메뉴 건너뛰기




Volumn 1858, Issue 3, 2016, Pages 467-474

On the translocation of botulinum and tetanus neurotoxins across the membrane of acidic intracellular compartments

Author keywords

Botulinum neurotoxin isoforms; Clostridia; Duration of neuroparalysis; Endocytosis; Presynaptic binding; Translocation

Indexed keywords

BOTULINUM TOXIN; METALLOPROTEINASE; SNARE PROTEIN; TETANUS TOXIN;

EID: 84956579271     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2015.08.014     Document Type: Review
Times cited : (73)

References (88)
  • 1
    • 84875806832 scopus 로고    scopus 로고
    • Genetic diversity within Clostridium botulinum serotypes, botulinum neurotoxin gene clusters and toxin subtypes
    • K.K. Hill, and T.J. Smith Genetic diversity within Clostridium botulinum serotypes, botulinum neurotoxin gene clusters and toxin subtypes Curr. Top. Microbiol. Immunol. 364 2013 1 20
    • (2013) Curr. Top. Microbiol. Immunol. , vol.364 , pp. 1-20
    • Hill, K.K.1    Smith, T.J.2
  • 2
    • 84904510042 scopus 로고    scopus 로고
    • Botulinum neurotoxins: Genetic, structural and mechanistic insights
    • O. Rossetto, M. Pirazzini, and C. Montecucco Botulinum neurotoxins: genetic, structural and mechanistic insights Nat. Rev. Microbiol. 12 2014 535 549
    • (2014) Nat. Rev. Microbiol. , vol.12 , pp. 535-549
    • Rossetto, O.1    Pirazzini, M.2    Montecucco, C.3
  • 3
    • 84924102121 scopus 로고    scopus 로고
    • On botulinum neurotoxin variability
    • C. Montecucco, and M.B. Rasotto On botulinum neurotoxin variability MBio 6 2015
    • (2015) MBio , vol.6
    • Montecucco, C.1    Rasotto, M.B.2
  • 5
    • 22144452934 scopus 로고    scopus 로고
    • Beyond BOTOX: Advantages and limitations of individual botulinum neurotoxins
    • B. Davletov, M. Bajohrs, and T. Binz Beyond BOTOX: advantages and limitations of individual botulinum neurotoxins Trends Neurosci. 28 2005 446 452
    • (2005) Trends Neurosci. , vol.28 , pp. 446-452
    • Davletov, B.1    Bajohrs, M.2    Binz, T.3
  • 6
    • 18744410709 scopus 로고    scopus 로고
    • Botulinal neurotoxins: Revival of an old killer
    • C. Montecucco, and J. Molgo Botulinal neurotoxins: revival of an old killer Curr. Opin. Pharmacol. 5 2005 274 279
    • (2005) Curr. Opin. Pharmacol. , vol.5 , pp. 274-279
    • Montecucco, C.1    Molgo, J.2
  • 7
    • 84864065068 scopus 로고    scopus 로고
    • Clinical applications of botulinum toxin
    • D. Dressler Clinical applications of botulinum toxin Curr. Opin. Microbiol. 15 2012 325 336
    • (2012) Curr. Opin. Microbiol. , vol.15 , pp. 325-336
    • Dressler, D.1
  • 9
    • 84877687939 scopus 로고    scopus 로고
    • Evidence-based review and assessment of botulinum neurotoxin for the treatment of movement disorders
    • M. Hallett, A. Albanese, D. Dressler, K.R. Segal, D.M. Simpson, D. Truong, and J. Jankovic Evidence-based review and assessment of botulinum neurotoxin for the treatment of movement disorders Toxicon 67 2013 94 114
    • (2013) Toxicon , vol.67 , pp. 94-114
    • Hallett, M.1    Albanese, A.2    Dressler, D.3    Segal, K.R.4    Simpson, D.M.5    Truong, D.6    Jankovic, J.7
  • 10
    • 0031712779 scopus 로고    scopus 로고
    • Crystal structure of botulinum neurotoxin type A and implications for toxicity
    • D.B. Lacy, W. Tepp, A.C. Cohen, B.R. DasGupta, and R.C. Stevens Crystal structure of botulinum neurotoxin type A and implications for toxicity Nat. Struct. Biol. 5 1998 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
    • 0033884053 scopus 로고    scopus 로고
    • Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B
    • S. Swaminathan, and S. Eswaramoorthy Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B Nat. Struct. Biol. 7 2000 693 699
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 693-699
    • Swaminathan, S.1    Eswaramoorthy, S.2
  • 12
    • 58549116147 scopus 로고    scopus 로고
    • Domain organization in Clostridium botulinum neurotoxin type E is unique: Its implication in faster translocation
    • D. Kumaran, S. Eswaramoorthy, W. Furey, J. Navaza, M. Sax, and S. Swaminathan Domain organization in Clostridium botulinum neurotoxin type E is unique: its implication in faster translocation J. Mol. Biol. 386 2009 233 245
