메뉴 건너뛰기




Volumn 302, Issue 4, 2003, Pages 691-696

The neurotoxic phospholipase A2 associates, through a non-phosphorylated binding motif, with 14-3-3 protein γ and ε isoforms

Author keywords

14 3 3 proteins; Ammodytoxin; Presynaptic neurotoxicity; Secreted phospholipase A2; Snake venom; Vipera ammodytes ammodytes

Indexed keywords

ISOPROTEIN; PHOSPHOLIPASE A2; PROTEIN SUBUNIT; AMMODYTOXIN C; PHOSPHOLIPASE A; PROTEIN 14 3 3; TYROSINE 3 MONOOXYGENASE; VIPER VENOM;

EID: 0038362168     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00228-6     Document Type: Article
Times cited : (46)

References (41)
  • 6
    • 0001252534 scopus 로고
    • Basic proteins of Vipera ammodytes venom: Studies of the structure and function
    • Gubenšek F., Ritonja A., Zupan J., Turk V. Basic proteins of Vipera ammodytes venom: studies of the structure and function. Period. Biol. 82:1980;443-447.
    • (1980) Period. Biol. , vol.82 , pp. 443-447
    • Gubenšek, F.1    Ritonja, A.2    Zupan, J.3    Turk, V.4
  • 7
    • 0032534227 scopus 로고    scopus 로고
    • 2 -induced neurotoxicity and epileptic seizures after intracerebral administration: An unexplained heterogeneity as emphasized with paradoxin and crotoxin
    • 2 -induced neurotoxicity and epileptic seizures after intracerebral administration: an unexplained heterogeneity as emphasized with paradoxin and crotoxin J. Neurosci. Res. 54:1998;848-862.
    • (1998) J. Neurosci. Res. , vol.54 , pp. 848-862
    • Dorandeu, F.1    Pernot-Marino, I.2    Veyret, J.3    Perrichon, C.4    Lallement, G.5
  • 10
    • 0032912951 scopus 로고    scopus 로고
    • Nerve terminal damage by β-bungarotoxin: Its clinical significance
    • Dixon R.W., Harris J.B. Nerve terminal damage by β-bungarotoxin: its clinical significance. Am. J. Pathol. 154:1999;447-455.
    • (1999) Am. J. Pathol. , vol.154 , pp. 447-455
    • Dixon, R.W.1    Harris, J.B.2
  • 11
    • 0030293125 scopus 로고    scopus 로고
    • 2 neurotoxin: Its effect on protein phosphorylation in rat brain synaptosomes
    • 2 neurotoxin: its effect on protein phosphorylation in rat brain synaptosomes Toxicon. 34:1996;1219-1227.
    • (1996) Toxicon , vol.34 , pp. 1219-1227
    • Ueno, E.1    Rosenberg, P.2
  • 15
    • 0028909615 scopus 로고
    • Novel reticular calcium binding protein is purified on taipoxin columns
    • Dodds D., Schlimgen A.K., Lu S.-Y., Perin M.S. Novel reticular calcium binding protein is purified on taipoxin columns. J. Neurochem. 64:1995;2339-2344.
    • (1995) J. Neurochem. , vol.64 , pp. 2339-2344
    • Dodds, D.1    Schlimgen, A.K.2    Lu, S.-Y.3    Perin, M.S.4
  • 19
    • 0036479325 scopus 로고    scopus 로고
    • 14-3-3 proteins: Active cofactors in cellular regulation by serine/threonine phosphorylation
    • Tzivion G., Avruch J. 14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation. J. Biol. Chem. 277:2002;3061-3064.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3061-3064
    • Tzivion, G.1    Avruch, J.2
  • 20
    • 0037138389 scopus 로고    scopus 로고
    • How do 14-3-3 proteins work? Gatekeeper phosphorylation and the molecular anvil hypothesis
    • Yaffe M.B. How do 14-3-3 proteins work? Gatekeeper phosphorylation and the molecular anvil hypothesis. FEBS Lett. 513:2002;53-57.
    • (2002) FEBS Lett. , vol.513 , pp. 53-57
    • Yaffe, M.B.1
  • 21
    • 0037112329 scopus 로고    scopus 로고
    • Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals
    • O'Kelly I., Butler M.H., Zilberberg N., Goldstein S.A. Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals. Cell. 111:2002;577-588.
    • (2002) Cell , vol.111 , pp. 577-588
    • O'Kelly, I.1    Butler, M.H.2    Zilberberg, N.3    Goldstein, S.A.4
  • 22
    • 0027371622 scopus 로고
    • Antibodies against the major brain isoforms of 14-3-3 protein. An antibody specific for the N-acetylated amino-terminus of a protein
    • Martin H., Patel Y., Jones D., Howell S., Robinson K., Aitken A. Antibodies against the major brain isoforms of 14-3-3 protein. An antibody specific for the N-acetylated amino-terminus of a protein. FEBS Lett. 331:1993;296-303.
    • (1993) FEBS Lett. , vol.331 , pp. 296-303
    • Martin, H.1    Patel, Y.2    Jones, D.3    Howell, S.4    Robinson, K.5    Aitken, A.6
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0019492995 scopus 로고
