메뉴 건너뛰기




Volumn 357, Issue 2, 2006, Pages 574-582

Identification of the amino acid residues rendering TI-VAMP insensitive toward botulinum neurotoxin B

Author keywords

Botulinum neurotoxin; Membrane fusion; Synaptobrevin; TI VAMP; VAMP

Indexed keywords

BOTULINUM TOXIN B; CELLUBREVIN; SYNAPTOBREVIN; SYNAPTOBREVIN 1; SYNAPTOBREVIN 2; UNCLASSIFIED DRUG; VAMP 7;

EID: 33344472881     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.12.075     Document Type: Article
Times cited : (20)

References (30)
  • 1
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • T. Sollner, M.K. Bennett, S.W. Whiteheart, R.H. Scheller, and J.E. Rothman A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion Cell 75 1993 409 418
    • (1993) Cell , vol.75 , pp. 409-418
    • Sollner, T.1    Bennett, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 2
    • 0032562808 scopus 로고    scopus 로고
    • Seven novel mammalian SNARE proteins localize to distinct membrane compartments
    • R.J. Advani, H.R. Bae, J.B. Bock, D.S. Chao, Y.C. Doung, and R. Prekeris Seven novel mammalian SNARE proteins localize to distinct membrane compartments J. Biol. Chem. 273 1998 10317 10324
    • (1998) J. Biol. Chem. , vol.273 , pp. 10317-10324
    • Advani, R.J.1    Bae, H.R.2    Bock, J.B.3    Chao, D.S.4    Doung, Y.C.5    Prekeris, R.6
  • 3
    • 0031814298 scopus 로고    scopus 로고
    • A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells
    • T. Galli, A. Zahraoui, V.V. Vaidyanathan, G. Raposo, J.M. Tian, and M. Karin A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells Mol. Biol. Cell 9 1998 1437 1448
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1437-1448
    • Galli, T.1    Zahraoui, A.2    Vaidyanathan, V.V.3    Raposo, G.4    Tian, J.M.5    Karin, M.6
  • 4
    • 17444401398 scopus 로고    scopus 로고
    • The tetanus neurotoxin-sensitive and insensitive routes to and from the plasma membrane: Fast and slow pathways?
    • V. Proux-Gillardeaux, R. Rudge, and T. Galli The tetanus neurotoxin-sensitive and insensitive routes to and from the plasma membrane: fast and slow pathways? Traffic 6 2005 366 373
    • (2005) Traffic , vol.6 , pp. 366-373
    • Proux-Gillardeaux, V.1    Rudge, R.2    Galli, T.3
  • 5
    • 23944501982 scopus 로고    scopus 로고
    • SNARE complexes prepare for membrane fusion
    • J.B. Sorensen SNARE complexes prepare for membrane fusion Trends Neurosci. 28 2005 453 455
    • (2005) Trends Neurosci. , vol.28 , pp. 453-455
    • Sorensen, J.B.1
  • 6
    • 0028491306 scopus 로고
    • Clostridial neurotoxins as tools to investigate the molecular events of neurotransmitter release
    • G. Schiavo, O. Rossetto, and C. Montecucco Clostridial neurotoxins as tools to investigate the molecular events of neurotransmitter release Semin. Cell Biol. 5 1994 221 229
    • (1994) Semin. Cell Biol. , vol.5 , pp. 221-229
    • Schiavo, G.1    Rossetto, O.2    Montecucco, C.3
  • 7
    • 0028268948 scopus 로고
    • Clostridial neurotoxins: New tools for dissecting exocytosis
    • H. Niemann, J. Blasi, and R. Jahn Clostridial neurotoxins: new tools for dissecting exocytosis Trends Cell Biol. 4 1994 179 185
    • (1994) Trends Cell Biol. , vol.4 , pp. 179-185
    • Niemann, H.1    Blasi, J.2    Jahn, R.3
  • 9
    • 0028558884 scopus 로고
    • Differences in the protease activities of tetanus and botulinum B toxins revealed by the cleavage of vesicle-associated membrane protein and various sized fragments
