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Volumn 91, Issue 6, 2004, Pages 1461-1472

Botulinum neurotoxin type D enables cytosolic delivery of enzymatically active cargo proteins to neurones via unfolded translocation intermediates

Author keywords

Dihydrofolate reductase; Fusion protein; Green fluorescent protein; Luciferase; Neuronal transporter protein; Recombinant botulinum neurotoxin

Indexed keywords

BACTERIAL PROTEIN; BOTULINUM TOXIN; BOTULINUM TOXIN D; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; LUCIFERASE; NEUROTOXIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 10644230055     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2004.02844.x     Document Type: Article
Times cited : (91)

References (60)
  • 1
    • 0034737317 scopus 로고    scopus 로고
    • Cyclophilin promoted folding of mouse dihydrofolate reductase does not include the slow conversion of the late-folding intermediate to the active enzyme
    • von Ahsen O., Lim J. H., Caspers P., Martin F., Schonfeld H. J., Rassow J. and Pfanner N. (2000) Cyclophilin promoted folding of mouse dihydrofolate reductase does not include the slow conversion of the late-folding intermediate to the active enzyme. J. Mol. Biol. 297, 809-818.
    • (2000) J. Mol. Biol. , vol.297 , pp. 809-818
    • Von Ahsen, O.1    Lim, J.H.2    Caspers, P.3    Martin, F.4    Schonfeld, H.J.5    Rassow, J.6    Pfanner, N.7
  • 2
    • 0030857977 scopus 로고    scopus 로고
    • Ricin A chain can transport unfolded dihydrofolate reductase into the cytosol
    • Beaumelle B., Taupiac M. P., Lord J. M. and Roberts L. M. (1997) Ricin A chain can transport unfolded dihydrofolate reductase into the cytosol. J. Biol. Chem. 272, 22 097-22 102.
    • (1997) J. Biol. Chem. , vol.272
    • Beaumelle, B.1    Taupiac, M.P.2    Lord, J.M.3    Roberts, L.M.4
  • 5
    • 0021162559 scopus 로고
    • Low pH induces a hydrophobic domain in the tetanus toxin molecule
    • Boquet P., Duflot E. and Hauttecoeur B. (1984) Low pH induces a hydrophobic domain in the tetanus toxin molecule. Eur. J. Biochem. 144, 339-344.
    • (1984) Eur. J. Biochem. , vol.144 , pp. 339-344
    • Boquet, P.1    Duflot, E.2    Hauttecoeur, B.3
  • 6
    • 0034528086 scopus 로고    scopus 로고
    • Duration of effect of botulinum toxin type A in adult patients with cervical dystonia: A retrospective chart review
    • Brashear A., Watts M. W., Marchetti A., Magar R., Lau H. and Wang L. (2000) Duration of effect of botulinum toxin type A in adult patients with cervical dystonia: a retrospective chart review. Clin. Ther. 22, 1516-1524.
    • (2000) Clin. Ther. , vol.22 , pp. 1516-1524
    • Brashear, A.1    Watts, M.W.2    Marchetti, A.3    Magar, R.4    Lau, H.5    Wang, L.6
  • 7
    • 0030953638 scopus 로고    scopus 로고
    • Structural basis for dual excitation and photoisomerization of the Aequorea victoria green fluorescent protein
    • Brejc K., Sixma T. K., Kitts P. A., Kain S. R., Tsien R. Y., Ormo M. and Remington S. J. (1997) Structural basis for dual excitation and photoisomerization of the Aequorea victoria green fluorescent protein. Proc. Natl Acad. Sci. USA 94, 2306-2311.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 2306-2311
    • Brejc, K.1    Sixma, T.K.2    Kitts, P.A.3    Kain, S.R.4    Tsien, R.Y.5    Ormo, M.6    Remington, S.J.7
  • 8
    • 0027990854 scopus 로고
    • Evidence that protein kinase C activities involved in regulating neurite growth are localized to distal neurites
    • Campenot R. B., Draker D. D. and Senger D. L. (1994) Evidence that protein kinase C activities involved in regulating neurite growth are localized to distal neurites. J. Neurochem. 63, 868-878.
