메뉴 건너뛰기




Volumn 16, Issue 1, 2011, Pages 202-220

Small molecule inhibitors as countermeasures for botulinum neurotoxin intoxication

Author keywords

Botulinum neurotoxin; Drug discovery; Inhibitor

Indexed keywords

ACETYLCHOLINE; BOTULINUM TOXIN;

EID: 79251532110     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules16010202     Document Type: Review
Times cited : (38)

References (92)
  • 2
    • 0037503914 scopus 로고    scopus 로고
    • Therapy and prophylaxis of inhaled biological toxins
    • Paddle, B. M. Therapy and prophylaxis of inhaled biological toxins. J. Appl. Toxicol. 2003, 23, 139-170.
    • (2003) J. Appl. Toxicol. , vol.23 , pp. 139-170
    • Paddle, B.M.1
  • 3
    • 18244379063 scopus 로고    scopus 로고
    • The evolving field of biodefense: Therapeutic developments and diagnostics
    • Burnett, J. C.; Henchal, E. A.; Schmaljohn, A. L.; Bavari, S. The evolving field of biodefense: Therapeutic developments and diagnostics. Nat. Rev. Drug Discov. 2005, 4, 281-297.
    • (2005) Nat. Rev. Drug Discov. , vol.4 , pp. 281-297
    • Burnett, J.C.1    Henchal, E.A.2    Schmaljohn, A.L.3    Bavari, S.4
  • 5
    • 1542505543 scopus 로고    scopus 로고
    • Botulin toxin: A weapon in terrorism
    • Josko, D. Botulin toxin: A weapon in terrorism. Clin. Lab. Sci. 2004, 17, 30-34.
    • (2004) Clin. Lab. Sci. , vol.17 , pp. 30-34
    • Josko, D.1
  • 6
    • 16444381146 scopus 로고    scopus 로고
    • Bacteria as potential tools in bioterrorism, with an emphasis on bacterial toxins
    • Clarke, S. C. Bacteria as potential tools in bioterrorism, with an emphasis on bacterial toxins. Br. J. Biomed. Sci. 2005, 62, 40-46.
    • (2005) Br. J. Biomed. Sci. , vol.62 , pp. 40-46
    • Clarke, S.C.1
  • 8
    • 18244379063 scopus 로고    scopus 로고
    • The evolving field of biodefense: Therapeutic developments and diagnostics
    • Burnett, J. C.; Henchal, E. A.; Schmaljohn, A. L.; Bavari, S. The evolving field of biodefense: Therapeutic developments and diagnostics. Nat. Rev. Drug Discov. 2005, 4, 281-297.
    • (2005) Nat. Rev. Drug Discov. , vol.4 , pp. 281-297
    • Burnett, J.C.1    Henchal, E.A.2    Schmaljohn, A.L.3    Bavari, S.4
  • 9
    • 16244423360 scopus 로고    scopus 로고
    • Clostridium botulinum: A bug with beauty and weapon
    • Shukla, H. D.; Sharma, S. K. Clostridium botulinum: A bug with beauty and weapon. Crit. Rev. Microbiol. 2005, 31, 11-18.
    • (2005) Crit. Rev. Microbiol. , vol.31 , pp. 11-18
    • Shukla, H.D.1    Sharma, S.K.2
  • 10
    • 2442458014 scopus 로고    scopus 로고
    • Botulinum toxins in neurological disease
    • Comella, C. L.; Pullman, S. L. Botulinum toxins in neurological disease. Muscle Nerve 2004, 29, 628-644.
    • (2004) Muscle Nerve , vol.29 , pp. 628-644
    • Comella, C.L.1    Pullman, S.L.2
  • 11
    • 0036840945 scopus 로고    scopus 로고
    • Review of the use of botulinum toxin for hyperhidrosis and cosmetic purposes
    • Glogau, R. G. Review of the use of botulinum toxin for hyperhidrosis and cosmetic purposes. Clin. J. Pain 2002, 18 (6 Suppl.), S191-S197.
    • (2002) Clin. J. Pain , vol.18 , Issue.6 SUPPL.
    • Glogau, R.G.1
  • 12
    • 4344715045 scopus 로고    scopus 로고
    • Medical aspects of biologic toxins
    • Marks, J. D. Medical aspects of biologic toxins. Anesthesiol. Clin. N. Amer. 2004, 22, 509-532.
