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Volumn 430, Issue 1, 2013, Pages 38-42

Time course and temperature dependence of the membrane translocation of tetanus and botulinum neurotoxins C and D in neurons

Author keywords

Botulinum neurotoxin; Botulism; Tetanus; Tetanus neurotoxin; Time course

Indexed keywords

BOTULINUM TOXIN; BOTULINUM TOXIN C; BOTULINUM TOXIN D; SNARE PROTEIN; TETANUS TOXIN; TETANUS TOXIN C; TETANUS TOXIN D; UNCLASSIFIED DRUG;

EID: 84872394663     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.11.048     Document Type: Article
Times cited : (28)

References (60)
  • 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., et al. Crystal structure of botulinum neurotoxin type A and implications for toxicity. Natl. Struct. Biol. 1998, 5:898-902.
    • (1998) Natl. Struct. Biol. , vol.5 , pp. 898-902
    • Lacy, D.B.1    Tepp, W.2    Cohen, A.C.3
  • 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. Natl. Struct. Biol. 2000, 7:693-699.
    • (2000) Natl. Struct. Biol. , vol.7 , pp. 693-699
    • Swaminathan, S.1    Eswaramoorthy, S.2
  • 7
    • 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
  • 8
    • 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., et al. 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
  • 9
    • 77953642001 scopus 로고    scopus 로고
    • Botulinum neurotoxin: a marvel of protein design
    • Montal M. Botulinum neurotoxin: a marvel of protein design. Annu. Rev. Biochem. 2010, 79:591-617.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 591-617
    • Montal, M.1
  • 10
    • 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
  • 11
    • 59649101806 scopus 로고    scopus 로고
    • The N-terminal half of the receptor domain of botulinum neurotoxin A binds to microdomains of the plasma membrane
    • Muraro L., Tosatto S., Motterlini L., et al. The N-terminal half of the receptor domain of botulinum neurotoxin A binds to microdomains of the plasma membrane. Biochem. Biophys. Res. Commun. 2009, 380:76-80.
    • (2009) Biochem. Biophys. Res. Commun. , vol.380 , pp. 76-80
    • Muraro, L.1    Tosatto, S.2    Motterlini, L.3
  • 12
    • 84857049268 scopus 로고    scopus 로고
    • The receptor binding domain of botulinum neurotoxin serotype C binds phosphoinositides
    • Zhang Y., Varnum S.M. The receptor binding domain of botulinum neurotoxin serotype C binds phosphoinositides. Biochimie 2012, 94:920-923.
    • (2012) Biochimie , vol.94 , pp. 920-923
    • Zhang, Y.1    Varnum, S.M.2
  • 13
    • 0037459107 scopus 로고    scopus 로고
    • Two carbohydrate binding sites in the H(CC)-domain of tetanus neurotoxin are required for toxicity
    • Rummel A., Bade S., Alves J., et al. Two carbohydrate binding sites in the H(CC)-domain of tetanus neurotoxin are required for toxicity. J. Mol. Biol. 2003, 326:835-847.
    • (2003) J. Mol. Biol. , vol.326 , pp. 835-847
    • Rummel, A.1    Bade, S.2    Alves, J.3
  • 14
    • 46849085158 scopus 로고    scopus 로고
    • Molecular basis for tetanus toxin coreceptor interactions
    • Chen C., Baldwin M.R., Barbieri J.T. Molecular basis for tetanus toxin coreceptor interactions. Biochemistry 2008, 47:7179-7186.
    • (2008) Biochemistry , vol.47 , pp. 7179-7186
    • Chen, C.1    Baldwin, M.R.2    Barbieri, J.T.3
  • 15
    • 70350371732 scopus 로고    scopus 로고
    • Gangliosides as high affinity receptors for tetanus neurotoxin
    • Chen C., Fu Z., Kim J.J., Barbieri J.T., et al. Gangliosides as high affinity receptors for tetanus neurotoxin. J. Biol. Chem. 2009, 284:26569-26577.