    • (1994) J. Neurochem. , vol.63 , pp. 868-878
    • Campenot, R.B.1    Draker, D.D.2    Senger, D.L.3
  • 9
    • 0034114106 scopus 로고    scopus 로고
    • Inhibition of vesicular secretion in both neuronal and nonneuronal cells by a retargeted endopeptidase derivative of Clostridium botulinum neurotoxin type A
    • Chaddock J. A., Purkiss J. R., Friis L. M., Broadbridge J. D., Duggan M. J., Fooks S. J., Shone C. C., Quinn C. P. and Foster K. A. (2000a) Inhibition of vesicular secretion in both neuronal and nonneuronal cells by a retargeted endopeptidase derivative of Clostridium botulinum neurotoxin type A. Infect. Immun. 68, 2587-2593.
    • (2000) Infect. Immun. , vol.68 , pp. 2587-2593
    • Chaddock, J.A.1    Purkiss, J.R.2    Friis, L.M.3    Broadbridge, J.D.4    Duggan, M.J.5    Fooks, S.J.6    Shone, C.C.7    Quinn, C.P.8    Foster, K.A.9
  • 10
    • 0033800350 scopus 로고    scopus 로고
    • A conjugate composed of nerve growth factor coupled to a non-toxic derivative of Clostridium botulinum neurotoxin type A can inhibit neurotransmitter release in vitro
    • Chaddock J. A., Purkiss J. R., Duggan M. J., Quinn C. P., Shone C. C. and Foster K. A. (2000b) A conjugate composed of nerve growth factor coupled to a non-toxic derivative of Clostridium botulinum neurotoxin type A can inhibit neurotransmitter release in vitro. Growth Factors 18, 147-155.
    • (2000) Growth Factors , vol.18 , pp. 147-155
    • Chaddock, J.A.1    Purkiss, J.R.2    Duggan, M.J.3    Quinn, C.P.4    Shone, C.C.5    Foster, K.A.6
  • 11
    • 0026510667 scopus 로고
    • Neuronal lysosomal enzyme replacement using fragment C of tetanus toxin
    • Dobrenis K., Joseph A. and Rattazzi M. C. (1992) Neuronal lysosomal enzyme replacement using fragment C of tetanus toxin. Proc. Natl Acad. Sci. USA 89, 2297-2301.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 2297-2301
    • Dobrenis, K.1    Joseph, A.2    Rattazzi, M.C.3
  • 13
    • 0037144403 scopus 로고    scopus 로고
    • Inhibition of release of neurotransmitters from rat dorsal root ganglia by a novel conjugate of a Clostridium botulinum toxin A endopeptidase fragment and Erythrina cristagalli lectin
    • Duggan M. J., Quinn C. P., Chaddock J. A. et al. (2002) Inhibition of release of neurotransmitters from rat dorsal root ganglia by a novel conjugate of a Clostridium botulinum toxin A endopeptidase fragment and Erythrina cristagalli lectin. J. Biol. Chem. 277, 34846-34852.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34846-34852
    • Duggan, M.J.1    Quinn, C.P.2    Chaddock, J.A.3
  • 14
    • 0022515029 scopus 로고
    • Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria
    • Eilers M. and Schatz G. (1986) Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria. Nature 322, 228-232.
    • (1986) Nature , vol.322 , pp. 228-232
    • Eilers, M.1    Schatz, G.2
  • 15
    • 0032884864 scopus 로고    scopus 로고
    • Interaction of influenza virus polymerase with viral RNA in the 'corkscrew' conformation
    • Flick R. and Hobom G. (1999) Interaction of influenza virus polymerase with viral RNA in the 'corkscrew' conformation. J. Gen. Virol. 80, 2565-2572.
    • (1999) J. Gen. Virol. , vol.80 , pp. 2565-2572
    • Flick, R.1    Hobom, G.2
  • 16
    • 0029034875 scopus 로고
    • CuZn superoxide dismutase (SOD-1): Tetanus toxin fragment C hybrid protein for targeted delivery of SOD-1 to neuronal cells
    • Francis J. W., Hosler B. A., Brown R. H. Jr and Fishman P. S. (1995) CuZn superoxide dismutase (SOD-1): tetanus toxin fragment C hybrid protein for targeted delivery of SOD-1 to neuronal cells. J. Biol. Chem. 270, 15 434-15 442.
