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Volumn 3, Issue 5, 2011, Pages 469-488

Botulinum neurotoxins and botulism: A novel therapeutic approach

Author keywords

Botulinum neurotoxin; Botulism; Cell penetrating peptide (CPP); Chimeric antibody; Heavy chain antibody (HCAb); Humanized antibody; Humanized camel phage display library; Immunotherapy; Nanobody; Phage display; Serum therapy; Single chain antibody variable fragment (ScFV); Single domain antibody (sdAb); Therapeutic antibody; Transbody; VHH; VH; VL; Zinc metalloprotease

Indexed keywords

BIVALENT EQUINE ANTITOXIN; BOTULINUM ANTISERUM; BOTULINUM TOXIN; BOTULINUM TOXIN A; BOTULINUM TOXIN B; BOTULINUM TOXIN C; BOTULINUM TOXIN D; BOTULINUM TOXIN E; BOTULINUM TOXIN F; BOTULINUM TOXIN G; CELL PENETRATING PEPTIDE; FULLY HUMAN MONOCLONAL ANTIBODY; HEPTAVALENT EQUINE ANTITOXIN; HUMAN BOTULISM IMMUNE GLOBULIN; HUMAN MOUSE CHIMERIC ANTIBODY; HYBRID PROTEIN; METALLOPROTEINASE; MONOCLONAL ANTIBODY; MONOVALENT EQUINE ANTITOXIN; MOUSE MONOCLONAL ANTIBODY; POLYCLONAL ANTIBODY; RECOMBINANT ANTITOXIN; SINGLE DOMAIN ANTIBODY; TRIVALENT EQUINE ANTITOXIN; UNCLASSIFIED DRUG;

EID: 79958033240     PISSN: None     EISSN: 20726651     Source Type: Journal    
DOI: 10.3390/toxins3050469     Document Type: Review
Times cited : (29)

References (127)
  • 1
    • 0019161371 scopus 로고
    • Clostridium botulinum neurotoxin
    • Sugiyama, H. Clostridium botulinum neurotoxin. Microbiol. Rev. 1980, 44, 419-448.
    • (1980) Microbiol. Rev , vol.44 , pp. 419-448
    • Sugiyama, H.1
  • 2
    • 0020073392 scopus 로고
    • Bacterial toxins: A table of lethal amounts
    • Gill, D.M. Bacterial toxins: A table of lethal amounts. Microbiol. Rev. 1982, 46, 86-94.
    • (1982) Microbiol. Rev , vol.46 , pp. 86-94
    • Gill, D.M.1
  • 6
    • 68849102962 scopus 로고    scopus 로고
    • novel function of botulinum toxin-associated proteins: HA proteins disrupt intestinal epithelial barrier to increase toxin absorption
    • Fuginaga, Y.; Matsumura, T.; Jin, Y.; Takegahara, Y.; Sugawara, Y. A novel function of botulinum toxin-associated proteins: HA proteins disrupt intestinal epithelial barrier to increase toxin absorption. Toxicon 2009, 54, 583-586.
    • (2009) Toxicon , vol.54 , pp. 583-586
    • Fuginaga, Y.1    Matsumura, T.2    Jin, Y.3    Takegahara, Y.4    Sugawara, Y.A.5
  • 7
    • 67649292434 scopus 로고    scopus 로고
    • How to botulinum neurotoxins block neurotransmitter release: From botulism to the molecular mechanism of action
    • Poulain, B.; Popoff, M.R.; Molgo, J. How to botulinum neurotoxins block neurotransmitter release: From botulism to the molecular mechanism of action. The Botulinum J. 2008, 1, 14-56.
    • (2008) The Botulinum J , vol.1 , pp. 14-56
    • Poulain, B.1    Popoff, M.R.2    Molgo, J.3
  • 8
    • 0026721240 scopus 로고
    • Molecular cloning of the Clostridium botulinum structural gene encoding the type B neurotoxin and determination of its entire nucleotide sequence
    • Whelan, S.M.; Elmore, M.J.; Bodsworth, N.J.; Brehm, J.K.; Atkinson, T.; Minton, N.P. Molecular cloning of the Clostridium botulinum structural gene encoding the type B neurotoxin and determination of its entire nucleotide sequence. Appl. Environ. Microbiol. 1992, 58, 2345-2354.
    • (1992) Appl. Environ. Microbiol , vol.58 , pp. 2345-2354
    • Whelan, S.M.1    Elmore, M.J.2    Bodsworth, N.J.3    Brehm, J.K.4    Atkinson, T.5    Minton, N.P.6
  • 10
    • 0014702295 scopus 로고
    • Conversion of toxigenicity in Clostridium botulinum type C
    • Inoue, K.; Iida, H. Conversion of toxigenicity in Clostridium botulinum type C. Jpn. J. Microbiol. 1970, 14, 87-89.
    • (1970) Jpn. J. Microbiol , vol.14 , pp. 87-89
    • Inoue, K.1    Iida, H.2
  • 11
    • 0015494431 scopus 로고
    • Bacteriophage and the toxigenicity of Clostridium botulinum type D
    • Eklund, M.W.; Poysky, F.T.; Reed, S.M. Bacteriophage and the toxigenicity of Clostridium botulinum type D. Nat. New Biol. 1972, 235, 16-17.