    • (2009) J. Biol. Chem. , vol.284 , pp. 26569-26577
    • Chen, C.1    Fu, Z.2    Kim, J.J.3    Barbieri, J.T.4
  • 16
    • 79959549721 scopus 로고    scopus 로고
    • The biological activity of botulinum neurotoxin type C is dependent upon novel types of ganglioside binding sites
    • Strotmeier J., Gu S., Jutzi S., Mahrhold S., et al. The biological activity of botulinum neurotoxin type C is dependent upon novel types of ganglioside binding sites. Mol. Microbiol. 2011, 81:143-156.
    • (2011) Mol. Microbiol. , vol.81 , pp. 143-156
    • Strotmeier, J.1    Gu, S.2    Jutzi, S.3    Mahrhold, S.4
  • 17
    • 77956591091 scopus 로고    scopus 로고
    • Identification of a unique ganglioside binding loop within botulinum neurotoxins C and D-SA
    • Karalewitz A.P., Kroken A.R., Fu Z., et al. Identification of a unique ganglioside binding loop within botulinum neurotoxins C and D-SA. Biochemistry 2010, 49:8117-8126.
    • (2010) Biochemistry , vol.49 , pp. 8117-8126
    • Karalewitz, A.P.1    Kroken, A.R.2    Fu, Z.3
  • 18
    • 77957906825 scopus 로고    scopus 로고
    • Botulinum neurotoxin serotype D attacks neurons via two carbohydrate-binding sites in a ganglioside-dependent manner
    • Strotmeier J., Lee K., Volker A.K., et al. Botulinum neurotoxin serotype D attacks neurons via two carbohydrate-binding sites in a ganglioside-dependent manner. Biochem. J. 2010, 431:207-216.
    • (2010) Biochem. J. , vol.431 , pp. 207-216
    • Strotmeier, J.1    Lee, K.2    Volker, A.K.3
  • 19
    • 78650892621 scopus 로고    scopus 로고
    • Crystal structure of the receptor binding domain of the botulinum C-D mosaic neurotoxin reveals potential roles of lysines 1118 and 1136 in membrane interactions
    • Zhang Y., Buchko G.W., Qin L., et al. Crystal structure of the receptor binding domain of the botulinum C-D mosaic neurotoxin reveals potential roles of lysines 1118 and 1136 in membrane interactions. Biochem. Biophys. Res. Commun. 2011, 404:407-412.
    • (2011) Biochem. Biophys. Res. Commun. , vol.404 , pp. 407-412
    • Zhang, Y.1    Buchko, G.W.2    Qin, L.3
  • 20
    • 81555216752 scopus 로고    scopus 로고
    • Unique ganglioside binding by botulinum neurotoxins C and D-SA
    • Kroken A.R., Karalewitz A.P., Fu Z., et al. Unique ganglioside binding by botulinum neurotoxins C and D-SA. FEBS J. 2011, 278:4486-4496.
    • (2011) FEBS J. , vol.278 , pp. 4486-4496
    • Kroken, A.R.1    Karalewitz, A.P.2    Fu, Z.3
  • 21
    • 80054105849 scopus 로고    scopus 로고
    • Double anchorage to the membrane and intact inter-chain disulfide bond are required for the low pH induced entry of tetanus and botulinum neurotoxins into neurons
    • Pirazzini M., Rossetto O., Bolognese P., et al. Double anchorage to the membrane and intact inter-chain disulfide bond are required for the low pH induced entry of tetanus and botulinum neurotoxins into neurons. Cell Microbiol. 2011, 13:1731-1743.
    • (2011) Cell Microbiol. , vol.13 , pp. 1731-1743
    • Pirazzini, M.1    Rossetto, O.2    Bolognese, P.3
  • 22
    • 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
  • 23
    • 0027946632 scopus 로고
    • Bafilomycin A1 inhibits the action of tetanus toxin in spinal cord neurons in cell culture
    • Williamson L.C., Neale E.A. Bafilomycin A1 inhibits the action of tetanus toxin in spinal cord neurons in cell culture. J. Neurochem. 1994, 63:2342-2345.