    • Antibodies against the major brain isoforms of 14-3-3 protein. An antibody specific for the N-acetylated amino-terminus of a protein
    • Merril C.R., Goldman D., Sedman S.A., Ebert M.A. Antibodies against the major brain isoforms of 14-3-3 protein. An antibody specific for the N-acetylated amino-terminus of a protein. Science. 211:1981;1437-1438.
    • (1981) Science , vol.211 , pp. 1437-1438
    • Merril, C.R.1    Goldman, D.2    Sedman, S.A.3    Ebert, M.A.4
  • 25
    • 0033760051 scopus 로고    scopus 로고
    • Comparison of proteins expressed by Pseudomonas aeruginosa strains representing initial and chronic isolates from a cystic fibrosis patient: An analysis by 2-D gel electrophoresis and capillary column liquid chromatography-tandem mass spectrometry
    • Hanna S.L., Sherman N.E., Kinter M.T., Goldberg J.B. Comparison of proteins expressed by Pseudomonas aeruginosa strains representing initial and chronic isolates from a cystic fibrosis patient: an analysis by 2-D gel electrophoresis and capillary column liquid chromatography-tandem mass spectrometry. Microbiology. 146:2000;2495-2508.
    • (2000) Microbiology , vol.146 , pp. 2495-2508
    • Hanna, S.L.1    Sherman, N.E.2    Kinter, M.T.3    Goldberg, J.B.4
  • 26
    • 0025364856 scopus 로고
    • Protein kinase C inhibitor proteins. Purification from sheep brain and sequence similarity to lipocortins and 14-3-3 protein
    • Toker A., Ellis C.A., Sellers L.A., Aitken A. Protein kinase C inhibitor proteins. Purification from sheep brain and sequence similarity to lipocortins and 14-3-3 protein. Eur. J. Biochem. 191:1990;421-429.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 421-429
    • Toker, A.1    Ellis, C.A.2    Sellers, L.A.3    Aitken, A.4
  • 28
    • 0030795295 scopus 로고    scopus 로고
    • Reliable determination of binding affinity and kinetics using surface plasmon resonance biosensors
    • Schuck P. Reliable determination of binding affinity and kinetics using surface plasmon resonance biosensors. Curr. Opin. Biotech. 8:1997;498-502.
    • (1997) Curr. Opin. Biotech. , vol.8 , pp. 498-502
    • Schuck, P.1
  • 30
    • 0028063607 scopus 로고
    • Subcellular localisation of 14-3-3 isoforms in rat brain using specific antibodies
    • Martin H., Rostas J., Patel Y., Aitken A. Subcellular localisation of 14-3-3 isoforms in rat brain using specific antibodies. J. Neurochem. 63:1994;2259-2265.
    • (1994) J. Neurochem. , vol.63 , pp. 2259-2265
    • Martin, H.1    Rostas, J.2    Patel, Y.3    Aitken, A.4
  • 33
    • 0033120915 scopus 로고    scopus 로고
    • In vivo and in vitro association of 14-3-3 epsilon isoform with calmodulin: Implication for signal transduction and cell proliferation
    • Luk S.C., Ngai S.M., Tsui S.K., Fung K.P., Lee C.Y., Waye M.M. In vivo and in vitro association of 14-3-3 epsilon isoform with calmodulin: implication for signal transduction and cell proliferation. J. Cell. Biochem. 73:1999;31-35.
    • (1999) J. Cell. Biochem. , vol.73 , pp. 31-35
    • Luk, S.C.1    Ngai, S.M.2    Tsui, S.K.3    Fung, K.P.4    Lee, C.Y.5    Waye, M.M.6
  • 36
    • 0036670527 scopus 로고    scopus 로고
    • Exoenzyme S binds its cofactor 14-3-3 through a non-phosphorylated motif
    • Hallberg B. Exoenzyme S binds its cofactor 14-3-3 through a non-phosphorylated motif. Biochem. Soc. Trans. 30:2002;401-405.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 401-405
    • Hallberg, B.1
  • 39
    • 0036417225 scopus 로고    scopus 로고
    • β-Bungarotoxin is a potent inducer of apoptosis in cultured rat neurons by receptor-mediated internalization
    • Herkert M., Shakhman O., Schweins E., Becker C.-M. β-Bungarotoxin is a potent inducer of apoptosis in cultured rat neurons by receptor-mediated internalization. Eur. J. Neurosci. 14:2001;821-828.
    • (2001) Eur. J. Neurosci. , vol.14 , pp. 821-828
    • Herkert, M.1    Shakhman, O.2    Schweins, E.3    Becker, C.-M.4
  • 40
    • 0023159096 scopus 로고
    • The actions of presynaptic snake toxins on membrane currents of mouse motor nerve terminals
    • Dreyer F., Penner R. The actions of presynaptic snake toxins on membrane currents of mouse motor nerve terminals. J. Physiol. 386:1987;455-463.
    • (1987) J. Physiol. , vol.386 , pp. 455-463
    • Dreyer, F.1    Penner, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.