostridial neurotoxins
    • Alouf, J. E. and Freer, J. H., Eds., Academic Press, New York
    • Niemann, H., Molecular biology of clostridial neurotoxins, in Sourcebook of Protein Toxins, Alouf, J. E. and Freer, J. H., Eds., Academic Press, New York, 1991, 3203-384.
    • (1991) Sourcebook of Protein Toxins , pp. 3203-3384
    • Niemann, H.1
  • 50
    • 0030850192 scopus 로고    scopus 로고
    • Characterization of neurotoxin mutants in Clostridium botulinum type A
    • Johnson, E. A., Lin, W. J., Zhou, Y. T., and Bradshaw, M., Characterization of neurotoxin mutants in Clostridium botulinum type A, Clin. Infect. Diseases, 25, 2(Suppl.), 5168-5170, 1997.
    • (1997) Clin. Infect. Diseases , vol.25 , Issue.2 SUPPL. , pp. 5168-5170
    • Johnson, E.A.1    Lin, W.J.2    Zhou, Y.T.3    Bradshaw, M.4
  • 51
    • 0030028115 scopus 로고    scopus 로고
    • Molecular cloning of the gene encoding the mosaic neurotoxin, composed of parts of botulinum neurotoxin types C1 and D, and PCR detection of this gene from Clostridium botulinum type C organisms
    • Moriishi, K., Koura, M., Fujii, N., Fujinaga, Y., Inoue, K., Syuto, B., and Oguma K., Molecular cloning of the gene encoding the mosaic neurotoxin, composed of parts of botulinum neurotoxin types C1 and D, and PCR detection of this gene from Clostridium botulinum type C organisms, Appl. Environ. Microbiol., 62, 662-667, 1996.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 662-667
    • Moriishi, K.1    Koura, M.2    Fujii, N.3    Fujinaga, Y.4    Inoue, K.5    Syuto, B.6    Oguma, K.7
  • 52
    • 0029954333 scopus 로고    scopus 로고
    • Mosaic structures of neurotoxins produced from Clostridium botulinum types C and D organisms
    • Moriishi, K., Koura, M., Abe, N., Fujii, N., Fujinaga, Y., Inoue, K., and Ogumad K., Mosaic structures of neurotoxins produced from Clostridium botulinum types C and D organisms, Biochim. Biophys. Acta, 1307, 123-126, 1996.
    • (1996) Biochim. Biophys. Acta , vol.1307 , pp. 123-126
    • Moriishi, K.1    Koura, M.2    Abe, N.3    Fujii, N.4    Fujinaga, Y.5    Inoue, K.6    Ogumad, K.7
  • 54
    • 0029047219 scopus 로고
    • Structural predictions of the channel-forming region of botulinum neurotoxin heavy chain
    • Lebeda, F. J. and Olson, M. A., Structural predictions of the channel-forming region of botulinum neurotoxin heavy chain, Toxicon, 33, 559-567, 1995.
    • (1995) Toxicon , vol.33 , pp. 559-567
    • Lebeda, F.J.1    Olson, M.A.2
  • 55
    • 0029115961 scopus 로고
    • Formation of ion channels in lipid bilayers by a peptide with the predicted transmembrane sequence of botulinum neurotoxin A
    • Oblatt-Montal, M., Yamazaki, M., Nelson, R., and Montal, M., Formation of ion channels in lipid bilayers by a peptide with the predicted transmembrane sequence of botulinum neurotoxin A, Protein Sci., 4, 1490-1497, 1995.
    • (1995) Protein Sci. , vol.4 , pp. 1490-1497
    • Oblatt-Montal, M.1    Yamazaki, M.2    Nelson, R.3    Montal, M.4
  • 56
    • 0026323081 scopus 로고
    • Crystallization and preliminary X-ray analysis of botulinum neurotoxin type A
    • Stevens, R. C., Evenson, M. L., Tepp, W., and Das Gupta, B. R., Crystallization and preliminary X-ray analysis of botulinum neurotoxin type A, J. Mol. Biol., 222, 877-880, 1991.
    • (1991) J. Mol. Biol. , vol.222 , pp. 877-880
    • Stevens, R.C.1    Evenson, M.L.2    Tepp, W.3    Das Gupta, B.R.4
  • 57
    • 0031282024 scopus 로고    scopus 로고
    • Recombinant expression and purification of the botulinum neurotoxin type A translocation domain
    • Lacy, D. B. and Stevens, R. C., Recombinant expression and purification of the botulinum neurotoxin type A translocation domain, Protein Expression Purification, 11, 195-200, 1997.
    • (1997) Protein Expression Purification , vol.11 , pp. 195-200
    • Lacy, D.B.1    Stevens, R.C.2
  • 58
    • 0031259280 scopus 로고    scopus 로고
    • Electron density projection map of the botulinum neurotoxin 900-kilodalton complex by electron crystallography
    • Burkard, F., Chen, F., Kuziemko, G. M., and Stevens R. C., Electron density projection map of the botulinum neurotoxin 900-kilodalton complex by electron crystallography, J. Struct. Biol., 120, 78-84, 1997.
    • (1997) J. Struct. Biol. , vol.120 , pp. 78-84
    • Burkard, F.1    Chen, F.2    Kuziemko, G.M.3    Stevens, R.C.4
  • 59
    • 85008433827 scopus 로고
    • Botulism studies on the manner in which the toxin of Clostridium botulinum acts upon the body. II. The effect on the voluntary nervous system
    • Dickson, E. C. and Shevky, R., Botulism studies on the manner in which the toxin of Clostridium botulinum acts upon the body. II. The effect on the voluntary nervous system, J. Exp. Med., 37, 327-346, 1923.
    • (1923) J. Exp. Med. , vol.37 , pp. 327-346
    • Dickson, E.C.1    Shevky, R.2
  • 60
    • 0000690684 scopus 로고
    • Botulism studies on the manner in which the toxin of Clostndium botulinum acts upon the body. I. The effect upon the autonomic nervous system
    • Dickson, E. C. and Shevky, R., Botulism studies on the manner in which the toxin of Clostndium botulinum acts upon the body. I. The effect upon the autonomic nervous system, J. Exp. Med., 37, 711-731, 1923.
    • (1923) J. Exp. Med. , vol.37 , pp. 711-731
    • Dickson, E.C.1    Shevky, R.2
  • 61
    • 0002301979 scopus 로고
    • The action of botulinum toxin on the neuromuscular junction
    • Burgen, A. S. V., Dickens, F., and Zatman, L. J., The action of botulinum toxin on the neuromuscular junction, J. Physiol. (London), 109, 10-24, 1949.
    • (1949) J. Physiol. (London) , vol.109 , pp. 10-24
    • Burgen, A.S.V.1    Dickens, F.2    Zatman, L.J.3
  • 62
    • 0000131648 scopus 로고
    • The neurotoxins of Clostridium botulinum and Clostridium tetani
    • Wright, G. P., The neurotoxins of Clostridium botulinum and Clostridium tetani, Pharmacol. Rev., 7, 413-465, 1955.
    • (1955) Pharmacol. Rev. , vol.7 , pp. 413-465
    • Wright, G.P.1
  • 63
    • 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, 155-188, 1981.
    • (1981) Pharmacol. Rev. , vol.33 , pp. 155-188
    • Simpson, L.L.1
  • 64
    • 0019191156 scopus 로고
    • The effects of botulinum toxin on the synthesis, storage, and release of acetylcholine
    • Gundersen, C. B., The effects of botulinum toxin on the synthesis, storage, and release of acetylcholine, Prog. Neurobiol., 14, 99-119, 1980.
    • (1980) Prog. Neurobiol. , vol.14 , pp. 99-119
    • Gundersen, C.B.1
  • 65
    • 0020048729 scopus 로고
    • Tetanus toxin action on cultured nerve cells. Does it modify a neurotonal protein?
    • Wendon, L. M. B. and Gill, D. M., Tetanus toxin action on cultured nerve cells. Does it modify a neurotonal protein? Brain Res., 238, 292-297, 1982.
    • (1982) Brain Res. , vol.238 , pp. 292-297
    • Wendon, L.M.B.1    Gill, D.M.2
  • 67
    • 0001481379 scopus 로고
    • Peripheral actions of the botulinum toxins
    • Simpson, L. L., Ed., Academic Press, New York
    • Simpson, L. L., Peripheral actions of the botulinum toxins, in Botulinum Neurotoxin and Tetanus Toxin, Simpson, L. L., Ed., Academic Press, New York, 1989, 153-178.
    • (1989) Botulinum Neurotoxin and Tetanus Toxin , pp. 153-178
    • Simpson, L.L.1
  • 68
    • 0017350046 scopus 로고
    • Response of cultured mammalian cells to the exotoxins of Pseudomonas aeruginosa and Corynebacterium diphtheria. Differential cytotoxicity
    • Middlebrook, J. L. and Dorland, R. B., Response of cultured mammalian cells to the exotoxins of Pseudomonas aeruginosa and Corynebacterium diphtheria. Differential cytotoxicity, Can. J. Microbiol., 23, 183-189, 1977.
    • (1977) Can. J. Microbiol. , vol.23 , pp. 183-189
    • Middlebrook, J.L.1    Dorland, R.B.2
  • 69
    • 0018367313 scopus 로고
    • Protection of mammalian cells from diphtheria toxin by exogenous nucleotides
    • Middlebrook, J. L. and Dorland, R. B., Protection of mammalian cells from diphtheria toxin by exogenous nucleotides, Can. J. Microbiol., 25, 285-290, 1979.
    • (1979) Can. J. Microbiol. , vol.25 , pp. 285-290
    • Middlebrook, J.L.1    Dorland, R.B.2
  • 70
    • 0018068693 scopus 로고
    • Association of diphtheria toxin with Vero cells: Demonstration of a receptor
    • Middlebrook, J. L., Dorland, R. B., and Leppla, S. H., Association of diphtheria toxin with Vero cells: Demonstration of a receptor, J. Biol Chem., 253, 7325-7330, 1978.
    • (1978) J. Biol Chem. , vol.253 , pp. 7325-7330
    • Middlebrook, J.L.1    Dorland, R.B.2    Leppla, S.H.3
  • 71
    • 0018773124 scopus 로고
    • Effects of lectins on the interaction of diphtheria toxin with mammalian cells
    • Middlebrook, J. L., Dorland, R. B., and Leppla, S. H., Effects of lectins on the interaction of diphtheria toxin with mammalian cells, Exp. Cell Res., 121, 95-101, 1979.
    • (1979) Exp. Cell Res. , vol.121 , pp. 95-101
    • Middlebrook, J.L.1    Dorland, R.B.2    Leppla, S.H.3
  • 72
    • 0019814639 scopus 로고
    • Effect of energy inhibitors on cell surface diphtheria toxin receptor numbers
    • Middlebrook, J. L., Effect of energy inhibitors on cell surface diphtheria toxin receptor numbers, J. Biol. Chem., 256, 7898-7904, 1981.
    • (1981) J. Biol. Chem. , vol.256 , pp. 7898-7904
    • Middlebrook, J.L.1
  • 73
    • 0015126099 scopus 로고
    • The binding of botulinum toxin to membrane lipids, sphingolipids, steroids and fatty acids
    • Simpson, L. L. and Rapport, M. M., The binding of botulinum toxin to membrane lipids, sphingolipids, steroids and fatty acids, J. Neurochem., 18, 1751-1759, 1971.
    • (1971) J. Neurochem. , vol.18 , pp. 1751-1759
    • Simpson, L.L.1    Rapport, M.M.2
  • 74
    • 0018867612 scopus 로고
    • Interaction between Clostridium botulinum neurotoxin and gangliosides
    • Kitamura, M., Iwamori, M., and Nagai, Y., Interaction between Clostridium botulinum neurotoxin and gangliosides, Biochim. Biophys. Acta, 628, 328-335, 1980.