    • (1994) J. Neurochem. , vol.63 , pp. 2342-2345
    • Williamson, L.C.1    Neale, E.A.2
  • 24
    • 0345570658 scopus 로고
    • Channels formed by botulinum, tetanus, and diphtheria toxins in planar lipid bilayers: relevance to translocation of proteins across membranes
    • Hoch D.H., Romero-Mira M., Ehrlich B.E., et al. Channels formed by botulinum, tetanus, and diphtheria toxins in planar lipid bilayers: relevance to translocation of proteins across membranes. Proc. Natl. Acad. Sci. USA 1985, 82:1692-1696.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1692-1696
    • Hoch, D.H.1    Romero-Mira, M.2    Ehrlich, B.E.3
  • 25
    • 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
  • 26
    • 0023662110 scopus 로고
    • The N-terminal half of the heavy chain of botulinum type A neurotoxin forms channels in planar phospholipid bilayers
    • Blaustein R.O., Germann W.J., Finkelstein A., et al. The N-terminal half of the heavy chain of botulinum type A neurotoxin forms channels in planar phospholipid bilayers. FEBS Lett. 1987, 226:115-120.
    • (1987) FEBS Lett. , vol.226 , pp. 115-120
    • Blaustein, R.O.1    Germann, W.J.2    Finkelstein, A.3
  • 27
    • 0023658427 scopus 로고
    • A 50-kDa fragment from the NH2-terminus 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-terminus 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
  • 28
    • 80052994116 scopus 로고    scopus 로고
    • Receptor binding enables botulinum neurotoxin B to sense low pH for translocation channel assembly
    • Sun S., Suresh S., Liu H., et al. Receptor binding enables botulinum neurotoxin B to sense low pH for translocation channel assembly. Cell Host Microb. 2011, 10:237-247.
    • (2011) Cell Host Microb. , vol.10 , pp. 237-247
    • Sun, S.1    Suresh, S.2    Liu, H.3
  • 29
    • 0037222077 scopus 로고    scopus 로고
    • Translocation of botulinum neurotoxin light chain protease through the heavy chain channel
    • Koriazova L.K., Montal M. Translocation of botulinum neurotoxin light chain protease through the heavy chain channel. Nat. Struct. Biol. 2003, 10:13-18.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 13-18
    • Koriazova, L.K.1    Montal, M.2
  • 30
    • 35748961106 scopus 로고    scopus 로고
    • Crucial role of the disulfide bridge between botulinum neurotoxin light and heavy chains in protease translocation across membranes
    • Fischer A., Montal M. Crucial role of the disulfide bridge between botulinum neurotoxin light and heavy chains in protease translocation across membranes. J. Biol. Chem. 2007, 282:29604-29611.
    • (2007) J. Biol. Chem. , vol.282 , pp. 29604-29611
    • Fischer, A.1    Montal, M.2
  • 31
    • 34547509346 scopus 로고    scopus 로고
    • Single molecule detection of intermediates during botulinum neurotoxin translocation across membranes
    • Fischer A., Montal M. Single molecule detection of intermediates during botulinum neurotoxin translocation across membranes. Proc. Natl. Acad. Sci. USA 2007, 104:10447-10452.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 10447-10452
    • Fischer, A.1    Montal, M.2
  • 32
    • 58149252452 scopus 로고    scopus 로고
    • Botulinum neurotoxin devoid of receptor binding domain translocates active protease
    • Fischer A., Mushrush D.J., Lacy D.B., et al. Botulinum neurotoxin devoid of receptor binding domain translocates active protease. PLoS Pathog. 2008, 4.
    • (2008) PLoS Pathog. , vol.4
    • Fischer, A.1    Mushrush, D.J.2    Lacy, D.B.3
  • 33
    • 68849127717 scopus 로고    scopus 로고
    • Translocation of botulinum neurotoxin light chain protease by the heavy chain protein-conducting channel
    • Montal M. Translocation of botulinum neurotoxin light chain protease by the heavy chain protein-conducting channel. Toxicon 2009, 54:565-569.
    • (2009) Toxicon , vol.54 , pp. 565-569
    • Montal, M.1
  • 34
    • 0028355349 scopus 로고
    • Tetanus and botulinum neurotoxins are zinc proteases specific for components of the neuroexocytosis apparatus
    • Schiavo G., Rossetto O., Benfenati F., et al. Tetanus and botulinum neurotoxins are zinc proteases specific for components of the neuroexocytosis apparatus. Ann. NY Acad. Sci. 1994, 710:65-75.