    • (2009) J. Mol. Biol. , vol.386 , pp. 233-245
    • Kumaran, D.1    Eswaramoorthy, S.2    Furey, W.3    Navaza, J.4    Sax, M.5    Swaminathan, S.6
  • 13
    • 59649101806 scopus 로고    scopus 로고
    • The N-terminal half of the receptor domain of botulinum neurotoxin A binds to microdomains of the plasma membrane
    • L. Muraro, S. Tosatto, L. Motterlini, O. Rossetto, and C. Montecucco The N-terminal half of the receptor domain of botulinum neurotoxin A binds to microdomains of the plasma membrane Biochem. Biophys. Res. Commun. 380 2009 76 80
    • (2009) Biochem. Biophys. Res. Commun. , vol.380 , pp. 76-80
    • Muraro, L.1    Tosatto, S.2    Motterlini, L.3    Rossetto, O.4    Montecucco, C.5
  • 14
    • 84857049268 scopus 로고    scopus 로고
    • The receptor binding domain of botulinum neurotoxin serotype C binds phosphoinositides
    • Y. Zhang, and S.M. Varnum The receptor binding domain of botulinum neurotoxin serotype C binds phosphoinositides Biochimie 94 2012 920 923
    • (2012) Biochimie , vol.94 , pp. 920-923
    • Zhang, Y.1    Varnum, S.M.2
  • 15
    • 65949090949 scopus 로고    scopus 로고
    • Cell entry strategy of clostridial neurotoxins
    • T. Binz, and A. Rummel Cell entry strategy of clostridial neurotoxins J. Neurochem. 109 2009 1584 1595
    • (2009) J. Neurochem. , vol.109 , pp. 1584-1595
    • Binz, T.1    Rummel, A.2
  • 16
    • 84893825555 scopus 로고    scopus 로고
    • The blockade of the neurotransmitter release apparatus by botulinum neurotoxins
    • S. Pantano, and C. Montecucco The blockade of the neurotransmitter release apparatus by botulinum neurotoxins Cell. Mol. Life Sci. 71 2013 739 811
    • (2013) Cell. Mol. Life Sci. , vol.71 , pp. 739-811
    • Pantano, S.1    Montecucco, C.2
  • 17
    • 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
    • M. Pirazzini, O. Rossetto, P. Bolognese, C.C. Shone, and C. Montecucco 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. 13 2011 1731 1743
    • (2011) Cell. Microbiol. , vol.13 , pp. 1731-1743
    • Pirazzini, M.1    Rossetto, O.2    Bolognese, P.3    Shone, C.C.4    Montecucco, C.5
  • 18
    • 84923190210 scopus 로고    scopus 로고
    • Botulinum neurotoxins: New questions arising from structural biology
    • R.A. Kammerer, and R.M. Benoit Botulinum neurotoxins: new questions arising from structural biology Trends Biochem. Sci. 39 2014 517 526
    • (2014) Trends Biochem. Sci. , vol.39 , pp. 517-526
    • Kammerer, R.A.1    Benoit, R.M.2
  • 21
    • 84880917746 scopus 로고    scopus 로고
    • Botulinum neurotoxin type A is internalized and translocated from small synaptic vesicles at the neuromuscular junction
    • C. Colasante, O. Rossetto, L. Morbiato, M. Pirazzini, J. Molgo, and C. Montecucco Botulinum neurotoxin type A is internalized and translocated from small synaptic vesicles at the neuromuscular junction Mol. Neurobiol. 48 2013 120 127
    • (2013) Mol. Neurobiol. , vol.48 , pp. 120-127
    • Colasante, C.1    Rossetto, O.2    Morbiato, L.3    Pirazzini, M.4    Molgo, J.5    Montecucco, C.6
  • 22
    • 84875809331 scopus 로고    scopus 로고
    • Double receptor anchorage of botulinum neurotoxins accounts for their exquisite neurospecificity
    • A. Rummel Double receptor anchorage of botulinum neurotoxins accounts for their exquisite neurospecificity Curr. Top. Microbiol. Immunol. 364 2013 61 90
    • (2013) Curr. Top. Microbiol. Immunol. , vol.364 , pp. 61-90
    • Rummel, A.1
  • 23
    • 0032500053 scopus 로고    scopus 로고
    • Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins
    • G. Miesenbock, D.A. De Angelis, and J.E. Rothman Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins Nature 394 1998 192 195
    • (1998) Nature , vol.394 , pp. 192-195
    • Miesenbock, G.1    De Angelis, D.A.2    Rothman, J.E.3
  • 24
    • 0033786834 scopus 로고    scopus 로고
    • Real-time measurements of vesicle-SNARE recycling in synapses of the central nervous system
    • S. Sankaranarayanan, and T.A. Ryan Real-time measurements of vesicle-SNARE recycling in synapses of the central nervous system Nat. Cell Biol. 2 2000 197 204
    • (2000) Nat. Cell Biol. , vol.2 , pp. 197-204