    • (1972) Nat. New Biol , vol.235 , pp. 16-17
    • Eklund, M.W.1    Poysky, F.T.2    Reed, S.M.3
  • 12
    • 0023878182 scopus 로고
    • Evidence for plasmid-mediated toxin and bacteriocin production in Clostridium botulinum type G
    • Eklund, M.W.; Poysky, F.T.; Mseitif, L.M.; Strom, M.S. Evidence for plasmid-mediated toxin and bacteriocin production in Clostridium botulinum type G. Appl. Environ. Microbiol. 1988, 54, 1405-1408.
    • (1988) Appl. Environ. Microbiol , vol.54 , pp. 1405-1408
    • Eklund, M.W.1    Poysky, F.T.2    Mseitif, L.M.3    Strom, M.S.4
  • 13
    • 62849108022 scopus 로고    scopus 로고
    • Evidence that plasmid-borne botulinum neurotoxin type B genes are widespread among Clostridium botulinum serotype B strains
    • Franciosa, G.; Maugliani, A.; Scalfaro, C.; Aureli, P. Evidence that plasmid-borne botulinum neurotoxin type B genes are widespread among Clostridium botulinum serotype B strains. PLoS ONE 2009, 4, e4829.
    • (2009) PLoS ONE , vol.4
    • Franciosa, G.1    Maugliani, A.2    Scalfaro, C.3    Aureli, P.4
  • 14
    • 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
  • 15
    • 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
  • 17
    • 68949179783 scopus 로고    scopus 로고
    • Receptor and substrate interactions of clostridial neurotoxins
    • Brunger, A.T.; Rummel, A. Receptor and substrate interactions of clostridial neurotoxins. Toxicon 2009, 54, 550-560.
    • (2009) Toxicon , vol.54 , pp. 550-560
    • Brunger, A.T.1    Rummel, A.2
  • 19
    • 0032555584 scopus 로고    scopus 로고
    • Binding and transcytosis of botulinum neurotoxin by polarized human colon carcinoma cells
    • Maksymowych, A.B.; Simpson, L.L. Binding and transcytosis of botulinum neurotoxin by polarized human colon carcinoma cells. J. Biol. Chem. 1998, 273, 21950-21957.
    • (1998) J. Biol. Chem , vol.273 , pp. 21950-21957
    • Maksymowych, A.B.1    Simpson, L.L.2
  • 21
    • 38049036925 scopus 로고    scopus 로고
    • Mechanism of botulinum neurotoxin B and G entry into hippocampal neurons
    • Dong, M.; Tepp, W.H.; Liu, H.; Johnson, E.A.; Chapman, E.R. Mechanism of botulinum neurotoxin B and G entry into hippocampal neurons. J. Cell. Biol. 2007, 179, 1511-1522.
    • (2007) J. Cell. Biol , vol.179 , pp. 1511-1522
    • Dong, M.1    Tepp, W.H.2    Liu, H.3    Johnson, E.A.4    Chapman, E.R.5
  • 23
    • 0027282605 scopus 로고
    • Direct visualization of botulinum neurotoxin-induced channels in phospholipid vesicles
    • Schmidt, 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
    • Schmidt, M.F.1    Robinson, J.P.2    Dasgupta, B.R.3
  • 24
    • 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
  • 25
    • 49249106612 scopus 로고    scopus 로고
    • Highly specific interaction between botulinum neurotoxins and synaptic vesicle proteins
    • Brunger. A.T.; Jin, R.; Breidenbach, M.A. Highly specific interaction 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    Jin, R.2    Breidenbach, M.A.3
  • 30
    • 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
  • 31
    • 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
  • 32
    • 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 Laureto, P.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 Laureto, P.P.5    Dasgupta, B.R.6    Montecucco, C.7
  • 33
    • 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
  • 37
    • 0027979896 scopus 로고
    • Antagonism of the intracellular action of botulinum neurotoxin type A with monoclonal antibodies that map to light-chain epitopes
    • Cenci di Bello, I.; Poulain, B.; Shone, C.C.; Tauc, L.; Dolly, J.O. Antagonism of the intracellular action of botulinum neurotoxin type A with monoclonal antibodies that map to light-chain epitopes. Eur. J. Biochem. 1994, 219, 161-169.
    • (1994) Eur. J. Biochem , vol.219 , pp. 161-169
    • Cenci di Bello, I.1    Poulain, B.2    Shone, C.C.3    Tauc, L.4    Dolly, J.O.5
  • 39
    • 2442600067 scopus 로고    scopus 로고
    • Small tripeptide surrogates with low nanomolar affinity as potent inhibitors of botulinum neurotoxin B metallo-proteolytic activity
    • Blommaert, A.; Turcaud, S.; Anne, C.; Roques, B.P. Small tripeptide surrogates with low nanomolar affinity as potent inhibitors of botulinum neurotoxin B metallo-proteolytic activity. Bioorg. Med. Chem. 2004, 12, 3055-3062.
