메뉴 건너뛰기




Volumn 38, Issue 3, 2000, Pages 429-442

Isolation of a funnel-web spider polypeptide with homology to mamba intestinal toxin 1 and the embryonic head inducer Dickkopf-1

Author keywords

[No Author keywords available]

Indexed keywords

COLIPASE; SPIDER VENOM;

EID: 0033991706     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0041-0101(99)00174-9     Document Type: Article
Times cited : (42)

References (23)
  • 2
    • 0032102712 scopus 로고    scopus 로고
    • Purification and characterisation of human procolipase expressed in yeast cells
    • Cordle R.A., Lowe M.E. Purification and characterisation of human procolipase expressed in yeast cells. Prot. Expr. Purif. 13:1998;30-35.
    • (1998) Prot. Expr. Purif. , vol.13 , pp. 30-35
    • Cordle, R.A.1    Lowe, M.E.2
  • 3
    • 0028968179 scopus 로고
    • Crystallographic study of the structure of colipase and of the interaction with pancreatic lipase
    • Egloff M-P., Sarda L., Verger R., Cambillau C., van Tilbeurgh H. Crystallographic study of the structure of colipase and of the interaction with pancreatic lipase. Prot. Sci. 4:1995;44-57.
    • (1995) Prot. Sci. , vol.4 , pp. 44-57
    • Egloff, M.-P.1    Sarda, L.2    Verger, R.3    Cambillau, C.4    Van Tilbeurgh, H.5
  • 4
    • 0014959663 scopus 로고
    • Isolation of bradykinin-potentiating peptides from Bothrops jararaca venom
    • Ferreira S.H., Bartelt D.C., Greene L.J. Isolation of bradykinin-potentiating peptides from Bothrops jararaca venom. Biochemistry. 9:1970;2583-2593.
    • (1970) Biochemistry , vol.9 , pp. 2583-2593
    • Ferreira, S.H.1    Bartelt, D.C.2    Greene, L.J.3
  • 6
    • 0030727613 scopus 로고    scopus 로고
    • The structure of versutoxin (δ-atracotoxin-Hv1) provides insights into the binding of site-3 neurotoxins to the voltage-gated sodium channel
    • Fletcher J.I., Chapman B.E., Mackay J.P., Howden M.E.H., King G.F. The structure of versutoxin (δ-atracotoxin-Hv1) provides insights into the binding of site-3 neurotoxins to the voltage-gated sodium channel. Structure. 5:1997;1525-1535.
    • (1997) Structure , vol.5 , pp. 1525-1535
    • Fletcher, J.I.1    Chapman, B.E.2    MacKay, J.P.3    Howden, M.E.H.4    King, G.F.5
  • 7
    • 0343312812 scopus 로고
    • The isolated chick biventer cervicis nerve-muscle preparation
    • Ginsborg B.L., Warriner J. The isolated chick biventer cervicis nerve-muscle preparation. Br. J. Pharmac. 15:1960;410-411.
    • (1960) Br. J. Pharmac. , vol.15 , pp. 410-411
    • Ginsborg, B.L.1    Warriner, J.2
  • 8
    • 0032556910 scopus 로고    scopus 로고
    • Dickkopf-1 is a member of a new family of secreted proteins and functions in head induction
    • Glinka A., Wu W., Delius H., Monaghan A.P., Blemenstock C., Niehrs C. Dickkopf-1 is a member of a new family of secreted proteins and functions in head induction. Nature. 391:1998;357-362.
    • (1998) Nature , vol.391 , pp. 357-362
    • Glinka, A.1    Wu, W.2    Delius, H.3    Monaghan, A.P.4    Blemenstock, C.5    Niehrs, C.6
  • 9
    • 0001500617 scopus 로고
    • Distribution of the funnel web spiders
    • J. Covacevich, P. Davie, & J. Peran. Brisbane: Queensland Museum
    • Gray M.R. Distribution of the funnel web spiders. Covacevich J., Davie P., Peran J. Toxic plants and animals - a guide for Australia. 1987;312-321 Queensland Museum, Brisbane.
    • (1987) Toxic Plants and Animals - A Guide for Australia , pp. 312-321
    • Gray, M.R.1
  • 10
    • 0001882353 scopus 로고
    • Aspects of the systematics of the Australian funnel web spiders (Araneae:Hexathelidae:Atracinae) based upon morphological and electrophoretic data
    • A.D. Austin, & N.W. Heather. Brisbane: The Australian Entomological Society
    • Gray M.R. Aspects of the systematics of the Australian funnel web spiders (Araneae:Hexathelidae:Atracinae) based upon morphological and electrophoretic data. Austin A.D., Heather N.W. Australian arachnology. 1988;113-1125 The Australian Entomological Society, Brisbane.
    • (1988) Australian Arachnology , pp. 113-1125
    • Gray, M.R.1
  • 11
    • 0019957999 scopus 로고
    • Hydrolysis of substance P and bradykinin by black widow spider venom gland extract
    • Huidobro-Toro J.P., Chelala C.A., Musacchio J.M. Hydrolysis of substance P and bradykinin by black widow spider venom gland extract. Biochem. Pharmac. 31:1982;3323-3328.
    • (1982) Biochem. Pharmac. , vol.31 , pp. 3323-3328
    • Huidobro-Toro, J.P.1    Chelala, C.A.2    Musacchio, J.M.3
