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Volumn 18, Issue 4, 2010, Pages 164-172

Gaining ground: Assays for therapeutics against botulinum neurotoxin

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIUM CHLORIDE; BAFILOMYCIN A1; BOTULINUM TOXIN; BOTULINUM TOXIN A; BOTULINUM TOXIN B; CONCANAMYCIN A; METHYLAMMONIUM; PEPTIDOMIMETIC AGENT; SNARE PROTEIN; SYNAPTOBREVIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25;

EID: 77950858619     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tim.2010.02.001     Document Type: Review
Times cited : (30)

References (67)
  • 1
    • 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
  • 2
    • 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
  • 3
    • 0026548114 scopus 로고
    • Properties and use of botulinum toxin and other microbial neurotoxins in medicine
    • Schantz E.J., Johnson E.A. Properties and use of botulinum toxin and other microbial neurotoxins in medicine. Microbiol. Rev. 1992, 56:80-99.
    • (1992) Microbiol. Rev. , vol.56 , pp. 80-99
    • Schantz, E.J.1    Johnson, E.A.2
  • 4
    • 23144438784 scopus 로고    scopus 로고
    • New insights into clostridial neurotoxin-SNARE interactions
    • Breidenbach M.A., Brunger A.T. New insights into clostridial neurotoxin-SNARE interactions. Trends Mol. Med. 2005, 11:377-381.
    • (2005) Trends Mol. Med. , vol.11 , pp. 377-381
    • Breidenbach, M.A.1    Brunger, A.T.2
  • 5
    • 22244493924 scopus 로고    scopus 로고
    • Analyzing a bioterror attack on the food supply: the case of botulinum toxin in milk
    • Wein L.M., Liu Y. Analyzing a bioterror attack on the food supply: the case of botulinum toxin in milk. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:9984-9989.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 9984-9989
    • Wein, L.M.1    Liu, Y.2
  • 6
    • 0035961566 scopus 로고    scopus 로고
    • Botulinum toxin as a biological weapon: medical and public health management
    • Arnon S.S., et al. Botulinum toxin as a biological weapon: medical and public health management. JAMA 2001, 285:1059-1070.
    • (2001) JAMA , vol.285 , pp. 1059-1070
    • Arnon, S.S.1
  • 7
    • 33747174581 scopus 로고    scopus 로고
    • Botulinum neurotoxin - from laboratory to bedside
    • Foster K.A., et al. Botulinum neurotoxin - from laboratory to bedside. Neurotox Res. 2006, 9:133-140.
    • (2006) Neurotox Res. , vol.9 , pp. 133-140
    • Foster, K.A.1
  • 8
    • 65749116965 scopus 로고    scopus 로고
    • Neuro-exocytosis: botulinum toxins as inhibitory probes and versatile therapeutics
    • Dolly J.O., et al. Neuro-exocytosis: botulinum toxins as inhibitory probes and versatile therapeutics. Curr. Opin. Pharmacol. 2009, 9:326-335.
    • (2009) Curr. Opin. Pharmacol. , vol.9 , pp. 326-335
    • Dolly, J.O.1
  • 10
    • 67249103849 scopus 로고    scopus 로고
    • Engineering botulinum neurotoxin to extend therapeutic intervention
    • Chen S., Barbieri J.T. Engineering botulinum neurotoxin to extend therapeutic intervention. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:9180-9184.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 9180-9184
    • Chen, S.1    Barbieri, J.T.2
  • 11
    • 77950859996 scopus 로고    scopus 로고
    • Botulism and vaccines for its prevention
    • Smith L.A. Botulism and vaccines for its prevention. Vaccine 2009, 27(Suppl 4):D33-39.
    • (2009) Vaccine , vol.27 , Issue.SUPPL. 4
    • Smith, L.A.1
  • 12
    • 24944466936 scopus 로고    scopus 로고
    • Botulinum toxin
    • viii
    • Horowitz B.Z. Botulinum toxin. Crit. Care Clin. 2005, 21:825-839. viii.
    • (2005) Crit. Care Clin. , vol.21 , pp. 825-839
    • Horowitz, B.Z.1
  • 13
    • 49249106612 scopus 로고    scopus 로고
    • Highly specific interactions between botulinum neurotoxins and synaptic vesicle proteins
    • Brunger A.T., et al. Highly specific interactions between botulinum neurotoxins and synaptic vesicle proteins. Cell Mol. Life Sci. 2008, 65:2296-2306.