    • (2004) Bioorg. Med. Chem , vol.12 , pp. 3055-3062
    • Blommaert, A.1    Turcaud, S.2    Anne, C.3    Roques, B.P.4
  • 40
    • 0014478524 scopus 로고
    • Trivalent botulinus antotoxin
    • Koenig, M.G. Trivalent botulinus antotoxin. Ann. Intern. Med. 1969, 70, 643-645.
    • (1969) Ann. Intern. Med , vol.70 , pp. 643-645
    • Koenig, M.G.1
  • 41
    • 77949581390 scopus 로고    scopus 로고
    • Investigational heptavalent botulinum antitoxin (HBAT) to replace licensed botulinum antitoxin AB and investigational botulinum antitoxin E
    • Investigational heptavalent botulinum antitoxin (HBAT) to replace licensed botulinum antitoxin AB and investigational botulinum antitoxin E. MMWR 2010, 59, 299.
    • (2010) MMWR , vol.59 , pp. 299
  • 42
    • 84878265331 scopus 로고    scopus 로고
    • U.S. Food and Drug
    • Available online, UCM149970.pdf, accessed on 27 March 2077
    • U.S. Food and Drug. Alphabetical List of Licensed Products: Information Updated through February 28, 2011. Available online: http://www.fda.gov/downloads/BiologicsBloodVaccines/ UCM149970.pdf (accessed on 27 March 2011).
    • (2011) Alphabetical List of Licensed Products: Information Updated Through February , vol.28
  • 44
    • 34147140020 scopus 로고    scopus 로고
    • Creation and development of the public service orphan drug human botulism immune globulin
    • Arnon, S.S. Creation and development of the public service orphan drug human botulism immune globulin. Pediatrics 2007, 119, 785-789.
    • (2007) Pediatrics , vol.119 , pp. 785-789
    • Arnon, S.S.1
  • 46
    • 33751546855 scopus 로고    scopus 로고
    • Fine and Domain-level epitope mapping of botulinum neurotoxin type A neutralizing antibodies by yeast surface display
    • Levy, R.; Forsyth, C.M.; LaPorte, S.L.; Geren, I.N.; Smith, L.A.; Marks, J.D. Fine and Domain-level epitope mapping of botulinum neurotoxin type A neutralizing antibodies by yeast surface display. J. Mol. Biol. 2007, 365, 196-210.
    • (2007) J. Mol. Biol , vol.365 , pp. 196-210
    • Levy, R.1    Forsyth, C.M.2    Laporte, S.L.3    Geren, I.N.4    Smith, L.A.5    Marks, J.D.6
  • 48
    • 68849120868 scopus 로고    scopus 로고
    • Immune recognition of BoNTs A and B: How anti-toxin antibodies that bind to the heavy chain obstruct toxin action
    • Atassi, M.Z. Immune recognition of BoNTs A and B: how anti-toxin antibodies that bind to the heavy chain obstruct toxin action. Toxicon 2009, 54, 600-613.
    • (2009) Toxicon , vol.54 , pp. 600-613
    • Atassi, M.Z.1
  • 49
  • 50
    • 0033793926 scopus 로고    scopus 로고
    • Passive immunity in prevention of infectious diseases
    • Keller, M.A.; Stiehm, E.R. Passive immunity in prevention of infectious diseases. Clin. Microbiol. Rev. 2000, 13, 602-614.
    • (2000) Clin. Microbiol. Rev , vol.13 , pp. 602-614
    • Keller, M.A.1    Stiehm, E.R.2
  • 51
    • 79958073441 scopus 로고
    • Human antitetanus serum in the treatment of tetanus
    • Ellis, M.; Chir, B. Human antitetanus serum in the treatment of tetanus. Br. Med. J. 1963, 1, 1123-1126.
    • (1963) Br. Med. J , vol.1 , pp. 1123-1126
    • Ellis, M.1    Chir, B.2
  • 52
    • 0242714972 scopus 로고
    • Use of convalescent measles serum to control measles in a preparatory school
    • Gallagher, J.R. Use of convalescent measles serum to control measles in a preparatory school. Am. J. Public Health Nations Health 1935, 25, 595-598.
    • (1935) Am. J. Public Health Nations Health , vol.25 , pp. 595-598
    • Gallagher, J.R.1
  • 53
    • 7044231869 scopus 로고    scopus 로고
    • New concepts in antibody-mediated immunity
    • Casadevall, A.; Pirofski, L.A. New concepts in antibody-mediated immunity. Infect. Immun. 2004, 72, 6191-6196.
    • (2004) Infect. Immun , vol.72 , pp. 6191-6196
    • Casadevall, A.1    Pirofski, L.A.2
  • 56
    • 0028902204 scopus 로고
    • Urease-specific monoclonal antibodies prevent Helicobacter felis infection in mice
    • Blanchard, T.G.; Czinn, S.J.; Maurer, R.; Thomas, W.; Soman, G.; Nedrud, J.G. Urease-specific monoclonal antibodies prevent Helicobacter felis infection in mice. Infect. Immun. 1995, 63, 1394-1399.