    • (1994) Ann. NY Acad. Sci. , vol.710 , pp. 65-75
    • Schiavo, G.1    Rossetto, O.2    Benfenati, F.3
  • 35
    • 0028268948 scopus 로고
    • Clostridial neurotoxins: new tools for dissecting exocytosis
    • Niemann H., Blasi J., Jahn R. Clostridial neurotoxins: new tools for dissecting exocytosis. Trends Cell Biol. 1994, 4:179-185.
    • (1994) Trends Cell Biol. , vol.4 , pp. 179-185
    • Niemann, H.1    Blasi, J.2    Jahn, R.3
  • 36
    • 0032953048 scopus 로고    scopus 로고
    • Proteolysis of SNAP-25 isoforms by botulinum neurotoxin types A, C, and E: domains and amino acid residues controlling the formation of enzyme-substrate complexes and cleavage
    • Vaidyanathan V.V., Yoshino K., Jahnz M., et al. Proteolysis of SNAP-25 isoforms by botulinum neurotoxin types A, C, and E: domains and amino acid residues controlling the formation of enzyme-substrate complexes and cleavage. J. Neurochem. 1999, 72:327-337.
    • (1999) J. Neurochem. , vol.72 , pp. 327-337
    • Vaidyanathan, V.V.1    Yoshino, K.2    Jahnz, M.3
  • 37
    • 0032776446 scopus 로고    scopus 로고
    • Persistence of botulinum neurotoxin action in cultured spinal cord cells
    • Keller J.E., Neale E.A., Oyler G., Adler M., et al. Persistence of botulinum neurotoxin action in cultured spinal cord cells. FEBS Lett. 1999, 456:137-142.
    • (1999) FEBS Lett. , vol.456 , pp. 137-142
    • Keller, J.E.1    Neale, E.A.2    Oyler, G.3    Adler, M.4
  • 38
    • 0032842847 scopus 로고    scopus 로고
    • Functional characterisation of tetanus and botulinum neurotoxins binding domains
    • Lalli G., Herreros J., Osborne S.L., et al. Functional characterisation of tetanus and botulinum neurotoxins binding domains. J. Cell. Sci. 1999, 112:2715-2724.
    • (1999) J. Cell. Sci. , vol.112 , pp. 2715-2724
    • Lalli, G.1    Herreros, J.2    Osborne, S.L.3
  • 39
    • 33749268212 scopus 로고    scopus 로고
    • Entering neurons: botulinum toxins and synaptic vesicle recycling
    • Verderio C., Rossetto O., Grumelli C., et al. Entering neurons: botulinum toxins and synaptic vesicle recycling. EMBO Rep. 2006, 7:995-999.
    • (2006) EMBO Rep. , vol.7 , pp. 995-999
    • Verderio, C.1    Rossetto, O.2    Grumelli, C.3
  • 40
    • 34047147339 scopus 로고    scopus 로고
    • Primary cultures of embryonic chicken neurons for sensitive cell-based assay of botulinum neurotoxin: implications for therapeutic discovery
    • Stahl A.M., Ruthel G., Torres-Melendez E., et al. Primary cultures of embryonic chicken neurons for sensitive cell-based assay of botulinum neurotoxin: implications for therapeutic discovery. J. Biomol. Screening 2007, 12:370-377.
    • (2007) J. Biomol. Screening , vol.12 , pp. 370-377
    • Stahl, A.M.1    Ruthel, G.2    Torres-Melendez, E.3
  • 41
    • 0031840854 scopus 로고    scopus 로고
    • Gating and permeability of ion channels produced by botulinum toxin types A and E in PC12 cell membranes
    • Sheridan R.E. Gating and permeability of ion channels produced by botulinum toxin types A and E in PC12 cell membranes. Toxicon 1998, 36:703-717.
    • (1998) Toxicon , vol.36 , pp. 703-717
    • Sheridan, R.E.1
  • 42
    • 15944364137 scopus 로고    scopus 로고
    • Primary cell culture for evaluation of botulinum neurotoxin antagonists
    • Sheridan R.E., Smith T.J., Adler M. Primary cell culture for evaluation of botulinum neurotoxin antagonists. Toxicon 2005, 45:377-382.
