메뉴 건너뛰기




Volumn 150, Issue 2, 1997, Pages 203-208

Cleavage of the synaptobrevin/vesicle-associated membrane protein (VAMP) of the mouse brain by the recombinant light chain of Clostridium botulinum type B toxin

Author keywords

Clostridium botulinum type B toxin; Light chain; Synaptobrevin VAMP

Indexed keywords

BOTULINUM TOXIN B; CHELATING AGENT; RECOMBINANT PROTEIN; SYNAPTOBREVIN;

EID: 0031005892     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(97)00114-6     Document Type: Article
Times cited : (10)

References (21)
  • 2
    • 0022555430 scopus 로고
    • Molecular pharmacology of botulinum toxin and tetanus toxin
    • Simpson, L.L. (1986) Molecular pharmacology of botulinum toxin and tetanus toxin. Annu. Rev. Pharmacol. Toxicol. 26, 427-453.
    • (1986) Annu. Rev. Pharmacol. Toxicol. , vol.26 , pp. 427-453
    • Simpson, L.L.1
  • 3
    • 0027176523 scopus 로고
    • Snappy exotoxins
    • Huttner, W.B. (1993) Snappy exotoxins. Nature 365, 104-105.
    • (1993) Nature , vol.365 , pp. 104-105
    • Huttner, W.B.1
  • 7
    • 0029874232 scopus 로고    scopus 로고
    • Botulinum neurotoxin C1 cleaves both syntaxin and SNAP-25 in intact and permeablized chromaffin cells: Correlation with its blockade of catecholamine release
    • Foran, P., Lawrence, G.W., Shone, C.C., Foster, K.A. and Dolly, J.O. (1996) Botulinum neurotoxin C1 cleaves both syntaxin and SNAP-25 in intact and permeablized chromaffin cells: Correlation with its blockade of catecholamine release. Biochemistry 35, 2630-2636.
    • (1996) Biochemistry , vol.35 , pp. 2630-2636
    • Foran, P.1    Lawrence, G.W.2    Shone, C.C.3    Foster, K.A.4    Dolly, J.O.5
  • 8
    • 0026497466 scopus 로고
    • Tetanus and botulinum-B neurotoxin block neurotransmitter release by proteolytic cleavage of synaptobrevin
    • Schiavo, G., Benfenati, F., Poulain, B., Rossetto, O., Laureto, P.P., DasGupta, B.R., and Montecucco, C. (1993) Tetanus and botulinum-B neurotoxin block neurotransmitter release by proteolytic cleavage of synaptobrevin. Nature. 359, 832-835.
    • (1993) Nature , vol.359 , pp. 832-835
    • Schiavo, G.1    Benfenati, F.2    Poulain, B.3    Rossetto, O.4    Laureto, P.P.5    Dasgupta, B.R.6    Montecucco, C.7
  • 11
    • 0027265710 scopus 로고
    • Cellubrevin is a ubiquitous tetanus toxin substrate homologous to a putative synaptic vesicle fusion protein
    • McMahon, H.T., Ushkaryov, Y.A., Eelmann, L., Link, E., Binz, T., Niemann, H., Jahn, R., and Sudhof, T.C. (1993) Cellubrevin is a ubiquitous tetanus toxin substrate homologous to a putative synaptic vesicle fusion protein. Nature 364, 346-349.
    • (1993) Nature , vol.364 , pp. 346-349
    • McMahon, H.T.1    Ushkaryov, Y.A.2    Eelmann, L.3    Link, E.4    Binz, T.5    Niemann, H.6    Jahn, R.7    Sudhof, T.C.8
  • 12
    • 0029980484 scopus 로고    scopus 로고
    • Clostridail neurotoxins and substrate proteolysis in intact neurons: botulinum neurotoxin C acts on synaptosomal-associated protein of 25 kDa
    • Williamson, L.C., Halpern, J.L. Montecucco, C., Brown, J.E., and Neale E.A. (1996) Clostridail neurotoxins and substrate proteolysis in intact neurons: botulinum neurotoxin C acts on synaptosomal-associated protein of 25 kDa. J. Biol. Chem. 271, 7694-7699.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7694-7699
    • Williamson, L.C.1    Halpern, J.L.2    Montecucco, C.3    Brown, J.E.4    Neale, E.A.5
  • 13
    • 0026816007 scopus 로고
    • Cloning of a Clostridium botulinum type B toxin gene fragment encoding the N-terminus of the heavy chain
    • Jung, H.H., Rhee, S.D., and Yang, K.H. (1992) Cloning of a Clostridium botulinum type B toxin gene fragment encoding the N-terminus of the heavy chain. FEMS Microbiol. Lett. 91, 69-72.
    • (1992) FEMS Microbiol. Lett. , vol.91 , pp. 69-72
    • Jung, H.H.1    Rhee, S.D.2    Yang, K.H.3