    • (1995) Infect. Immun , vol.63 , pp. 1394-1399
    • Blanchard, T.G.1    Czinn, S.J.2    Maurer, R.3    Thomas, W.4    Soman, G.5    Nedrud, J.G.6
  • 57
    • 0141452289 scopus 로고    scopus 로고
    • Neutralization of measles virus infectivity and antibody-dependent cell-mediated cytotoxicity activity against an Epstein-Barr virus-infected cell line by intravenous administration of immunoglobulin G
    • Colomar, M.; Puga, I.; López, M.; Massot, M.; Jorquera, J.I.; Reina, M.; Vilaró, S.; Espel, E. Neutralization of measles virus infectivity and antibody-dependent cell-mediated cytotoxicity activity against an Epstein-Barr virus-infected cell line by intravenous administration of immunoglobulin G. Clin. Diagn. Lab. Immunol. 2003, 10, 751-756.
    • (2003) Clin. Diagn. Lab. Immunol , vol.10 , pp. 751-756
    • Colomar, M.1    Puga, I.2    López, M.3    Massot, M.4    Jorquera, J.I.5    Reina, M.6    Vilaró, S.7    Espel, E.8
  • 58
    • 0035424137 scopus 로고    scopus 로고
    • Complement is essential for protection by an IgM and an IgG3 monoclonal antibody against experimental hematogenously disseminated candidiasis
    • Han, Y.; Kozel, T.R.; Zhang, M.X.; MacGill, R.S.; Carroll, M.C.; Cutler, J.E. Complement is essential for protection by an IgM and an IgG3 monoclonal antibody against experimental hematogenously disseminated candidiasis. J. Immunol. 2001, 167, 1550-1557.
    • (2001) J. Immunol , vol.167 , pp. 1550-1557
    • Han, Y.1    Kozel, T.R.2    Zhang, M.X.3    Macgill, R.S.4    Carroll, M.C.5    Cutler, J.E.6
  • 59
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Köhler, G.; Milstein, C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 1975, 256, 495-497.
    • (1975) Nature , vol.256 , pp. 495-497
    • Köhler, G.1    Milstein, C.2
  • 60
    • 33745192259 scopus 로고    scopus 로고
    • Recombinant polyclonal antibodies: The next generation of antibody therapeutics?
    • Haurum, J.S. Recombinant polyclonal antibodies: The next generation of antibody therapeutics? Drug Discov. Today 2006, 11, 655-660.
    • (2006) Drug Discov. Today , vol.11 , pp. 655-660
    • Haurum, J.S.1
  • 61
    • 0029032565 scopus 로고
    • Return to the past: The case for antibody-based therapies in infectious diseases
    • Casadevall, A.; Scharff, M.D. Return to the past: The case for antibody-based therapies in infectious diseases. Clin. Infect. Dis. 1995, 21, 150-161.
    • (1995) Clin. Infect. Dis , vol.21 , pp. 150-161
    • Casadevall, A.1    Scharff, M.D.2
  • 62
    • 64349107630 scopus 로고    scopus 로고
    • Development trends for therapeutic antibody fragments
    • Nelson, A.L.; Reichert, J.M. Development trends for therapeutic antibody fragments. Nat. Biotechnol. 2009, 27, 331-337.
    • (2009) Nat. Biotechnol , vol.27 , pp. 331-337
    • Nelson, A.L.1    Reichert, J.M.2
  • 63
    • 77956381860 scopus 로고    scopus 로고
    • Research and development of next generation of antibody-based therapeutics
    • Li, J.; Zhu, Z. Research and development of next generation of antibody-based therapeutics. Acta. Pharmacol. Sin. 2010, 31, 1198-1207.
    • (2010) Acta. Pharmacol. Sin , vol.31 , pp. 1198-1207
    • Li, J.1    Zhu, Z.2
  • 64
    • 77957879208 scopus 로고    scopus 로고
    • Characterization of botulinum neurotoxin type A neutralizing monoclonal antibodies and influence of their half-lives on therapeutic activity
    • Mazuet, C.; Dano, J.; Popoff, M.R.; Créminon, C.; Volland, H. Characterization of botulinum neurotoxin type A neutralizing monoclonal antibodies and influence of their half-lives on therapeutic activity. PLoS ONE 2010, 5, e12416.
    • (2010) PLoS ONE , vol.5
    • Mazuet, C.1    Dano, J.2    Popoff, M.R.3    Créminon, C.4    Volland, H.5
  • 65
    • 0019188771 scopus 로고
    • Immunoglobulin chain loss in hybridoma lines
    • Köhler, G. Immunoglobulin chain loss in hybridoma lines. Proc. Natl. Acad. Sci. USA 1980, 77, 2197-2199.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 2197-2199
    • Köhler, G.1
  • 66
    • 0023197965 scopus 로고
    • Preexisting human anti-murine immunoglobulin reactivity due to polyclonal rheumatoid factors
    • Courtenay-Luck, N.S.; Epenetos, A.A.; Winearls, C.G.; Ritter, M.A. Preexisting human anti-murine immunoglobulin reactivity due to polyclonal rheumatoid factors. Cancer Res. 1987, 47, 4520-4525.
