메뉴 건너뛰기




Volumn 36, Issue 12, 1998, Pages 1871-1885

Four new postsynaptic neurotoxins from Naja naja sputatrix venom: cDNA cloning, protein expression, and phylogenetic analysis

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; NEUROTOXIN; SNAKE VENOM;

EID: 0032402082     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0041-0101(98)00108-1     Document Type: Article
Times cited : (27)

References (41)
  • 2
    • 0016753216 scopus 로고
    • Transfer of proteins across membranes. I - Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma
    • Blobel, G. and Dobberstein, B. (1975) Transfer of proteins across membranes. I - Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J. Cell Biol. 67, 852-862.
    • (1975) J. Cell Biol. , vol.67 , pp. 852-862
    • Blobel, G.1    Dobberstein, B.2
  • 3
    • 0020065043 scopus 로고
    • Separation of intermediates in the refolding of reduced erabutoxin b by analytical isoelectric focusing in layers of polyacrylamide gel
    • Bouet, F., Menez, A., Hider, R. C. and Fromageot, P. (1982) Separation of intermediates in the refolding of reduced erabutoxin b by analytical isoelectric focusing in layers of polyacrylamide gel. Biochem. J. 201, 495-499.
    • (1982) Biochem. J. , vol.201 , pp. 495-499
    • Bouet, F.1    Menez, A.2    Hider, R.C.3    Fromageot, P.4
  • 5
    • 0000950985 scopus 로고
    • κ-neurotoxins and α-neurotoxins: Effects on neuronal nicotinic acetylcholine receptors
    • ed. A. L. Harvey, Pergamon, New York
    • Chiappinelli, V. A. (1991) κ-neurotoxins and α-neurotoxins: Effects on neuronal nicotinic acetylcholine receptors. In Snake Toxins, ed. A. L. Harvey, pp. 223-258. Pergamon, New York.
    • (1991) Snake Toxins , pp. 223-258
    • Chiappinelli, V.A.1
  • 6
    • 0018639079 scopus 로고
    • Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease
    • Chirgwin, J. M., Przybyla, A. E., MacDonald, R. A. and Rutter, W. J. (1979) Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 18, 5294-5299.
    • (1979) Biochemistry , vol.18 , pp. 5294-5299
    • Chirgwin, J.M.1    Przybyla, A.E.2    MacDonald, R.A.3    Rutter, W.J.4
  • 7
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • Chou, P. Y. and Fasman, G. D. (1974) Prediction of protein conformation. Biochemistry 13, 222-245.
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 8
    • 0010301578 scopus 로고    scopus 로고
    • Genbank databases, Accession Numbers U42582, U58519, U58520, U58521, U77490, U77491 and U77492
    • Chu, R. C., and Yang, C. C. (1996) Genbank databases, Accession Numbers U42582, U58519, U58520, U58521, U77490, U77491 and U77492.
    • (1996)
    • Chu, R.C.1    Yang, C.C.2
  • 9
    • 0028149948 scopus 로고
    • The amino acid sequences of two postsynaptic neurotoxins isolated from Malayan cobra (Naja naja sputatrix) venom
    • Chung, M. C. M., Tan, N.-H. and Armugam, A. (1994) The amino acid sequences of two postsynaptic neurotoxins isolated from Malayan cobra (Naja naja sputatrix) venom. Toxicon 32, 1471-1474.
    • (1994) Toxicon , vol.32 , pp. 1471-1474
    • Chung, M.C.M.1    Tan, N.-H.2    Armugam, A.3
  • 10
    • 0024962029 scopus 로고
    • The crystal structure of erabutoxin a at 2.0-A resolution
    • Corfield, P. W., Lee, T.-S. and Low, B. W. (1989) The crystal structure of erabutoxin a at 2.0-A resolution. J. Biol. Chem. 264, 9239-9242.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9239-9242
    • Corfield, P.W.1    Lee, T.-S.2    Low, B.W.3
  • 11
    • 0030030033 scopus 로고    scopus 로고
    • Diet and snake venom evolution
    • Daltry, J. C., Wuster, W. and Thorpe, R. S. (1996) Diet and snake venom evolution. Nature 379, 537-540.
    • (1996) Nature , vol.379 , pp. 537-540
    • Daltry, J.C.1    Wuster, W.2    Thorpe, R.S.3
  • 13
    • 0025355079 scopus 로고
    • Nucleotide sequence and structure analysis of cDNAs encoding short-chain neurotoxin from venom glands of a sea snake (Aipysurus laevis)