    • (1995) J. Biol. Chem. , vol.270
    • Francis, J.W.1    Hosler, B.A.2    Brown Jr., R.H.3    Fishman, P.S.4
  • 19
    • 0018838743 scopus 로고
    • Tetanus toxin blocks the neuromuscular transmission in vitro like botulinum A toxin
    • Habermann E., Dreyer F. and Bigalke H. (1980) Tetanus toxin blocks the neuromuscular transmission in vitro like botulinum A toxin. Naunyn Schmiedebergs Arch. Pharmacol. 311, 33-40.
    • (1980) Naunyn Schmiedebergs Arch. Pharmacol. , vol.311 , pp. 33-40
    • Habermann, E.1    Dreyer, F.2    Bigalke, H.3
  • 20
    • 0035168442 scopus 로고    scopus 로고
    • Lipid rafts act as specialized domains for tetanus toxin binding and internalization into neurons
    • Herreros J., Ng T. and Schiavo G. (2001) Lipid rafts act as specialized domains for tetanus toxin binding and internalization into neurons. Mol. Biol. Cell 12, 2947-2960.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2947-2960
    • Herreros, J.1    Ng, T.2    Schiavo, G.3
  • 21
    • 0036494705 scopus 로고    scopus 로고
    • Extracellular Bad fused to toxin transport domains induces apoptosis
    • Ichinose M., Liu X. H., Hagihara N. and Youle R. J. (2002) Extracellular Bad fused to toxin transport domains induces apoptosis. Cancer Res. 62, 1433-1438.
    • (2002) Cancer Res. , vol.62 , pp. 1433-1438
    • Ichinose, M.1    Liu, X.H.2    Hagihara, N.3    Youle, R.J.4
  • 22
    • 0032748657 scopus 로고    scopus 로고
    • Clostridial toxins as therapeutic agents: Benefits of nature's most toxic proteins
    • Johnson E. A. (1999) Clostridial toxins as therapeutic agents: benefits of nature's most toxic proteins. Annu. Rev. Microbiol. 53, 551-575.
    • (1999) Annu. Rev. Microbiol. , vol.53 , pp. 551-575
    • Johnson, E.A.1
  • 23
    • 0016188191 scopus 로고
    • Isolation of synaptic plasma membrane from brain by combined flotation-sedimentation density gradient centrifugation
    • Jones D. H. and Malus A. I. (1974) Isolation of synaptic plasma membrane from brain by combined flotation-sedimentation density gradient centrifugation. Biochim. Biophys. Acta 356, 276-287.
    • (1974) Biochim. Biophys. Acta , vol.356 , pp. 276-287
    • Jones, D.H.1    Malus, A.I.2
  • 24
    • 0027952867 scopus 로고
    • Involvement of phospholipids in the intoxication mechanism of botulinum neurotoxin
    • Kamata Y., Kimura Y. and Kozaki S. (1994) Involvement of phospholipids in the intoxication mechanism of botulinum neurotoxin. Biochim. Biophys. Acta 1199, 65-68.
    • (1994) Biochim. Biophys. Acta , vol.1199 , pp. 65-68
    • Kamata, Y.1    Kimura, Y.2    Kozaki, S.3
  • 25
    • 0026599858 scopus 로고
    • Reductive cleavage of tetanus toxin and botulinum neurotoxin A by the thioredoxin system from brain. Evidence for two redox isomers of tetanus toxin
    • Kistner A. and Habermann E. (1992) Reductive cleavage of tetanus toxin and botulinum neurotoxin A by the thioredoxin system from brain. Evidence for two redox isomers of tetanus toxin. Naunyn Schmiedebergs Arch. Pharmacol. 345, 227-234.
    • (1992) Naunyn Schmiedebergs Arch. Pharmacol. , vol.345 , pp. 227-234
    • Kistner, A.1    Habermann, E.2
  • 26
    • 0030044491 scopus 로고    scopus 로고
    • Ability of methotrexate to inhibit translocation to the cytosol of dihydrofolate reductase fused to diphtheria toxin
    • Klingenberg O. and Olsnes S. (1996) Ability of methotrexate to inhibit translocation to the cytosol of dihydrofolate reductase fused to diphtheria toxin. Biochem. J. 313, 647-653.
    • (1996) Biochem. J. , vol.313 , pp. 647-653
    • Klingenberg, O.1    Olsnes, S.2
  • 27
    • 0035042252 scopus 로고    scopus 로고
    • Localization of lysobisphosphatidic acid-rich membrane domains in late endosomes
    • Kobayashi T., Startchev K., Whitney A. J. and Gruenberg J. (2001) Localization of lysobisphosphatidic acid-rich membrane domains in late endosomes. Biol. Chem. 382, 483-485.
