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Volumn , Issue , 2009, Pages 705-720

Botulinus Toxin, Tetanus Toxin, and Anthrax Lethal Factor Inhibitors

Author keywords

Botulinus toxin, tetanus toxin and anthrax lethal factor inhibitors; Inhibitors of BoNT and TeNT zinc proteases; Tetanus and botulinum neurotoxins Clostridium tetani and Clostridium botulinum

Indexed keywords


EID: 79958185412     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470508169.ch29     Document Type: Chapter
Times cited : (8)

References (42)
  • 2
    • 0034121745 scopus 로고    scopus 로고
    • Howbotulinum and tetanus neurotoxins block neurotransmitter release
    • Humeau,Y.; Doussau, F.; Grant, N. J.; Poulain, B. Howbotulinum and tetanus neurotoxins block neurotransmitter release. Biochimie 2000, 82, 427-446.
    • (2000) Biochimie , vol.82 , pp. 427-446
    • Humeau, Y.1    Doussau, F.2    Grant, N.J.3    Poulain, B.4
  • 5
    • 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
  • 6
    • 0033884053 scopus 로고    scopus 로고
    • Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B
    • Swaminathan, S.; Eswaramoorthy, S. Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B. Nat. Struct. Biol. 2000, 7, 617-619.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 617-619
    • Swaminathan, S.1    Eswaramoorthy, S.2
  • 7
    • 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
  • 8
    • 33644859288 scopus 로고    scopus 로고
    • Structure of botulinum neurotoxin type D light chain at 1.65Åresolution: 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 1.65Åresolution: 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
  • 9
    • 0033887403 scopus 로고    scopus 로고
    • Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0Åresolution
    • Hanson, M. A.; Stevens, R. C. Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0Åresolution. Nat. Struct. Biol. 2000, 7, 687-692.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 687-692
    • Hanson, M.A.1    Stevens, R.C.2
  • 10
    • 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
  • 11
    • 51049112074 scopus 로고    scopus 로고
    • Substrate recognition ofVAMP-2 by botulinumneurotoxin B and tetanus neurotoxin
    • Chen, S.;Hall, C.; Barbieri, J. T. Substrate recognition ofVAMP-2 by botulinumneurotoxin B and tetanus neurotoxin. J. Biol. Chem. 2008, 283, 21153-21159.
    • (2008) J. Biol. Chem. , vol.283 , pp. 21153-21159
    • Chen, S.1    Hall, C.2    Barbieri, J.T.3
  • 12
    • 19344372277 scopus 로고    scopus 로고
    • Structural analysis of the catalytic domain of tetanus neurotoxin
    • Rao, K. N.; Kumaran, D.; Binz, T.; Swaminathan, S. Structural analysis of the catalytic domain of tetanus neurotoxin. Toxicon 2005, 45, 929-939.
    • (2005) Toxicon , vol.45 , pp. 929-939
    • Rao, K.N.1    Kumaran, D.2    Binz, T.3    Swaminathan, S.4
  • 13
    • 0032572832 scopus 로고    scopus 로고
    • b-Amino-thiols inhibit the zinc metallopeptidase activity of tetanus toxin light chain
    • Martin, L.; Cornille, F.; Coric, P.; Roques, B. P.; Fournié-Zaluski, M. C. b-Amino-thiols inhibit the zinc metallopeptidase activity of tetanus toxin light chain. J. Med. Chem. 1998, 41, 3450-3460.
    • (1998) J. Med. Chem. , vol.41 , pp. 3450-3460
    • Martin, L.1    Cornille, F.2    Coric, P.3    Roques, B.P.4    Fournié-Zaluski, M.C.5
  • 15
    • 38849143765 scopus 로고    scopus 로고
    • Carbonic anhydrases: novel therapeutic applications for inhibitors and activators
    • Supuran, C. T. Carbonic anhydrases: novel therapeutic applications for inhibitors and activators. Nat. Rev. Drug Discov. 2008, 7, 168-181.
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 168-181
    • Supuran, C.T.1
  • 18