    • Sankaranarayanan, S.1    Ryan, T.A.2
  • 25
    • 77953642001 scopus 로고    scopus 로고
    • Botulinum neurotoxin: A marvel of protein design
    • M. Montal Botulinum neurotoxin: a marvel of protein design Annu. Rev. Biochem. 79 2010 591 617
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 591-617
    • Montal, M.1
  • 26
    • 84885297288 scopus 로고    scopus 로고
    • Molecular dissection of botulinum neurotoxin reveals interdomain chaperone function
    • A. Fischer, and M. Montal Molecular dissection of botulinum neurotoxin reveals interdomain chaperone function Toxicon 75 2013 101 107
    • (2013) Toxicon , vol.75 , pp. 101-107
    • Fischer, A.1    Montal, M.2
  • 27
    • 0345570658 scopus 로고
    • Channels formed by botulinum, tetanus, and diphtheria toxins in planar lipid bilayers: Relevance to translocation of proteins across membranes
    • D.H. Hoch, M. Romero-Mira, B.E. Ehrlich, A. Finkelstein, B.R. DasGupta, and L.L. Simpson Channels formed by botulinum, tetanus, and diphtheria toxins in planar lipid bilayers: relevance to translocation of proteins across membranes Proc. Natl. Acad. Sci. U. S. A. 82 1985 1692 1696
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 1692-1696
    • Hoch, D.H.1    Romero-Mira, M.2    Ehrlich, B.E.3    Finkelstein, A.4    DasGupta, B.R.5    Simpson, L.L.6
  • 28
    • 0022485787 scopus 로고
    • Ion-conducting channels produced by botulinum toxin in planar lipid membranes
    • J.J. Donovan, and J.L. Middlebrook Ion-conducting channels produced by botulinum toxin in planar lipid membranes Biochemistry 25 1986 2872 2876
    • (1986) Biochemistry , vol.25 , pp. 2872-2876
    • Donovan, J.J.1    Middlebrook, J.L.2
  • 29
    • 0029613765 scopus 로고
    • Structure and function of tetanus and botulinum neurotoxins
    • C. Montecucco, and G. Schiavo Structure and function of tetanus and botulinum neurotoxins Q. Rev. Biophys. 28 1995 423 472
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 423-472
    • Montecucco, C.1    Schiavo, G.2
  • 30
    • 0037222077 scopus 로고    scopus 로고
    • Translocation of botulinum neurotoxin light chain protease through the heavy chain channel
    • L.K. Koriazova, and M. Montal Translocation of botulinum neurotoxin light chain protease through the heavy chain channel Nat. Struct. Biol. 10 2003 13 18
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 13-18
    • Koriazova, L.K.1    Montal, M.2
  • 31
    • 34547509346 scopus 로고    scopus 로고
    • Single molecule detection of intermediates during botulinum neurotoxin translocation across membranes
    • A. Fischer, and M. Montal Single molecule detection of intermediates during botulinum neurotoxin translocation across membranes Proc. Natl. Acad. Sci. U. S. A. 104 2007 10447 10452
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 10447-10452
    • Fischer, A.1    Montal, M.2
  • 33
    • 35748961106 scopus 로고    scopus 로고
    • Crucial role of the disulfide bridge between botulinum neurotoxin light and heavy chains in protease translocation across membranes
    • A. Fischer, and M. Montal Crucial role of the disulfide bridge between botulinum neurotoxin light and heavy chains in protease translocation across membranes J. Biol. Chem. 282 2007 29604 29611
    • (2007) J. Biol. Chem. , vol.282 , pp. 29604-29611
    • Fischer, A.1    Montal, M.2
  • 34
    • 0031840854 scopus 로고    scopus 로고
    • Gating and permeability of ion channels produced by botulinum toxin types A and E in PC12 cell membranes
    • R.E. Sheridan Gating and permeability of ion channels produced by botulinum toxin types A and E in PC12 cell membranes Toxicon 36 1998 703 717
    • (1998) Toxicon , vol.36 , pp. 703-717
    • Sheridan, R.E.1
  • 35
  • 36
    • 84863961448 scopus 로고    scopus 로고
    • Botulinum neurotoxins B and E translocate at different rates and exhibit divergent responses to GT1b and low pH
    • S. Sun, W.H. Tepp, E.A. Johnson, and E.R. Chapman Botulinum neurotoxins B and E translocate at different rates and exhibit divergent responses to GT1b and low pH Biochemistry 51 2012 5655 5662
    • (2012) Biochemistry , vol.51 , pp. 5655-5662