    • (2001) Biol. Chem. , vol.382 , pp. 483-485
    • Kobayashi, T.1    Startchev, K.2    Whitney, A.J.3    Gruenberg, J.4
  • 28
    • 0037222077 scopus 로고    scopus 로고
    • Translocation of botulinum neurotoxin light chain protease through the heavy chain channel
    • Koriazova L. K. and Montal M. (2003) Translocation of botulinum neurotoxin light chain protease through the heavy chain channel. Nat. Struct. Biol. 10, 13-18.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 13-18
    • Koriazova, L.K.1    Montal, M.2
  • 29
    • 0026344827 scopus 로고
    • Firefly luciferase as a marker for herpesvirus (pseudorabies virus) replication in vitro and in vivo
    • Kovacs F. and Mettenleiter T. C. (1991) Firefly luciferase as a marker for herpesvirus (pseudorabies virus) replication in vitro and in vivo. J. Gen. Virol. 72, 2999-3008.
    • (1991) J. Gen. Virol. , vol.72 , pp. 2999-3008
    • Kovacs, F.1    Mettenleiter, T.C.2
  • 31
    • 0039842494 scopus 로고    scopus 로고
    • Spectroscopic analysis of pH-induced changes in the molecular features of type A botulinum neurotoxin light chain
    • Li L. and Singh B. R. (2000) Spectroscopic analysis of pH-induced changes in the molecular features of type A botulinum neurotoxin light chain. Biochemistry 39, 6466-6474.
    • (2000) Biochemistry , vol.39 , pp. 6466-6474
    • Li, L.1    Singh, B.R.2
  • 33
    • 0033578394 scopus 로고    scopus 로고
    • Receptor-mediated uptake of an extracellular Bcl-x (L) fusion protein inhibits apoptosis
    • Liu X.-H., Castelli J. C. and Youle R. J. (1999) Receptor-mediated uptake of an extracellular Bcl-x (L) fusion protein inhibits apoptosis. Proc. Natl Acad. Sci. USA 96, 9563-9567.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 9563-9567
    • Liu, X.-H.1    Castelli, J.C.2    Youle, R.J.3
  • 34
    • 0035824569 scopus 로고    scopus 로고
    • Inhibition of axotomy-induced neuronal apoptosis by extracellular delivery of a Bcl-XL fusion protein
    • Liu X.-H., Collier R. J. and Youle R. J. (2001) Inhibition of axotomy-induced neuronal apoptosis by extracellular delivery of a Bcl-XL fusion protein. J. Biol. Chem. 276, 46 326-46 332.
    • (2001) J. Biol. Chem. , vol.276
    • Liu, X.-H.1    Collier, R.J.2    Youle, R.J.3
  • 35
    • 0021222922 scopus 로고
    • Bacterial toxins: Cellular mechanisms of actions
    • Middlebrook J. L. and Dorland R. B. (1984) Bacterial toxins: cellular mechanisms of actions. Microbiol. Rev. 48, 199-221.
    • (1984) Microbiol. Rev. , vol.48 , pp. 199-221
    • Middlebrook, J.L.1    Dorland, R.B.2
  • 36
    • 46149134882 scopus 로고
    • How do tetanus and botulinum toxins bind to neuronal membranes?
    • Montecucco C. (1986) How do tetanus and botulinum toxins bind to neuronal membranes? Trends Biochem. Sci. 11, 314-317.
    • (1986) Trends Biochem. Sci. , vol.11 , pp. 314-317
    • Montecucco, C.1
  • 37
    • 0028310404 scopus 로고
    • Mechanism of action of tetanus and botulinum neurotoxins
    • Montecucco C. and Schiavo G. (1994) Mechanism of action of tetanus and botulinum neurotoxins. Mol. Microbiol. 13, 1-8.
    • (1994) Mol. Microbiol. , vol.13 , pp. 1-8
    • Montecucco, C.1    Schiavo, G.2
  • 38
    • 0034651211 scopus 로고    scopus 로고
    • Uses of botulinum toxin injection in medicine today
    • Münchau A. and Bhatia K. P. (2000) Uses of botulinum toxin injection in medicine today. Br. Med. J. 320, 161-165.