  • 14
    • 0023048904 scopus 로고
    • Botulinum neurotoxin type B: Its purification, radioiodination and interaction with rat-brain synaptosomal membranes
    • Evans, D.M., Williams, R.S., Shone, C.C., Hambleton, P., Melling, J., and Dolly, J.O. (1986) Botulinum neurotoxin type B: its purification, radioiodination and interaction with rat-brain synaptosomal membranes. Eur. J. Biochem. 154, 409-416.
    • (1986) Eur. J. Biochem. , vol.154 , pp. 409-416
    • Evans, D.M.1    Williams, R.S.2    Shone, C.C.3    Hambleton, P.4    Melling, J.5    Dolly, J.O.6
  • 16
    • 0009482260 scopus 로고
    • Electrophoretic transfer of protein from polyacrylamide gel to nitrocellulose sheets: procedure and application
    • Towbin, H., Staehelin, T., and Gordon, J. (1979) Electrophoretic transfer of protein from polyacrylamide gel to nitrocellulose sheets: procedure and application. Proc. Natl. Acad. Sci. USA 76, 4350-4353.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4353
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 17
    • 0027442891 scopus 로고
    • Chelation of zinc antagonizes the neuromuscular blocking properties of the seven serotypes of botulinum neurotoxin as well as tetanus toxin
    • Simpson, L.L., Coffield, J.A., and Bakry, N. (1993) Chelation of zinc antagonizes the neuromuscular blocking properties of the seven serotypes of botulinum neurotoxin as well as tetanus toxin. J. Pharmacol. Exp. Ther. 267, 720-727.
    • (1993) J. Pharmacol. Exp. Ther. , vol.267 , pp. 720-727
    • Simpson, L.L.1    Coffield, J.A.2    Bakry, N.3
  • 18
    • 0028810969 scopus 로고
    • Expression and purification of the light chain of botulinum neurotoxin A: A single mutation abolishes its cleavage of SNAP-25 and neurotoxicity after reconstitution with the heavy chain
    • Zhou, L., de Paiva, A., Liu, D., and Dolly, J.O. (1995) Expression and purification of the light chain of botulinum neurotoxin A: a single mutation abolishes its cleavage of SNAP-25 and neurotoxicity after reconstitution with the heavy chain. Biochemistry 34, 15175-15181.
    • (1995) Biochemistry , vol.34 , pp. 15175-15181
    • Zhou, L.1    De Paiva, A.2    Liu, D.3    Dolly, J.O.4
  • 19
    • 0027294626 scopus 로고
    • Production of biologically active light chain of tetanus toxin in Escherichia coli: Evidence for the important of the C-terminal 16 amino acids for full biologically activity
    • Fairweather, N.F., Sanders, D., Salter, D., Hudel, M., Habermann, E., and Weller, U. (1993) Production of biologically active light chain of tetanus toxin in Escherichia coli: evidence for the important of the C-terminal 16 amino acids for full biologically activity. FEBS Lett. 323, 218-222.
    • (1993) FEBS Lett. , vol.323 , pp. 218-222
    • Fairweather, N.F.1    Sanders, D.2    Salter, D.3    Hudel, M.4    Habermann, E.5    Weller, U.6
  • 20
    • 0025233759 scopus 로고
    • Cloning and expression of functional fragment C of tetanus toxin
    • Halpern, J.L., Habig, W.H., Nealle, E.A., and Stibitz, S. (1990) Cloning and expression of functional fragment C of tetanus toxin. Infect. Immun. 58, 1004-1009.
    • (1990) Infect. Immun. , vol.58 , pp. 1004-1009
    • Halpern, J.L.1    Habig, W.H.2    Nealle, E.A.3    Stibitz, S.4
  • 21
    • 0024787893 scopus 로고
    • Expression of tetanus toxin fragment C in E. coli high level expression by removing rare codons
    • Makoff, A.J., Oxer, M.D., Romanos, M.A., Fairweather, N.F., and Ballantine, S. (1989) Expression of tetanus toxin fragment C in E. coli high level expression by removing rare codons. Nucleic Acids Res. 17, 10191-10202.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 10191-10202
    • Makoff, A.J.1    Oxer, M.D.2    Romanos, M.A.3    Fairweather, N.F.4    Ballantine, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.