    • (1980) Biochim. Biophys. Acta , vol.628 , pp. 328-335
    • Kitamura, M.1    Iwamori, M.2    Nagai, Y.3
  • 75
    • 0021324093 scopus 로고
    • Inhibitory effect of ganglioside GT1B on the activities of Clostridium botulinum toxins
    • Kozaki, S., Sakaguchi, G., Nishimura, M., Iwamori, M., and Nagai, Y., Inhibitory effect of ganglioside GT1B on the activities of Clostridium botulinum toxins, FEMS Microbiol. Lett., 21, 219-223, 1984.
    • (1984) FEMS Microbiol. Lett. , vol.21 , pp. 219-223
    • Kozaki, S.1    Sakaguchi, G.2    Nishimura, M.3    Iwamori, M.4    Nagai, Y.5
  • 76
    • 0022648666 scopus 로고
    • Binding of Clostridium botulinum neurotoxin to gangliosides
    • Ochanda, J. O., Syuto, B., Ohishi, I., Naiki, M., and Kubo, S., Binding of Clostridium botulinum neurotoxin to gangliosides, J. Biochem., 100, 27-33, 1986.
    • (1986) J. Biochem. , vol.100 , pp. 27-33
    • Ochanda, J.O.1    Syuto, B.2    Ohishi, I.3    Naiki, M.4    Kubo, S.5
  • 77
    • 0023521287 scopus 로고
    • Antigenic structure of Clostridium botulinum type B neurotoxin and its interaction with gangliosides, cerebrosides, and free fatty acids
    • Kozaki, S., Ogasawara, J., Shimote, Y., Kamata, Y., and Sakaguchi, G., Antigenic structure of Clostridium botulinum type B neurotoxin and its interaction with gangliosides, cerebrosides, and free fatty acids, Infect. Immun., 55, 3051-3056, 1987.
    • (1987) Infect. Immun. , vol.55 , pp. 3051-3056
    • Kozaki, S.1    Ogasawara, J.2    Shimote, Y.3    Kamata, Y.4    Sakaguchi, G.5
  • 78
    • 0017166250 scopus 로고
    • Binding of botulinum neurotoxin to the synaptosome fraction of rat brain
    • Kitamura, M., Binding of botulinum neurotoxin to the synaptosome fraction of rat brain, Naunyn-Schmiedeberg's Arch. Pharmacol., 295, 171-175, 1976.
    • (1976) Naunyn-Schmiedeberg's Arch. Pharmacol. , vol.295 , pp. 171-175
    • Kitamura, M.1
  • 79
    • 0018635117 scopus 로고
    • Different neurotoxin serotypes do not share a common receptor
    • Kozaki, S., Different neurotoxin serotypes do not share a common receptor, Naunyn-Schmiedeberg's Arch. Pharmacol., 308, 67-70, 1979.
    • (1979) Naunyn-Schmiedeberg's Arch. Pharmacol. , vol.308 , pp. 67-70
    • Kozaki, S.1
  • 80
    • 0020805784 scopus 로고
    • Binding of Clostridium botulinum type C neurotoxin to rat brain synaptosomes
    • Agui, T., Syuto, B., Oguma, K., Iida, H., and Kubo, S., Binding of Clostridium botulinum type C neurotoxin to rat brain synaptosomes, J. Biochem., 94, 521-527, 1983.
    • (1983) J. Biochem. , vol.94 , pp. 521-527
    • Agui, T.1    Syuto, B.2    Oguma, K.3    Iida, H.4    Kubo, S.5
  • 81
    • 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., and Kozaki, S., Identification of protein receptor for Clostridium botulinum type B neurotoxin in rat brain synaptosomes, J. Biol. Chem., 269, 10498-503, 1994.
    • (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
  • 82
    • 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., Binding to mouse brain synaptosomes of Clostridium botulinum type E derivative toxin before and after tryptic activation, Toxicon, 20, 841-846, 1982.
    • (1982) Toxicon , vol.20 , pp. 841-846
    • Kozaki, S.1    Sakaguchi, G.2
  • 83
    • 0017659283 scopus 로고
    • Isolation of pure cholinergic nerve endings from Torpedo electric organ. Evaluation of their metabolic properties
    • Morel, N., Israel, M., Manaranche, R., and Mastour-Franchon, P., Isolation of pure cholinergic nerve endings from Torpedo electric organ. Evaluation of their metabolic properties, J. Cell Biol., 75, 43-55, 1977.
    • (1977) J. Cell Biol. , vol.75 , pp. 43-55
    • Morel, N.1    Israel, M.2    Manaranche, R.3    Mastour-Franchon, P.4
  • 84
    • 0018395948 scopus 로고
    • Binding of Clostridium botulinum neurotoxin to the presynaptic membrane in the central nervous system
    • Hirokawa, N. and Kitamura, M., Binding of Clostridium botulinum neurotoxin to the presynaptic membrane in the central nervous system, J. Cell Biol., 81, 43-49, 1979.
    • (1979) J. Cell Biol. , vol.81 , pp. 43-49
    • Hirokawa, N.1    Kitamura, M.2
  • 86
    • 0022556315 scopus 로고
    • 125I-labeled botulinum neurotoxins with nerve terminals. II. Autoradiographic evidence for its uptake into motor nerves by acceptor-mediated endocytosis
    • 125I-labeled botulinum neurotoxins with nerve terminals. II. Autoradiographic evidence for its uptake into motor nerves by acceptor-mediated endocytosis, J. Cell Biol., 103, 535-544, 1986.
    • (1986) J. Cell Biol. , vol.103 , pp. 535-544
    • Black, J.D.1    Dolly, J.O.2
  • 87
    • 0024316287 scopus 로고
    • Immunological characterization of papain-induced fragments of Clostridium botulinum type A neurotoxin and interaction of the fragments with brain synaptosomes
    • Kozaki, S., Akira, M., Yoichi, K., Jun, O., and Genji, S., Immunological characterization of papain-induced fragments of Clostridium botulinum type A neurotoxin and interaction of the fragments with brain synaptosomes, Infect. Immun., 57, 2634-2639, 1989.
    • (1989) Infect. Immun. , vol.57 , pp. 2634-2639
    • Kozaki, S.1    Akira, M.2    Yoichi, K.3    Jun, O.4    Genji, S.5
  • 88
    • 0029950636 scopus 로고    scopus 로고
    • Ganglioside-induced adherence of botulinum and tetanus neurotoxins to adducin
    • Schengrund, C. L., DasGupta, B. R., Hughes, C. A., and Ringler, N. J., Ganglioside-induced adherence of botulinum and tetanus neurotoxins to adducin, J. Neurochem., 66, 2556-2561, 1996.
    • (1996) J. Neurochem. , vol.66 , pp. 2556-2561
    • Schengrund, C.L.1    DasGupta, B.R.2    Hughes, C.A.3    Ringler, N.J.4
  • 89
    • 0030742486 scopus 로고    scopus 로고
    • Interaction between botulinum neurotoxin type A and ganglioside: Ganglioside inactivates the neurotoxin and quenches its tryptophan fluorescence
    • Kamata, Y., Yoshimoto, M., and Kozaki, S., Interaction between botulinum neurotoxin type A and ganglioside: ganglioside inactivates the neurotoxin and quenches its tryptophan fluorescence, Toxicon, 35, 1337-1340, 1997.
    • (1997) Toxicon , vol.35 , pp. 1337-1340
    • Kamata, Y.1    Yoshimoto, M.2    Kozaki, S.3
  • 90
    • 0029987985 scopus 로고    scopus 로고
    • Synaptotagmin II immunoreactivity in normal and botulinum type-A treated mouse motor nerve terminals
    • Juzans, P., Molgo, J., Faille, L., and Angaut-Petit, D., Synaptotagmin II immunoreactivity in normal and botulinum type-A treated mouse motor nerve terminals, Pflugers Archiv-Eur. J. Physiol., 431(Suppl 2), R283-284, 1996.
    • (1996) Pflugers Archiv-Eur. J. Physiol. , vol.431 , Issue.SUPPL. 2
    • Juzans, P.1    Molgo, J.2    Faille, L.3    Angaut-Petit, D.4
  • 91
    • 0030064241 scopus 로고    scopus 로고
    • The high-affinity binding of Clostridium botulinum type B neurotoxin to synaptotagmin II associated with gangliosides GT1b/GD1a
    • Nishiki, T., Tokuyama, Y., Kamata, Y., Nemoto, Y., Yoshida, A., Sato, K., Sekiguchi, M., Takahashi M., and Kozaki, S., The high-affinity binding of Clostridium botulinum type B neurotoxin to synaptotagmin II associated with gangliosides GT1b/ GD1a, FEBS Lett., 378, 253-257, 1996.
    • (1996) FEBS Lett. , vol.378 , pp. 253-257
    • Nishiki, T.1    Tokuyama, Y.2    Kamata, Y.3    Nemoto, Y.4    Yoshida, A.5    Sato, K.6    Sekiguchi, M.7    Takahashi, M.8    Kozaki, S.9
  • 92
    • 0029912989 scopus 로고    scopus 로고
    • Binding of botulinum type B neurotoxin to Chinese hamster ovary cells transfected with rat synaptotagmin II cDNA
    • Nishiki, T., Tokuyama, Y., Kamata, Y., Nemoto, Y., Yoshida, A., Sekiguchi M., Takahashi M., and Kozaki, S., Binding of botulinum type B neurotoxin to Chinese hamster ovary cells transfected with rat synaptotagmin II cDNA, Neurosci. Lett., 208, 105-8, 1996.
    • (1996) Neurosci. Lett. , vol.208 , pp. 105-108
    • Nishiki, T.1    Tokuyama, Y.2    Kamata, Y.3    Nemoto, Y.4    Yoshida, A.5    Sekiguchi, M.6    Takahashi, M.7    Kozaki, S.8
  • 93
    • 0022555430 scopus 로고
    • Molecular pharmacology of botulinum toxin and tetanous toxin
    • Simpson, L. L., Molecular pharmacology of botulinum toxin and tetanous toxin, Ann. Rev. Pharmacol. Toxicol., 26, 427-453, 1986.
    • (1986) Ann. Rev. Pharmacol. Toxicol. , vol.26 , pp. 427-453
    • Simpson, L.L.1
  • 94
    • 0023664001 scopus 로고
    • Role of the heavy and light chains of botulinum neurotoxin in neuromuscular paralysis
    • Bandyopadhyay, S., Clark, A. W., Das Gupta, B., and Sathyamoorthy, V., Role of the heavy and light chains of botulinum neurotoxin in neuromuscular paralysis, J. Biol. Chem., 262, 2660-2663, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2660-2663
    • Bandyopadhyay, S.1    Clark, A.W.2    Das Gupta, B.3    Sathyamoorthy, V.4
  • 95
    • 0016298703 scopus 로고
    • Mild trypsin action of type E toxicity increased 90-fold
    • Kozaki, S., Sakaguchi, S., and Sakaguchi, G., Mild trypsin action of type E toxicity increased 90-fold, Infect. Immun., 10, 750-756, 1974.
    • (1974) Infect. Immun. , vol.10 , pp. 750-756
    • Kozaki, S.1    Sakaguchi, S.2    Sakaguchi, G.3
  • 96
    • 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., 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., 15, 75-82, 1985.
    • (1985) Eur. J. Biochem. , vol.15 , pp. 75-82
    • Shone, C.C.1    Hambleton, P.2    Melling, J.3
  • 97
    • 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., and Montecucco, C., Botulinum neurotoxin type C cleaves a single Lys-Ala bond within the carboxyl-terminal region of syntaxins, J. Biol. Chem., 270, 10566-10570, 1995.
    • (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
  • 99
    • 0029688379 scopus 로고    scopus 로고
    • The mechanism of action of tetanus and botulinum neurotoxins
    • Montecucco, C., Schiavo, G., and Rossetto, O., The mechanism of action of tetanus and botulinum neurotoxins, Arch. Toxicol., Supplement, 18, 342-354, 1996.
    • (1996) Arch. Toxicol., Supplement , vol.18 , pp. 342-354
    • Montecucco, C.1    Schiavo, G.2    Rossetto, O.3
  • 100
    • 0028829335 scopus 로고
    • Bacterial neurotoxins-a thousand years later
    • Linial M., Bacterial neurotoxins-a thousand years later, Israel J. Med. Sci., 31, 591-595, 1995.
