메뉴 건너뛰기




Volumn 381, Issue 1, 2009, Pages 50-53

Crystal structure of a catalytically active, non-toxic endopeptidase derivative of Clostridium botulinum toxin A

Author keywords

Botulinum neurotoxin; Crystal structure; Fusion; Protein engineering; Therapeutics

Indexed keywords

BOTULINUM TOXIN A; PROTEINASE; SYNAPTOSOMAL ASSOCIATED PROTEIN 25;

EID: 61649127494     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.02.003     Document Type: Article
Times cited : (22)

References (20)
  • 1
    • 61649107455 scopus 로고    scopus 로고
    • Introduction to the clinical use of Botulinum neurotoxins
    • Foster K.A., Hambleton P., and Shone C.C. (Eds), CRC press, Boca Raton, Florida
    • Barnes M.P. Introduction to the clinical use of Botulinum neurotoxins. In: Foster K.A., Hambleton P., and Shone C.C. (Eds). Treatments from toxins-the therapeutic potential of Clostridial neurotoxins (2007), CRC press, Boca Raton, Florida 139-162
    • (2007) Treatments from toxins-the therapeutic potential of Clostridial neurotoxins , pp. 139-162
    • Barnes, M.P.1
  • 2
    • 61649092832 scopus 로고    scopus 로고
    • Expanding clinical uses of Botulinum neurotoxins
    • Foster K.A., Hambleton P., and Shone C.C. (Eds), CRC press, Boca Raton, Florida
    • Moore A.P. Expanding clinical uses of Botulinum neurotoxins. In: Foster K.A., Hambleton P., and Shone C.C. (Eds). Treatments from toxins-the therapeutic potential of Clostridial neurotoxins (2007), CRC press, Boca Raton, Florida 163-194
    • (2007) Treatments from toxins-the therapeutic potential of Clostridial neurotoxins , pp. 163-194
    • Moore, A.P.1
  • 4
    • 0022416338 scopus 로고
    • Inactivation of Clostridium botulinum type A neurotoxin by trypsin and purification of two tryptic fragments. Proteolytic action near the COOH-terminus of the heavy subunit destroys toxin-binding activity
    • Shone C.C., Hambleton P., and Melling J. Inactivation of Clostridium botulinum type A neurotoxin by trypsin and purification of two tryptic fragments. Proteolytic action near the COOH-terminus of the heavy subunit destroys toxin-binding activity. Eur. J. Biochem. 151 (1985) 75-82
    • (1985) Eur. J. Biochem. , vol.151 , pp. 75-82
    • Shone, C.C.1    Hambleton, P.2    Melling, J.3
  • 6
    • 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. Inhibition of vesicular secretion in both neuronal and nonneuronal cells by a retargeted endopeptidase derivative of Clostridium botulinum neurotoxin type A. Infect. Immun. 68 (2000) 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
  • 7
    • 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. 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 (2000) 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
  • 8
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 9
    • 0028103275 scopus 로고
    • Number 4. The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography, Acta Cryst. D50 (1994) 760-763.
    • (1994) Acta Cryst , vol.D50 , pp. 760-763
  • 11
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Cryst. D 60 (2004) 2126-2132
    • (2004) Acta Cryst. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 12
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26 (1993) 283-291
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 14
    • 34848840291 scopus 로고    scopus 로고
    • Botulinum neurotoxin heavy chain belt as an intramolecular chaperone for the light chain
    • Brunger A.T., Breidenbach M.A., Jin R., Fischer A., Santos J.S., and Montal M. Botulinum neurotoxin heavy chain belt as an intramolecular chaperone for the light chain. PLoS Pathog. 3 (2007) 1191-1194
    • (2007) PLoS Pathog. , vol.3 , pp. 1191-1194
    • Brunger, A.T.1    Breidenbach, M.A.2    Jin, R.3    Fischer, A.4    Santos, J.S.5    Montal, M.6
  • 15
    • 55549106809 scopus 로고    scopus 로고
    • Membrane interaction of botulinum neurotoxin A translocation (T) doma
    • The belt region is a regulatory loop for membrane interaction
    • Galloux M., Vitrac H., Montagner C., Raffestin S., Popoff M.R., Chenal A., Forge V., and Gillet D. Membrane interaction of botulinum neurotoxin A translocation (T) doma. 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
  • 17
    • 0037222077 scopus 로고    scopus 로고
    • Translocation of botulinum neurotoxin light chain protease through the heavy chain channel
    • Koriazova L.K., and Montal M. 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
  • 18
    • 33645086131 scopus 로고    scopus 로고
    • Clostridial neurotoxins: structure-function led design of new therapeutics
    • Chaddock J.A., and Marks P.M.H. Clostridial neurotoxins: structure-function led design of new therapeutics. Cell. Mol. Life Sci. 63 (2006) 540-551
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 540-551
    • Chaddock, J.A.1    Marks, P.M.H.2
  • 19
    • 17444423708 scopus 로고    scopus 로고
    • A new wrinkle on pain relief: re-engineering Clostridial neurotoxins for analgesics
    • Foster K.A. A new wrinkle on pain relief: re-engineering Clostridial neurotoxins for analgesics. Drug Discov. Today 10 (2005) 563-569
    • (2005) Drug Discov. Today , vol.10 , pp. 563-569
    • Foster, K.A.1
  • 20
    • 38049093742 scopus 로고    scopus 로고
    • Botulinum neurotoxin vaccines: past, present, and future
    • Smith L.A., and Rusnak J.M. Botulinum neurotoxin vaccines: past, present, and future. Crit. Rev. Immunol. 27 (2007) 303-318
    • (2007) Crit. Rev. Immunol. , vol.27 , pp. 303-318
    • Smith, L.A.1    Rusnak, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.