    • (2008) Cell Mol. Life Sci. , vol.65 , pp. 2296-2306
    • Brunger, A.T.1
  • 14
    • 0141641129 scopus 로고    scopus 로고
    • Synaptotagmins I and II mediate entry of botulinum neurotoxin B into cells
    • Dong M., et al. Synaptotagmins I and II mediate entry of botulinum neurotoxin B into cells. J. Cell. Biol. 2003, 162:1293-1303.
    • (2003) J. Cell. Biol. , vol.162 , pp. 1293-1303
    • Dong, M.1
  • 15
    • 33646248918 scopus 로고    scopus 로고
    • SV2 is the protein receptor for botulinum neurotoxin A
    • Dong M., et al. SV2 is the protein receptor for botulinum neurotoxin A. Science 2006, 312:592-596.
    • (2006) Science , vol.312 , pp. 592-596
    • Dong, M.1
  • 16
    • 33846096319 scopus 로고    scopus 로고
    • Identification of the protein receptor binding site of botulinum neurotoxins B and G proves the double-receptor concept
    • Rummel A., et al. Identification of the protein receptor binding site of botulinum neurotoxins B and G proves the double-receptor concept. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:359-364.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 359-364
    • Rummel, A.1
  • 17
    • 0025943451 scopus 로고
    • Lectins from Triticum vulgaris and Limax flavus are universal antagonists of botulinum neurotoxin and tetanus toxin
    • Bakry N., et al. 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
  • 18
    • 34047134638 scopus 로고    scopus 로고
    • Synthesis of soluble multivalent glycoconjugates that target the Hc region of botulinum neurotoxin A
    • Kale R.R., et al. Synthesis of soluble multivalent glycoconjugates that target the Hc region of botulinum neurotoxin A. Bioorg. Med. Chem. Lett. 2007, 17:2459-2464.
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , pp. 2459-2464
    • Kale, R.R.1
  • 19
    • 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
  • 20
    • 0028293577 scopus 로고
    • Inhibition of vacuolar adenosine triphosphatase antagonizes the effects of clostridial neurotoxins but not phospholipase A2 neurotoxins
    • Simpson L.L., et al. 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
  • 21
    • 0345832207 scopus 로고    scopus 로고
    • Uptake of botulinum neurotoxin into cultured neurons
    • Keller J.E., et al. Uptake of botulinum neurotoxin into cultured neurons. Biochemistry 2004, 43:526-532.
    • (2004) Biochemistry , vol.43 , pp. 526-532
    • Keller, J.E.1
  • 22
    • 23944501982 scopus 로고    scopus 로고
    • SNARE complexes prepare for membrane fusion
    • Sorensen J.B. SNARE complexes prepare for membrane fusion. Trends Neurosci. 2005, 28:453-455.
    • (2005) Trends Neurosci. , vol.28 , pp. 453-455
    • Sorensen, J.B.1
  • 23
    • 54249097347 scopus 로고    scopus 로고
    • The strange case of the botulinum neurotoxin: using chemistry and biology to modulate the most deadly poison
    • Willis B., et al. The strange case of the botulinum neurotoxin: using chemistry and biology to modulate the most deadly poison. Angew. Chem. Int. Ed. Engl. 2008, 47:8360-8379.
    • (2008) Angew. Chem. Int. Ed. Engl. , vol.47 , pp. 8360-8379
    • Willis, B.1
  • 24
    • 53249152019 scopus 로고    scopus 로고
    • A potent peptidomimetic inhibitor of botulinum neurotoxin serotype A has a very different conformation than SNAP-25 substrate
    • Zuniga J.E., et al. A potent peptidomimetic inhibitor of botulinum neurotoxin serotype A has a very different conformation than SNAP-25 substrate. Structure 2008, 16:1588-1597.
    • (2008) Structure , vol.16 , pp. 1588-1597
    • Zuniga, J.E.1
  • 25
    • 14844365792 scopus 로고    scopus 로고
    • Botulinum neurotoxin serotype F: identification of substrate recognition requirements and development of inhibitors with low nanomolar affinity
    • Schmidt J.J., Stafford R.G. Botulinum neurotoxin serotype F: identification of substrate recognition requirements and development of inhibitors with low nanomolar affinity. Biochemistry 2005, 44:4067-4073.