    • Sun, S.1    Tepp, W.H.2    Johnson, E.A.3    Chapman, E.R.4
  • 37
    • 0033135752 scopus 로고    scopus 로고
    • Conductive properties and gating of channels formed by syringopeptin 25A, a bioactive lipodepsipeptide from Pseudomonas syringae pv. Syringae, in planar lipid membranes, Mol. Plant Microbe
    • M. Dalla Serra, I. Bernhart, P. Nordera, D. Di Giorgio, A. Ballio, and G. Menestrina Conductive properties and gating of channels formed by syringopeptin 25A, a bioactive lipodepsipeptide from Pseudomonas syringae pv. syringae, in planar lipid membranes, Mol. Plant Microbe Interactions 12 1999 401 409
    • (1999) Interactions , vol.12 , pp. 401-409
    • Dalla Serra, M.1    Bernhart, I.2    Nordera, P.3    Di Giorgio, D.4    Ballio, A.5    Menestrina, G.6
  • 38
    • 33847117686 scopus 로고    scopus 로고
    • Comparative membrane channel size and activity of botulinum neurotoxins A and E
    • S. Parikh, and B.R. Singh Comparative membrane channel size and activity of botulinum neurotoxins A and E Protein J. 26 2007 19 28
    • (2007) Protein J. , vol.26 , pp. 19-28
    • Parikh, S.1    Singh, B.R.2
  • 40
    • 58149252452 scopus 로고    scopus 로고
    • Botulinum neurotoxin devoid of receptor binding domain translocates active protease
    • A. Fischer, D.J. Mushrush, D.B. Lacy, and M. Montal Botulinum neurotoxin devoid of receptor binding domain translocates active protease PLoS Pathog. 4 2008 e1000245
    • (2008) PLoS Pathog. , vol.4
    • Fischer, A.1    Mushrush, D.J.2    Lacy, D.B.3    Montal, M.4
  • 42
    • 0025648954 scopus 로고
    • An intact interchain disulfide bond is required for the neurotoxicity of tetanus toxin
    • G. Schiavo, E. Papini, G. Genna, and C. Montecucco An intact interchain disulfide bond is required for the neurotoxicity of tetanus toxin Infect. Immun. 58 1990 4136 4141
    • (1990) Infect. Immun. , vol.58 , pp. 4136-4141
    • Schiavo, G.1    Papini, E.2    Genna, G.3    Montecucco, C.4
  • 43
    • 0027442858 scopus 로고
    • A role for the interchain disulfide or its participating thiols in the internalization of botulinum neurotoxin A revealed by a toxin derivative that binds to ecto-acceptors and inhibits transmitter release intracellularly
    • A. de Paiva, B. Poulain, G.W. Lawrence, C.C. Shone, L. Tauc, and J.O. Dolly A role for the interchain disulfide or its participating thiols in the internalization of botulinum neurotoxin A revealed by a toxin derivative that binds to ecto-acceptors and inhibits transmitter release intracellularly J. Biol. Chem. 268 1993 20838 20844
    • (1993) J. Biol. Chem. , vol.268 , pp. 20838-20844
    • De Paiva, A.1    Poulain, B.2    Lawrence, G.W.3    Shone, C.C.4    Tauc, L.5    Dolly, J.O.6
  • 44
    • 10644230055 scopus 로고    scopus 로고
    • Botulinum neurotoxin type D enables cytosolic delivery of enzymatically active cargo proteins to neurones via unfolded translocation intermediates
    • S. Bade, A. Rummel, C. Reisinger, T. Karnath, G. Ahnert-Hilger, H. Bigalke, and T. Binz Botulinum neurotoxin type D enables cytosolic delivery of enzymatically active cargo proteins to neurones via unfolded translocation intermediates J. Neurochem. 91 2004 1461 1472
    • (2004) J. Neurochem. , vol.91 , pp. 1461-1472
    • Bade, S.1    Rummel, A.2    Reisinger, C.3    Karnath, T.4    Ahnert-Hilger, G.5    Bigalke, H.6    Binz, T.7
  • 45
    • 1442349932 scopus 로고    scopus 로고
    • Role of metals in the biological activity of Clostridium botulinum neurotoxins
    • S. Eswaramoorthy, D. Kumaran, J. Keller, and S. Swaminathan Role of metals in the biological activity of Clostridium botulinum neurotoxins Biochemistry 43 2004 2209 2216
    • (2004) Biochemistry , vol.43 , pp. 2209-2216
    • Eswaramoorthy, S.1    Kumaran, D.2    Keller, J.3    Swaminathan, S.4
  • 46
    • 55549106809 scopus 로고    scopus 로고
    • Membrane Interaction of botulinum neurotoxin A translocation (T) domain. The belt region is a regulatory loop for membrane interaction
    • M. Galloux, H. Vitrac, C. Montagner, S. Raffestin, M.R. Popoff, A. Chenal, V. Forge, and D. Gillet Membrane Interaction of botulinum neurotoxin A translocation (T) domain. The belt region is a regulatory loop for membrane interaction J. Biol. Chem. 283 2008 27668 27676