    • (2004) Anesthesiol. Clin. N. Amer. , vol.22 , pp. 509-532
    • Marks, J.D.1
  • 13
    • 18744410709 scopus 로고    scopus 로고
    • Botulinal neurotoxins: Revival of an old killer
    • Montecucco, C.; Molgo, J. Botulinal neurotoxins: Revival of an old killer. Curr. Opin. Pharmacol. 2005, 5, 274-279.
    • (2005) Curr. Opin. Pharmacol. , vol.5 , pp. 274-279
    • Montecucco, C.1    Molgo, J.2
  • 14
  • 15
    • 26044454078 scopus 로고    scopus 로고
    • Medical aspects of toxin weapons
    • Bigalke, H.; Rummel, A. Medical aspects of toxin weapons. Toxicology 2005, 214, 210-220.
    • (2005) Toxicology , vol.214 , pp. 210-220
    • Bigalke, H.1    Rummel, A.2
  • 16
    • 17444423708 scopus 로고    scopus 로고
    • A new wrinkle on pain relief: Re-engineering clostridial neurotoxins for analgesics
    • Foster, K. A. A new wrinkle on pain relief: Re-engineering clostridial neurotoxins for analgesics. Drug Discov. Today 2005, 10, 563-569.
    • (2005) Drug Discov. Today , vol.10 , pp. 563-569
    • Foster, K.A.1
  • 17
    • 23944527141 scopus 로고    scopus 로고
    • Botulinum toxin type A injections: Adverse events reported to the US food and drug administration in therapeutic and cosmetic cases
    • Cote, T. R.; Mohan, A. K.; Polder, J. A.; Walton, M. K.; Braun, M. M. Botulinum toxin type A injections: Adverse events reported to the US Food and Drug Administration in therapeutic and cosmetic cases. J. Am. Acad. Dermatol. 2005, 53, 407-415.
    • (2005) J. Am. Acad. Dermatol. , vol.53 , pp. 407-415
    • Cote, T.R.1    Mohan, A.K.2    Polder, J.A.3    Walton, M.K.4    Braun, M.M.5
  • 19
    • 0037428398 scopus 로고    scopus 로고
    • Evaluation of the therapeutic usefulness of botulinum neurotoxins B, C1, E, and F compared with the long lasting type A. Basis for distinct durations of inhibition of exocytosis in central neurons
    • Foran, P. G.; Mohammed, N.; Lisk, G. O.; Nagwaney, S.; Lawrence, G. W.; Johnson, E.; Smith, L.; Aoki, K. R.; Dolly, J. O. Evaluation of the therapeutic usefulness of botulinum neurotoxins B, C1, E, and F compared with the long lasting type A. Basis for distinct durations of inhibition of exocytosis in central neurons. J. Biol. Chem. 2003, 278, 1363-1371.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1363-1371
    • Foran, P.G.1    Mohammed, N.2    Lisk, G.O.3    Nagwaney, S.4    Lawrence, G.W.5    Johnson, E.6    Smith, L.7    Aoki, K.R.8    Dolly, J.O.9
  • 22
    • 0037396608 scopus 로고    scopus 로고
    • Dynamics of motor nerve terminal remodeling unveiled using SNARE-cleaving botulinum toxins: The extent and duration are dictated by the sites of SNAP-25 truncation
    • Meunier, F. A.; Lisk, G.; Sesardic, D.; Dolly, J. O. Dynamics of motor nerve terminal remodeling unveiled using SNARE-cleaving botulinum toxins: the extent and duration are dictated by the sites of SNAP-25 truncation. Mol. Cell. Neurosci. 2003, 22, 454-466.
    • (2003) Mol. Cell. Neurosci. , vol.22 , pp. 454-466
    • Meunier, F.A.1    Lisk, G.2    Sesardic, D.3    Dolly, J.O.4
  • 23
    • 0031712779 scopus 로고    scopus 로고
    • Crystal structure of botulinum neurotoxin type A and implications for toxicity
    • Lacy, D. B.; Tepp, W.; Cohen, A. C.; DasGupta, B. R.; Stevens, R. C. Crystal structure of botulinum neurotoxin type A and implications for toxicity. Nat. Struct. Biol. 1998, 5, 898-902.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 898-902
    • Lacy, D.B.1    Tepp, W.2    Cohen, A.C.3    DasGupta, B.R.4    Stevens, R.C.5
  • 24
    • 1342323663 scopus 로고    scopus 로고
    • Identification of the major steps in botulinum toxin action
    • Simpson, L. L. Identification of the major steps in botulinum toxin action. Annu. Rev. Pharmacol. Toxicol. 2004, 44, 167-193.