    • Ducancel, F., Gutgnery-Frelat, G., Boulain, J.-C. and Menez, A. (1990) Nucleotide sequence and structure analysis of cDNAs encoding short-chain neurotoxin from venom glands of a sea snake (Aipysurus laevis). Toxicon 28, 119-123.
    • (1990) Toxicon , vol.28 , pp. 119-123
    • Ducancel, F.1    Gutgnery-Frelat, G.2    Boulain, J.-C.3    Menez, A.4
  • 14
    • 0020556816 scopus 로고
    • Conformational properties of the neurotoxins and cytotoxins isolated from elapid snake venoms
    • Dufton, M. J. and Hider, R. C. (1983) Conformational properties of the neurotoxins and cytotoxins isolated from elapid snake venoms. CRC Crit. Rev. Biochem. 14, 113-171.
    • (1983) CRC Crit. Rev. Biochem. , vol.14 , pp. 113-171
    • Dufton, M.J.1    Hider, R.C.2
  • 15
    • 0002687075 scopus 로고
    • Structure-function relationships of postsynaptic neurotoxins from snake venom
    • ed. A. L. Harvey, Pergamon, New York
    • Endo, T., and Tamiya, N. (1991) Structure-function relationships of postsynaptic neurotoxins from snake venom. In Snake Toxins, ed. A. L. Harvey, pp. 165-222. Pergamon, New York.
    • (1991) Snake Toxins , pp. 165-222
    • Endo, T.1    Tamiya, N.2
  • 17
    • 0025107412 scopus 로고
    • Structure of the short-chain neurotoxin, erabutoxin c, precursor gene
    • Fuse, N., Tsuchiya, T., Nonomura, Y., Menez, A. and Tamiya, T. (1990) Structure of the short-chain neurotoxin, erabutoxin c, precursor gene. Eur. J. Biochem. 193, 629-633.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 629-633
    • Fuse, N.1    Tsuchiya, T.2    Nonomura, Y.3    Menez, A.4    Tamiya, T.5
  • 18
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Garnier, J., Osguthrope, D. J. and Robson, B. (1978) Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120, 97-120.
    • (1978) J. Mol. Biol. , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthrope, D.J.2    Robson, B.3
  • 19
    • 0017665730 scopus 로고
    • Amino acid sequences of neurotoxin I and III of the elapidae snake Naja mossambica mossambica
    • Gregoire, J. and Rochat, H. (1977) Amino acid sequences of neurotoxin I and III of the elapidae snake Naja mossambica mossambica. Eur. J. Biochem. 80, 283-293.
    • (1977) Eur. J. Biochem. , vol.80 , pp. 283-293
    • Gregoire, J.1    Rochat, H.2
  • 21
    • 0028937979 scopus 로고
    • The structural loop II of cobrotoxin is the main binding region for nAChR and epitope in the region is conformation dependent
    • Kuo, K.-W., Chang, L.-S. and Chang, C.-C. (1995) The structural loop II of cobrotoxin is the main binding region for nAChR and epitope in the region is conformation dependent. J. Biochem. 117, 438-442.
    • (1995) J. Biochem. , vol.117 , pp. 438-442
    • Kuo, K.-W.1    Chang, L.-S.2    Chang, C.-C.3
  • 22
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. and Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 23
    • 84908803978 scopus 로고
    • The three-dimensional structure of postsynaptic snake neurotoxins: Consideration of structure and function
    • ed. C.-Y. Lee, Springer-Verlag, New York
    • Low, B. W. (1979) The three-dimensional structure of postsynaptic snake neurotoxins: consideration of structure and function. In Snake venoms, ed. C.-Y. Lee, pp. 213-257. Springer-Verlag, New York.
    • (1979) Snake Venoms , pp. 213-257
    • Low, B.W.1
  • 24
    • 0017284145 scopus 로고
    • Isolation, properties and amino acid sequences of three neurotoxins from the venom of a sea snake, Aipysurus laevis
    • Maeda, N. and Tamiya, N. (1976) Isolation, properties and amino acid sequences of three neurotoxins from the venom of a sea snake, Aipysurus laevis. Biochem. J. 153, 79-87.
    • (1976) Biochem. J. , vol.153 , pp. 79-87
    • Maeda, N.1    Tamiya, N.2
  • 25
    • 0019201316 scopus 로고
    • Refolding of reduced short neurotoxins: Circular dichroism analysis
    • Menez, A., Bouet, F., Guschlbauer, W. and Fromageot, P. (1980) Refolding of reduced short neurotoxins: Circular dichroism analysis. Biochemistry 19, 4166-4172.
    • (1980) Biochemistry , vol.19 , pp. 4166-4172
    • Menez, A.1    Bouet, F.2    Guschlbauer, W.3    Fromageot, P.4