    • (2008) J. Biol. Chem. , vol.283 , pp. 27668-27676
    • Galloux, M.1    Vitrac, H.2    Montagner, C.3    Raffestin, S.4    Popoff, M.R.5    Chenal, A.6    Forge, V.7    Gillet, D.8
  • 47
    • 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
    • F.N. Fu, D.D. Busath, and B.R. Singh Spectroscopic analysis of low pH and lipid-induced structural changes in type A botulinum neurotoxin relevant to membrane channel formation and translocation Biophys. Chem. 99 2002 17 29
    • (2002) Biophys. Chem. , vol.99 , pp. 17-29
    • Fu, F.N.1    Busath, D.D.2    Singh, B.R.3
  • 48
    • 2442719960 scopus 로고    scopus 로고
    • Comparison of the pH-induced conformational change of different clostridial neurotoxins
    • A. Puhar, E.A. Johnson, O. Rossetto, and C. Montecucco Comparison of the pH-induced conformational change of different clostridial neurotoxins Biochem. Biophys. Res. Commun. 319 2004 66 71
    • (2004) Biochem. Biophys. Res. Commun. , vol.319 , pp. 66-71
    • Puhar, A.1    Johnson, E.A.2    Rossetto, O.3    Montecucco, C.4
  • 50
    • 0024506750 scopus 로고
    • Effect of pH on the interaction of botulinum neurotoxins A, B and E with liposomes
    • C. Montecucco, G. Schiavo, and B.R. Dasgupta Effect of pH on the interaction of botulinum neurotoxins A, B and E with liposomes Biochem. J. 259 1989 47 53
    • (1989) Biochem. J. , vol.259 , pp. 47-53
    • Montecucco, C.1    Schiavo, G.2    Dasgupta, B.R.3
  • 51
    • 10044247127 scopus 로고    scopus 로고
    • Evidence that translocation of anthrax toxin's lethal factor is initiated by entry of its N terminus into the protective antigen channel
    • S. Zhang, A. Finkelstein, and R.J. Collier Evidence that translocation of anthrax toxin's lethal factor is initiated by entry of its N terminus into the protective antigen channel Proc. Natl. Acad. Sci. U. S. A. 101 2004 16756 16761
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 16756-16761
    • Zhang, S.1    Finkelstein, A.2    Collier, R.J.3
  • 52
    • 33644689443 scopus 로고    scopus 로고
    • Anthrax lethal factor (LF) mediated block of the anthrax protective antigen (PA) ion channel: Effect of ionic strength and voltage
    • T. Neumeyer, F. Tonello, F. Dal Molin, B. Schiffler, F. Orlik, and R. Benz Anthrax lethal factor (LF) mediated block of the anthrax protective antigen (PA) ion channel: effect of ionic strength and voltage Biochemistry 45 2006 3060 3068
    • (2006) Biochemistry , vol.45 , pp. 3060-3068
    • Neumeyer, T.1    Tonello, F.2    Dal Molin, F.3    Schiffler, B.4    Orlik, F.5    Benz, R.6
  • 53
    • 79955650637 scopus 로고    scopus 로고
    • Trapping a translocating protein within the anthrax toxin channel: Implications for the secondary structure of permeating proteins
    • D. Basilio, L.D. Jennings-Antipov, K.S. Jakes, and A. Finkelstein Trapping a translocating protein within the anthrax toxin channel: implications for the secondary structure of permeating proteins J. Gen. Physiol. 137 2011 343 356
    • (2011) J. Gen. Physiol. , vol.137 , pp. 343-356
    • Basilio, D.1    Jennings-Antipov, L.D.2    Jakes, K.S.3    Finkelstein, A.4
  • 55
    • 28644432877 scopus 로고    scopus 로고
    • Very fast empirical prediction and rationalization of protein pKa values
    • H. Li, A.D. Robertson, and J.H. Jensen Very fast empirical prediction and rationalization of protein pKa values Proteins 61 2005 704 721
    • (2005) Proteins , vol.61 , pp. 704-721
    • Li, H.1    Robertson, A.D.2    Jensen, J.H.3
  • 56
    • 84888003275 scopus 로고    scopus 로고
    • Neutralisation of specific surface carboxylates speeds up translocation of botulinum neurotoxin type B enzymatic domain
    • M. Pirazzini, T. Henke, O. Rossetto, S. Mahrhold, N. Krez, A. Rummel, C. Montecucco, and T. Binz Neutralisation of specific surface carboxylates speeds up translocation of botulinum neurotoxin type B enzymatic domain FEBS Lett. 587 2013 3831 3836
    • (2013) FEBS Lett. , vol.587 , pp. 3831-3836
    • Pirazzini, M.1    Henke, T.2    Rossetto, O.3    Mahrhold, S.4    Krez, N.5    Rummel, A.6    Montecucco, C.7    Binz, T.8
  • 57