    • (2005) Biochemistry , vol.44 , pp. 4067-4073
    • Schmidt, J.J.1    Stafford, R.G.2
  • 26
    • 0032508565 scopus 로고    scopus 로고
    • Type A botulinum neurotoxin proteolytic activity: development of competitive inhibitors and implications for substrate specificity at the S1' binding subsite
    • Schmidt J.J., et al. Type A botulinum neurotoxin proteolytic activity: development of competitive inhibitors and implications for substrate specificity at the S1' binding subsite. FEBS Lett. 1998, 435:61-64.
    • (1998) FEBS Lett. , vol.435 , pp. 61-64
    • Schmidt, J.J.1
  • 27
    • 1542615800 scopus 로고    scopus 로고
    • Synthesis of substrates and inhibitors of botulinum neurotoxin type A metalloprotease
    • Sukonpan C., et al. Synthesis of substrates and inhibitors of botulinum neurotoxin type A metalloprotease. J. Pept. Res. 2004, 63:181-193.
    • (2004) J. Pept. Res. , vol.63 , pp. 181-193
    • Sukonpan, C.1
  • 28
    • 33747165341 scopus 로고    scopus 로고
    • The 5th International Conference on Basic and Therapeutic Aspects of Botulinum and Tetanus Neurotoxins. Workshop review: assays and detection
    • Shone C., et al. The 5th International Conference on Basic and Therapeutic Aspects of Botulinum and Tetanus Neurotoxins. Workshop review: assays and detection. Neurotox. Res. 2006, 9:205-216.
    • (2006) Neurotox. Res. , vol.9 , pp. 205-216
    • Shone, C.1
  • 29
    • 0037228895 scopus 로고    scopus 로고
    • Fluorigenic substrates for the protease activities of botulinum neurotoxins, serotypes A, B, and F
    • Schmidt J.J., Stafford R.G. Fluorigenic 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
    • 9444236182 scopus 로고    scopus 로고
    • Inhibition of the protease activity of the light chain of type A botulinum neurotoxin by aqueous extract from stinging nettle (Urtica dioica) leaf
    • Gul N., et al. Inhibition of the protease activity of the light chain of type A botulinum neurotoxin by aqueous extract from stinging nettle (Urtica dioica) leaf. Basic Clin. Pharmacol. Toxicol. 2004, 95:215-219.
    • (2004) Basic Clin. Pharmacol. Toxicol. , vol.95 , pp. 215-219
    • Gul, N.1
  • 31
    • 0345169964 scopus 로고    scopus 로고
    • A capillary electrophoresis technique for evaluating botulinum neurotoxin B light chain activity
    • Adler M., et al. A capillary electrophoresis technique for evaluating botulinum neurotoxin B light chain activity. J. Protein Chem. 2003, 22:441-448.
    • (2003) J. Protein Chem. , vol.22 , pp. 441-448
    • Adler, M.1
  • 32
    • 23644442553 scopus 로고    scopus 로고
    • Partial protection against Botulinum B neurotoxin-induced blocking of exocytosis by a potent inhibitor of its metallopeptidase activity
    • Anne C., et al. Partial protection against Botulinum B neurotoxin-induced blocking of exocytosis by a potent inhibitor of its metallopeptidase activity. Chembiochem 2005, 6:1375-1380.
    • (2005) Chembiochem , vol.6 , pp. 1375-1380
    • Anne, C.1
  • 33
    • 0141625732 scopus 로고    scopus 로고
    • Novel small molecule inhibitors of botulinum neurotoxin A metalloprotease activity
    • Burnett J.C., et al. Novel small molecule inhibitors of botulinum neurotoxin A metalloprotease activity. Biochem. Biophys. Res. Commun. 2003, 310:84-93.
    • (2003) Biochem. Biophys. Res. Commun. , vol.310 , pp. 84-93
    • Burnett, J.C.1
  • 34
    • 0035119874 scopus 로고    scopus 로고
    • Cleavage of intracellular substrates of botulinum toxins A, C and D in a mammalian target tissue
    • Kalandakanond S., Coffield J.A. Cleavage of intracellular substrates of botulinum toxins A, C and D in a mammalian target tissue. J. Pharmacol. Exp. Ther. 2001, 296:749-755.
    • (2001) J. Pharmacol. Exp. Ther. , vol.296 , pp. 749-755
    • Kalandakanond, S.1    Coffield, J.A.2
  • 35
    • 27744463673 scopus 로고    scopus 로고
    • Synaptic vesicle chips to assay botulinum neurotoxins
    • Ferracci G., et al. Synaptic vesicle chips to assay botulinum neurotoxins. Biochem. J. 2005, 391:659-666.