    • (2005) Toxicon , vol.45 , pp. 377-382
    • Sheridan, R.E.1    Smith, T.J.2    Adler, M.3
  • 43
    • 79953249923 scopus 로고    scopus 로고
    • Post-intoxication inhibition of botulinum neurotoxin serotype A within neurons by small-molecule, non-peptidic inhibitors
    • Ruthel G., Burnett J.C., Nuss J.E., et al. Post-intoxication inhibition of botulinum neurotoxin serotype A within neurons by small-molecule, non-peptidic inhibitors. Toxins (Basel) 2011, 3:207-217.
    • (2011) Toxins (Basel) , vol.3 , pp. 207-217
    • Ruthel, G.1    Burnett, J.C.2    Nuss, J.E.3
  • 44
    • 0029061475 scopus 로고
    • Tetanus and botulism neurotoxins: isolation and assay
    • Schiavo G., Montecucco C. Tetanus and botulism neurotoxins: isolation and assay. Meth. Enzymol. 1995, 248:643-652.
    • (1995) Meth. Enzymol. , vol.248 , pp. 643-652
    • Schiavo, G.1    Montecucco, C.2
  • 45
    • 0029161741 scopus 로고
    • Growth of clostridia and preparation of their neurotoxins
    • Shone C.C., Tranter H.S. Growth of clostridia and preparation of their neurotoxins. Curr. Top Microbiol. Immunol. 1995, 195:143-160.
    • (1995) Curr. Top Microbiol. Immunol. , vol.195 , pp. 143-160
    • Shone, C.C.1    Tranter, H.S.2
  • 46
    • 10644230055 scopus 로고    scopus 로고
    • Botulinum neurotoxin type D enables cytosolic delivery of enzymatically active cargo proteins to neurones via unfolded translocation intermediates
    • Bade S., Rummel A., Reisinger C., et al. Botulinum neurotoxin type D enables cytosolic delivery of enzymatically active cargo proteins to neurones via unfolded translocation intermediates. J. Neurochem. 2004, 91:1461-1472.
    • (2004) J. Neurochem. , vol.91 , pp. 1461-1472
    • Bade, S.1    Rummel, A.2    Reisinger, C.3
  • 47
    • 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., et al. 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
  • 48
    • 0029847230 scopus 로고    scopus 로고
    • Synaptic vesicle endocytosis mediates the entry of tetanus neurotoxin into hippocampal neurons
    • Matteoli M., Verderio C., Rossetto O., et al. Synaptic vesicle endocytosis mediates the entry of tetanus neurotoxin into hippocampal neurons. Proc. Natl. Acad. Sci. USA 1996, 93:13310-13315.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13310-13315
    • Matteoli, M.1    Verderio, C.2    Rossetto, O.3
  • 49
    • 0000131648 scopus 로고
    • The neurotoxins of Clostridium botulinum and of Clostridium tetani
    • Payling Wright G. The neurotoxins of Clostridium botulinum and of Clostridium tetani. Pharmacol. Res. 1955, 7:413-465.
    • (1955) Pharmacol. Res. , vol.7 , pp. 413-465
    • Payling Wright, G.1
  • 51
    • 72949138418 scopus 로고
    • The action of tetanus toxin in frogs
    • Rowson K.E. The action of tetanus toxin in frogs. J. Gen. Microbiol. 1961, 25:315-329.
    • (1961) J. Gen. Microbiol. , vol.25 , pp. 315-329
    • Rowson, K.E.1
  • 52
    • 84862836776 scopus 로고
    • Clostridium botulinum type C associated with a limberneck-like disease in chicken and ducks
    • Graham R., Boughton I.B. Clostridium botulinum type C associated with a limberneck-like disease in chicken and ducks. J. Am. Vet. Assoc. 1924, 64:723-727.