    • 0019884688 scopus 로고
    • Lipids of synaptic vesicles: Relevance to the mechanism of membrane fusion
    • J.W. Deutsch, and R.B. Kelly Lipids of synaptic vesicles: relevance to the mechanism of membrane fusion Biochemistry 20 1981 378 385
    • (1981) Biochemistry , vol.20 , pp. 378-385
    • Deutsch, J.W.1    Kelly, R.B.2
  • 58
    • 0027482702 scopus 로고
    • Ganglioside composition of subcellular fractions, including pre- and postsynaptic membranes, from Torpedo electric organ
    • R.W. Ledeen, M.F. Diebler, G. Wu, Z.H. Lu, and H. Varoqui Ganglioside composition of subcellular fractions, including pre- and postsynaptic membranes, from Torpedo electric organ Neurochem. Res. 18 1993 1151 1155
    • (1993) Neurochem. Res. , vol.18 , pp. 1151-1155
    • Ledeen, R.W.1    Diebler, M.F.2    Wu, G.3    Lu, Z.H.4    Varoqui, H.5
  • 59
    • 0343471423 scopus 로고    scopus 로고
    • The adsorption of Pseudomonas aeruginosa exotoxin A to phospholipid monolayers is controlled by pH and surface potential
    • P. Nordera, M.D. Serra, and G. Menestrina The adsorption of Pseudomonas aeruginosa exotoxin A to phospholipid monolayers is controlled by pH and surface potential Biophys. J. 73 1997 1468 1478
    • (1997) Biophys. J. , vol.73 , pp. 1468-1478
    • Nordera, P.1    Serra, M.D.2    Menestrina, G.3
  • 60
    • 9144247030 scopus 로고    scopus 로고
    • The role of lipids in membrane insertion and translocation of bacterial proteins
    • A. van Dalen, and B. de Kruijff The role of lipids in membrane insertion and translocation of bacterial proteins Biochim. Biophys. Acta 1694 2004 97 109
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 97-109
    • Van Dalen, A.1    De Kruijff, B.2
  • 61
    • 0023710642 scopus 로고
    • The 'molten globule' state is involved in the translocation of proteins across membranes?
    • V.E. Bychkova, R.H. Pain, and O.B. Ptitsyn The 'molten globule' state is involved in the translocation of proteins across membranes? FEBS Lett. 238 1988 231 234
    • (1988) FEBS Lett. , vol.238 , pp. 231-234
    • Bychkova, V.E.1    Pain, R.H.2    Ptitsyn, O.B.3
  • 62
  • 63
    • 0025932041 scopus 로고
    • A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A
    • F.G. van der Goot, J.M. Gonzalez-Manas, J.H. Lakey, and F. Pattus A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A Nature 354 1991 408 410
    • (1991) Nature , vol.354 , pp. 408-410
    • Van Der Goot, F.G.1    Gonzalez-Manas, J.M.2    Lakey, J.H.3    Pattus, F.4
  • 64
    • 28244483285 scopus 로고    scopus 로고
    • Biologically active novel conformational state of botulinum, the most poisonous poison
    • R. Kukreja, and B. Singh Biologically active novel conformational state of botulinum, the most poisonous poison J. Biol. Chem. 280 2005 39346 39352
    • (2005) J. Biol. Chem. , vol.280 , pp. 39346-39352
    • Kukreja, R.1    Singh, B.2
  • 65
    • 79953184288 scopus 로고    scopus 로고
    • A dileucine in the protease of botulinum toxin A underlies its long-lived neuroparalysis: Transfer of longevity to a novel potential therapeutic
    • J. Wang, T.H. Zurawski, J. Meng, G. Lawrence, W.M. Olango, D.P. Finn, L. Wheeler, and J.O. Dolly A dileucine in the protease of botulinum toxin A underlies its long-lived neuroparalysis: transfer of longevity to a novel potential therapeutic J. Biol. Chem. 286 2011 6375 6385
    • (2011) J. Biol. Chem. , vol.286 , pp. 6375-6385
    • Wang, J.1    Zurawski, T.H.2    Meng, J.3    Lawrence, G.4    Olango, W.M.5    Finn, D.P.6    Wheeler, L.7    Dolly, J.O.8
  • 66
    • 0345668477 scopus 로고    scopus 로고
    • The cytosolic entry of diphtheria toxin catalytic domain requires a host cell cytosolic translocation factor complex
    • R. Ratts, H. Zeng, E.A. Berg, C. Blue, M.E. McComb, C.E. Costello, J.C. vanderSpek, and J.R. Murphy The cytosolic entry of diphtheria toxin catalytic domain requires a host cell cytosolic translocation factor complex J. Cell Biol. 160 2003 1139 1150
    • (2003) J. Cell Biol. , vol.160 , pp. 1139-1150
    • Ratts, R.1    Zeng, H.2    Berg, E.A.3    Blue, C.4    McComb, M.E.5    Costello, C.E.6    VanderSpek, J.C.7    Murphy, J.R.8
  • 67
    • 84896403067 scopus 로고    scopus 로고