    • (2000) Br. Med. J. , vol.320 , pp. 161-165
    • Münchau, A.1    Bhatia, K.P.2
  • 40
    • 0028268948 scopus 로고
    • Clostridial neurotoxins: New tools for dissecting exocytosis
    • Niemann H., Blasi J. and Jahn R. (1994) Clostridial neurotoxins: new tools for dissecting exocytosis. Trends Cell Biol. 4, 179-185.
    • (1994) Trends Cell Biol. , vol.4 , pp. 179-185
    • Niemann, H.1    Blasi, J.2    Jahn, R.3
  • 41
    • 0028341442 scopus 로고
    • Identification of protein receptor for Clostridium botulinum type B neurotoxin in rat brain synaptosomes
    • Nishiki T., Kamata Y., Nemoto Y., Omori A., Ito T., Takahashi M. and Kozaki S. (1994) Identification of protein receptor for Clostridium botulinum type B neurotoxin in rat brain synaptosomes. J. Biol. Chem. 269, 10 498-10 503.
    • (1994) J. Biol. Chem. , vol.269
    • Nishiki, T.1    Kamata, Y.2    Nemoto, Y.3    Omori, A.4    Ito, T.5    Takahashi, M.6    Kozaki, S.7
  • 43
    • 0016738156 scopus 로고
    • Tetanus toxin: Direct evidence for retrograde intraaxonal transport
    • Price D. L., Griffin J., Young A., Peck K. and Stocks A. (1975) Tetanus toxin: direct evidence for retrograde intraaxonal transport. Science 188, 945-947.
    • (1975) Science , vol.188 , pp. 945-947
    • Price, D.L.1    Griffin, J.2    Young, A.3    Peck, K.4    Stocks, A.5
  • 45
    • 0033532355 scopus 로고    scopus 로고
    • Interaction of diphtheria toxin T domain with molten globule-like proteins and its implications for translocation
    • Ren J., Kachel K., Kim H., Malenbaum S. E., Collier R. J. and London E. (1999) Interaction of diphtheria toxin T domain with molten globule-like proteins and its implications for translocation. Science 284, 955-957.
    • (1999) Science , vol.284 , pp. 955-957
    • Ren, J.1    Kachel, K.2    Kim, H.3    Malenbaum, S.E.4    Collier, R.J.5    London, E.6
  • 46
    • 0021802697 scopus 로고
    • Interaction of tetanus toxin with lipid vesicles at low pH. Protection of specific polypeptides against proteolysis
    • Roa M. and Boquet P. (1985) Interaction of tetanus toxin with lipid vesicles at low pH. Protection of specific polypeptides against proteolysis. J. Biol. Chem. 260, 6827-6835.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6827-6835
    • Roa, M.1    Boquet, P.2
  • 48
    • 3142735021 scopus 로고    scopus 로고
    • Synaptotagmins I and II act as nerve cell receptors for botulinum neurotoxin G
    • Rummel A., Karnath T., Henke T., Bigalke H. and Binz T. (2004) Synaptotagmins I and II act as nerve cell receptors for botulinum neurotoxin G. J. Biol. Chem. 279, 30 865-30 870.
    • (2004) J. Biol. Chem. , vol.279
    • Rummel, A.1    Karnath, T.2    Henke, T.3    Bigalke, H.4    Binz, T.5
  • 49
    • 0027282605 scopus 로고
    • Direct visualization of botulinum neurotoxin-induced channels in phospholipid vesicles
    • Schmid M. F., Robinson J. P. and DasGupta B. R. (1993) Direct visualization of botulinum neurotoxin-induced channels in phospholipid vesicles. Nature 364, 827-830.
    • (1993) Nature , vol.364 , pp. 827-830
    • Schmid, M.F.1    Robinson, J.P.2    DasGupta, B.R.3
  • 50
    • 0034689054 scopus 로고    scopus 로고
    • Cholera toxin is exported from microsomes by the Sec61p complex
    • Schmitz A., Herrgen H., Winkeler A. and Herzog V. (2000) Cholera toxin is exported from microsomes by the Sec61p complex. J. Cell Biol. 148, 1203-1212.
    • (2000) J. Cell Biol. , vol.148 , pp. 1203-1212
    • Schmitz, A.1    Herrgen, H.2    Winkeler, A.3    Herzog, V.4
  • 52
    • 0025823443 scopus 로고
    • Modulation of firefly luciferase stability and impact on studies of gene regulation
    • Thompson J. F., Hayes L. S. and Lloyd D. B. (1991) Modulation of firefly luciferase stability and impact on studies of gene regulation. Gene 103, 171-177.