    • (2005) Biochem. J. , vol.391 , pp. 659-666
    • Ferracci, G.1
  • 36
    • 56549105165 scopus 로고    scopus 로고
    • A protein chip membrane-capture assay for botulinum neurotoxin activity
    • Marconi S., et al. A protein chip membrane-capture assay for botulinum neurotoxin activity. Toxicol. Appl. Pharmacol. 2008, 233:439-446.
    • (2008) Toxicol. Appl. Pharmacol. , vol.233 , pp. 439-446
    • Marconi, S.1
  • 37
    • 38949154627 scopus 로고    scopus 로고
    • Use of a recombinant fluorescent substrate with cleavage sites for all botulinum neurotoxins in high-throughput screening of natural product extracts for inhibitors of serotypes A, B and E
    • Hines H.B., et al. Use of a recombinant fluorescent substrate with cleavage sites for all botulinum neurotoxins in high-throughput screening of natural product extracts for inhibitors of serotypes A, B and E. Appl. Environ. Microbiol. 2008, 74:653-659.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 653-659
    • Hines, H.B.1
  • 38
    • 0035870840 scopus 로고    scopus 로고
    • High-throughput fluorogenic assay for determination of botulinum type B neurotoxin protease activity
    • Anne C., et al. High-throughput fluorogenic assay for determination of botulinum type B neurotoxin protease activity. Anal. Biochem. 2001, 291:253-261.
    • (2001) Anal. Biochem. , vol.291 , pp. 253-261
    • Anne, C.1
  • 39
    • 29144449996 scopus 로고    scopus 로고
    • Integrated bioassays in microfluidic devices: botulinum toxin assays
    • Mangru S., et al. Integrated bioassays in microfluidic devices: botulinum toxin assays. J. Biomol. Screen. 2005, 10:788-794.
    • (2005) J. Biomol. Screen. , vol.10 , pp. 788-794
    • Mangru, S.1
  • 40
    • 6944237312 scopus 로고    scopus 로고
    • Using fluorescent sensors to detect botulinum neurotoxin activity in vitro and in living cells
    • Dong M., et al. Using fluorescent sensors to detect botulinum neurotoxin activity in vitro and in living cells. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:14701-14706.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 14701-14706
    • Dong, M.1
  • 41
    • 60449094897 scopus 로고    scopus 로고
    • Tandem fluorescent proteins as enhanced FRET-based substrates for botulinum neurotoxin activity
    • Pires-Alves M., et al. Tandem fluorescent proteins as enhanced FRET-based substrates for botulinum neurotoxin activity. Toxicon 2009, 53:392-399.
    • (2009) Toxicon , vol.53 , pp. 392-399
    • Pires-Alves, M.1
  • 42
    • 44349120485 scopus 로고    scopus 로고
    • Attomolar detection of botulinum toxin type A in complex biological matrices
    • Bagramyan K., et al. Attomolar detection of botulinum toxin type A in complex biological matrices. PLoS ONE 2008, 3:e2041.
    • (2008) PLoS ONE , vol.3
    • Bagramyan, K.1
  • 43
    • 67649582935 scopus 로고    scopus 로고
    • Detection and quantification of botulinum neurotoxin type a by a novel rapid in vitro fluorimetric assay
    • Poras H., et al. Detection and quantification of botulinum neurotoxin type a by a novel rapid in vitro fluorimetric assay. Appl. Environ. Microbiol. 2009, 75:4382-4390.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 4382-4390
    • Poras, H.1
  • 44
    • 70349432307 scopus 로고    scopus 로고
    • Antibody protection against botulinum neurotoxin intoxication in mice
    • Cheng L.W., et al. Antibody protection against botulinum neurotoxin intoxication in mice. Infect. Immun. 2009, 77:4305-4313.
    • (2009) Infect. Immun. , vol.77 , pp. 4305-4313
    • Cheng, L.W.1
  • 45
    • 21644452600 scopus 로고    scopus 로고
    • From the mouse to the mass spectrometer: detection and differentiation of the endoproteinase activities of botulinum neurotoxins A-G by mass spectrometry
    • Boyer A.E., et al. From the mouse to the mass spectrometer: detection and differentiation of the endoproteinase activities of botulinum neurotoxins A-G by mass spectrometry. Anal. Chem. 2005, 77:3916-3924.