    • (1987) Cancer Res , vol.47 , pp. 4520-4525
    • Courtenay-Luck, N.S.1    Epenetos, A.A.2    Winearls, C.G.3    Ritter, M.A.4
  • 67
    • 0025611725 scopus 로고
    • Development of human anti-murine antibody (HAMA) response in patients
    • Tjandra, J.J.; Ramadi, L.; McKenzie, I.F.C. Development of human anti-murine antibody (HAMA) response in patients. Immunol. Cell Biol. 1990, 68, 367-376.
    • (1990) Immunol. Cell Biol , vol.68 , pp. 367-376
    • Tjandra, J.J.1    Ramadi, L.2    McKenzie, I.F.C.3
  • 68
    • 0025156771 scopus 로고
    • Human immune response to anti-carcinoembryonic antigen murine monoclonal antibodies
    • Losman, M.J.; DeJager, R.L.; Monostier, M.; Sharkey, R.M.; Goldenberg, D.M. Human immune response to anti-carcinoembryonic antigen murine monoclonal antibodies. Cancer Res. 1990, 1, 1055-1058.
    • (1990) Cancer Res , vol.1 , pp. 1055-1058
    • Losman, M.J.1    Dejager, R.L.2    Monostier, M.3    Sharkey, R.M.4    Goldenberg, D.M.5
  • 69
    • 0021716682 scopus 로고
    • Chimeric human antibody molecules: Mouse antigen-binding domains with human constant region domains
    • Morrison, S.L.; Johnson, M.J.; Herzenberg, L.A.; Oi, V.T. Chimeric human antibody molecules: Mouse antigen-binding domains with human constant region domains. Proc. Natl. Acad. Sci. USA 1984, 81, 6851-6855.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 6851-6855
    • Morrison, S.L.1    Johnson, M.J.2    Herzenberg, L.A.3    Oi, V.T.4
  • 70
    • 15244351004 scopus 로고    scopus 로고
    • Overview of monoclonal antibodies in cancer therapy: Present and promise
    • Stern, M.; Herrmann, R. Overview of monoclonal antibodies in cancer therapy: Present and promise. Crit. Rev. Oncol. Hematol. 2005, 54, 11-29.
    • (2005) Crit. Rev. Oncol. Hematol , vol.54 , pp. 11-29
    • Stern, M.1    Herrmann, R.2
  • 71
    • 0014747543 scopus 로고
    • Why antibody inhibits vascular clearance of staphylococcal enterotoxin B
    • Normann, S.J. Why antibody inhibits vascular clearance of staphylococcal enterotoxin B. J. Immunol. 1970, 104, 673-678.
    • (1970) J. Immunol , vol.104 , pp. 673-678
    • Normann, S.J.1
  • 72
    • 0034834559 scopus 로고    scopus 로고
    • Construction and functional evaluation of a single-chain antibody fragment that neutralizes toxin AahI from the venom of the scorpion Androctonus australis hector
    • Devaux C.; Moreau, E.; Goyffon, M.; Rochat, H.; Billiald, P. Construction and functional evaluation of a single-chain antibody fragment that neutralizes toxin AahI from the venom of the scorpion Androctonus australis hector. Eur. J. Biochem. 2001, 268, 694-702.
    • (2001) Eur. J. Biochem , vol.268 , pp. 694-702
    • Devaux, C.1    Moreau, E.2    Goyffon, M.3    Rochat, H.4    Billiald, P.5
  • 74
  • 77
    • 0342437532 scopus 로고    scopus 로고
    • Production of human antibody repertoires in transgenic mice
    • Brüggemannand, M.; Taussig, M.J. Production of human antibody repertoires in transgenic mice. Curr. Opin. Biotechnol. 1997, 8, 455-458.
    • (1997) Curr. Opin. Biotechnol , vol.8 , pp. 455-458
    • Brüggemannand, M.1    Taussig, M.J.2
  • 78
    • 0019993740 scopus 로고
    • Use of Epstein-Barr virus-transformed B cell lines for the generation of immunoglobulin-producing human B cell hybridomas
    • Chiorazzi, N.; Wasserman, R.L.; Kunkel, H.G. Use of Epstein-Barr virus-transformed B cell lines for the generation of immunoglobulin-producing human B cell hybridomas. J. Exp. Med. 1982, 156, 930-935.
    • (1982) J. Exp. Med , vol.156 , pp. 930-935
    • Chiorazzi, N.1    Wasserman, R.L.2    Kunkel, H.G.3
  • 79
    • 0020529369 scopus 로고
    • Human monoclonal antibodies to a genus-specific chlamydial antigen produced by EBV-transformed B cells
    • Rosen, A.; Persson, K.; Klein, G. Human monoclonal antibodies to a genus-specific chlamydial antigen produced by EBV-transformed B cells. J. Immunol. 1983, 130, 2899-2902.
    • (1983) J. Immunol , vol.130 , pp. 2899-2902
    • Rosen, A.1    Persson, K.2    Klein, G.3
  • 80
    • 0022602869 scopus 로고
    • Human monoclonal antibody to purified protein derivative of tuberculin produced by hybrids constructed with Epstein-Barr virus-transformed B lymphocytes and mouse myeloma cells
    • Garzelli, C.; Puglisi, C.; Falcone, G. Human monoclonal antibody to purified protein derivative of tuberculin produced by hybrids constructed with Epstein-Barr virus-transformed B lymphocytes and mouse myeloma cells. Eur. J. Immunol. 1986, 16, 584-587.