    • (1995) Israel J. Med. Sci. , vol.31 , pp. 591-595
    • Linial, M.1
  • 101
    • 0029074299 scopus 로고
    • Molecular aspects of tetanus and botulinum neurotoxin poisoning
    • Ahnert-Hilger, G. and Bigalke H., Molecular aspects of tetanus and botulinum neurotoxin poisoning, Prog. Neurobiol., 46, 83-96, 1995.
    • (1995) Prog. Neurobiol. , vol.46 , pp. 83-96
    • Ahnert-Hilger, G.1    Bigalke, H.2
  • 102
    • 0028903373 scopus 로고
    • Structure and function of Clostridium botulinum toxins
    • Oguma, K., Fujinaga, Y., and Inoue, K., Structure and function of Clostridium botulinum toxins, Microbiol. Immunol., 39, 161-168, 1995.
    • (1995) Microbiol. Immunol. , vol.39 , pp. 161-168
    • Oguma, K.1    Fujinaga, Y.2    Inoue, K.3
  • 103
    • 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., Role of zinc in the structure and toxic activity of botulinum neurotoxin, Biochemistry, 37, 5267-5278, 1998.
    • (1998) Biochemistry , vol.37 , pp. 5267-5278
    • Fu, F.N.1    Lomneth, R.B.2    Cai, S.3    Singh, B.R.4
  • 104
    • 0030607217 scopus 로고    scopus 로고
    • Adrenal chromaffin cells contain functionally different SNAP-25 monomers and SNAP-25/syntaxin heterodimers
    • Hohne-Zell, B. and Gratzl, M., Adrenal chromaffin cells contain functionally different SNAP-25 monomers and SNAP-25/syntaxin heterodimers, FEBS Lett., 394, 109-116, 1996.
    • (1996) FEBS Lett. , vol.394 , pp. 109-116
    • Hohne-Zell, B.1    Gratzl, M.2
  • 106
    • 0030464997 scopus 로고    scopus 로고
    • Insulin-stimulated translocation of GLUT4 glucose transporters requires SNARE-complex proteins
    • Cheatham, B., Volchuk, A., Kahn, C. R., Wang, L., Rhodes, C. J., and Klip, A., Insulin-stimulated translocation of GLUT4 glucose transporters requires SNARE-complex proteins, Proc. Natl. Acad. Sci. U.S.A., 93, 15169-15173, 1996.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 15169-15173
    • Cheatham, B.1    Volchuk, A.2    Kahn, C.R.3    Wang, L.4    Rhodes, C.J.5    Klip, A.6
  • 107
    • 0031010616 scopus 로고    scopus 로고
    • Botulinum neurotoxin B inhibits insulin-stimulated glucose uptake into 3T3L1 adipocytes and cleaves cellubrevin unlike BoNT A which failed to proteolyze the SNAP-23 present
    • Chen, F., Foran, P., Shone, C. C., Foster, K. A., Melling, J., and Dolly, J. O., Botulinum neurotoxin B inhibits insulin-stimulated glucose uptake into 3T3L1 adipocytes and cleaves cellubrevin unlike BoNT A which failed to proteolyze the SNAP-23 present, Biochemistry, 36, 5719-5728, 1997.
    • (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
  • 108
    • 0030917678 scopus 로고    scopus 로고
    • Functional studies in 3T3L1 cells support a role for SNARE proteins in insulin stimulation of GLUT4 translocation
    • Macaulay, S. L., Hewish, D. R., Gough, K. H., Stoichevska, V., MacPherson, S. F., Jagadish, M., and Ward, C. W., Functional studies in 3T3L1 cells support a role for SNARE proteins in insulin stimulation of GLUT4 translocation, Biochem. J., 324, 217-224, 1997.
    • (1997) Biochem. J. , vol.324 , pp. 217-224
    • Macaulay, S.L.1    Hewish, D.R.2    Gough, K.H.3    Stoichevska, V.4    MacPherson, S.F.5    Jagadish, M.6    Ward, C.W.7
  • 109
    • 0028815453 scopus 로고
    • The t-SNAREs syntaxin 1 and SNAP-25 are present on organelles that participate in synaptic vesicle recycling
    • Walch-Solimena, C., Blasi, J., Edelmann, L., Chapman, E. R., von Mollard, G. F., and Jahn, R., The t-SNAREs syntaxin 1 and SNAP-25 are present on organelles that participate in synaptic vesicle recycling, J. Cell. Biol., 128, 637-645, 1995.
    • (1995) J. Cell. Biol. , vol.128 , pp. 637-645
    • Walch-Solimena, C.1    Blasi, J.2    Edelmann, L.3    Chapman, E.R.4    Von Mollard, G.F.5    Jahn, R.6
  • 110
    • 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., 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.
    • (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
  • 111
    • 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., and Montecucco, C., The interaction of synaptic vesicle-associated membrane protein/synaptobrevin with botulinum neurotoxins D and F, FEBS Lett., 409, 339-342, 1997.
    • (1997) FEBS Lett. , vol.409 , pp. 339-342
    • Pellizzari, R.1    Mason, S.2    Shone, C.C.3    Montecucco, C.4
  • 112
    • 0029560840 scopus 로고
    • Proteolysis of synthetic peptides by type A botulinum neurotoxin
    • Schmidt, J. J. and Bostian, K. A., Proteolysis of synthetic peptides by type A botulinum neurotoxin, J. Prot. Chem., 14, 703-708, 1995.
    • (1995) J. Prot. Chem. , vol.14 , pp. 703-708
    • Schmidt, J.J.1    Bostian, K.A.2
  • 113
    • 0029164314 scopus 로고
    • Poisoning by botulinum neurotoxin A does not inhibit formation or disassembly of the synaptosomal fusion complex
    • Otto, H., Hanson, P. I., Chapman, E. R., Blasi, J., and Jahn, R., Poisoning by botulinum neurotoxin A does not inhibit formation or disassembly of the synaptosomal fusion complex, Biochem. Biophys. Res. Commun., 212, 945-952, 1995.
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , pp. 945-952
    • Otto, H.1    Hanson, P.I.2    Chapman, E.R.3    Blasi, J.4    Jahn, R.5
  • 115
    • 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., 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.
    • (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
  • 116
    • 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
    • Wictome, M., Rossetto, O., Montecucco, C., and 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., 386, 133-136, 1996.
    • (1996) FEBS Lett. , vol.386 , pp. 133-136
    • Wictome, M.1    Rossetto, O.2    Montecucco, C.3    Shone, C.C.4
  • 117
    • 0031005892 scopus 로고    scopus 로고
    • Cleavage of the synaptobrevin/ vesicle-associated membrane protein (VAMP) of the mouse brain by the recombinant light chain of Clostridium botulinum type B toxin
    • Rhee, S. D., Jung, H. H., Yang, G. H., Moon, Y. S., and Yang, K. H., Cleavage of the synaptobrevin/ vesicle-associated membrane protein (VAMP) of the mouse brain by the recombinant light chain of Clostridium botulinum type B toxin, FEMS Microbiol. Lett., 150, 203-208, 1997.
    • (1997) FEMS Microbiol. Lett. , vol.150 , pp. 203-208
    • Rhee, S.D.1    Jung, H.H.2    Yang, G.H.3    Moon, Y.S.4    Yang, K.H.5
  • 118
    • 0029057212 scopus 로고
    • Blockade by botulinum neurotoxin B of catecholamine release from adrenochromaffin cells correlates with its cleavage of synaptobrevin and a homologue present on the granules
    • Foran, P., Lawrence, G., and Dolly, J. O., Blockade by botulinum neurotoxin B of catecholamine release from adrenochromaffin cells correlates with its cleavage of synaptobrevin and a homologue present on the granules, Biochemistry, 34, 5494-5503, 1995.
    • (1995) Biochemistry , vol.34 , pp. 5494-5503
    • Foran, P.1    Lawrence, G.2    Dolly, J.O.3
  • 119
    • 0031029132 scopus 로고    scopus 로고
    • Cleavage of syntaxin prevents G-protein regulation of presynaptic calcium channels
    • Stanley, E. F. and Mirotznik, R. R., Cleavage of syntaxin prevents G-protein regulation of presynaptic calcium channels, Nature, 385, 340-343, 1997.
    • (1997) Nature , vol.385 , pp. 340-343
    • Stanley, E.F.1    Mirotznik, R.R.2
  • 120
    • 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., and Sollner, 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. U.S.A., 94, 769-772; 997-1001, 1997.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 769-772
    • Schiavo, G.1    Stenbeck, G.2    Rothman, J.E.3    Sollner, T.H.4
  • 121
    • 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, 7190-7202, 1997.
    • (1997) J. Neurosci. , vol.17 , pp. 7190-7202
    • Capogna, M.1    McKinney, R.A.2    O'Connor, V.3    Gahwiler, B.H.4    Thompson, S.M.5
  • 122
    • 0030782182 scopus 로고    scopus 로고
    • Recombinant SNAP-25 is an effective substrate for Clostridium botulinum type A toxin endopeptidase activity in vitro
    • Ekong, T. A., Feavers, I. M., and Sesardic, D., Recombinant SNAP-25 is an effective substrate for Clostridium botulinum type A toxin endopeptidase activity in vitro, Microbiology, 143, 3337-347, 1997.
    • (1997) Microbiology , vol.143 , pp. 3337-3347
    • Ekong, T.A.1    Feavers, I.M.2    Sesardic, D.3
  • 125
    • 0029984090 scopus 로고    scopus 로고
    • Botulinum neurotoxin light chains inhibit both Ca(2+)-induced and GTP analogue-induced catecholamine release from permeabilised adrenal chromaffin cells
    • Glenn, D. E. and Burgoyne, R. D., Botulinum neurotoxin light chains inhibit both Ca(2+)-induced and GTP analogue-induced catecholamine release from permeabilised adrenal chromaffin cells, FEBS Lett., 386, 137-140, 1996.
    • (1996) FEBS Lett. , vol.386 , pp. 137-140
    • Glenn, D.E.1    Burgoyne, R.D.2
  • 126
    • 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., and 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, 3061-3067, 1997.
    • (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
  • 127
    • 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., and Montal, M., A peptide that mimics the C-terminal sequence of SNAP-25 inhibits secretory vesicle docking in chromaffin cells, J. Biol. Chem., 211, 2634-2639, 1997.
    • (1997) J. Biol. Chem. , vol.211 , 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
  • 128
    • 0029898850 scopus 로고    scopus 로고
    • Phosphorylation of 25-kDa synaptosome-associated protein. Possible involvement in protein kinase C-mediated regulation of neurotransmitter release
    • Shimazaki, Y., Nishiki, T., Omori, A., Sekiguchi, M., Kamata, Y., Kozaki, S., and Takahashi, M., Phosphorylation of 25-kDa synaptosome-associated protein. Possible involvement in protein kinase C-mediated regulation of neurotransmitter release, J. Biol. Chem., 271, 14548-14553, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14548-14553
    • Shimazaki, Y.1    Nishiki, T.2    Omori, A.3    Sekiguchi, M.4    Kamata, Y.5    Kozaki, S.6    Takahashi, M.7
  • 129
    • 0018401007 scopus 로고
    • Mode of action of Botulinum toxin and the effect of drug antagonist
    • Thesleff, S. and Lundh, H., Mode of action of Botulinum toxin and the effect of drug antagonist, Adv. Cytopharmacol., 3, 35-43, 1979.
    • (1979) Adv. Cytopharmacol. , vol.3 , pp. 35-43
    • Thesleff, S.1    Lundh, H.2
  • 130
    • 0344678957 scopus 로고
    • Pharmacologic antagonism of clostridial toxins
    • Simpson, L.L., Ed., Academic Press, New York
    • Thesleff, S., Pharmacologic antagonism of clostridial toxins, in Botulinum Neurotoxin and Tetanus Toxin, Simpson, L.L., Ed., Academic Press, New York, 1989, 281-298.