    • (2004) Annu. Rev. Pharmacol. Toxicol. , vol.44 , pp. 167-193
    • Simpson, L.L.1
  • 25
    • 0033887387 scopus 로고    scopus 로고
    • Intimate details of the most poisonous poison
    • Singh, B. R. Intimate details of the most poisonous poison. Nat. Struct. Biol. 2000, 7, 617-619.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 617-619
    • Singh, B.R.1
  • 26
    • 0036850282 scopus 로고    scopus 로고
    • Botulinum and tetanus neurotoxins: Structure, function and therapeutic utility
    • Turton, K.; Chaddock, J. A.; Acharya, K. R. Botulinum and tetanus neurotoxins: Structure, function and therapeutic utility. Trends Biochem. Sci. 2002, 27, 552-558.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 552-558
    • Turton, K.1    Chaddock, J.A.2    Acharya, K.R.3
  • 28
    • 0037228895 scopus 로고    scopus 로고
    • Fluorogenic substrates for the protease activities of botulinum neurotoxins, serotypes A, B, and F
    • Schmidt, J. J.; Stafford, R. G. Fluorogenic substrates for the protease activities of botulinum neurotoxins, serotypes A, B, and F. Appl. Environ. Microbiol. 2003, 69, 297-303.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 297-303
    • Schmidt, J.J.1    Stafford, R.G.2
  • 30
    • 0026497466 scopus 로고
    • Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin
    • Schiavo, G.; Benfenati, F.; Poulain, B.; Rossetto, O.; de Polverino, L. P.; DasGupta, B. R.; Montecucco, C. Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin. Nature 1992, 359, 832-835.
    • (1992) Nature , vol.359 , pp. 832-835
    • Schiavo, G.1    Benfenati, F.2    Poulain, B.3    Rossetto, O.4    De Polverino, L.P.5    DasGupta, B.R.6    Montecucco, C.7
  • 32
    • 0027241009 scopus 로고
    • Botulinum neurotoxin serotype F is a zinc endopeptidase specific for VAMP/synaptobrevin
    • Schiavo, G.; Shone, C. C.; Rossetto, O.; Alexander, F. C.; Montecucco, C. Botulinum neurotoxin serotype F is a zinc endopeptidase specific for VAMP/synaptobrevin. J. Biol. Chem. 1993, 268, 11516-11519.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11516-11519
    • Schiavo, G.1    Shone, C.C.2    Rossetto, O.3    Alexander, F.C.4    Montecucco, C.5
  • 33
    • 0027432376 scopus 로고
    • Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC-1/syntaxin
    • Blasi, J.; Chapman, E. R.; Yamasaki, S.; Binz, T.; Niemann, H.; Jahn, R. Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC-1/syntaxin. EMBO. J. 1993, 12, 4821-4828.
    • (1993) EMBO. J. , vol.12 , pp. 4821-4828
    • Blasi, J.1    Chapman, E.R.2    Yamasaki, S.3    Binz, T.4    Niemann, H.5    Jahn, R.6
  • 34
    • 0033884053 scopus 로고    scopus 로고
    • Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B
    • DOI 10.1038/78005
    • Swaminathan, S.; Eswaramoorthy, S. Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B. Nat. Struct. Biol. 2000, 7, 693-699. (Pubitemid 30636683)
    • (2000) Nature Structural Biology , vol.7 , Issue.8 , pp. 693-699
    • Swaminathan, S.1    Eswaramoorthy, S.2
  • 35
    • 58549116147 scopus 로고    scopus 로고
    • Domain organization in Clostridium botulinum neurotoxin type E is unique: Its implication in faster translocation
    • Kumaran, D.; Eswaramoorthy, S.; Furey, W.; Navaza, J.; Sax, M.; Swaminathan, S. Domain organization in Clostridium botulinum neurotoxin type E is unique: Its implication in faster translocation. J. Mol. Biol. 2009, 386, 233-245.
    • (2009) J. Mol. Biol. , vol.386 , pp. 233-245
    • Kumaran, D.1    Eswaramoorthy, S.2    Furey, W.3    Navaza, J.4    Sax, M.5    Swaminathan, S.6
  • 36
  • 37
    • 44349178037 scopus 로고    scopus 로고
    • Catalytic features of the botulinum neurotoxin A light chain revealed by high resolution structure of an inhibitory peptide complex
    • Silvaggi, N. R.; Wilson, D.; Tzipori, S.; Allen, K. N. Catalytic features of the botulinum neurotoxin A light chain revealed by high resolution structure of an inhibitory peptide complex. Biochemistry 2008, 47, 5736-5745.