    • (1986) Eur. J. Immunol , vol.16 , pp. 584-587
    • Garzelli, C.1    Puglisi, C.2    Falcone, G.3
  • 82
    • 79958056563 scopus 로고    scopus 로고
    • 5th ed.; W.H. Freeman and Company: New York, NY, USA
    • Goldsby, R.A.; Kindt, T.J.; Osborne, B.A. Kuby Immunology, 5th ed.; W.H. Freeman and Company: New York, NY, USA, 2003; Chapter 5, pp. 105-136.
    • (2003) Kuby Immunology , vol.5 , pp. 105-136
    • Goldsby, R.A.1    Kindt, T.J.2    Osborne, B.A.3
  • 83
    • 27644489367 scopus 로고    scopus 로고
    • Immunoglobulin gene diversification
    • Maizels, N. Immunoglobulin gene diversification. Annu. Rev. Genet. 2005, 39, 23-46.
    • (2005) Annu. Rev. Genet , vol.39 , pp. 23-46
    • Maizels, N.1
  • 84
    • 0030994634 scopus 로고    scopus 로고
    • Yeast surface display for screening combinatorial polypeptide libraries
    • Boder, E.T.; Wittrup, K.D. Yeast surface display for screening combinatorial polypeptide libraries. Nat. Biotechnol. 1997, 15, 553-557.
    • (1997) Nat. Biotechnol , vol.15 , pp. 553-557
    • Boder, E.T.1    Wittrup, K.D.2
  • 85
    • 0032797898 scopus 로고    scopus 로고
    • Development of an optimized expression system for the screening of antibody libraries displayed on the Escherichia coli surface
    • Daugherty, P.S.; Olsen, M.J.; Iverson, B.L.; Georgiou, G. Development of an optimized expression system for the screening of antibody libraries displayed on the Escherichia coli surface. Protein Eng. 1999, 12, 613-621.
    • (1999) Protein Eng , vol.12 , pp. 613-621
    • Daugherty, P.S.1    Olsen, M.J.2    Iverson, B.L.3    Georgiou, G.4
  • 87
    • 0030974119 scopus 로고    scopus 로고
    • In vitro selection and evolution of functional proteins by using ribosome display
    • Hanes, J.; Plückthun, A. In vitro selection and evolution of functional proteins by using ribosome display. Proc. Natl. Acad. Sci. USA 1997, 94, 4937-4942.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4937-4942
    • Hanes, J.1    Plückthun,, A.2
  • 88
    • 0021818675 scopus 로고
    • Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface
    • Smith, G.P. Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface. Science 1985, 228, 1315-1317.
    • (1985) Science , vol.228 , pp. 1315-1317
    • Smith, G.P.1
  • 89
    • 27144431943 scopus 로고    scopus 로고
    • Selecting and screening recombinant antibody libraries
    • Hoogenboom, H.R. Selecting and screening recombinant antibody libraries. Nat. Biotechnol. 2005, 23, 1105-1116.
    • (2005) Nat. Biotechnol , vol.23 , pp. 1105-1116
    • Hoogenboom, H.R.1
  • 91
    • 0036366705 scopus 로고    scopus 로고
    • Overview of antibody phage-display technology and its applications
    • O'Brien, P.M., Aitken, R., Eds.; Humana Press Inc.: Totowa, NJ, USA
    • Hoogenboom, H.R. Overview of antibody phage-display technology and its applications. In Antibody Phage Display: Methods and Protocols; O'Brien, P.M., Aitken, R., Eds.; Humana Press Inc.: Totowa, NJ, USA, 2002; pp. 1-37.
    • (2002) Antibody , pp. 1-37
    • Hoogenboom, H.R.1
  • 92
    • 33751080719 scopus 로고    scopus 로고
    • Synthetic therapeutic antibodies
    • Sidhu, S.S.; Fellouse, F.A. Synthetic therapeutic antibodies. Nat. Chem. Biol. 2006, 2, 682-688.
    • (2006) Nat. Chem. Biol , vol.2 , pp. 682-688
    • Sidhu, S.S.1    Fellouse, F.A.2
  • 98
    • 0142232284 scopus 로고    scopus 로고
    • The production of antibody fragments and antibody fusion proteins by yeasts and filamentous fungi
    • Joosten, V.; Lokman, C.; van den Hondel, C.A.; Punt, P.J. The production of antibody fragments and antibody fusion proteins by yeasts and filamentous fungi. Microb. Cell. Fact. 2003, 2, 1-15.
    • (2003) Microb. Cell. Fact , vol.2 , pp. 1-15
    • Joosten, V.1    Lokman, C.2    van den Hondel, C.A.3    Punt, P.J.4
  • 100
    • 0027953603 scopus 로고
    • Camelising human antibody fragments: NMR studies on VH domains
    • Davies, J.; Riechmann, L. Camelising human antibody fragments: NMR studies on VH domains. FEBS Lett. 1994, 339, 285-290.