    • (1989) Botulinum Neurotoxin and Tetanus Toxin , pp. 281-298
    • Thesleff, S.1
  • 131
    • 0026032612 scopus 로고
    • Microtubule-dissociating drugs and A23187 reveal differences in the inhibition of synaptosomal transmitter release by botulinum neurotoxins types A and B
    • Ashton, A. C. and Dolly, J. O., Microtubule-dissociating drugs and A23187 reveal differences in the inhibition of synaptosomal transmitter release by botulinum neurotoxins types A and B, J. Neurochem., 56, 827-835, 1991.
    • (1991) J. Neurochem. , vol.56 , pp. 827-835
    • Ashton, A.C.1    Dolly, J.O.2
  • 132
    • 0028998816 scopus 로고
    • Antagonism of botulinum toxin-induced muscle weakness by 3,4-diaminopyridine in rat phrenic nerve-hemidiaphragm preparations
    • Adler, M., Scovill, J., Parker, G., Lebeda, F. J., Piotrowski, J., and Deshpande, S. S., Antagonism of botulinum toxin-induced muscle weakness by 3,4-diaminopyridine in rat phrenic nerve-hemidiaphragm preparations, Toxicon, 33, 527-537, 1995.
    • (1995) Toxicon , vol.33 , pp. 527-537
    • Adler, M.1    Scovill, J.2    Parker, G.3    Lebeda, F.J.4    Piotrowski, J.5    Deshpande, S.S.6
  • 133
    • 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., and Parker, G. W., Effect of 3,4-diaminopyridine on rat extensor digitorum longus muscle paralyzed by local injection of botulinum neurotoxin, Toxicon, 34, 237-249, 1996.
    • (1996) Toxicon , vol.34 , pp. 237-249
    • Adler, M.1    Macdonald, D.A.2    Sellin, L.C.3    Parker, G.W.4
  • 134
    • 0018954098 scopus 로고
    • Inhibition of diphtheria toxin degradation and cytotoxic action by chloroquine
    • Leppla, S., Dorland, R. B., and Middlebrook, J. L., Inhibition of diphtheria toxin degradation and cytotoxic action by chloroquine, J. Biol. Chem., 255, 2247-2250, 1980.
    • (1980) J. Biol. Chem. , vol.255 , pp. 2247-2250
    • Leppla, S.1    Dorland, R.B.2    Middlebrook, J.L.3
  • 135
    • 0019824268 scopus 로고
    • Effect of ammonium chloride on receptor-mediated uptake of diphtheria toxin by vero cells
    • Dorland, R. B., Middlebrook, J. L., and Leppla, S. H., Effect of ammonium chloride on receptor-mediated uptake of diphtheria toxin by vero cells, Exp. Cell Res., 134, 319-327, 1981.
    • (1981) Exp. Cell Res. , vol.134 , pp. 319-327
    • Dorland, R.B.1    Middlebrook, J.L.2    Leppla, S.H.3
  • 136
    • 0018967650 scopus 로고
    • Receptor mediated internalization of pseudomonas toxin by mouse fibroblasts
    • Fitzgerald, D., Morris, R. E., and Saelinger, C. B., Receptor mediated internalization of pseudomonas toxin by mouse fibroblasts, Cell, 21, 867-873, 1980.
    • (1980) Cell , vol.21 , pp. 867-873
    • Fitzgerald, D.1    Morris, R.E.2    Saelinger, C.B.3
  • 137
    • 0031106637 scopus 로고
    • Efficacy of certain quinolines as pharmacological antagonists in botulinum neurotoxin poisoning
    • Deshpande, S. S., Sheridan, R. E., and Adler, M., Efficacy of certain quinolines as pharmacological antagonists in botulinum neurotoxin poisoning, Toxicon, 1997 35, 433-445, 1980.
    • (1980) Toxicon , vol.35 , pp. 433-445
    • Deshpande, S.S.1    Sheridan, R.E.2    Adler, M.3
  • 138
    • 0030723415 scopus 로고    scopus 로고
    • Structural features of aminoquinolines necessary for antagonist activity against botulinum neurotoxin
    • Sheridan, R. E., Deshpande, S. S., Nicholson, J. D., and Adler, M., Structural features of aminoquinolines necessary for antagonist activity against botulinum neurotoxin, Toxicon, 35, 1439-1451, 1997.
    • (1997) Toxicon , vol.35 , pp. 1439-1451
    • Sheridan, R.E.1    Deshpande, S.S.2    Nicholson, J.D.3    Adler, M.4
  • 139
    • 0025943451 scopus 로고
    • Lectins from triticum vulgaris and limax flavus are universal antagonists of botulinum neurotoxin and tetanus toxin
    • Bakry, N., Yoichi, K., and Simpson, L., Lectins from triticum vulgaris and limax flavus are universal antagonists of botulinum neurotoxin and tetanus toxin, J. Phamacol. Exp. Therap., 258, 830-836, 1991.
    • (1991) J. Phamacol. Exp. Therap. , vol.258 , pp. 830-836
    • Bakry, N.1    Yoichi, K.2    Simpson, L.3
  • 140
    • 0029074183 scopus 로고
    • A study of zinc-dependent metalloendopeptidase inhibitors as pharmacological antagonists in botulinum neurotoxin poisoning
    • Deshpande, S. S., Sheridan, R. E., and Adler, M., A study of zinc-dependent metalloendopeptidase inhibitors as pharmacological antagonists in botulinum neurotoxin poisoning, Toxicon, 33, 551-557, 1995.
    • (1995) Toxicon , vol.33 , pp. 551-557
    • Deshpande, S.S.1    Sheridan, R.E.2    Adler, M.3
  • 141
    • 0030832320 scopus 로고    scopus 로고
    • Protection by the heavy metal chelator N,N,N′,N′-tetrakis(2-pyridylmethyl)ethylenediamine (TPEN) against the lethal action of botulinum neurotoxin A and B
    • Adler, M., Dinterman, R. E., and Wannemacher, R. W., Protection by the heavy metal chelator N,N,N′,N′-tetrakis(2-pyridylmethyl)ethylenediamine (TPEN) against the lethal action of botulinum neurotoxin A and B, Toxicon, 35, 1089-1100, 1997.
    • (1997) Toxicon , vol.35 , pp. 1089-1100
    • Adler, M.1    Dinterman, R.E.2    Wannemacher, R.W.3
  • 143
    • 0029977787 scopus 로고    scopus 로고
    • Botulinum toxin therapy, immunologic resistance, and problems with available materials
    • Borodic, G., Johnson, E., Goodnough, M., and Schantz, E., Botulinum toxin therapy, immunologic resistance, and problems with available materials, Neurology, 46, 26-29, 1996.
    • (1996) Neurology , vol.46 , pp. 26-29
    • Borodic, G.1    Johnson, E.2    Goodnough, M.3    Schantz, E.4
  • 144
    • 0030077479 scopus 로고    scopus 로고
    • Historical note on the therapeutic use of botulinum toxin in neurological disorders
    • Erbguth, F. J., Historical note on the therapeutic use of botulinum toxin in neurological disorders, J. Neurol., Neurosurg. Psych., 60, 151, 1996.
    • (1996) J. Neurol., Neurosurg. Psych. , vol.60 , pp. 151
    • Erbguth, F.J.1
  • 145
    • 0030248299 scopus 로고    scopus 로고
    • Mechanism of action, clinical indication, and results of treatment of botulinum toxin
    • Lagueny, A. and Burbaud, P., Mechanism of action, clinical indication, and results of treatment of botulinum toxin, Neurophysiologie Clinique, 26, 216-226, 1996.
    • (1996) Neurophysiologie Clinique , vol.26 , pp. 216-226
    • Lagueny, A.1    Burbaud, P.2
  • 146
    • 0030256824 scopus 로고    scopus 로고
    • Botulinum neurotoxins: Mechanism of action and therapeutic applications
    • Montecucco, C., Schiavo, G., Tugnoli, V., and de Grandis, D., Botulinum neurotoxins: mechanism of action and therapeutic applications, Mol. Med. Today, 2, 418-424, 1996.
    • (1996) Mol. Med. Today , vol.2 , pp. 418-424
    • Montecucco, C.1    Schiavo, G.2    Tugnoli, V.3    De Grandis, D.4
  • 147
    • 0029956621 scopus 로고    scopus 로고
    • Botulinum toxin as a therapeutic agent
    • Tsui, J. K., Botulinum toxin as a therapeutic agent, Pharmacol. Therapeutics, 72, 13-24, 1996.
    • (1996) Pharmacol. Therapeutics , vol.72 , pp. 13-24
    • Tsui, J.K.1
  • 148
    • 0031086319 scopus 로고    scopus 로고
    • Botulinum toxin: The story of its development for the treatment of human disease
    • Schantz, E. J. and Johnson, E. A., Botulinum toxin: the story of its development for the treatment of human disease, Perspectives Biol. Med., 40, 317-327, 1997.
    • (1997) Perspectives Biol. Med. , vol.40 , pp. 317-327
    • Schantz, E.J.1    Johnson, E.A.2
  • 149
    • 0031037256 scopus 로고    scopus 로고
    • Therapeutic uses of botulinum toxin
    • Wheeler, A. H., Therapeutic uses of botulinum toxin, Am. Family Physician, 55, 541-545, 548, 1997.
    • (1997) Am. Family Physician , vol.55 , pp. 541-545
    • Wheeler, A.H.1
  • 150
    • 0030923446 scopus 로고    scopus 로고
    • Botulinum toxin: From poison to remedy
    • Kessler, K. R. and Benecke, R., Botulinum toxin: from poison to remedy, Neurotoxicology, 18, 761-770, 1997.
    • (1997) Neurotoxicology , vol.18 , pp. 761-770
    • Kessler, K.R.1    Benecke, R.2
  • 151
    • 0030694576 scopus 로고    scopus 로고
    • Pharmacologic characterization of botulinum toxin for basic science and medicine
    • Pearce, L. B., First, E. R., MacCallum, R. D., and Gupta, A., Pharmacologic characterization of botulinum toxin for basic science and medicine, Toxicon, 35, 1373-1412, 1997.
    • (1997) Toxicon , vol.35 , pp. 1373-1412
    • Pearce, L.B.1    First, E.R.2    MacCallum, R.D.3    Gupta, A.4
  • 154
    • 0030842423 scopus 로고    scopus 로고
    • Human response to botulinum toxin injection: Type B compared with type A
    • Sloop, R. R., Cole, B. A., and Escutin, R. O., Human response to botulinum toxin injection: Type B compared with type A, Neurology, 49, 189-194, 1997.
    • (1997) Neurology , vol.49 , pp. 189-194
    • Sloop, R.R.1    Cole, B.A.2    Escutin, R.O.3
  • 155
    • 0030901704 scopus 로고    scopus 로고
    • Botulinum neurotoxin serotype C: A novel effective botulinum toxin therapy in human
    • Eleopra, R., Tugnoli, V., Rossetto, O., Montecucco, C., and De Grandis, D., Botulinum neurotoxin serotype C: a novel effective botulinum toxin therapy in human, Neurosci. Lett, 224, 91-94, 1997.
    • (1997) Neurosci. Lett. , vol.224 , pp. 91-94
    • Eleopra, R.1    Tugnoli, V.2    Rossetto, O.3    Montecucco, C.4    De Grandis, D.5
  • 156
    • 6844266275 scopus 로고    scopus 로고
    • What is the optimal dose of botulinum toxin A in the treatment of cervical dystonia? Results of a double blind, placebo controlled, dose ranging study using Dysport
    • German Dystonia Study Group
    • Poewe, W., Deuschl, G., Nebe, A., Feifel, E., Wissel, J., Benecke, R., Kessler, K. R., Ceballos-Baumann, A. O., Ohly, A., Oertel, W., and Kunig, G., What is the optimal dose of botulinum toxin A in the treatment of cervical dystonia? Results of a double blind, placebo controlled, dose ranging study using Dysport. German Dystonia Study Group, J. Neurol. Neurosurg. Psychiatry, 64, 13-17, 1998.