    • (2008) Biochemistry , vol.47 , pp. 5736-5745
    • Silvaggi, N.R.1    Wilson, D.2    Tzipori, S.3    Allen, K.N.4
  • 38
    • 11144341950 scopus 로고    scopus 로고
    • Substrate recognition strategy for botulinum neurotoxin serotype A
    • Breidenbach, M. A.; Brunger, A. T. Substrate recognition strategy for botulinum neurotoxin serotype A. Nature 2004, 432, 925-929.
    • (2004) Nature , vol.432 , pp. 925-929
    • Breidenbach, M.A.1    Brunger, A.T.2
  • 39
    • 0033887403 scopus 로고    scopus 로고
    • Co-crystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 Å resolution
    • Hanson, M. A.; Stevens, R. C. Co-crystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 Å resolution. Nat. Struct. Biol. 2000, 7, 687-692.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 687-692
    • Hanson, M.A.1    Stevens, R.C.2
  • 40
    • 2542517864 scopus 로고    scopus 로고
    • Structural analysis of botulinum neurotoxin type E catalytic domain and its mutant Glu212->Gln reveals the pivotal role of the Glu212 carboxylate in the catalytic pathway
    • Agarwal, R.; Eswaramoorthy, S.; Kumaran, D.; Binz, T.; Swaminathan, S. Structural analysis of botulinum neurotoxin type E catalytic domain and its mutant Glu212->Gln reveals the pivotal role of the Glu212 carboxylate in the catalytic pathway. Biochemistry 2004, 43, 6637-6644.
    • (2004) Biochemistry , vol.43 , pp. 6637-6644
    • Agarwal, R.1    Eswaramoorthy, S.2    Kumaran, D.3    Binz, T.4    Swaminathan, S.5
  • 41
    • 24344470084 scopus 로고    scopus 로고
    • Structural analysis of botulinum neurotoxin serotype F light chain: Implications on substrate binding and inhibitor design
    • Agarwal, R.; Binz, T.; Swaminathan, S. Structural analysis of botulinum neurotoxin serotype F light chain: implications on substrate binding and inhibitor design. Biochemistry 2005, 44, 11758-11765.
    • (2005) Biochemistry , vol.44 , pp. 11758-11765
    • Agarwal, R.1    Binz, T.2    Swaminathan, S.3
  • 42
    • 22244456750 scopus 로고    scopus 로고
    • Crystal structure of botulinum neurotoxin type G light chain: Serotype divergence in substrate recognition
    • Arndt, J. W.; Yu, W.; Bi, F.; Stevens, R. C. Crystal structure of botulinum neurotoxin type G light chain: Serotype divergence in substrate recognition. Biochemistry 2005, 44, 9574-9580.
    • (2005) Biochemistry , vol.44 , pp. 9574-9580
    • Arndt, J.W.1    Yu, W.2    Bi, F.3    Stevens, R.C.4
  • 43
    • 33644859288 scopus 로고    scopus 로고
    • Structure of botulinum neurotoxin type D light chain at 1.65 Å resolution: Repercussions for VAMP-2 substrate specificity
    • Arndt, J. W.; Chai, Q.; Christian, T.; Stevens, R. C. Structure of botulinum neurotoxin type D light chain at 1.65 Å resolution: repercussions for VAMP-2 substrate specificity. Biochemistry 2006, 45, 3255-3262.
    • (2006) Biochemistry , vol.45 , pp. 3255-3262
    • Arndt, J.W.1    Chai, Q.2    Christian, T.3    Stevens, R.C.4
  • 44
    • 0029613765 scopus 로고
    • Structure and function of tetanus and botulinum neurotoxins
    • Montecucco, C.; Schiavo, G. Structure and function of tetanus and botulinum neurotoxins. Q. Rev. Biophys. 1995, 28, 423-472.
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 423-472
    • Montecucco, C.1    Schiavo, G.2
  • 45
    • 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.; 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. Protein. Chem. 1994, 13, 49-57.