    • The chaperone Hsp90 and PPIases of the cyclophilin and FKBP families facilitate membrane translocation of Photorhabdus luminescens ADP-ribosyltransferases
    • A.E. Lang, K. Ernst, H. Lee, P. Papatheodorou, C. Schwan, H. Barth, and K. Aktories The chaperone Hsp90 and PPIases of the cyclophilin and FKBP families facilitate membrane translocation of Photorhabdus luminescens ADP-ribosyltransferases Cell. Microbiol. 16 2014 490 503
    • (2014) Cell. Microbiol. , vol.16 , pp. 490-503
    • Lang, A.E.1    Ernst, K.2    Lee, H.3    Papatheodorou, P.4    Schwan, C.5    Barth, H.6    Aktories, K.7
  • 69
    • 84866388574 scopus 로고    scopus 로고
    • Bacterial protein translocation requires only one copy of the SecY complex in vivo
    • E. Park, and T.A. Rapoport Bacterial protein translocation requires only one copy of the SecY complex in vivo J. Cell Biol. 198 2012 881 893
    • (2012) J. Cell Biol. , vol.198 , pp. 881-893
    • Park, E.1    Rapoport, T.A.2
  • 70
    • 0033735495 scopus 로고    scopus 로고
    • The diphtheria toxin channel-forming T-domain translocates its own NH2-terminal region and the catalytic domain across planar phospholipid bilayers
    • A. Finkelstein, K.J. Oh, L. Senzel, M. Gordon, R.O. Blaustein, and R.J. Collier The diphtheria toxin channel-forming T-domain translocates its own NH2-terminal region and the catalytic domain across planar phospholipid bilayers Int. J. Med. Microbiol.IJMM 290 2000 435 440
    • (2000) Int. J. Med. Microbiol.IJMM , vol.290 , pp. 435-440
    • Finkelstein, A.1    Oh, K.J.2    Senzel, L.3    Gordon, M.4    Blaustein, R.O.5    Collier, R.J.6
  • 71
    • 0035169411 scopus 로고    scopus 로고
    • The number of subunits comprising the channel formed by the T domain of diphtheria toxin
    • M. Gordon, and A. Finkelstein The number of subunits comprising the channel formed by the T domain of diphtheria toxin J. Gen. Physiol. 118 2001 471 480
    • (2001) J. Gen. Physiol. , vol.118 , pp. 471-480
    • Gordon, M.1    Finkelstein, A.2
  • 73
    • 79956338948 scopus 로고    scopus 로고
    • Phrenic nerve-hemidiaphragm as a highly sensitive replacement assay for determination of functional botulinum toxin antibodies
    • C. Rasetti-Escargueil, Y. Liu, P. Rigsby, R.G. Jones, and D. Sesardic Phrenic nerve-hemidiaphragm as a highly sensitive replacement assay for determination of functional botulinum toxin antibodies Toxicon 57 2011 1008 1016
    • (2011) Toxicon , vol.57 , pp. 1008-1016
    • Rasetti-Escargueil, C.1    Liu, Y.2    Rigsby, P.3    Jones, R.G.4    Sesardic, D.5
  • 74
    • 84919763571 scopus 로고    scopus 로고
    • Protein co-translocational unfolding depends on the direction of pulling
    • D. Rodriguez-Larrea, and H. Bayley Protein co-translocational unfolding depends on the direction of pulling Nat. Commun. 5 2014 4841
    • (2014) Nat. Commun. , vol.5 , pp. 4841
    • Rodriguez-Larrea, D.1    Bayley, H.2
  • 75
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • E.S. Arner, and A. Holmgren Physiological functions of thioredoxin and thioredoxin reductase Eur. J. Biochem. 267 2000 6102 6109
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6102-6109
    • Arner, E.S.1    Holmgren, A.2
  • 76
    • 73349133007 scopus 로고    scopus 로고
    • Thioredoxins and glutaredoxins: Unifying elements in redox biology
    • Y. Meyer, B.B. Buchanan, F. Vignols, and J.P. Reichheld Thioredoxins and glutaredoxins: unifying elements in redox biology Annu. Rev. Genet. 43 2009 335 367
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 335-367
    • Meyer, Y.1    Buchanan, B.B.2    Vignols, F.3    Reichheld, J.P.4
  • 77
    • 84876917760 scopus 로고    scopus 로고
    • Thioredoxins, glutaredoxins, and peroxiredoxins - Molecular mechanisms and health significance: From cofactors to antioxidants to redox signaling
    • E.M. Hanschmann, J.R. Godoy, C. Berndt, C. Hudemann, and C.H. Lillig Thioredoxins, glutaredoxins, and peroxiredoxins - molecular mechanisms and health significance: from cofactors to antioxidants to redox signaling Antioxid. Redox Signal. 19 2013 1539 1605
    • (2013) Antioxid. Redox Signal. , vol.19 , pp. 1539-1605