    • (1998) J. Neurol. Neurosurg. Psychiatry , vol.64 , pp. 13-17
    • Poewe, W.1    Deuschl, G.2    Nebe, A.3    Feifel, E.4    Wissel, J.5    Benecke, R.6    Kessler, K.R.7    Ceballos-Baumann, A.O.8    Ohly, A.9    Oertel, W.10    Kunig, G.11
  • 157
    • 0030883601 scopus 로고    scopus 로고
    • Effects of botulinum toxin on vocal tract steadiness in patients with spasmodic dysphonia
    • Zwirner, P., Murry, T., and Woodson, G. E., Effects of botulinum toxin on vocal tract steadiness in patients with spasmodic dysphonia, European Archives of Oto-Rhino-Laryngology, 254, 391-395, 1997.
    • (1997) European Archives of Oto-Rhino-Laryngology , vol.254 , pp. 391-395
    • Zwirner, P.1    Murry, T.2    Woodson, G.E.3
  • 159
    • 0030976433 scopus 로고    scopus 로고
    • Gastrointestinal uses of botulinum toxin
    • Bhutani, M. S., Gastrointestinal uses of botulinum toxin, Am. J. Gastroenterol., 92, 929-933, 1997.
    • (1997) Am. J. Gastroenterol. , vol.92 , pp. 929-933
    • Bhutani, M.S.1
  • 161
    • 0029874722 scopus 로고    scopus 로고
    • Development of general weakness in a patient with amyotrophic lateral sclerosis after focal botulinum toxin injection
    • Mezaki, T., Kaji, R., Kohara, N., and Kimura, J., Development of general weakness in a patient with amyotrophic lateral sclerosis after focal botulinum toxin injection, Neurology, 46, 845-846, 1996.
    • (1996) Neurology , vol.46 , pp. 845-846
    • Mezaki, T.1    Kaji, R.2    Kohara, N.3    Kimura, J.4
  • 163
    • 0031011249 scopus 로고    scopus 로고
    • Cosmetic upper-facial rejuvenation with botulinum
    • Ellis, D. A. and Tan, A. K., Cosmetic upper-facial rejuvenation with botulinum, J. Otolaryngol., 26, 92-96, 1997.
    • (1997) J. Otolaryngol. , vol.26 , pp. 92-96
    • Ellis, D.A.1    Tan, A.K.2
  • 164
    • 0030857338 scopus 로고    scopus 로고
    • Cosmetic botulinum toxin injections
    • Carter, S. R. and Seiff, S. R., Cosmetic botulinum toxin injections, Int. Ophthalmol. Clin., 37, 69-79, 1997.
    • (1997) Int. Ophthalmol. Clin. , vol.37 , pp. 69-79
    • Carter, S.R.1    Seiff, S.R.2
  • 165
    • 0030639556 scopus 로고    scopus 로고
    • Cosmetic uses of botulinum A exotoxin
    • Carruthers, A. and Carruthers, J., Cosmetic uses of botulinum A exotoxin, Advances Dermatol., 12, 325-348, 1997.
    • (1997) Advances Dermatol. , vol.12 , pp. 325-348
    • Carruthers, A.1    Carruthers, J.2
  • 166
    • 0030921534 scopus 로고    scopus 로고
    • Refinement in the rehabilitation of the paralyzed face using botulinum toxin
    • Bikhazi, N. B. and Maas, C. S., Refinement in the rehabilitation of the paralyzed face using botulinum toxin, Otolaryngology-Head Neck Surg., 117, 303-307, 1997.
    • (1997) Otolaryngology-Head Neck Surg. , vol.117 , pp. 303-307
    • Bikhazi, N.B.1    Maas, C.S.2
  • 167
    • 0031254907 scopus 로고    scopus 로고
    • Facial rejuvenation with botulinum
    • Ellis, D. A., Chi, P. L., and Tan, A. K., Facial rejuvenation with botulinum, Dermatol. Nursing, 9, 329-333, 365, 1997.
    • (1997) Dermatol. Nursing , vol.9 , pp. 329-333
    • Ellis, D.A.1    Chi, P.L.2    Tan, A.K.3
  • 168
    • 0031425691 scopus 로고    scopus 로고
    • Botulinum toxin management of childhood intermittent exotropia
    • Spencer, R. F., Tucker, M. G., Choi, R. Y., and McNeer, K. W., Botulinum toxin management of childhood intermittent exotropia, Ophthalmology, 104, 1762-1767, 1997.
    • (1997) Ophthalmology , vol.104 , pp. 1762-1767
    • Spencer, R.F.1    Tucker, M.G.2    Choi, R.Y.3    McNeer, K.W.4
  • 169
    • 0030808501 scopus 로고    scopus 로고
    • Neuromuscular retraining for facial paralysis
    • Diels, H. J. and Combs, D., Neuromuscular retraining for facial paralysis, Otolaryngologic Clinics N. Am., 30, 727-743, 1997.
    • (1997) Otolaryngologic Clinics N. Am. , vol.30 , pp. 727-743
    • Diels, H.J.1    Combs, D.2
  • 170
    • 0029400437 scopus 로고
    • Treatment of essential tremor
    • Marchand, L., Treatment of essential tremor, Union Medicale du Canada, 124, 32-34, 1995.
    • (1995) Union Medicale du Canada , vol.124 , pp. 32-34
    • Marchand, L.1
  • 172
    • 0029873564 scopus 로고    scopus 로고
    • A randomized, double-blind, placebo-controlled study to evaluate botulinum toxin type A in essential hand tremor
    • Jankovic, J., Schwartz, K., Clemence, W., Aswad, A., and Mordaunt, J., A randomized, double-blind, placebo-controlled study to evaluate botulinum toxin type A in essential hand tremor, Movement Disorders, 11, 250-256, 1996.
    • (1996) Movement Disorders , vol.11 , pp. 250-256
    • Jankovic, J.1    Schwartz, K.2    Clemence, W.3    Aswad, A.4    Mordaunt, J.5
  • 175
    • 0030884685 scopus 로고    scopus 로고
    • Quantitative assessment of botulinum toxin treatment in 43 patients with head tremor
    • Wissel, J., Masuhr, F., Schelosky, L., Ebersbach, G., and Poewe, W., Quantitative assessment of botulinum toxin treatment in 43 patients with head tremor, Movement Disorders, 12, 722-726, 1997.
    • (1997) Movement Disorders , vol.12 , pp. 722-726
    • Wissel, J.1    Masuhr, F.2    Schelosky, L.3    Ebersbach, G.4    Poewe, W.5
  • 176
    • 0031923285 scopus 로고    scopus 로고
    • The use of botulinum toxin in localizing neuromyotonia to the terminal branches of the peripheral nerve
    • Deymeer, F., Oge, A. E., Serdaroglu, P., Yazici, J., Ozdemir, C., and Baslo, A., The use of botulinum toxin in localizing neuromyotonia to the terminal branches of the peripheral nerve, Muscle Nerve, 21, 643-646, 1998.
    • (1998) Muscle Nerve , vol.21 , pp. 643-646
    • Deymeer, F.1    Oge, A.E.2    Serdaroglu, P.3    Yazici, J.4    Ozdemir, C.5    Baslo, A.6
  • 179
    • 0031572332 scopus 로고    scopus 로고
    • Management of spasticity
    • Ko, C. K. and Ward, A. B., Management of spasticity, Br. J. Hosp. Med., 58, 400-405, 1997.
    • (1997) Br. J. Hosp. Med. , vol.58 , pp. 400-405
    • Ko, C.K.1    Ward, A.B.2
  • 180
    • 0029939239 scopus 로고    scopus 로고
    • Botulinum neurotoxin A in ophthalmology
    • Bentley, C., Botulinum neurotoxin A in ophthalmology, Ophthalmic Physiological Optics, 16(Suppl. 1), S9-S14, 1997.
    • (1997) Ophthalmic Physiological Optics , vol.16 , Issue.SUPPL. 1
    • Bentley, C.1
  • 181
    • 0030468745 scopus 로고    scopus 로고
    • Botulinum A exotoxin in clinical ophthalmology
    • Carruthers, J. D. and Carruthers, A., Botulinum A exotoxin in clinical ophthalmology, Can. J. Ophthalmol., 31, 389-400, 1996.
    • (1996) Can. J. Ophthalmol. , vol.31 , pp. 389-400
    • Carruthers, J.D.1    Carruthers, A.2
  • 184
    • 0031049572 scopus 로고    scopus 로고
    • Use of botulinum toxin in ophthalmology: Current concepts and problems
    • Tapiero, B., Robert, P. Y., Adenis, J. P., and Riss, I., Use of botulinum toxin in ophthalmology: Current concepts and problems, J. Francais d' Ophtalmologie, 20, 134-145, 1997.
    • (1997) J. Francais d' Ophtalmologie , vol.20 , pp. 134-145
    • Tapiero, B.1    Robert, P.Y.2    Adenis, J.P.3    Riss, I.4
  • 185
    • 0031976309 scopus 로고    scopus 로고
    • Dissociated effects of botulinum toxin chemodenervation on ocular deviation and saccade dynamics in chronic lateral rectus palsy
    • Acheson, J. F., Bentley, C. R., Shallo-Hoffmann, J., and Gresty, M. A., Dissociated effects of botulinum toxin chemodenervation on ocular deviation and saccade dynamics in chronic lateral rectus palsy, Br. J. Ophthalmol., 82, 67-71, 1998.
    • (1998) Br. J. Ophthalmol. , vol.82 , pp. 67-71
    • Acheson, J.F.1    Bentley, C.R.2    Shallo-Hoffmann, J.3    Gresty, M.A.4
  • 187
    • 0030883170 scopus 로고    scopus 로고
    • Experience with botulinum toxin in the treatment of cerebral palsy
    • Arens, L. J., Leary, P. M., and Goldschmidt, R. B., Experience with botulinum toxin in the treatment of cerebral palsy, S. Afr. Med. J., 87, 1001-1003, 1997.
    • (1997) S. Afr. Med. J. , vol.87 , pp. 1001-1003
    • Arens, L.J.1    Leary, P.M.2    Goldschmidt, R.B.3
  • 189
    • 0028797637 scopus 로고
    • Botulinum toxin in therapy of anal fissure
    • Jost, W. H. and Schimrigk, K., Botulinum toxin in therapy of anal fissure, Lancet, 345, 188-189, 1995.
    • (1995) Lancet , vol.345 , pp. 188-189
    • Jost, W.H.1    Schimrigk, K.2
  • 190
    • 0029187684 scopus 로고
    • Botulinum toxin in the management of anal fissure: Innovative use of a familiar agent
    • Goel, A. K. and Seenu, V., Botulinum toxin in the management of anal fissure: innovative use of a familiar agent, Tropical Gastroenterol., 16, 68-69, 1995.
    • (1995) Tropical Gastroenterol. , vol.16 , pp. 68-69
    • Goel, A.K.1    Seenu, V.2
  • 191
    • 0030810514 scopus 로고    scopus 로고
    • One hundred cases of anal fissure treated with botulin toxin: Early and long-term results
    • Jost, W. H., One hundred cases of anal fissure treated with botulin toxin: early and long-term results, Diseases Colon Rectum, 40, 1029-1032, 1997.
    • (1997) Diseases Colon Rectum , vol.40 , pp. 1029-1032
    • Jost, W.H.1
  • 192
    • 0032556991 scopus 로고    scopus 로고
    • A comparison of botulinum toxin and saline for the treatment of chronic anal fissure
    • 338, 217-220
    • Maria, G., Cassetta, E., Gui, D., Brisinda, G., Bentivoglio, A. R., and Albanese, A., A comparison of botulinum toxin and saline for the treatment of chronic anal fissure, N. Engl. J. Med., 338, 257-259. 338, 217-220, 1998.