    • (1994) J. Protein. Chem. , vol.13 , pp. 49-57
    • Krieglstein, K.G.1    DasGupta, B.R.2    Henschen, A.H.3
  • 46
    • 53149122548 scopus 로고    scopus 로고
    • Dichain structure of botulinum neurotoxin: Identification of cleavage sites in types C, D, and F neurotoxin molecules
    • Sagane, Y.; Watanabe, T.; Kouguchi, H.; Sunagawa, H.; Inoue, K.; Fujinaga, Y.; Oguma, K.; Ohyama, T. Dichain structure of botulinum neurotoxin: Identification of cleavage sites in types C, D, and F neurotoxin molecules. J. Protein. Chem. 1999, 18, 885-892.
    • (1999) J. Protein. Chem. , vol.18 , pp. 885-892
    • Sagane, Y.1    Watanabe, T.2    Kouguchi, H.3    Sunagawa, H.4    Inoue, K.5    Fujinaga, Y.6    Oguma, K.7    Ohyama, T.8
  • 47
    • 77958500381 scopus 로고    scopus 로고
    • Light chain separated from the rest of the type a botulinum neurotoxin molecule is the most catalytically active form
    • Gul, N.; Smith, L. A.; Ahmed, S. A. Light chain separated from the rest of the type a botulinum neurotoxin molecule is the most catalytically active form. PLoS One 2010, 5, e12872.
    • (2010) PLoS One , vol.5
    • Gul, N.1    Smith, L.A.2    Ahmed, S.A.3
  • 48
    • 0028922592 scopus 로고
    • Botulinum neurotoxin type C cleaves a single Lys-Ala bond within the carboxyl-terminal region of syntaxins
    • Schiavo, G.; Shone, C. C.; Bennett, M. K.; Scheller, R. H.; Montecucco, C. Botulinum neurotoxin type C cleaves a single Lys-Ala bond within the carboxyl-terminal region of syntaxins. J. Biol. Chem. 1995, 270, 10566-10570.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10566-10570
    • Schiavo, G.1    Shone, C.C.2    Bennett, M.K.3    Scheller, R.H.4    Montecucco, C.5
  • 49
  • 51
    • 54249097347 scopus 로고    scopus 로고
    • The strange case of the botulinum neurotoxin: Using chemistry and biology to modulate the most deadly poison
    • Willis, B.; Eubanks, L. M.; Dickerson, T. J.; Janda, K. D. The strange case of the botulinum neurotoxin: Using chemistry and biology to modulate the most deadly poison. Angew. Chem. Int. Ed. 2008, 47, 8360-8379.
    • (2008) Angew. Chem. Int. Ed. , vol.47 , pp. 8360-8379
    • Willis, B.1    Eubanks, L.M.2    Dickerson, T.J.3    Janda, K.D.4
  • 55
    • 34248594822 scopus 로고    scopus 로고
    • Structures of clostridium botulinum neurotoxin serotype A light chain complexed with smallmolecule inhibitors highlight active-site flexibility
    • Silvaggi, N. R.; Boldt, G. E.; Hixon, M. S.; Kennedy, J. P.; Tzipori, S.; Janda, K. D.; Allen, K. N. Structures of clostridium botulinum neurotoxin serotype A light chain complexed with smallmolecule inhibitors highlight active-site flexibility. Chem. Biol. 2007, 14, 533-542.
    • (2007) Chem. Biol. , vol.14 , pp. 533-542
    • Silvaggi, N.R.1    Boldt, G.E.2    Hixon, M.S.3    Kennedy, J.P.4    Tzipori, S.5    Janda, K.D.6    Allen, K.N.7
  • 56
    • 0029560840 scopus 로고
    • Proteolysis of synthetic peptides by type A botulinum neurotoxin
    • Schmidt, J. J.; Bostian, K. A. Proteolysis of synthetic peptides by type A botulinum neurotoxin. J. Protein Chem. 1995, 14, 703-708.
    • (1995) J. Protein Chem. , vol.14 , pp. 703-708
    • Schmidt, J.J.1    Bostian, K.A.2
  • 58
    • 4043119057 scopus 로고    scopus 로고
    • Progress toward development of an inhalation vaccine against botulinum toxin
    • Park, J. B.; Simpson, L. L. Progress toward development of an inhalation vaccine against botulinum toxin. Expert Rev. Vaccines 2004, 3, 477-487.
    • (2004) Expert Rev. Vaccines , vol.3 , pp. 477-487
    • Park, J.B.1    Simpson, L.L.2
  • 59
    • 0033748727 scopus 로고    scopus 로고
    • Development of vaccines for prevention of botulism
    • Byrne, M. P.; Smith, L. A. Development of vaccines for prevention of botulism. Biochimie 2000, 82, 955-966.