    • (2005) Anal. Chem. , vol.77 , pp. 3916-3924
    • Boyer, A.E.1
  • 46
    • 33644933631 scopus 로고    scopus 로고
    • The use of Endopep-MS for the detection of botulinum toxins A, B, E and F in serum and stool samples
    • Kalb S.R., et al. The use of Endopep-MS for the detection of botulinum toxins A, B, E and F in serum and stool samples. Anal. Biochem. 2006, 351:84-92.
    • (2006) Anal. Biochem. , vol.351 , pp. 84-92
    • Kalb, S.R.1
  • 47
    • 0032402832 scopus 로고    scopus 로고
    • Intracellular detection assays for high-throughput screening
    • Gonzalez J.E., Negulescu P.A. Intracellular detection assays for high-throughput screening. Curr. Opin. Biotechnol. 1998, 9:624-631.
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 624-631
    • Gonzalez, J.E.1    Negulescu, P.A.2
  • 48
    • 34250155247 scopus 로고    scopus 로고
    • Botulism diagnostics: from clinical symptoms to in vitro assays
    • Cai S., et al. Botulism diagnostics: from clinical symptoms to in vitro assays. Crit. Rev. Microbiol. 2007, 33:109-125.
    • (2007) Crit. Rev. Microbiol. , vol.33 , pp. 109-125
    • Cai, S.1
  • 49
    • 25844466999 scopus 로고    scopus 로고
    • Vitamin B2-mediated cellular photoinhibition of botulinum neurotoxin A
    • Eubanks L.M., et al. Vitamin B2-mediated cellular photoinhibition of botulinum neurotoxin A. FEBS Lett. 2005, 579:5361-5364.
    • (2005) FEBS Lett. , vol.579 , pp. 5361-5364
    • Eubanks, L.M.1
  • 50
    • 2942626055 scopus 로고    scopus 로고
    • Novel application of an in vitro technique to the detection and quantification of botulinum neurotoxin antibodies
    • Hall Y.H., et al. Novel application of an in vitro technique to the detection and quantification of botulinum neurotoxin antibodies. J. Immunol. Methods 2004, 288:55-60.
    • (2004) J. Immunol. Methods , vol.288 , pp. 55-60
    • Hall, Y.H.1
  • 51
    • 34948874826 scopus 로고    scopus 로고
    • A neuronal cell-based botulinum neurotoxin assay for highly sensitive and specific detection of neutralizing serum antibodies
    • Pellett S., et al. A neuronal cell-based botulinum neurotoxin assay for highly sensitive and specific detection of neutralizing serum antibodies. FEBS Lett. 2007, 581:4803-4808.
    • (2007) FEBS Lett. , vol.581 , pp. 4803-4808
    • Pellett, S.1
  • 52
    • 0037428398 scopus 로고    scopus 로고
    • Evaluation of the therapeutic usefulness of botulinum neurotoxin 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., et al. Evaluation of the therapeutic usefulness of botulinum neurotoxin 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
  • 53
    • 15944364137 scopus 로고    scopus 로고
    • Primary cell culture for evaluation of botulinum neurotoxin antagonists
    • Sheridan R.E., et al. 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
  • 54
    • 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., et al. Primary cultures of embryonic chicken neurons for sensitive cell-based assay of botulinum neurotoxin: implications for therapeutic discovery. J. Biomol. Screen. 2007, 12:370-377.
    • (2007) J. Biomol. Screen. , vol.12 , pp. 370-377
    • Stahl, A.M.1
  • 55
    • 77949354718 scopus 로고    scopus 로고
    • Development of cell-based assays to measure botulinum neurotoxin serotype A activity using cleavage-sensitive antibodies
    • Nuss J.E., et al. Development of cell-based assays to measure botulinum neurotoxin serotype A activity using cleavage-sensitive antibodies. J. Biomol. Screen. 2010, 15:42-51.
    • (2010) J. Biomol. Screen. , vol.15 , pp. 42-51
    • Nuss, J.E.1
  • 56
    • 33646476127 scopus 로고    scopus 로고
    • A yeast assay probes the interaction between botulinum neurotoxin serotype B and its SNARE substrate
    • Fang H., et al. A yeast assay probes the interaction between botulinum neurotoxin serotype B and its SNARE substrate. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:6958-6963.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 6958-6963
    • Fang, H.1
  • 57
    • 70350445543 scopus 로고    scopus 로고
    • Capsaicin protects mouse neuromuscular junctions from the neuroparalytic effects of botulinum neurotoxin A
    • Thyagarajan B., et al. Capsaicin protects mouse neuromuscular junctions from the neuroparalytic effects of botulinum neurotoxin A. J. Pharmacol. Exp. Ther. 2009, 331:361-371.