    • (1998) N. Engl. J. Med. , vol.338 , pp. 257-259
    • Maria, G.1    Cassetta, E.2    Gui, D.3    Brisinda, G.4    Bentivoglio, A.R.5    Albanese, A.6
  • 193
    • 0345131689 scopus 로고    scopus 로고
    • Involuntary contractions of the striated anal sphincters as a cause of constipation: Report of a case
    • Jost, W. H., Muller-Lobeck, H., and Merkle, W., Involuntary contractions of the striated anal sphincters as a cause of constipation: report of a case, Diseases Colon Rectum, 41, 258-260, 1998.
    • (1998) Diseases Colon Rectum , vol.41 , pp. 258-260
    • Jost, W.H.1    Muller-Lobeck, H.2    Merkle, W.3
  • 194
    • 0030969006 scopus 로고    scopus 로고
    • Botulinum toxin: Novel treatment for dramatic urethral dilatation associated with dysfunctional voiding
    • Steinhardt, G. F., Naseer, S., and Cruz, O. A., Botulinum toxin: novel treatment for dramatic urethral dilatation associated with dysfunctional voiding, J. Urol., 158, 190-191, 1997.
    • (1997) J. Urol. , vol.158 , pp. 190-191
    • Steinhardt, G.F.1    Naseer, S.2    Cruz, O.A.3
  • 195
    • 0030794140 scopus 로고    scopus 로고
    • Recent advances. Otorhinolaryngology
    • Werner, J. A. and Gottschlich, S., Recent advances. Otorhinolaryngology, Br. Med. J., 315, 354-357, 1997.
    • (1997) Br. Med. J. , vol.315 , pp. 354-357
    • Werner, J.A.1    Gottschlich, S.2
  • 196
    • 0031438040 scopus 로고    scopus 로고
    • The use of botulinum toxin in Otorhinolaryngology - Experiences and outlook
    • Laskawi, R., The use of botulinum toxin in Otorhinolaryngology - experiences and outlook (German), Laryngo-Rhino-Otologie, 76, 656-659, 1997.
    • (1997) Laryngo-Rhino-Otologie , vol.76 , pp. 656-659
    • Laskawi, R.1
  • 198
    • 0030693152 scopus 로고    scopus 로고
    • Botulinum toxin A improves muscle spasms and rigidity in stiff-person syndrome
    • Liguori, R., Cordivari, C., Lugaresi, E., and Montagna, P., Botulinum toxin A improves muscle spasms and rigidity in stiff-person syndrome, Movement Disorders, 12, 1060-1063, 1997.
    • (1997) Movement Disorders , vol.12 , pp. 1060-1063
    • Liguori, R.1    Cordivari, C.2    Lugaresi, E.3    Montagna, P.4
  • 200
    • 0029037504 scopus 로고
    • Frey's syndrome: Treatment with botulinum toxin
    • Drobik, C. and Laskawi, R., Frey's syndrome: treatment with botulinum toxin, Acta Oto-Laryngologica, 115, 459-461, 1995.
    • (1995) Acta Oto-Laryngologica , vol.115 , pp. 459-461
    • Drobik, C.1    Laskawi, R.2
  • 201
    • 0030029698 scopus 로고    scopus 로고
    • Botulinum toxin in the therapy of gustatory sweating
    • Schulze-Bonhage, A., Schroder, M., and Ferbert, A., Botulinum toxin in the therapy of gustatory sweating, J. Neurol., 243, 143-146, 1996.
    • (1996) J. Neurol. , vol.243 , pp. 143-146
    • Schulze-Bonhage, A.1    Schroder, M.2    Ferbert, A.3
  • 202
    • 0030823225 scopus 로고    scopus 로고
    • Frey's syndrome: Treatment with botulinum toxin
    • Bjerkhoel, A. and Trobbe, O., Frey's syndrome: treatment with botulinum toxin, J. Laryngol. Otol., 111, 839-844, 1997.
    • (1997) J. Laryngol. Otol. , vol.111 , pp. 839-844
    • Bjerkhoel, A.1    Trobbe, O.2
  • 204
    • 0031906710 scopus 로고    scopus 로고
    • Up-to-date report of botulinum toxin type A treatment in patients with gustatory sweating (Frey's syndrome)
    • Laskawi, R., Drobik, C., and Schonebeck, C., Up-to-date report of botulinum toxin type A treatment in patients with gustatory sweating (Frey's syndrome), Laryngoscope, 108, 381-384, 1998.
    • (1998) Laryngoscope , vol.108 , pp. 381-384
    • Laskawi, R.1    Drobik, C.2    Schonebeck, C.3
  • 205
    • 0031890877 scopus 로고    scopus 로고
    • Focal hyperhidrosis: Effective treatment with intracutaneous botulinum toxin
    • Naumann, M., Hofmann, U., Bergmann, I., Hamm, H., Toyka, K. V., and Reiners, K., Focal hyperhidrosis: effective treatment with intracutaneous botulinum toxin, Arch. Dermatol., 134, 301-304, 1998.
    • (1998) Arch. Dermatol. , vol.134 , pp. 301-304
    • Naumann, M.1    Hofmann, U.2    Bergmann, I.3    Hamm, H.4    Toyka, K.V.5    Reiners, K.6
  • 207
    • 0031051419 scopus 로고    scopus 로고
    • Sensitive assay for measurement of Abs to Clostridium botulinum neurotoxins A, B, and E: Use of hapten-labeled-Ab elution to isolate specific complexes
    • Doellgast, G. J., Brown, J. E., Koufman, J. A., and Hatheway, C. L., Sensitive assay for measurement of Abs to Clostridium botulinum neurotoxins A, B, and E: use of hapten-labeled-Ab elution to isolate specific complexes, J. Clin. Microbiol., 35, 578-583, 1997.
    • (1997) J. Clin. Microbiol. , vol.35 , pp. 578-583
    • Doellgast, G.J.1    Brown, J.E.2    Koufman, J.A.3    Hatheway, C.L.4
  • 208
    • 0029991962 scopus 로고    scopus 로고
    • Response to botulinum toxin F in seronegative botulinum toxin A-resistant patients
    • Greene, P. E. and Fahn, S., Response to botulinum toxin F in seronegative botulinum toxin A-resistant patients, Movement Disorders, 11, 181-184, 1996.
    • (1996) Movement Disorders , vol.11 , pp. 181-184
    • Greene, P.E.1    Fahn, S.2
  • 209
    • 0031239673 scopus 로고    scopus 로고
    • Botulinum A toxin therapy: Neutralizing and nonneutralizing Abs - Therapeutic consequences
    • Goschel, H., Wohlfarth, K., Frevert, J., Dengler, R., and Bigalke, H., Botulinum A toxin therapy: neutralizing and nonneutralizing Abs - therapeutic consequences, Exp. Neurol., 147, 96-102, 1997.
    • (1997) Exp. Neurol. , vol.147 , pp. 96-102
    • Goschel, H.1    Wohlfarth, K.2    Frevert, J.3    Dengler, R.4    Bigalke, H.5
  • 212
    • 0002348547 scopus 로고
    • Chemical modification and cleavage of proteins and chemical strategy in immunochemical studies of proteins
    • Atassi, M. Z., Ed., Plenum Press, New York
    • Atassi, M. Z., Chemical modification and cleavage of proteins and chemical strategy in immunochemical studies of proteins, in Immunochemistry of Proteins, vol. 1, Atassi, M. Z., Ed., Plenum Press, New York, 1977, 1-161.
    • (1977) Immunochemistry of Proteins , vol.1 , pp. 1-161
    • Atassi, M.Z.1
  • 213
    • 0017665326 scopus 로고
    • Development of anti-toxin with each of two complementary fragments of Clostridium botulinum type B derivative toxin
    • Kozaki, S., Miyazaki, S., and Sakaguchi, G., Development of anti-toxin with each of two complementary fragments of Clostridium botulinum type B derivative toxin, Infect. Immun., 18, 761-766, 1977.
    • (1977) Infect. Immun. , vol.18 , pp. 761-766
    • Kozaki, S.1    Miyazaki, S.2    Sakaguchi, G.3
  • 214
    • 0022596945 scopus 로고
    • The use of monoclonal antibodies to analyze the structure of Clostridium botulinum type E derivative toxin
    • Kozaki, S., Kamata, Y., Nagai, T., Ogasawara, J., and Sakaguchi, G., The use of monoclonal antibodies to analyze the structure of Clostridium botulinum type E derivative toxin, Infect. Immun., 52, 786-791, 1986.
    • (1986) Infect. Immun. , vol.52 , pp. 786-791
    • Kozaki, S.1    Kamata, Y.2    Nagai, T.3    Ogasawara, J.4    Sakaguchi, G.5
  • 215
    • 0025092840 scopus 로고
    • The study of clostridial and related toxins. The search for unique mechanisms and common denominators
    • Simpson, L. L., The study of clostridial and related toxins. The search for unique mechanisms and common denominators, J. Physiol. (Paris), 84, 143-151, 1990.
    • (1990) J. Physiol. (Paris) , vol.84 , pp. 143-151
    • Simpson, L.L.1
  • 216
    • 0023883114 scopus 로고
    • Establishment of a monoclonal antibody recognizing an antigenic site common to Clostridium botulinum type b, C1, D, and E toxins and tetanus toxin
    • Tsuzuki, K., Yokosawa, N., Syuto, B., Ohishi, I., Fujii, N., Kimura, K., and Oguma, K., Establishment of a monoclonal antibody recognizing an antigenic site common to Clostridium botulinum type b, C1, D, and E toxins and tetanus toxin, Infect. Immun., 56, 898-902, 1988.
    • (1988) Infect. Immun. , vol.56 , pp. 898-902
    • Tsuzuki, K.1    Yokosawa, N.2    Syuto, B.3    Ohishi, I.4    Fujii, N.5    Kimura, K.6    Oguma, K.7
  • 218
    • 0027979896 scopus 로고
    • Antagonism of the intracellular action of botulinum neurotoxin type A by monoclonal antibodies that map to light chain epitopes
    • Cenci di Bello, I., Poulain, B., Shone, C. C., Tauc, L., and Dolly, J. O., Antagonism of the intracellular action of botulinum neurotoxin type A by monoclonal antibodies that map to light chain epitopes, Eur. J. Biochem., 219, 161-169, 1994.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 161-169
    • Cenci Di Bello, I.1    Poulain, B.2    Shone, C.C.3    Tauc, L.4    Dolly, J.O.5
  • 219
    • 0024805591 scopus 로고
    • Processing of tetanus toxin by human antigen-presenting cells. Evidence for donor and epitope-specific processing pathways
    • Demotz, S., Matricardi, P. M., Irle, C., Panina, P., Lanzavecchia, A., and Corradin, G., Processing of tetanus toxin by human antigen-presenting cells. Evidence for donor and epitope-specific processing pathways, J. Immunol., 143, 3881-3886, 1989.
    • (1989) J. Immunol. , vol.143 , pp. 3881-3886
    • Demotz, S.1    Matricardi, P.M.2    Irle, C.3    Panina, P.4    Lanzavecchia, A.5    Corradin, G.6
  • 222
    • 0027440690 scopus 로고
    • Mapping the major human T helper epitopes of tetanus toxin. The emerging picture
    • Reece, J. C., Geysen, H. M., and Rodda, S. J., Mapping the major human T helper epitopes of tetanus toxin. The emerging picture, J. Immunol., 151, 6175-6184, 1993.
    • (1993) J. Immunol. , vol.151 , pp. 6175-6184
    • Reece, J.C.1    Geysen, H.M.2    Rodda, S.J.3
  • 223
    • 0027973872 scopus 로고
    • Synthetic peptide antigens of tetanus toxin
    • Fischer, P. M. and Howden, M. E. H., Synthetic peptide antigens of tetanus toxin, Mol. Immunol., 31, 1141-1148, 1994.
    • (1994) Mol. Immunol. , vol.31 , pp. 1141-1148
    • Fischer, P.M.1    Howden, M.E.H.2
  • 224
    • 0024435932 scopus 로고
    • Expression of tetanus toxin fragment C in E. coli: Its purification and potential use as a vaccine
    • Makoff, A. J., Ballantine, S. P., Smallwood, A. E., and Fairweather, N. F., Expression of tetanus toxin fragment C in E. coli: its purification and potential use as a vaccine, Bio/Technology, 7, 1043-1046, 1989.