    • (2000) Biochimie , vol.82 , pp. 955-966
    • Byrne, M.P.1    Smith, L.A.2
  • 61
    • 3142735021 scopus 로고    scopus 로고
    • Synaptotagmins I and II act as nerve cell receptors for botulinum neurotoxin G
    • Rummel, A.; Karnath, T.; Henke, T.; Bigalke, H.; Binz, T. Synaptotagmins I and II act as nerve cell receptors for botulinum neurotoxin G. J. Biol. Chem. 2004, 279, 30865-30870.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30865-30870
    • Rummel, A.1    Karnath, T.2    Henke, T.3    Bigalke, H.4    Binz, T.5
  • 63
    • 0025943451 scopus 로고
    • Lectins from Triticum vulgaris and Limax flavus are universal antagonists of botulinum neurotoxin and tetanus toxin
    • Bakry, N.; Kamata, Y.; Simpson, L. L. Lectins from Triticum vulgaris and Limax flavus are universal antagonists of botulinum neurotoxin and tetanus toxin. J. Pharmacol. Exp. Ther. 1991, 258, 830-836.
    • (1991) J. Pharmacol. Exp. Ther. , vol.258 , pp. 830-836
    • Bakry, N.1    Kamata, Y.2    Simpson, L.L.3
  • 65
    • 34248208151 scopus 로고    scopus 로고
    • Biological effects of toosendanin, a triterpenoid extracted from Chinese traditional medicine
    • Shi, Y.-L.; Li, M.-F. Biological effects of toosendanin, a triterpenoid extracted from Chinese traditional medicine. Prog. Neurobiol. 2007, 82, 1-10.
    • (2007) Prog. Neurobiol. , vol.82 , pp. 1-10
    • Shi, Y.-L.1    Li, M.-F.2
  • 66
    • 2942599724 scopus 로고    scopus 로고
    • Cure of experimental botulism and antibotulismic effect of toosendanin
    • Shi, Y.-L.; Wang, Z.-F. Cure of experimental botulism and antibotulismic effect of toosendanin. Acta Pharmacol. Sin. 2004, 25, 839-848.
    • (2004) Acta Pharmacol. Sin. , vol.25 , pp. 839-848
    • Shi, Y.-L.1    Wang, Z.-F.2
  • 69
    • 58949093579 scopus 로고    scopus 로고
    • Function-oriented synthesis applied to the anti-botulinum natural product toosendanin
    • Nakai, Y.; Tepp, W. H.; Dickerson, T. J.; Johnson, E. A.; Janda, K. D. Function-oriented synthesis applied to the anti-botulinum natural product toosendanin. Bioorg. Med. Chem. 2009, 17, 1152-1157.
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 1152-1157
    • Nakai, Y.1    Tepp, W.H.2    Dickerson, T.J.3    Johnson, E.A.4    Janda, K.D.5
  • 70
    • 75149115102 scopus 로고    scopus 로고
    • Toosendanin: Synthesis of the AB-ring and investigations of its anti-botulinum properties (Part II)
    • Nakai, Y.; Pellett, S.; Tepp, W. H.; Johnson, E. A.; Janda, K. D. Toosendanin: Synthesis of the AB-ring and investigations of its anti-botulinum properties (Part II). Bioorg. Med. Chem. 2010, 18, 1280-1287.
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 1280-1287
    • Nakai, Y.1    Pellett, S.2    Tepp, W.H.3    Johnson, E.A.4    Janda, K.D.5
  • 71
    • 38949138457 scopus 로고    scopus 로고
    • Function-oriented synthesis, step economy, and drug design
    • Wender, P. A.; Verma, V. A.; Paxton, T. J.; Pillow, T. H. Function-oriented synthesis, step economy, and drug design. Acc. Chem. Res. 2008, 41, 40-49.
    • (2008) Acc. Chem. Res. , vol.41 , pp. 40-49
    • Wender, P.A.1    Verma, V.A.2    Paxton, T.J.3    Pillow, T.H.4
  • 72
    • 0019956937 scopus 로고
    • The interaction between aminoquinolines and presynaptically acting neurotoxins
    • Simpson, L. L. The interaction between aminoquinolines and presynaptically acting neurotoxins. J. Pharmacol. Exp. Ther. 1982, 222, 43-48.
    • (1982) J. Pharmacol. Exp. Ther. , vol.222 , pp. 43-48
    • Simpson, L.L.1
  • 73
    • 0020522175 scopus 로고
    • Ammonium chloride and methylamine hydrochloride antagonize clostridial neurotoxins
    • Simpson, L. L. Ammonium chloride and methylamine hydrochloride antagonize clostridial neurotoxins. J. Pharmacol. Exp. Ther. 1983, 225, 546-552.