    • (1924) J. Am. Vet. Assoc. , vol.64 , pp. 723-727
    • Graham, R.1    Boughton, I.B.2
  • 53
    • 0037065664 scopus 로고    scopus 로고
    • Arg(362) and Tyr(365) of the botulinum neurotoxin type A light chain are involved in transition state stabilization
    • Binz T., Bade S., Rummel A., et al. Arg(362) and Tyr(365) of the botulinum neurotoxin type A light chain are involved in transition state stabilization. Biochemistry 2002, 41:1717-1723.
    • (2002) Biochemistry , vol.41 , pp. 1717-1723
    • Binz, T.1    Bade, S.2    Rummel, A.3
  • 54
    • 34248213125 scopus 로고    scopus 로고
    • Mechanism of substrate recognition by botulinum neurotoxin serotype A
    • Chen S., Kim J.J., Barbieri J.T. Mechanism of substrate recognition by botulinum neurotoxin serotype A. J. Biol. Chem. 2007, 13:9621-9627.
    • (2007) J. Biol. Chem. , vol.13 , pp. 9621-9627
    • Chen, S.1    Kim, J.J.2    Barbieri, J.T.3
  • 55
    • 34548688418 scopus 로고    scopus 로고
    • Structural and biochemical studies of botulinum neurotoxin serotype C1 light chain protease: implications for dual substrate specificity
    • Jin R., Sikorra S., Stegmann C.M., et al. Structural and biochemical studies of botulinum neurotoxin serotype C1 light chain protease: implications for dual substrate specificity. Biochemistry 2007, 37:10685-10693.
    • (2007) Biochemistry , vol.37 , pp. 10685-10693
    • Jin, R.1    Sikorra, S.2    Stegmann, C.M.3
  • 56
    • 51049104533 scopus 로고    scopus 로고
    • Substrate recognition mechanism of VAMP/synaptobrevin-cleaving clostridial neurotoxins
    • Sikorra S., Henke T., Galli T., Binz T., et al. Substrate recognition mechanism of VAMP/synaptobrevin-cleaving clostridial neurotoxins. J. Biol. Chem. 2008, 283:21145-21152.
    • (2008) J. Biol. Chem. , vol.283 , pp. 21145-21152
    • Sikorra, S.1    Henke, T.2    Galli, T.3    Binz, T.4
  • 57
    • 64849090643 scopus 로고    scopus 로고
    • Catalytic properties of botulinum neurotoxin subtypes A3 and A4
    • Henkel J.S., Jacobson M., Tepp W., et al. Catalytic properties of botulinum neurotoxin subtypes A3 and A4. Biochemistry 2009, 48:2522-2528.
    • (2009) Biochemistry , vol.48 , pp. 2522-2528
    • Henkel, J.S.1    Jacobson, M.2    Tepp, W.3
  • 58
    • 84860759738 scopus 로고    scopus 로고
    • Insights into the different catalytic activities of Clostridium neurotoxins
    • Chen S., Karalewitz A.P., Barbieri J.T. Insights into the different catalytic activities of Clostridium neurotoxins. Biochemistry 2012, 51:3941-3947.
    • (2012) Biochemistry , vol.51 , pp. 3941-3947
    • Chen, S.1    Karalewitz, A.P.2    Barbieri, J.T.3
  • 59
    • 0038743050 scopus 로고    scopus 로고
    • VAMP/synaptobrevin cleavage by tetanus and botulinum neurotoxins is strongly enhanced by acidic liposomes
    • Caccin P., Rossetto O., Rigoni M., et al. VAMP/synaptobrevin cleavage by tetanus and botulinum neurotoxins is strongly enhanced by acidic liposomes. FEBS Lett. 2003, 542:132-136.
    • (2003) FEBS Lett. , vol.542 , pp. 132-136
    • Caccin, P.1    Rossetto, O.2    Rigoni, M.3
  • 60
    • 44949127614 scopus 로고
    • Nouvelles recherches sur le botulisme et ses cinq types toxiniques
    • Prevot A.R., Brygoo E.R. Nouvelles recherches sur le botulisme et ses cinq types toxiniques. Ann. Inst. Pasteur 1953, 85:545-575.
    • (1953) Ann. Inst. Pasteur , vol.85 , pp. 545-575
    • Prevot, A.R.1    Brygoo, E.R.2


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