    • (1994) FEBS Lett , vol.339 , pp. 285-290
    • Davies, J.1    Riechmann, L.2
  • 101
    • 0028168145 scopus 로고
    • Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains
    • Muyldermans, S.; Atarhouch, T.; Saldanha, J.; Barbosa, J.A.; Hamers, R. Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains. Protein Eng. 1994, 7, 1129-1135.
    • (1994) Protein Eng , vol.7 , pp. 1129-1135
    • Muyldermans, S.1    Atarhouch, T.2    Saldanha, J.3    Barbosa, J.A.4    Hamers, R.5
  • 102
    • 0034161488 scopus 로고    scopus 로고
    • Camel heavy-chain antibodies: Diverse germline V(H)H and specific mechanisms enlarge the antigen-binding repertoire
    • Nguyen, V.K.; Hamers, R.; Muyldermans, S. Camel heavy-chain antibodies: Diverse germline V(H)H and specific mechanisms enlarge the antigen-binding repertoire. EMBO J. 2000, 19, 921-930.
    • (2000) EMBO J , vol.19 , pp. 921-930
    • Nguyen, V.K.1    Hamers, R.2    Muyldermans, S.3
  • 103
    • 0037303456 scopus 로고    scopus 로고
    • Emergence and evolution of functional heavy-chain antibodies in Camelidae
    • Conrath, K.E.; Wernery, U.; Muyldermans, S.; Nguyen, V.K. Emergence and evolution of functional heavy-chain antibodies in Camelidae. Dev. Comp. Immunol. 2003, 27, 87-103.
    • (2003) Dev. Comp. Immunol , vol.27 , pp. 87-103
    • Conrath, K.E.1    Wernery, U.2    Muyldermans, S.3    Nguyen, V.K.4
  • 104
    • 0027212854 scopus 로고
    • Length distribution of CDRH3 in antibodies
    • Wu, T.T.; Johnson, G.; Kabat, E.A. Length distribution of CDRH3 in antibodies. Proteins 1993, 16, 1-7.
    • (1993) Proteins , vol.16 , pp. 1-7
    • Wu, T.T.1    Johnson, G.2    Kabat, E.A.3
  • 105
    • 0035715877 scopus 로고    scopus 로고
    • Single domain camel antibodies: Current status
    • Muyldermans, S. Single domain camel antibodies: Current status. J. Biotechnol. 2001, 74, 277-302.
    • (2001) J. Biotechnol , vol.74 , pp. 277-302
    • Muyldermans, S.1
  • 106
    • 0035854724 scopus 로고    scopus 로고
    • Antigen specificity and high affinity binding provided by one single loop of a camel single-domain antibody
    • Desmyter, A.; Decanniere, K.; Muyldermans, S.; Wyns, L. Antigen specificity and high affinity binding provided by one single loop of a camel single-domain antibody. J. Biol. Chem. 2001, 276, 26285-26290.
    • (2001) J. Biol. Chem , vol.276 , pp. 26285-26290
    • Desmyter, A.1    Decanniere, K.2    Muyldermans, S.3    Wyns, L.4
  • 110
    • 0030767656 scopus 로고    scopus 로고
    • Selection and identification of single domain antibody fragments from camel heavy-chain antibodies
    • Ghahroudi, M.A.; Desmyter, A.; Wyns, L.; Hamers, R.; Muyldermans, S. Selection and identification of single domain antibody fragments from camel heavy-chain antibodies. FEBS Lett. 1997, 414, 521-526.
    • (1997) FEBS Lett , vol.414 , pp. 521-526
    • Ghahroudi, M.A.1    Desmyter, A.2    Wyns, L.3    Hamers, R.4    Muyldermans, S.5
  • 111
    • 35348819390 scopus 로고    scopus 로고
    • Properties, production, and applications of camelid single-domain antibody fragments
    • Harmsen, M.M.; de Haard, H.J. Properties, production, and applications of camelid single-domain antibody fragments. Appl. Microbiol. Biotechnol. 2007, 77, 13-22.
    • (2007) Appl. Microbiol. Biotechnol , vol.77 , pp. 13-22
    • Harmsen, M.M.1    de Haard, H.J.2
  • 113
    • 0035312546 scopus 로고    scopus 로고
    • Recognition of antigens by single domain antibody fragments: The superfluous luxury of paired domains
    • Muyldermans, S.; Cambillau, C.; Wyns, L. Recognition of antigens by single domain antibody fragments: The superfluous luxury of paired domains. TIBS 2001, 26, 230-235.
    • (2001) TIBS , vol.26 , pp. 230-235
    • Muyldermans, S.1    Cambillau, C.2    Wyns, L.3
  • 114
    • 77950022629 scopus 로고    scopus 로고
    • A single-domain llama antibody potently inhibits the enzymatic activity of botulinum neurotoxin by binding to the non-catalytic α-exosite binding region
    • Dong, J.; Thompson, A.A.; Fan, Y.; Lou, J.; Conrad, F.; Ho, M.; Pires-Alves, M.; Wilson, B.A.; Stevens, R.C.; Marks, J.D. A single-domain llama antibody potently inhibits the enzymatic activity of botulinum neurotoxin by binding to the non-catalytic α-exosite binding region. J. Mol. Biol. 2010, 397, 1106-1118.