    • (1983) J. Pharmacol. Exp. Ther. , vol.225 , pp. 546-552
    • Simpson, L.L.1
  • 74
    • 0028293577 scopus 로고
    • Inhibition of vacuolar adenosine triphosphatase antagonizes the effects of clostridial neurotoxins but not phospholipase A2 neurotoxins
    • Simpson, L. L.; Coffield, J. A.; Bakry, N. Inhibition of vacuolar adenosine triphosphatase antagonizes the effects of clostridial neurotoxins but not phospholipase A2 neurotoxins. J. Pharmacol. Exp. Ther. 1994, 269, 256-262.
    • (1994) J. Pharmacol. Exp. Ther. , vol.269 , pp. 256-262
    • Simpson, L.L.1    Coffield, J.A.2    Bakry, N.3
  • 80
    • 69949102167 scopus 로고    scopus 로고
    • Pharmacophore-guided lead optimization: The rational design of a non-zinc coordinating, sub-micromolar inhibitor of the botulinum neurotoxin serotype A metalloprotease
    • Burnett, J. C.; Wang, C.; Nuss, J. E.; Nguyen, T. L.; Hermone, A. R.; Schmidt, J. J.; Gussio, R.; Wipf, P.; Bavari, S. Pharmacophore-guided lead optimization: The rational design of a non-zinc coordinating, sub-micromolar inhibitor of the botulinum neurotoxin serotype A metalloprotease. Bioorg. Med. Chem. Lett. 2009, 19, 5811-5813.
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 5811-5813
    • Burnett, J.C.1    Wang, C.2    Nuss, J.E.3    Nguyen, T.L.4    Hermone, A.R.5    Schmidt, J.J.6    Gussio, R.7    Wipf, P.8    Bavari, S.9
  • 82
    • 79251516218 scopus 로고    scopus 로고
    • Butler, M. M.; Cardinale, S. C.; Li, B.; Pai, R.; Ruthel, G.; Nuss, J. E.; Wanner, L. M.; Park, J.-B.; Rich, C.; Basu, A.; Mills, D.; Williams, J. D.; Peet, N. P.; Moir, D.; Bavari, S.; Bowlin, T. L. Unpublished results
    • Butler, M. M.; Cardinale, S. C.; Li, B.; Pai, R.; Ruthel, G.; Nuss, J. E.; Wanner, L. M.; Park, J.-B.; Rich, C.; Basu, A.; Mills, D.; Williams, J. D.; Peet, N. P.; Moir, D.; Bavari, S.; Bowlin, T. L. Unpublished results.
  • 84
    • 70350343490 scopus 로고    scopus 로고
    • Quinolinol and peptide inhibitors of zinc protease in botulinum neurotoxin A: Effects of zinc ion and peptides on inhibition
    • Lai, H.; Feng, M.; Roxas-Duncan, V.; Dakshanamurthy, S.; Smith, L. A.; Yang, D. C. H. Quinolinol and peptide inhibitors of zinc protease in botulinum neurotoxin A: Effects of zinc ion and peptides on inhibition. Arch. Biochem. Biophys. 2009, 491, 75-84.
    • (2009) Arch. Biochem. Biophys. , vol.491 , pp. 75-84
    • Lai, H.1    Feng, M.2    Roxas-Duncan, V.3    Dakshanamurthy, S.4    Smith, L.A.5    Yang, D.C.H.6
  • 85
    • 70450179895 scopus 로고    scopus 로고
    • Potent new small molecule inhibitor of botulinum neurotoxin serotype A endopeptidase developed by synthesis-based computer-aided molecular design
    • Pang, Y.-P.; Vummenthala, A.; Mishra, R. K.; Park, J. G.; Wang, S.; Davis, J.; Millard, C. B.; Schmidt, J. J. Potent new small molecule inhibitor of botulinum neurotoxin serotype A endopeptidase developed by synthesis-based computer-aided molecular design. PLos One 2009, 4, e7730.
    • (2009) PLos One , vol.4
    • Pang, Y.-P.1    Vummenthala, A.2    Mishra, R.K.3    Park, J.G.4    Wang, S.5    Davis, J.6    Millard, C.B.7    Schmidt, J.J.8
  • 86
    • 77956316779 scopus 로고    scopus 로고
    • Small molecules showing significant protection of mice against botulinum neurotoxin serotype A
    • Pang, Y.-P.; Davis, J.; Wang, S.; Park, J. G.; Nambiar, M. P.; Schmidt, J. J.; Millard, C. B. Small molecules showing significant protection of mice against botulinum neurotoxin serotype A. PLoS One 2010, 5, e10129.