    • P. Foran, C.C. Shone, and J.O. Dolly Differences in the protease activities of tetanus and botulinum B toxins revealed by the cleavage of vesicle-associated membrane protein and various sized fragments Biochemistry 33 1994 15365 15374
    • (1994) Biochemistry , vol.33 , pp. 15365-15374
    • Foran, P.1    Shone, C.C.2    Dolly, J.O.3
  • 10
    • 0027376762 scopus 로고
    • Proteolytic cleavage of synthetic fragments of vesicle-associated membrane protein, isoform-2 by botulinum type B neurotoxin
    • C.C. Shone, C.P. Quinn, R. Wait, B. Hallis, S.G. Fooks, and P. Hambleton Proteolytic cleavage of synthetic fragments of vesicle-associated membrane protein, isoform-2 by botulinum type B neurotoxin Eur. J. Biochem. 217 1993 965 971
    • (1993) Eur. J. Biochem. , vol.217 , pp. 965-971
    • Shone, C.C.1    Quinn, C.P.2    Wait, R.3    Hallis, B.4    Fooks, S.G.5    Hambleton, P.6
  • 12
    • 0030732413 scopus 로고    scopus 로고
    • Botulinum neurotoxin types a and e require the SNARE motif in SNAP-25 for proteolysis
    • P. Washbourne, R. Pellizzari, G. Baldini, M.C. Wilson, and C. Montecucco Botulinum neurotoxin types A and E require the SNARE motif in SNAP-25 for proteolysis FEBS Letters 418 1997 1 5
    • (1997) FEBS Letters , vol.418 , pp. 1-5
    • Washbourne, P.1    Pellizzari, R.2    Baldini, G.3    Wilson, M.C.4    Montecucco, C.5
  • 13
    • 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
    • V.V. Vaidyanathan, K. Yoshino, M. Jahnz, C. Dorries, S. Bade, and S. Nauenburg 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 1999 327 337
    • (1999) J. Neurochem. , vol.72 , pp. 327-337
    • Vaidyanathan, V.V.1    Yoshino, K.2    Jahnz, M.3    Dorries, C.4    Bade, S.5    Nauenburg, S.6
  • 14
    • 14844365792 scopus 로고    scopus 로고
    • Botulinum neurotoxin serotype F: Identification of substrate recognition requirements and development of inhibitors with low nanomolar affinity
    • J.J. Schmidt, and R.G. Stafford Botulinum neurotoxin serotype F: identification of substrate recognition requirements and development of inhibitors with low nanomolar affinity Biochemistry 44 2005 4067 4073
    • (2005) Biochemistry , vol.44 , pp. 4067-4073
    • Schmidt, J.J.1    Stafford, R.G.2
  • 15
    • 0029811998 scopus 로고    scopus 로고
    • Structural determinants of the specificity for synaptic vesicle-associated membrane protein/synaptobrevin of tetanus and botulinum type B and G neurotoxins
    • R. Pellizzari, O. Rossetto, L. Lozzi, S. Giovedi, E. Johnson, C.C. Shone, and C. Montecucco Structural determinants of the specificity for synaptic vesicle-associated membrane protein/synaptobrevin of tetanus and botulinum type B and G neurotoxins J. Biol. Chem. 271 1996 20353 20358
    • (1996) J. Biol. Chem. , vol.271 , pp. 20353-20358
    • Pellizzari, R.1    Rossetto, O.2    Lozzi, L.3    Giovedi, S.4    Johnson, E.5    Shone, C.C.6    Montecucco, C.7
  • 17
    • 0030787389 scopus 로고    scopus 로고
    • The interaction of synaptic vesicle-associated membrane protein/synaptobrevin with botulinum neurotoxins D and F
    • R. Pellizzari, S. Mason, C.C. Shone, and C. Montecucco The interaction of synaptic vesicle-associated membrane protein/synaptobrevin with botulinum neurotoxins D and F FEBS Letters 409 1997 339 342
    • (1997) FEBS Letters , vol.409 , pp. 339-342
    • Pellizzari, R.1    Mason, S.2    Shone, C.C.3    Montecucco, C.4
  • 18
    • 0028199063 scopus 로고