    • (1989) Bio/Technology , vol.7 , pp. 1043-1046
    • Makoff, A.J.1    Ballantine, S.P.2    Smallwood, A.E.3    Fairweather, N.F.4
  • 225
    • 14744271884 scopus 로고
    • High-level expression of tetanus toxin fragment C in Pichia pastoris strains containing multiple tandem integrations of the gene
    • Clare, J. J., Rayment, F. B., Ballantine, S. P., Sreekrishna, K., and Romanos, M. A., High-level expression of tetanus toxin fragment C in Pichia pastoris strains containing multiple tandem integrations of the gene, Bio/Technology, 9, 455-460, 1991.
    • (1991) Bio/Technology , vol.9 , pp. 455-460
    • Clare, J.J.1    Rayment, F.B.2    Ballantine, S.P.3    Sreekrishna, K.4    Romanos, M.A.5
  • 226
    • 0028784961 scopus 로고
    • Expression of a large, nontoxic fragment of botulinum neurotoxin serotype A and its use as an immunogen
    • LaPenotiere, H. F., Clayton, M. A., and Middlebrook, J. L., Expression of a large, nontoxic fragment of botulinum neurotoxin serotype A and its use as an immunogen, Toxicon, 33, 1383-1386, 1995.
    • (1995) Toxicon , vol.33 , pp. 1383-1386
    • LaPenotiere, H.F.1    Clayton, M.A.2    Middlebrook, J.L.3
  • 227
    • 0029039466 scopus 로고
    • Protective vaccination with a recombinant fragment of Clostridium botulinum neurotoxin serotype A expressed from a synthetic gene in Escherichia coli
    • Clayton, M. A., Clayton, J. M., Brown, D. R., and Middlebrook, J. L., Protective vaccination with a recombinant fragment of Clostridium botulinum neurotoxin serotype A expressed from a synthetic gene in Escherichia coli, Infect. Immun., 63, 2738-2742, 1995.
    • (1995) Infect. Immun. , vol.63 , pp. 2738-2742
    • Clayton, M.A.1    Clayton, J.M.2    Brown, D.R.3    Middlebrook, J.L.4
  • 228
    • 0028876404 scopus 로고
    • Protection strategies against botulinum toxin
    • Middlebrook, J. L., Protection strategies against botulinum toxin, Adv. Exp. Med. Biol., 383, 93-98, 1995.
    • (1995) Adv. Exp. Med. Biol. , vol.383 , pp. 93-98
    • Middlebrook, J.L.1
  • 230
    • 0030294098 scopus 로고    scopus 로고
    • Mapping of protective and cross-reactive domains of the type A neurotoxin of Clostridium botulinum
    • Dertzbaugh, M. T. and West, M. W., Mapping of protective and cross-reactive domains of the type A neurotoxin of Clostridium botulinum, Vaccine, 14, 1538-1544, 1996.
    • (1996) Vaccine , vol.14 , pp. 1538-1544
    • Dertzbaugh, M.T.1    West, M.W.2
  • 231
    • 0030930268 scopus 로고    scopus 로고
    • Molecular characterization of murine humoral immune response to botulinum neurotoxin type A binding domain as assessed by using phage Ab libraries
    • Amersdorfer, P., Wong, C., Chen, S., Smith., T., Deshpande, S., Sheridan, R., Finnern, R., and Marks, J. D., Molecular characterization of murine humoral immune response to botulinum neurotoxin type A binding domain as assessed by using phage Ab libraries, Infect. Immun., 65, 3743-3752, 1997.
    • (1997) Infect. Immun. , vol.65 , pp. 3743-3752
    • Amersdorfer, P.1    Wong, C.2    Chen, S.3    Smith, T.4    Deshpande, S.5    Sheridan, R.6    Finnern, R.7    Marks, J.D.8
  • 233
    • 0030734570 scopus 로고    scopus 로고
    • Induction of an immune response by oral administration of recombinant botulinum toxin
    • Kiyatkin, N., Maksymowych, A. B., and Simpson, L. L., Induction of an immune response by oral administration of recombinant botulinum toxin, Infect. Immun., 65, 4586-4591, 1997.
    • (1997) Infect. Immun. , vol.65 , pp. 4586-4591
    • Kiyatkin, N.1    Maksymowych, A.B.2    Simpson, L.L.3
  • 234
    • 0017998988 scopus 로고
    • A proposal for the nomenclature of antigen sites in peptides and proteins
    • Atassi, M. Z. and Smith, J. A., A proposal for the nomenclature of antigen sites in peptides and proteins, Immunochemistry, 15, 609-610, 1978.
    • (1978) Immunochemistry , vol.15 , pp. 609-610
    • Atassi, M.Z.1    Smith, J.A.2
  • 235
    • 0019159026 scopus 로고
    • A novel and comprehensive synthetic approach for the elucidation of protein antigenic structures: Determination of the full antigenic profile of the α-chain of human haemoglobin
    • Kazim, A. L. and Atassi, M. Z., A novel and comprehensive synthetic approach for the elucidation of protein antigenic structures: Determination of the full antigenic profile of the α-chain of human haemoglobin, Biochem. J., 191, 261-264, 1980.
    • (1980) Biochem. J. , vol.191 , pp. 261-264
    • Kazim, A.L.1    Atassi, M.Z.2
  • 236
    • 0019975439 scopus 로고
    • Structurally inherent antigenic sites: Localization of the antigenic sites of the α-chain of human haemoglobin in three host species by a comprehensive synthetic approach
    • Kazim, A. L. and Atassi, M. Z., Structurally inherent antigenic sites: localization of the antigenic sites of the α-chain of human haemoglobin in three host species by a comprehensive synthetic approach, Biochem. J., 203, 201-208, 1982.
    • (1982) Biochem. J. , vol.203 , pp. 201-208
    • Kazim, A.L.1    Atassi, M.Z.2
  • 237
    • 84907110219 scopus 로고
    • Molecular localization of the full profile of the continuous regions recognized by myoglobin primed T cells using synthetic overlapping peptides encompassing the entire molecule
    • Bixler, G. S. and Atassi, M. Z., Molecular localization of the full profile of the continuous regions recognized by myoglobin primed T cells using synthetic overlapping peptides encompassing the entire molecule, Immunol. Commun., 12, 593-603, 1983.
    • (1983) Immunol. Commun. , vol.12 , pp. 593-603
    • Bixler, G.S.1    Atassi, M.Z.2
  • 238
    • 0021611223 scopus 로고
    • T-cell recognition of myoglobin. Localization of the sites stimulating T-cell proliferative responses by synthetic overlapping peptides encompassing the entire molecule
    • Bixler, G. S. and Atassi, M. Z., T-Cell recognition of myoglobin. Localization of the sites stimulating T-Cell proliferative responses by synthetic overlapping peptides encompassing the entire molecule, J. Immunogen., 11, 339-353, 1984.
    • (1984) J. Immunogen. , vol.11 , pp. 339-353
    • Bixler, G.S.1    Atassi, M.Z.2
  • 239
    • 0017625323 scopus 로고
    • Prediction and confirmation by synthesis of two antigenic sites in human haemoglobin by extrapolation from the known antigenic structure of sperm whale myoglobin
    • Kazim, A. L. and Atassi, M. Z., Prediction and confirmation by synthesis of two antigenic sites in human haemoglobin by extrapolation from the known antigenic structure of sperm whale myoglobin, Biochem. J., 167, 275-278, 1977.
    • (1977) Biochem. J. , vol.167 , pp. 275-278
    • Kazim, A.L.1    Atassi, M.Z.2
  • 240
    • 0018065580 scopus 로고
    • First consequences of the determination of the entire antigenic structure of sperm whale myoglobin
    • Kazim, A. L. and Atassi, M. Z., First consequences of the determination of the entire antigenic structure of sperm whale myoglobin, Adv. Exp. Med. Biol., 98, 19-40, 1978.
    • (1978) Adv. Exp. Med. Biol. , vol.98 , pp. 19-40
    • Kazim, A.L.1    Atassi, M.Z.2
  • 241
    • 0022498345 scopus 로고
    • Antigenic structure of human haemoglobin: Localization of the antigenic sites of the β-chain in three host species by synthetic overlapping peptides representing the entire chain
    • Yoshioka, N. and Atassi, M. Z., Antigenic structure of human haemoglobin: Localization of the antigenic sites of the β-chain in three host species by synthetic overlapping peptides representing the entire chain, Biochem. J., 234, 441-447, 1986.
    • (1986) Biochem. J. , vol.234 , pp. 441-447
    • Yoshioka, N.1    Atassi, M.Z.2
  • 242
    • 0021764621 scopus 로고
    • Antigenic structures of proteins. Their determination has revealed important aspects of immune recognition and generated strategies for synthetic mimicking of protein binding sites
    • Atassi, M. Z., Antigenic structures of proteins. Their determination has revealed important aspects of immune recognition and generated strategies for synthetic mimicking of protein binding sites, Eur. J. Biochem., 145, 1-20, 1984.
    • (1984) Eur. J. Biochem. , vol.145 , pp. 1-20
    • Atassi, M.Z.1
  • 243
    • 0028087645 scopus 로고
    • α-bungarotoxin peptides afford a synthetic vaccine against toxin poisoning
    • Dolimbek, B. Z. and Atassi, M. Z., α-bungarotoxin peptides afford a synthetic vaccine against toxin poisoning, J. Prot. Chem., 13, 490-493, 1994.
    • (1994) J. Prot. Chem. , vol.13 , pp. 490-493
    • Dolimbek, B.Z.1    Atassi, M.Z.2
  • 244
    • 0345109855 scopus 로고
    • Antibody and T-cell recognition of α-bungarotoxin and its synthetic loop peptides
    • Atassi, M. Z., Dolimbek, B. Z., and Manshouri, T., Antibody and T-cell recognition of α-bungarotoxin and its synthetic loop peptides, Mol. Immunol., 13, 927-932, 1995.
    • (1995) Mol. Immunol. , vol.13 , pp. 927-932
    • Atassi, M.Z.1    Dolimbek, B.Z.2    Manshouri, T.3
  • 245
    • 0041183282 scopus 로고
    • Regions of interaction between nicotinic acetylcholine receptor and α-neurotoxins and development of a synthetic vaccine against toxin poisoning
    • Atassi, M. Z. and Appella, E., Eds., Plenum Press, New York
    • Atassi, M. Z. and Dolimbek, B. Z., Regions of interaction between nicotinic acetylcholine receptor and α-neurotoxins and development of a synthetic vaccine against toxin poisoning, in Methods of Protein Structure Analysis, Atassi, M. Z. and Appella, E., Eds., Plenum Press, New York, 1995, 311-326.
    • (1995) Methods of Protein Structure Analysis , pp. 311-326
    • Atassi, M.Z.1    Dolimbek, B.Z.2
  • 246
    • 0030152066 scopus 로고    scopus 로고
    • Protection against α-bungarotoxin poisoning by immunization with synthetic toxin peptides
    • Dolimbek, B. Z. and Atassi, M. Z., Protection against α-bungarotoxin poisoning by immunization with synthetic toxin peptides, Mol. Immunol., 33, 681-689, 1996.
    • (1996) Mol. Immunol. , vol.33 , pp. 681-689
    • Dolimbek, B.Z.1    Atassi, M.Z.2
  • 247
    • 0030472583 scopus 로고    scopus 로고
    • Mapping of the antibody-binding regions on botulinum neurotoxin H-chain domain 855 to 1296 with anti-toxin antibodies from three host species
    • Atassi, M. Z., Dolimbek, B. Z., Hayakari, M., Middlebrook, J. L., Whitney, B., and Oshima, M., Mapping of the antibody-binding regions on botulinum neurotoxin H-chain domain 855 to 1296 with anti-toxin antibodies from three host species, J. Prot. Chem., 15, 691-700, 1996.
