메뉴 건너뛰기




Volumn 2, Issue 1, 2010, Pages 1-9

Protein domain analysis of C. botulinum type a neurotoxin and its relationship with other botulinum serotypes

Author keywords

BoNT serotypes; Coiled coil domain; Neurotoxin; Phylogenetic; Protein domain

Indexed keywords

BOTULINUM TOXIN; BOTULINUM TOXIN A; BOTULINUM TOXIN B; BOTULINUM TOXIN C; BOTULINUM TOXIN D; BOTULINUM TOXIN E; BOTULINUM TOXIN F; BOTULINUM TOXIN G; TETANUS TOXIN; UNCLASSIFIED DRUG; SYNAPTOSOMAL ASSOCIATED PROTEIN 25;

EID: 79952059061     PISSN: None     EISSN: 20726651     Source Type: Journal    
DOI: 10.3390/toxins2010001     Document Type: Article
Times cited : (3)

References (27)
  • 1
    • 34250004607 scopus 로고    scopus 로고
    • Neuromuscular paralysis and recovery in mice injected with botulinum neurotoxins A and C
    • Morbiato, L.; Carli, L.; Johnson, E.A.; Montecucco, C.; Molgo, J.; Rossetto, O. Neuromuscular paralysis and recovery in mice injected with botulinum neurotoxins A and C. Eur. J. Neurosci. 2007, 25, 2697-2704.
    • (2007) Eur. J. Neurosci , vol.25 , pp. 2697-2704
    • Morbiato, L.1    Carli, L.2    Johnson, E.A.3    Montecucco, C.4    Molgo, J.5    Rossetto, O.6
  • 2
    • 0033065263 scopus 로고    scopus 로고
    • Structure-function relationship of clostridial neurotoxins
    • Li, L.; Singh, B.R. Structure-function relationship of clostridial neurotoxins. J. Toxicol. Toxin Rev. 1999, 18, 95-112.
    • (1999) J. Toxicol. Toxin Rev , vol.18 , pp. 95-112
    • Li, L.1    Singh, B.R.2
  • 3
    • 0027248876 scopus 로고
    • Tetanus and botulism neurotoxins: A new group of zinc proteases
    • Montecucco, C.; Schiavo, G. Tetanus and botulism neurotoxins: A new group of zinc proteases. Trends Biochem. Sci. 1993, 18, 324-327.
    • (1993) Trends Biochem. Sci , vol.18 , pp. 324-327
    • Montecucco, C.1    Schiavo, G.2
  • 5
    • 0034653908 scopus 로고    scopus 로고
    • The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges
    • Burkhard, P.; Kemmerer, R.A.; Steinmetz, M.O.; Bourenkov, G.P.; Aebi, U. The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges. Structure 2000, 8, 223-230.
    • (2000) Structure , vol.8 , pp. 223-230
    • Burkhard, P.1    Kemmerer, R.A.2    Steinmetz, M.O.3    Bourenkov, G.P.4    Aebi, U.5
  • 6
    • 0035252931 scopus 로고    scopus 로고
    • Coiled coils: A highly versatile protein folding motif
    • Burkhard, P.; Stetefeld, J.; Strelkov, S.V. Coiled coils: A highly versatile protein folding motif. Trends. Cell. Biol. 2001, 11, 82-88.
    • (2001) Trends. Cell. Biol , vol.11 , pp. 82-88
    • Burkhard, P.1    Stetefeld, J.2    Strelkov, S.V.3
  • 7
    • 0033884053 scopus 로고    scopus 로고
    • Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B
    • Swaminathan, S.; Eswaramoorthy, S. Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B. Nat. Struct. Biol. 2000, 7, 693-699.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 693-699
    • Swaminathan, S.1    Eswaramoorthy, S.2
  • 8
    • 0033887403 scopus 로고    scopus 로고
    • Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 Å resolution
    • Hanson, M.A.; Stevens, R.C. Cocrystal 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
  • 9
    • 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
  • 11
    • 0033520494 scopus 로고    scopus 로고
    • Sequence homology and structural analysis of the clostridial neurotoxins
    • Lacy, D.B.; Stevens, R.C. Sequence homology and structural analysis of the clostridial neurotoxins. J. Mol. Biol. 1999, 291, 1091-1104.
    • (1999) J. Mol. Biol , vol.291 , pp. 1091-1104
    • Lacy, D.B.1    Stevens, R.C.2
  • 12
    • 34848840291 scopus 로고    scopus 로고
    • Botulinum neurotoxin heavy chain belt as an intramolecular chaperone for the light chain
    • Brunger, A.T.; Breidenbach, M.A.; Jin, R.; Fischer, A.; Santos, J.S.; Montal, M. Botulinum neurotoxin heavy chain belt as an intramolecular chaperone for the light chain. PLoS Pathog. 2007, 3, 1191-1194.
    • (2007) PLoS Pathog , vol.3 , pp. 1191-1194
    • Brunger, A.T.1    Breidenbach, M.A.2    Jin, R.3    Fischer, A.4    Santos, J.S.5    Montal, M.6
  • 13