    • (2010) PLoS One , vol.5
    • Pang, Y.-P.1    Davis, J.2    Wang, S.3    Park, J.G.4    Nambiar, M.P.5    Schmidt, J.J.6    Millard, C.B.7
  • 87
    • 57549112239 scopus 로고    scopus 로고
    • Three-dimensional database mining identifies a unique chemotype that unites structurally diverse botulinum neurotoxin serotype A inhibitors in a three-zone pharmacophore
    • Hermone, A. R.; Burnett, J. C.; Nuss, J. E.; Tressler, L. E.; Nguyen, T. L.; Solaja, B. A.; Vennerstrom, J. L.; Schmidt, J. J.; Wipf, P.; Bavari, S.; Gussio, R. Three-dimensional database mining identifies a unique chemotype that unites structurally diverse botulinum neurotoxin serotype A inhibitors in a three-zone pharmacophore. ChemMedChem 2008, 3, 1905-1912.
    • (2008) ChemMedChem , vol.3 , pp. 1905-1912
    • Hermone, A.R.1    Burnett, J.C.2    Nuss, J.E.3    Tressler, L.E.4    Nguyen, T.L.5    Solaja, B.A.6    Vennerstrom, J.L.7    Schmidt, J.J.8    Wipf, P.9    Bavari, S.10    Gussio, R.11
  • 88
    • 77958085443 scopus 로고    scopus 로고
    • Pharmacophore refinement guides the rational design of nanomolar-range inhibitors of the botulinum neurotoxin serotype A metalloprotease
    • Nuss, J. E.; Dong, Y.; Wanner, L. M.; Ruthel, G.; Wipf, P.; Gussio, R.; Vennerstrom, J. L.; Bavari, S.; Burnett, J. C. Pharmacophore refinement guides the rational design of nanomolar-range inhibitors of the botulinum neurotoxin serotype A metalloprotease. ACS Med. Chem. Lett. 2010, 1, 301-305.
    • (2010) ACS Med. Chem. Lett. , vol.1 , pp. 301-305
    • Nuss, J.E.1    Dong, Y.2    Wanner, L.M.3    Ruthel, G.4    Wipf, P.5    Gussio, R.6    Vennerstrom, J.L.7    Bavari, S.8    Burnett, J.C.9
  • 89
  • 90
    • 72049088765 scopus 로고    scopus 로고
    • Benzylidene cyclopentenediones: First irreversible inhibitors against botulinum neurotoxin A's zinc endopeptidase
    • Capkova, K.; Hixon, M. S.; Pellett, S.; Barbieri, J. T.; Johnson, E. A.; Janda, K. D. Benzylidene cyclopentenediones: First irreversible inhibitors against botulinum neurotoxin A's zinc endopeptidase. Bioorg. Med. Chem. Lett. 2009, 20, 206-208.
    • (2009) Bioorg. Med. Chem. Lett. , vol.20 , pp. 206-208
    • Capkova, K.1    Hixon, M.S.2    Pellett, S.3    Barbieri, J.T.4    Johnson, E.A.5    Janda, K.D.6
  • 91
    • 0037031282 scopus 로고    scopus 로고
    • A novel mechanism for clostridium botulinum neurotoxin inhibition
    • Eswaramoorthy, S.; Kumaran, D.; Swaminathan, S. A novel mechanism for clostridium botulinum neurotoxin inhibition. Biochemistry 2002, 41, 9795-9802.
    • (2002) Biochemistry , vol.41 , pp. 9795-9802
    • Eswaramoorthy, S.1    Kumaran, D.2    Swaminathan, S.3
  • 92
    • 0032537562 scopus 로고    scopus 로고
    • Efficacy of a novel metalloprotease inhibitor on botulinum neurotoxin B activity
    • Adler, M.; Nicholson, J. D.; Cornille, F.; Hackley, B. E., Jr. Efficacy of a novel metalloprotease inhibitor on botulinum neurotoxin B activity. FEBS Lett. 1998, 429, 234-238.
    • (1998) FEBS Lett. , vol.429 , pp. 234-238
    • Adler, M.1    Nicholson, J.D.2    Cornille, F.3    Hackley Jr., B.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.