    • (1996) J. Prot. Chem. , vol.15 , pp. 691-700
    • Atassi, M.Z.1    Dolimbek, B.Z.2    Hayakari, M.3    Middlebrook, J.L.4    Whitney, B.5    Oshima, M.6
  • 249
    • 0016734961 scopus 로고
    • Antigenic structure of myoglobin. The complete immunochemical anatomy of a protein and conclusions relating to antigenic structures of proteins
    • Atassi, M. Z., Antigenic structure of myoglobin. The complete immunochemical anatomy of a protein and conclusions relating to antigenic structures of proteins, Immunochemistry, 12, 423-438, 1975.
    • (1975) Immunochemistry , vol.12 , pp. 423-438
    • Atassi, M.Z.1
  • 250
    • 0019335323 scopus 로고
    • Precise determination of protein antigenie structures has unraveled the molecular immune recognition of proteins and provided a prototype for synthetic mimicking of other protein binding sites
    • Atassi, M. Z., Precise determination of protein antigenie structures has unraveled the molecular immune recognition of proteins and provided a prototype for synthetic mimicking of other protein binding sites, Mol. Cell. Biochem., 32, 21-44, 1980.
    • (1980) Mol. Cell. Biochem. , vol.32 , pp. 21-44
    • Atassi, M.Z.1
  • 251
    • 0018163026 scopus 로고
    • Genetic control of T-lymphocyte proliferative responses to sperm whale myoglobin and its synthetic antigenic sites in mice
    • Okuda, K., Twining, S. S., Atassi, M. Z., and David, C. S., Genetic control of T-lymphocyte proliferative responses to sperm whale myoglobin and its synthetic antigenic sites in mice, J. Immunol., 121,866-868, 1978.
    • (1978) J. Immunol. , vol.121 , pp. 866-868
    • Okuda, K.1    Twining, S.S.2    Atassi, M.Z.3    David, C.S.4
  • 252
    • 0018392860 scopus 로고
    • Immune response gene control of determinant selection. II. Genetic control of the murine T lymphocyte proliferative response to insulin
    • Rosenwasser, L. J., Barcinski, M. A., Schwartz, R. H., and Rosenthal, A. S., Immune response gene control of determinant selection. II. Genetic control of the murine T lymphocyte proliferative response to insulin, J. Immunol., 123, 471-476, 1979.
    • (1979) J. Immunol. , vol.123 , pp. 471-476
    • Rosenwasser, L.J.1    Barcinski, M.A.2    Schwartz, R.H.3    Rosenthal, A.S.4
  • 253
    • 0019396266 scopus 로고
    • Genetics of immune response: A survey
    • Krco, C. J. and David, C. S., Genetics of immune response: a survey, Crit. Rev. Immunol., 1, 211-257, 1981.
    • (1981) Crit. Rev. Immunol. , vol.1 , pp. 211-257
    • Krco, C.J.1    David, C.S.2
  • 254
    • 0018774701 scopus 로고
    • Genetic control of immune response to sperm whale myoglobin in mice. II. T lymphocyte proliferative response to the synthetic antigenic sites
    • Okuda, K., Twining, S. S., David, C. S., and Atassi, M. Z., Genetic control of immune response to sperm whale myoglobin in mice. II. T lymphocyte proliferative response to the synthetic antigenic sites, J. Immunol., 123, 182-188, 1979.
    • (1979) J. Immunol. , vol.123 , pp. 182-188
    • Okuda, K.1    Twining, S.S.2    David, C.S.3    Atassi, M.Z.4
  • 255
    • 84907108984 scopus 로고
    • Genetic control of the immune response to myoglobin. V. Analysis of the cross-reactivity of 12 myoglobins with sperm whale myoglobin antisera of inbred mouse strains in terms of substitutions in the antigenic sites and in the environmental residues of the sites
    • Atassi, M. Z., Twining, S. S., Lehmann, H., and David, C. S., Genetic control of the immune response to myoglobin. V. Analysis of the cross-reactivity of 12 myoglobins with sperm whale myoglobin antisera of inbred mouse strains in terms of substitutions in the antigenic sites and in the environmental residues of the sites, Immunol. Commun., 10, 359-365, 1981.
    • (1981) Immunol. Commun. , vol.10 , pp. 359-365
    • Atassi, M.Z.1    Twining, S.S.2    Lehmann, H.3    David, C.S.4
  • 256
    • 0020345735 scopus 로고
    • Genetic control and intersite influences on the immune response to Sperm Whale myoglobin
    • David, C. S. and Atassi, M. Z., Genetic control and intersite influences on the immune response to Sperm Whale myoglobin, Adv. Exp. Med. Biol., 150, 97-126, 1982.
    • (1982) Adv. Exp. Med. Biol. , vol.150 , pp. 97-126
    • David, C.S.1    Atassi, M.Z.2
  • 257
    • 0030741208 scopus 로고    scopus 로고
    • Localization of the regions on the C-terminal domain of the heavy chain of botulinum toxin A recognized by T-lymphocytes and by antibodies after immunization of mice with pentavalent toxoid
    • Rosenberg, J. S., Middlebrook, J. L., and Atassi, M. Z., Localization of the regions on the C-terminal domain of the heavy chain of botulinum toxin A recognized by T-lymphocytes and by antibodies after immunization of mice with pentavalent toxoid, Immunol. Invest., 26, 491-504, 1997.
    • (1997) Immunol. Invest. , vol.26 , pp. 491-504
    • Rosenberg, J.S.1    Middlebrook, J.L.2    Atassi, M.Z.3
  • 258
    • 0345109854 scopus 로고
    • Comparison of the submolecular recognition of proteins by T and B cells
    • Kohler, H. and LoVerde, P. T., Eds., Longman Scientific and Technical, Harlow, England
    • Atassi, M. Z. and Bixler, G. S., Jr., Comparison of the submolecular recognition of proteins by T and B cells, in Vaccines: New Concepts and Developments, Kohler, H. and LoVerde, P. T., Eds., Longman Scientific and Technical, Harlow, England, 1988, 58-70.
    • (1988) Vaccines: New Concepts and Developments , pp. 58-70
    • Atassi, M.Z.1    Bixler G.S., Jr.2
  • 259
    • 0024835526 scopus 로고
    • Cytotoxic and helper T-lymphocyte responses to antibody recognition regions on influenza virus hemagglutinin
    • Atassi, M. Z., Torres, J. V., and Wyde, P. R., Cytotoxic and helper T-lytnphocyte responses to antibody recognition regions on influenza virus hemagglutinin, Adv. Exp. Med. Biol., 251, 49-63, 1989.
    • (1989) Adv. Exp. Med. Biol. , vol.251 , pp. 49-63
    • Atassi, M.Z.1    Torres, J.V.2    Wyde, P.R.3
  • 260
    • 0025356424 scopus 로고
    • The T cell repertoire to a multideterminant antigen. Clonal heterogeneity of the T cell response, variation between syngeneic individuals, and in vitro selection of T cell specificities
    • Gammon, G., Klotz, J., Ando, D., and Sercarz, E. E., The T cell repertoire to a multideterminant antigen. Clonal heterogeneity of the T cell response, variation between syngeneic individuals, and in vitro selection of T cell specificities, J. Immunol., 144, 1571-1577, 1990.
    • (1990) J. Immunol. , vol.144 , pp. 1571-1577
    • Gammon, G.1    Klotz, J.2    Ando, D.3    Sercarz, E.E.4
  • 262
    • 0027993557 scopus 로고
    • Profile of the regions of acetylcholine receptor α chain recognized by T-lymphocytes and by antibodies in EAMG-susceptible and nonsusceptible mouse strains after different periods of immunization with the receptor
    • Oshima, M., Pachner, A. R., and Atassi, M. Z., Profile of the regions of acetylcholine receptor α chain recognized by T-lymphocytes and by antibodies in EAMG-susceptible and nonsusceptible mouse strains after different periods of immunization with the receptor, Mol. Immunol., 31, 833-843, 1994.
    • (1994) Mol. Immunol. , vol.31 , pp. 833-843
    • Oshima, M.1    Pachner, A.R.2    Atassi, M.Z.3
  • 264
    • 0021961348 scopus 로고
    • Antigen presentation of myoglobin: Profiles of T-cell proliferative responses following priming with synthetic overlapping peptides encompassing the entire protein molecule
    • Bixler, G. S., Jr. and Atassi, M. Z., Antigen presentation of myoglobin: profiles of T-cell proliferative responses following priming with synthetic overlapping peptides encompassing the entire protein molecule, Eur. J. Immunol., 15, 917-922, 1985.
    • (1985) Eur. J. Immunol. , vol.15 , pp. 917-922
    • Bixler G.S., Jr.1    Atassi, M.Z.2
  • 265
    • 0022220134 scopus 로고
    • Antigen presentation of lysozyme: T-cell recognition of peptide and intact protein after priming with synthetic overlapping peptides comprising the entire protein chain
    • Bixler, G. S., Jr., Yoshida, T., and Atassi, M. Z., Antigen presentation of lysozyme: T-cell recognition of peptide and intact protein after priming with synthetic overlapping peptides comprising the entire protein chain, Immunology, 56, 103-112, 1985.
    • (1985) Immunology , vol.56 , pp. 103-112
    • Bixler G.S., Jr.1    Yoshida, T.2    Atassi, M.Z.3
  • 267
    • 0019446322 scopus 로고
    • Genetic control of the immune response to myoglobin. VI. Inter-site influences in T-lymphocyte proliferative response from analysis of cross-reactions of ten myoglobins in terms of substitutions in the antigenic sites and in environmental residues of the sites
    • Atassi, M. Z., Yokota, S., Twining, S. S., Lehmann, H., and David, C. S., Genetic control of the immune response to myoglobin. VI. Inter-site influences in T-lymphocyte proliferative response from analysis of cross-reactions of ten myoglobins in terms of substitutions in the antigenic sites and in environmental residues of the sites, Mol. Immunol., 18, 961-967, 1981.
    • (1981) Mol. Immunol. , vol.18 , pp. 961-967
    • Atassi, M.Z.1    Yokota, S.2    Twining, S.S.3    Lehmann, H.4    David, C.S.5
  • 268
    • 0030266775 scopus 로고    scopus 로고
    • B-cell activation in vitro by helper T cells specific to region α146-162 of Torpedo californica acetylcholine receptor
    • Rosenberg, J. S., Oshima, M., and Atassi, M. Z., B-cell activation in vitro by helper T cells specific to region α146-162 of Torpedo californica acetylcholine receptor, J. Immunol., 157, 3192-3299, 1996.
    • (1996) J. Immunol. , vol.157 , pp. 3192-3299
    • Rosenberg, J.S.1    Oshima, M.2    Atassi, M.Z.3
  • 269
    • 0031862123 scopus 로고    scopus 로고
    • B-cell activation in vitro by helper T cells specific to a protein region that is recognized both T cells and by antibodies
    • Hamajima, S. and Atassi, M. Z., B-cell activation in vitro by helper T cells specific to a protein region that is recognized both T cells and by antibodies, Immunol. Invest., 27, 121-134, 1998.
    • (1998) Immunol. Invest. , vol.27 , pp. 121-134
    • Hamajima, S.1    Atassi, M.Z.2
  • 270
    • 0024796883 scopus 로고
    • Universally immunogenic T cell epitopes: Promiscuous binding to human MHC class II and promiscuous recognition by T cells
    • Panina-Bordignon, P., Tan, A., Termijtelen, A., Demotz, S., Corradin, G., and Lanzavecehia, A., Universally immunogenic T cell epitopes: promiscuous binding to human MHC class II and promiscuous recognition by T cells, Eur. J. Immunol., 19, 2237-2242, 1989.
    • (1989) Eur. J. Immunol. , vol.19 , pp. 2237-2242
    • Panina-Bordignon, P.1    Tan, A.2    Termijtelen, A.3    Demotz, S.4    Corradin, G.5    Lanzavecehia, A.6
  • 271
    • 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., Molecular cloning of the Clostridium botulinum structural gene encoding the type B neurotoxin and determination of its entire nucleotide sequence, Appl. Env. Microbiol, 58, 2345-2354, 1992.
    • (1992) Appl. Env. 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


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