    • (2009) J. Pharmacol. Exp. Ther. , vol.331 , pp. 361-371
    • Thyagarajan, B.1
  • 58
    • 12844286505 scopus 로고    scopus 로고
    • Comparison of the therapeutic indexes of different molecular forms of botulinum toxin type A
    • Yoneda S., et al. Comparison of the therapeutic indexes of different molecular forms of botulinum toxin type A. Eur. J. Pharmacol. 2005, 508:223-229.
    • (2005) Eur. J. Pharmacol. , vol.508 , pp. 223-229
    • Yoneda, S.1
  • 59
    • 67849126380 scopus 로고    scopus 로고
    • Identification and biochemical characterization of small-molecule inhibitors of Clostridium botulinum neurotoxin serotype A
    • Roxas-Duncan V., et al. Identification and biochemical characterization of small-molecule inhibitors of Clostridium botulinum neurotoxin serotype A. Antimicrob Agents Chemother. 2009, 53:3478-3486.
    • (2009) Antimicrob Agents Chemother. , vol.53 , pp. 3478-3486
    • Roxas-Duncan, V.1
  • 60
    • 22044438999 scopus 로고    scopus 로고
    • Botulinum neurotoxin type A causes shifts in myosin heavy chain composition in muscle
    • Dodd S.L., et al. Botulinum neurotoxin type A causes shifts in myosin heavy chain composition in muscle. Toxicon 2005, 46:196-203.
    • (2005) Toxicon , vol.46 , pp. 196-203
    • Dodd, S.L.1
  • 61
    • 33645861959 scopus 로고    scopus 로고
    • Recovery from botulinum neurotoxin poisoning in vivo
    • Keller J.E. Recovery from botulinum neurotoxin poisoning in vivo. Neuroscience 2006, 139:629-637.
    • (2006) Neuroscience , vol.139 , pp. 629-637
    • Keller, J.E.1
  • 62
    • 33746306794 scopus 로고    scopus 로고
    • Progress in applying the Three Rs to the potency testing of Botulinum toxin type A
    • Straughan D. Progress in applying the Three Rs to the potency testing of Botulinum toxin type A. Altern. Lab. Anim. 2006, 34:305-313.
    • (2006) Altern. Lab. Anim. , vol.34 , pp. 305-313
    • Straughan, D.1
  • 63
    • 50549084738 scopus 로고    scopus 로고
    • The in vivo rat muscle force model is a reliable and clinically relevant test of consistency among botulinum toxin preparations
    • Pickett A., et al. The in vivo rat muscle force model is a reliable and clinically relevant test of consistency among botulinum toxin preparations. Toxicon 2008, 52:455-464.
    • (2008) Toxicon , vol.52 , pp. 455-464
    • Pickett, A.1
  • 64
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • Hubbell W.L., et al. Identifying conformational changes with site-directed spin labeling. Nat. Struct. Biol. 2000, 7:735-739.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 735-739
    • Hubbell, W.L.1
  • 65
    • 0034620563 scopus 로고    scopus 로고
    • Time-resolved site-directed spin-labeling studies of bacteriorhodopsin: loop-specific conformational changes in M
    • Mollaaghababa R., et al. Time-resolved site-directed spin-labeling studies of bacteriorhodopsin: loop-specific conformational changes in M. Biochemistry 2000, 39:1120-1127.
    • (2000) Biochemistry , vol.39 , pp. 1120-1127
    • Mollaaghababa, R.1
  • 66
    • 0027972897 scopus 로고
    • Time-resolved detection of structural changes during the photocycle of spin-labeled bacteriorhodopsin
    • Steinhoff H.J., et al. Time-resolved detection of structural changes during the photocycle of spin-labeled bacteriorhodopsin. Science 1994, 266:105-107.
    • (1994) Science , vol.266 , pp. 105-107
    • Steinhoff, H.J.1
  • 67
    • 66849089268 scopus 로고    scopus 로고
    • Protein microarrays: high-throughput tools for proteomics
    • Stoevesandt O., et al. Protein microarrays: high-throughput tools for proteomics. Expert Rev. Proteomics 2009, 6:145-157.
    • (2009) Expert Rev. Proteomics , vol.6 , pp. 145-157
    • Stoevesandt, O.1


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