    • 0034612326 scopus 로고    scopus 로고
    • A quantitative study of the interactions of Bacillus anthracis edema factor and lethal factor with activated protective antigen
    • Elliott, J. L.; Mogridge, J.; Collier, R. J. A quantitative study of the interactions of Bacillus anthracis edema factor and lethal factor with activated protective antigen. Biochemistry 2000, 39, 6706-6713.
    • (2000) Biochemistry , vol.39 , pp. 6706-6713
    • Elliott, J.L.1    Mogridge, J.2    Collier, R.J.3
  • 19
    • 4243609533 scopus 로고    scopus 로고
    • Anthrax toxin lethal factor
    • In Handbook of Proteolytic Enzymes (CD-ROM); Barrett, A. J.; Rawlings, N. D.; Woessner, J. F. Jr.,Eds.; Academic Press: London, Chapter 511
    • Leppla, S. H. Anthrax toxin lethal factor. In Handbook of Proteolytic Enzymes (CD-ROM); Barrett, A. J.; Rawlings, N. D.; Woessner, J. F. Jr.,Eds.; Academic Press: London, 1998; Chapter 511.
    • (1998)
    • Leppla, S.H.1
  • 21
    • 0032581369 scopus 로고    scopus 로고
    • Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages
    • Vitale, G.; Pellizzari, R.; Recchi, C.; Napolitani, G.; Mock, M.; Montecucco, C. Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages. Biochem. Biophys. Res. Commun. 1998, 248, 706-711.
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 706-711
    • Vitale, G.1    Pellizzari, R.2    Recchi, C.3    Napolitani, G.4    Mock, M.5    Montecucco, C.6
  • 22
    • 0032755353 scopus 로고    scopus 로고
    • Anthrax lethal factor cleaves MKK3 in macrophages and inhibits the LPS/IFNgamma-induced release of NO and TNF-alpha
    • Pellizzari, R.; Guidi-Rontani, C.; Vitale, G.; Mock, M.; Montecucco, C. Anthrax lethal factor cleaves MKK3 in macrophages and inhibits the LPS/IFNgamma-induced release of NO and TNF-alpha. FEBS Lett. 1999, 462, 199-204.
    • (1999) FEBS Lett. , vol.462 , pp. 199-204
    • Pellizzari, R.1    Guidi-Rontani, C.2    Vitale, G.3    Mock, M.4    Montecucco, C.5
  • 23
    • 0029903392 scopus 로고    scopus 로고
    • The cytotoxic activity of Bacillus anthracis lethal factor is inhibited by leukotriene A4 hydrolase and metallopeptidase inhibitors
    • Menard, A.; Papini, E.; Mock, M.; Montecucco, C. The cytotoxic activity of Bacillus anthracis lethal factor is inhibited by leukotriene A4 hydrolase and metallopeptidase inhibitors. Biochem. J. 1996, 320, 687-691.
    • (1996) Biochem. J. , vol.320 , pp. 687-691
    • Menard, A.1    Papini, E.2    Mock, M.3    Montecucco, C.4
  • 25
    • 0346433832 scopus 로고    scopus 로고
    • Tyrosine-728 and glutamic acid-735 are essential for the metalloproteolytic activity of the lethal factor of Bacillus anthracis
    • Tonello, F.; Naletto, L.; Romanello, V.; Dal Molin, F.; Montecucco, C. Tyrosine-728 and glutamic acid-735 are essential for the metalloproteolytic activity of the lethal factor of Bacillus anthracis. Biochem. Biophys. Res. Commun. 2004, 313, 496-502.
    • (2004) Biochem. Biophys. Res. Commun. , vol.313 , pp. 496-502
    • Tonello, F.1    Naletto, L.2    Romanello, V.3    Dal Molin, F.4    Montecucco, C.5
  • 26
    • 0043167816 scopus 로고    scopus 로고
    • Design of weakly basic thrombin inhibitors incorporating novel P1 binding functions: Molecular and X-ray crystallographic studies
    • De Simone, G.; Menchise, V.; Omaggio, S.; Pedone, C.; Scozzafava, A.; Supuran, C. T. Design of weakly basic thrombin inhibitors incorporating novel P1 binding functions: Molecular and X-ray crystallographic studies. Biochemistry 2003, 42, 9013-9021.
    • (2003) Biochemistry , vol.42 , pp. 9013-9021
    • De Simone, G.1    Menchise, V.2    Omaggio, S.3    Pedone, C.4    Scozzafava, A.5    Supuran, C.T.6
  • 27
    • 39449131198 scopus 로고    scopus 로고