  • 12
    • 0018609118 scopus 로고
    • Separation and characterisation of venom components in Loxosceles reclusa - II. Protease enzyme activity
    • Jong Y-S., Norment B.R., Heitz J.R. Separation and characterisation of venom components in Loxosceles reclusa - II. Protease enzyme activity. Toxicon. 17:1979;529-537.
    • (1979) Toxicon , vol.17 , pp. 529-537
    • Jong, Y.-S.1    Norment, B.R.2    Heitz, J.R.3
  • 13
    • 0019122103 scopus 로고
    • Snake venom. The amino acid sequence of protein A from Dendroaspis polylepis polylepis (black mamba) venom
    • Joubert F.J., Strydom D.J. Snake venom. The amino acid sequence of protein A from Dendroaspis polylepis polylepis (black mamba) venom. Hoppe-Seyler's Z. Physiol. Chem. 361:1980;1787-1794.
    • (1980) Hoppe-Seyler's Z. Physiol. Chem , vol.361 , pp. 1787-1794
    • Joubert, F.J.1    Strydom, D.J.2
  • 14
    • 0023125054 scopus 로고
    • The origin of snakes and evolution of the venom apparatus
    • Kochva E. The origin of snakes and evolution of the venom apparatus. Toxicon. 25:1987;65-106.
    • (1987) Toxicon , vol.25 , pp. 65-106
    • Kochva, E.1
  • 15
    • 0028111357 scopus 로고
    • Modification of sodium channel gating and kinetics by versutoxin from the Australian funnel-web spider Hadronyche versuta
    • Nicholson G.M., Willow M., Howden M.E., Narahashi T. Modification of sodium channel gating and kinetics by versutoxin from the Australian funnel-web spider Hadronyche versuta. Pflügers Arch. (Eur. J. Physiol.). 428:1994;400-409.
    • (1994) Pflügers Arch. (Eur. J. Physiol.) , vol.428 , pp. 400-409
    • Nicholson, G.M.1    Willow, M.2    Howden, M.E.3    Narahashi, T.4
  • 16
    • 0031978687 scopus 로고    scopus 로고
    • Characterisation of the effects of robustoxin, the lethal neurotoxin from the Sydney funnel-web spider Atrax robustus, on sodium channel activation and inactivation
    • Nicholson G.M., Walsh R., Little M., Tyler M.I. Characterisation of the effects of robustoxin, the lethal neurotoxin from the Sydney funnel-web spider Atrax robustus, on sodium channel activation and inactivation. Pflügers Arch. (Eur. J. Physiol.). 436:1998;117-126.
    • (1998) Pflügers Arch. (Eur. J. Physiol.) , vol.436 , pp. 117-126
    • Nicholson, G.M.1    Walsh, R.2    Little, M.3    Tyler, M.I.4
  • 17
    • 0030954604 scopus 로고    scopus 로고
    • Application of physiologically active substances isolated from natural resources to pharmacological studies
    • Ohizumi Y. Application of physiologically active substances isolated from natural resources to pharmacological studies. Jpn J. Pharmac. 73:1997;263-289.
    • (1997) Jpn J. Pharmac. , vol.73 , pp. 263-289
    • Ohizumi, Y.1
  • 19
    • 0025113314 scopus 로고
    • Purification and pharmacological characterization of peptide toxins from the black mamba (Dendroaspis polylepis) venom
    • Schweitz H., Bidard J.N., Lazdunski M. Purification and pharmacological characterization of peptide toxins from the black mamba (Dendroaspis polylepis) venom. Toxicon. 28:1990;847-856.
    • (1990) Toxicon , vol.28 , pp. 847-856
    • Schweitz, H.1    Bidard, J.N.2    Lazdunski, M.3
  • 20
    • 0019157277 scopus 로고
    • Antivenom to the venom of the male Sydney funnel-web spider Atrax robustus: Preliminary report
    • Sutherland S.K. Antivenom to the venom of the male Sydney funnel-web spider Atrax robustus: preliminary report. Med. J. Aust. 2:1980;437-441.
    • (1980) Med. J. Aust. , vol.2 , pp. 437-441
    • Sutherland, S.K.1
  • 22
    • 0026687923 scopus 로고
    • Structure of the pancreatic lipase-procolipase complex
    • van Tilbeurgh H., Sarda L., Verger R., Cambillau C. Structure of the pancreatic lipase-procolipase complex. Nature. 359:1992;159-162.
    • (1992) Nature , vol.359 , pp. 159-162
    • Van Tilbeurgh, H.1    Sarda, L.2    Verger, R.3    Cambillau, C.4
  • 23
    • 0033199282 scopus 로고    scopus 로고
    • Structure-function studies of ω-atracotoxin, A potent antagonist of insect voltage-gated calcium channels
    • (in press)
    • Wang, X., Smith, R., Fletcher, J.I., Wilson, H., Wood, C.J., Howden, M.E.H., King, G.F., 1999 Structure-function studies of ω-atracotoxin, a potent antagonist of insect voltage-gated calcium channels, Eur. J. Biochem. (in press).
    • (1999) Eur. J. Biochem.
    • Wang, X.1    Smith, R.2    Fletcher, J.I.3    Wilson, H.4    Wood, C.J.5    Howden, M.E.H.6    King, G.F.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.