    • 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
  • 14
    • 0032992422 scopus 로고    scopus 로고
    • Membrane channel activity and translocation of tetanus and botulinum neurotoxins
    • Labeda, F.J.; Singh, B.R. Membrane channel activity and translocation of tetanus and botulinum neurotoxins. J. Toxicol.-Toxin Rev. 1999, 18, 45-76.
    • (1999) J. Toxicol.-Toxin Rev , vol.18 , pp. 45-76
    • Labeda, F.J.1    Singh, B.R.2
  • 15
    • 0028108437 scopus 로고
    • Quaternary structure of botulinum and tetanus neurotoxins as probed by chemical cross-linking and native gel electrophoresis
    • Ledoux, D.N.; Be, X.; Singh, B.R. Quaternary structure of botulinum and tetanus neurotoxins as probed by chemical cross-linking and native gel electrophoresis. Toxicon 1994, 32, 1095-1104.
    • (1994) Toxicon , vol.32 , pp. 1095-1104
    • Ledoux, D.N.1    Be, X.2    Singh, B.R.3
  • 16
    • 0023658427 scopus 로고
    • A 50-kDa fragment from the NH2 terminal of the heavy subunit of Clostridium Botulinum type A neurotoxin forms channels in lipid vesicles
    • Shone, C.C.; Hambleton, P.; Melling, J. A 50-kDa fragment from the NH2 terminal of the heavy subunit of Clostridium Botulinum type A neurotoxin forms channels in lipid vesicles. Eur. J. Biochem. 1987, 167, 175-180.
    • (1987) Eur. J. Biochem , vol.167 , pp. 175-180
    • Shone, C.C.1    Hambleton, P.2    Melling, J.3
  • 17
    • 0037015327 scopus 로고    scopus 로고
    • Spectroscopic analysis of low pH and lipid-induced structural changes in type A botulinum neurotoxin relevant to membrane channel formation and translocation
    • Fu, F.N.; Busath, D.D.; Singh B.R. Spectroscopic analysis of low pH and lipid-induced structural changes in type A botulinum neurotoxin relevant to membrane channel formation and translocation. Biophys. Chem. 2002, 99, 17-29.
    • (2002) Biophys. Chem , vol.99 , pp. 17-29
    • Fu, F.N.1    Busath, D.D.2    Singh, B.R.3
  • 18
    • 34848840291 scopus 로고    scopus 로고
    • Botulinum neurotoxin heavy chain belt as an intramolecular chaperone for the light chain
    • Brunger, A.T.; Breidenbach, M.A.; Jin, R.; Fischer, A.; Santos, J.S.; Montal, M. Botulinum neurotoxin heavy chain belt as an intramolecular chaperone for the light chain. PLoS Pathog. 2007, 3, 1191-1194.
    • (2007) PLoS Pathog , vol.3 , pp. 1191-1194
    • Brunger, A.T.1    Breidenbach, M.A.2    Jin, R.3    Fischer, A.4    Santos, J.S.5    Montal, M.6
  • 19
    • 65949090949 scopus 로고    scopus 로고
    • Cell entry strategy of clostridial neurotoxins
    • Binz, T.; Rummel, A. Cell entry strategy of clostridial neurotoxins. J. Neurochem. 2009, 109, 1584-1595.
    • (2009) J. Neurochem , vol.109 , pp. 1584-1595
    • Binz, T.1    Rummel, A.2
  • 20
    • 0027282605 scopus 로고
    • Direct visualization of botulinum neurotoxin- induced channels in phospholipid vesicles
    • Schmid, M.F.; Robinson, J.P.; DasGupta, B.R. Direct visualization of botulinum neurotoxin- induced channels in phospholipid vesicles. Nature 1993, 364, 827-830.
    • (1993) Nature , vol.364 , pp. 827-830
    • Schmid, M.F.1    Robinson, J.P.2    Dasgupta, B.R.3
  • 21
    • 0022485787 scopus 로고
    • Ion-conducting channels produced by botulinum toxin in planar lipid membranes
    • Donovan, J.J.; Middlebrook, J.L. Ion-conducting channels produced by botulinum toxin in planar lipid membranes. Biochemistry 1986, 25, 2872-2876.
    • (1986) Biochemistry , vol.25 , pp. 2872-2876
    • Donovan, J.J.1    Middlebrook, J.L.2
  • 23
    • 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
  • 24
    • 0026605537 scopus 로고
    • CLUSTAL V: Improved software for multiple sequence alignment
    • Higgins, D.G.; Bleasby, A.J.; Fuchs, R. CLUSTAL V: Improved software for multiple sequence alignment. Bioinformatics 1992, 8, 189-191.
    • (1992) Bioinformatics , vol.8 , pp. 189-191
    • Higgins, D.G.1    Bleasby, A.J.2    Fuchs, R.3
  • 27
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J.D.; Gibson, T.J.; Plewniak, F.; Jeanmougin, F.; Higgins, D.G. The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 1997, 25, 4876-4882.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.