    • (1991) Gene , vol.103 , pp. 171-177
    • Thompson, J.F.1    Hayes, L.S.2    Lloyd, D.B.3
  • 54
    • 0028846613 scopus 로고
    • Immunochemical analysis shows all three domains of diphtheria toxin penetrate across model membranes
    • Tortorella D., Sesardic D., Dawes C. S. and London E. (1995) Immunochemical analysis shows all three domains of diphtheria toxin penetrate across model membranes. J. Biol. Chem. 270, 27 446-27 452.
    • (1995) J. Biol. Chem. , vol.270
    • Tortorella, D.1    Sesardic, D.2    Dawes, C.S.3    London, E.4
  • 55
    • 0036850282 scopus 로고    scopus 로고
    • Botulinum and tetanus neurotoxins: Structure, function and therapeutic utility
    • Turton K., Chaddock J. A. and Acharya K. R. (2002) Botulinum and tetanus neurotoxins: structure, function and therapeutic utility. Trends Biochem. Sci. 27, 552-558.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 552-558
    • Turton, K.1    Chaddock, J.A.2    Acharya, K.R.3
  • 56
    • 0032953048 scopus 로고    scopus 로고
    • Proteolysis of SNAP-25 isoforms by botulinum neurotoxin types A, C, and E: Domains and amino acid residues controlling the formation of enzyme-substrate complexes and cleavage
    • Vaidyanathan V. V., Yoshino K., Jahnz M., Dörries C., Bade S., Nauenburg S., Niemann H. and Binz T. (1999) Proteolysis of SNAP-25 isoforms by botulinum neurotoxin types A, C, and E: domains and amino acid residues controlling the formation of enzyme-substrate complexes and cleavage. J. Neurochem. 72, 327-337.
    • (1999) J. Neurochem. , vol.72 , pp. 327-337
    • Vaidyanathan, V.V.1    Yoshino, K.2    Jahnz, M.3    Dörries, C.4    Bade, S.5    Nauenburg, S.6    Niemann, H.7    Binz, T.8
  • 57
    • 0000354574 scopus 로고
    • Tetanus and botulinum neurotoxins
    • (Herken, H. and Hucho, F., eds). Springer, Berlin
    • Wellhöner H. H. (1992) Tetanus and botulinum neurotoxins. In: Handbook of Experimental Pharmacology (Herken, H. and Hucho, F., eds), Vol. 102, pp. 357-417. Springer, Berlin.
    • (1992) Handbook of Experimental Pharmacology , vol.102 , pp. 357-417
    • Wellhöner, H.H.1
  • 58
    • 0027048990 scopus 로고
    • Tight folding of acidic fibroblast growth factor prevents its translocation to the cytosol with diphtheria toxin as vector
    • Wiedlocha A., Madshus I. H., Mach H., Middaugh C. R. and Olsnes S. (1992) Tight folding of acidic fibroblast growth factor prevents its translocation to the cytosol with diphtheria toxin as vector. EMBO J. 11, 4835-4842.
    • (1992) EMBO J. , vol.11 , pp. 4835-4842
    • Wiedlocha, A.1    Madshus, I.H.2    Mach, H.3    Middaugh, C.R.4    Olsnes, S.5
  • 59
    • 0027946632 scopus 로고
    • Bafilomycin A1 inhibits the action of tetanus toxin in spinal cord neurons in cell culture
    • Williamson L. C. and Neale E. A. (1994) Bafilomycin A1 inhibits the action of tetanus toxin in spinal cord neurons in cell culture. J. Neurochem. 63, 2342-2345.
    • (1994) J. Neurochem. , vol.63 , pp. 2342-2345
    • Williamson, L.C.1    Neale, E.A.2
  • 60
    • 0028199063 scopus 로고
    • Cleavage of members of the synaptobrevin/VAMP family by types D and F botulinal neurotoxins and tetanus toxin
    • Yamasaki S., Baumeister A., Binz T. et al. (1994) Cleavage of members of the synaptobrevin/VAMP family by types D and F botulinal neurotoxins and tetanus toxin. J. Biol. Chem. 269, 12 764-12 772.
    • (1994) J. Biol. Chem. , vol.269
    • Yamasaki, S.1    Baumeister, A.2    Binz, T.3


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