    • Hanschmann, E.M.1    Godoy, J.R.2    Berndt, C.3    Hudemann, C.4    Lillig, C.H.5
  • 78
    • 84872100030 scopus 로고    scopus 로고
    • The thioredoxin reductase-thioredoxin system is involved in the entry of tetanus and botulinum neurotoxins in the cytosol of nerve terminals
    • M. Pirazzini, F. Bordin, O. Rossetto, C.C. Shone, T. Binz, and C. Montecucco The thioredoxin reductase-thioredoxin system is involved in the entry of tetanus and botulinum neurotoxins in the cytosol of nerve terminals FEBS Lett. 587 2013 150 155
    • (2013) FEBS Lett. , vol.587 , pp. 150-155
    • Pirazzini, M.1    Bordin, F.2    Rossetto, O.3    Shone, C.C.4    Binz, T.5    Montecucco, C.6
  • 80
    • 84928389594 scopus 로고    scopus 로고
    • Thioredoxin reductase inhibitor auranofin prevents membrane transport of diphtheria toxin into the cytosol and protects human cells from intoxication
    • pii: S0041-0101(15)00109-9 [Epub ahead of print]
    • L. Schnell, L. Dmochewitz-Kück, P. Feigl, C. Montecucco, and H. Barth Thioredoxin reductase inhibitor auranofin prevents membrane transport of diphtheria toxin into the cytosol and protects human cells from intoxication Toxicon 2015 10.1016/j.toxicon.2015.04.012 pii: S0041-0101(15)00109-9 [Epub ahead of print]
    • (2015) Toxicon
    • Schnell, L.1    Dmochewitz-Kück, L.2    Feigl, P.3    Montecucco, C.4    Barth, H.5
  • 81
    • 0027510933 scopus 로고
    • Cell penetration of diphtheria toxin. Reduction of the interchain disulfide bridge is the rate-limiting step of translocation in the cytosol
    • E. Papini, R. Rappuoli, M. Murgia, and C. Montecucco Cell penetration of diphtheria toxin. Reduction of the interchain disulfide bridge is the rate-limiting step of translocation in the cytosol J. Biol. Chem. 268 1993 1567 1574
    • (1993) J. Biol. Chem. , vol.268 , pp. 1567-1574
    • Papini, E.1    Rappuoli, R.2    Murgia, M.3    Montecucco, C.4
  • 82
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution
    • R.B. Sutton, D. Fasshauer, R. Jahn, and A.T. Brunger Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution Nature 395 1998 347 353
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 84
    • 68949179783 scopus 로고    scopus 로고
    • Receptor and substrate interactions of clostridial neurotoxins
    • A.T. Brunger, and A. Rummel Receptor and substrate interactions of clostridial neurotoxins Toxicon 54 2009 550 560
    • (2009) Toxicon , vol.54 , pp. 550-560
    • Brunger, A.T.1    Rummel, A.2
  • 85
    • 84875805299 scopus 로고    scopus 로고
    • Clostridial neurotoxin light chains: Devices for SNARE cleavage mediated blockade of neurotransmission
    • T. Binz Clostridial neurotoxin light chains: devices for SNARE cleavage mediated blockade of neurotransmission Curr. Top. Microbiol. Immunol. 364 2013 139 157
    • (2013) Curr. Top. Microbiol. Immunol. , vol.364 , pp. 139-157
    • Binz, T.1
  • 86
    • 0034121745 scopus 로고    scopus 로고
    • How botulinum and tetanus neurotoxins block neurotransmitter release
    • Y. Humeau, F. Doussau, N.J. Grant, and B. Poulain How botulinum and tetanus neurotoxins block neurotransmitter release Biochimie 82 2000 427 446
    • (2000) Biochimie , vol.82 , pp. 427-446
    • Humeau, Y.1    Doussau, F.2    Grant, N.J.3    Poulain, B.4
  • 87
    • 79952096138 scopus 로고    scopus 로고
    • Clostridial neurotoxins: Mechanism of SNARE cleavage and outlook on potential substrate specificity reengineering
    • T. Binz, S. Sikorra, and S. Mahrhold Clostridial neurotoxins: mechanism of SNARE cleavage and outlook on potential substrate specificity reengineering Toxins 2 2010 665 682
    • (2010) Toxins , vol.2 , pp. 665-682
    • Binz, T.1    Sikorra, S.2    Mahrhold, S.3
  • 88
    • 84875808763 scopus 로고    scopus 로고
    • Synchronized chaperone function of botulinum neurotoxin domains mediates light chain translocation into neurons
    • A. Fischer Synchronized chaperone function of botulinum neurotoxin domains mediates light chain translocation into neurons Curr. Top. Microbiol. Immunol. 364 2013 115 137
    • (2013) Curr. Top. Microbiol. Immunol. , vol.364 , pp. 115-137
    • Fischer, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.