    • (2010) J. Mol. Biol , vol.397 , pp. 1106-1118
    • Dong, J.1    Thompson, A.A.2    Fan, Y.3    Lou, J.4    Conrad, F.5    Ho, M.6    Pires-Alves, M.7    Wilson, B.A.8    Stevens, R.C.9    Marks, J.D.10
  • 115
    • 77749320825 scopus 로고    scopus 로고
    • Llama single domain antibodies specific for the 7 botulinum neurotoxin serotypes as heptaplex immunoreagents
    • Conway, J.O.; Sherwood, L.J.; Collazo, M.T.; Garza, J.A.; Hayhurst, A. Llama single domain antibodies specific for the 7 botulinum neurotoxin serotypes as heptaplex immunoreagents. PLoS ONE 2010, 5, e8818.
    • (2010) PLoS ONE , vol.5
    • Conway, J.O.1    Sherwood, L.J.2    Collazo, M.T.3    Garza, J.A.4    Hayhurst, A.5
  • 116
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • Derossi, D.; Joliot, A.H.; Chassaing, G.; Prochiantz, A. The third helix of the Antennapedia homeodomain translocates through biological membranes. J. Biol. Chem. 1994, 269, 10444-10450.
    • (1994) J. Biol. Chem , vol.269 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 119
    • 33645881104 scopus 로고    scopus 로고
    • Protein transduction technology: A novel therapeutic perspective
    • Noguchi, H.; Matsumoto, S. Protein transduction technology: A novel therapeutic perspective. Acta Med. Okayama 2006, 60, 1-11.
    • (2006) Acta Med. Okayama , vol.60 , pp. 1-11
    • Noguchi, H.1    Matsumoto, S.2
  • 120
    • 0034910022 scopus 로고    scopus 로고
    • Is VP22 nuclear homing an artifact?
    • Lundberg, M.; Johansson, M. Is VP22 nuclear homing an artifact? Nat. Biotechnol. 2001, 19, 713-714.
    • (2001) Nat. Biotechnol , vol.19 , pp. 713-714
    • Lundberg, M.1    Johansson, M.2
  • 121
    • 0141942111 scopus 로고    scopus 로고
    • Membrane translocation of penetratin and its derivatives in different cell lines
    • Letoha, T.; Gaal, S.; Somlai, C.; Czajlik, A.; Perczel, A.; Penke, B. Membrane translocation of penetratin and its derivatives in different cell lines. J. Mol. Recognit. 2003, 16, 272-279.
    • (2003) J. Mol. Recognit , vol.16 , pp. 272-279
    • Letoha, T.1    Gaal, S.2    Somlai, C.3    Czajlik, A.4    Perczel, A.5    Penke, B.6
  • 123
    • 11844268027 scopus 로고    scopus 로고
    • Cationic TAT peptide transduction domain enters cells by macropinocytosis
    • Kaplan, I.M.; Wadia, J.S.; Dowdy, S.F. Cationic TAT peptide transduction domain enters cells by macropinocytosis. J. Control. Release 2005, 102, 247-253.
    • (2005) J. Control. Release , vol.102 , pp. 247-253
    • Kaplan, I.M.1    Wadia, J.S.2    Dowdy, S.F.3
  • 124
    • 17644386231 scopus 로고    scopus 로고
    • Cellular uptake of unconjugated TAT peptide involves clathrin-dependent endocytosis and heparin sulfate receptors
    • Richard, J.P.; Melikov, K.; Brooks, H.; Prevot, P.; Lebleu, B.; Chernomordik, L.V. Cellular uptake of unconjugated TAT peptide involves clathrin-dependent endocytosis and heparin sulfate receptors. J. Biol. Chem. 2005, 280, 15300-15306.
    • (2005) J. Biol. Chem , vol.280 , pp. 15300-15306
    • Richard, J.P.1    Melikov, K.2    Brooks, H.3    Prevot, P.4    Lebleu, B.5    Chernomordik, L.V.6
  • 125
    • 42049095153 scopus 로고    scopus 로고
    • Cell-penetrating peptides: From molecular mechanisms to therapeutics
    • Morris, M.C.; Deshayes, S.; Heitz, F.; Divita, G. Cell-penetrating peptides: From molecular mechanisms to therapeutics. Biol. Cell 2008, 100, 201-217.
    • (2008) Biol. Cell , vol.100 , pp. 201-217
    • Morris, M.C.1    Deshayes, S.2    Heitz, F.3    Divita, G.4
  • 127
    • 23944483437 scopus 로고    scopus 로고
    • Cell-penetrating peptides: Tools for intracellular delivery of therapeutics
    • Deshayes, S.; Morris, M.C.; Divita, G.; Heitz, F. Cell-penetrating peptides: Tools for intracellular delivery of therapeutics. Cell Mol. Life Sci. 2005, 62, 1839-1849.
    • (2005) Cell Mol. Life Sci , vol.62 , pp. 1839-1849
    • Deshayes, S.1    Morris, M.C.2    Divita, G.3    Heitz, F.4


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