    • Cleavage of members of the synaptobrevin/VAMP family by types D and F botulinal neurotoxins and tetanus toxin
    • S. Yamasaki, A. Baumeister, T. Binz, J. Blasi, E. Link, and F. Cornille Cleavage of members of the synaptobrevin/VAMP family by types D and F botulinal neurotoxins and tetanus toxin J. Biol. Chem. 269 1994 12764 12772
    • (1994) J. Biol. Chem. , vol.269 , pp. 12764-12772
    • Yamasaki, S.1    Baumeister, A.2    Binz, T.3    Blasi, J.4    Link, E.5    Cornille, F.6
  • 19
    • 24044552034 scopus 로고    scopus 로고
    • Analysis of the substrate recognition domain determinants of botulinum type B toxin using phage display
    • E.R. Evans, J.M. Sutton, A. Gravett, and C.C. Shone Analysis of the substrate recognition domain determinants of botulinum type B toxin using phage display Toxicon 46 2005 446 453
    • (2005) Toxicon , vol.46 , pp. 446-453
    • Evans, E.R.1    Sutton, J.M.2    Gravett, A.3    Shone, C.C.4
  • 20
    • 11144341950 scopus 로고    scopus 로고
    • Substrate recognition strategy for botulinum neurotoxin serotype a
    • M.A. Breidenbach, and A.T. Brunger Substrate recognition strategy for botulinum neurotoxin serotype A Nature 432 2004 925 929
    • (2004) Nature , vol.432 , pp. 925-929
    • Breidenbach, M.A.1    Brunger, A.T.2
  • 21
    • 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
  • 22
    • 0033887403 scopus 로고    scopus 로고
    • Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 a resolution
    • M.A. Hanson, and R.C. Stevens Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution Nature Struct. Biol. 7 2000 687 692
    • (2000) Nature Struct. Biol. , vol.7 , pp. 687-692
    • Hanson, M.A.1    Stevens, R.C.2
  • 23
    • 0034881411 scopus 로고    scopus 로고
    • Questions about the structure of the botulinum neurotoxin B light chain in complex with a target peptide
    • B. Rupp, and B. Segelke Questions about the structure of the botulinum neurotoxin B light chain in complex with a target peptide Nature Struct. Biol. 8 2001 663 664
    • (2001) Nature Struct. Biol. , vol.8 , pp. 663-664
    • Rupp, B.1    Segelke, B.2
  • 26
    • 0028065415 scopus 로고
    • Peptide substrate specificity and properties of the zinc-endopeptidase activity of botulinum type B neurotoxin
    • C.C. Shone, and A.K. Roberts Peptide substrate specificity and properties of the zinc-endopeptidase activity of botulinum type B neurotoxin Eur. J. Biochem. 225 1994 263 270
    • (1994) Eur. J. Biochem. , vol.225 , pp. 263-270
    • Shone, C.C.1    Roberts, A.K.2
  • 27
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • I. Schechter, and A. Berger On the size of the active site in proteases. I. Papain Biochem. Biophys. Res. Commun. 27 1967 157 162
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 28
    • 0029891288 scopus 로고    scopus 로고
    • Substrate residues N-terminal to the cleavage site of botulinum type B neurotoxin play a role in determining the specificity of its endopeptidase activity
    • M. Wictome, O. Rossetto, C. Montecucco, and C.C. Shone Substrate residues N-terminal to the cleavage site of botulinum type B neurotoxin play a role in determining the specificity of its endopeptidase activity FEBS Letters 386 1996 133 136
    • (1996) FEBS Letters , vol.386 , pp. 133-136
    • Wictome, M.1    Rossetto, O.2    Montecucco, C.3    Shone, C.C.4
  • 29
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å 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 Å 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.