    • Discovery and development of anthrax lethal factor metalloproteinase inhibitors
    • Turk, B. E. Discovery and development of anthrax lethal factor metalloproteinase inhibitors. Curr. Pharm. Biotechnol. 2008, 9, 24-33.
    • (2008) Curr. Pharm. Biotechnol. , vol.9 , pp. 24-33
    • Turk, B.E.1
  • 32
    • 2542627454 scopus 로고    scopus 로고
    • Chemical screening by mass spectrometry to identify inhibitors of anthrax lethal factor
    • Min, D. H.; Tang, W. J.; Mrksich, M. Chemical screening by mass spectrometry to identify inhibitors of anthrax lethal factor. Nat. Biotechnol. 2004, 22, 717-723.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 717-723
    • Min, D.H.1    Tang, W.J.2    Mrksich, M.3
  • 33
    • 0037493019 scopus 로고    scopus 로고
    • Structure-based inhibitor discovery against adenylyl cyclase toxins from pathogenic bacteria that cause anthrax and whooping cough
    • Soelaiman, S.;Wei, B. Q.; Bergson, P.; Lee, Y. S.; Shen, Y.; Mrksich, M.; Shoichet, B. K.; Tang, W. J. Structure-based inhibitor discovery against adenylyl cyclase toxins from pathogenic bacteria that cause anthrax and whooping cough. J. Biol. Chem. 2003, 278, 25990-25997.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25990-25997
    • Soelaiman, S.1    Wei, B.Q.2    Bergson, P.3    Lee, Y.S.4    Shen, Y.5    Mrksich, M.6    Shoichet, B.K.7    Tang, W.J.8
  • 34
    • 0018951535 scopus 로고
    • Botulinum toxin injection into extraocular muscles as an alternative to strabismus surgery
    • Scott, A. B. Botulinum toxin injection into extraocular muscles as an alternative to strabismus surgery. Ophthalmology 1980, 87, 1044-1049.
    • (1980) Ophthalmology , vol.87 , pp. 1044-1049
    • Scott, A.B.1
  • 36
    • 0034081445 scopus 로고    scopus 로고
    • Botulinum toxin type A for palmar and digital hyperhidrosis
    • Solomon, B. A.; Hayman, R. Botulinum toxin type A for palmar and digital hyperhidrosis. J. Am. Acad. Dermatol. 2000, 42, 1026-1029.
    • (2000) J. Am. Acad. Dermatol. , vol.42 , pp. 1026-1029
    • Solomon, B.A.1    Hayman, R.2
  • 37
    • 48949105287 scopus 로고    scopus 로고
    • Molecular biology of botulinum neurotoxin serotype A: a cosmetic perspective
    • Eapen, B. R. Molecular biology of botulinum neurotoxin serotype A: a cosmetic perspective. J. Cosmet. Dermatol. 2008, 7, 221-225.
    • (2008) J. Cosmet. Dermatol. , vol.7 , pp. 221-225
    • Eapen, B.R.1
  • 38
    • 49549084795 scopus 로고    scopus 로고
    • Use of botulinum toxin A in adult neurological disorders: efficacy, tolerability and safety
    • Schulte-Mattler, W. J. Use of botulinum toxin A in adult neurological disorders: efficacy, tolerability and safety. CNS Drugs 2008, 22, 725-738.
    • (2008) CNS Drugs , vol.22 , pp. 725-738
    • Schulte-Mattler, W.J.1
  • 40
    • 57249084772 scopus 로고    scopus 로고
    • Botulinum neurotoxins in the treatment of refractory pain
    • Jabbari, B. Botulinum neurotoxins in the treatment of refractory pain. Nat. Clin. Pract. Neurol. 2008, 4, 676-685.
    • (2008) Nat. Clin. Pract. Neurol. , vol.4 , pp. 676-685
    • Jabbari, B.1
  • 41
    • 57349089170 scopus 로고    scopus 로고
    • Botulinum toxin for urogenital conditions
    • Eccleston, K. J.;Woolley, P.D. Botulinum toxin for urogenital conditions. Int. J. STDAIDS 2008, 19, 797-799.
    • (2008) Int. J. STDAIDS , vol.19 , pp. 797-799
    • Eccleston, K.J.1    Woolley, P.D.2
  • 42
    • 48149111864 scopus 로고    scopus 로고
    • Botulinum toxin: future developments
    • De Ridder,D. Botulinum toxin: future developments. BJU Int. 2008, 102 (Suppl. 1), 20-22.
    • (2008) BJU Int , vol.102 , Issue.SUPPL. 1 , pp. 20-22
    • De Ridder, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.