  • 27
    • 0024822384 scopus 로고
    • Sequence analysis of a cDNA encoding erabutoxin b from the sea-snake Laticauda semifasciata
    • Obara, K., Fuse, N., Tsuchiye, T., Nonomura, T., Menez, A. and Tamiya, T. (1989) Sequence analysis of a cDNA encoding erabutoxin b from the sea-snake Laticauda semifasciata. Nucl. Acid Res. 17, 10490.
    • (1989) Nucl. Acid Res. , vol.17 , pp. 10490
    • Obara, K.1    Fuse, N.2    Tsuchiye, T.3    Nonomura, T.4    Menez, A.5    Tamiya, T.6
  • 28
    • 0027396750 scopus 로고
    • Genetic engineering of snake toxins, role of invariant residues in the structural and functional properties of a curaremimetic toxin, as probed by site-directed mutagenesis
    • Pillet, L., Tremeau, O., Ducancel, F., Drevet, P., Zinn-Justin, S., Pinkasfeld, S., Boulain, J.-C. and Menez, A. (1993) Genetic engineering of snake toxins, role of invariant residues in the structural and functional properties of a curaremimetic toxin, as probed by site-directed mutagenesis. J. Biol. Chem. 268, 909-916.
    • (1993) J. Biol. Chem. , vol.268 , pp. 909-916
    • Pillet, L.1    Tremeau, O.2    Ducancel, F.3    Drevet, P.4    Zinn-Justin, S.5    Pinkasfeld, S.6    Boulain, J.-C.7    Menez, A.8
  • 31
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H. and Von-Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von-Jagow, G.2
  • 32
    • 0014967258 scopus 로고
    • The properties and modification of tryptophan in a sea snake toxin, erabutoxin a
    • Seto, A., Sato, S. and Tamiya, N. (1970) The properties and modification of tryptophan in a sea snake toxin, erabutoxin a. Biochim. Biophys. Acta 214, 483-489.
    • (1970) Biochim. Biophys. Acta , vol.214 , pp. 483-489
    • Seto, A.1    Sato, S.2    Tamiya, N.3
  • 33
    • 0015523239 scopus 로고
    • Snake venom toxins. The amino acid sequences of two toxins from Dendroaspis polylepis polylepis (black mamba) venom
    • Strydom, D. J. (1972) Snake venom toxins. The amino acid sequences of two toxins from Dendroaspis polylepis polylepis (black mamba) venom. J. Biol. Chem. 247, 4029-4042.
    • (1972) J. Biol. Chem. , vol.247 , pp. 4029-4042
    • Strydom, D.J.1
  • 36
    • 0020624984 scopus 로고
    • Isolation and characterization of two toxins from the venom of the Malayan cobra (Naja naja sputatrix)
    • Tan, N. H. (1983) Isolation and characterization of two toxins from the venom of the Malayan cobra (Naja naja sputatrix). Toxicon 21, 201-207.
    • (1983) Toxicon , vol.21 , pp. 201-207
    • Tan, N.H.1
  • 37
    • 0028934293 scopus 로고
    • Genetic engineering of snake toxins, the functional site of erabutoxin a as delineated by site-directed mutagenesis, includes variant residues
    • Tremeau, O., Lemaire, C., Drevet, P., Pinkasfeld, S., Ducancel, F., Boulain, J.-C. and Menez, A. (1995) Genetic engineering of snake toxins, the functional site of erabutoxin a as delineated by site-directed mutagenesis, includes variant residues. J. Biol. Chem. 270, 9362-9369.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9362-9369
    • Tremeau, O.1    Lemaire, C.2    Drevet, P.3    Pinkasfeld, S.4    Ducancel, F.5    Boulain, J.-C.6    Menez, A.7
  • 38
    • 0015538917 scopus 로고
    • Neurotoxins of animal venoms: Snakes
    • Tu, A. T. (1973) Neurotoxins of animal venoms: Snakes. Annu. Rev. Biochem. 42, 235-238.
    • (1973) Annu. Rev. Biochem. , vol.42 , pp. 235-238
    • Tu, A.T.1
  • 40
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanish-Perron, C., Vieire, J. and Messing, J. (1985) Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33, 103-199.
    • (1985) Gene , vol.33 , pp. 103-199
    • Yanish-Perron, C.1    Vieire, J.2    Messing, J.3
  • 41
    • 0027510067 scopus 로고
    • Molecular cloning of a cardiotoxin structural gene from Malayan spitting cobra (Naja naja sputatrix)
    • Yeo, M. S. L., Jeyaseelan, K., Chung, M. C. M., Gopalakrishnakone, P., Tan, C. H. and Wong, H. A. (1993) Molecular cloning of a cardiotoxin structural gene from Malayan spitting cobra (Naja naja sputatrix). Toxicon 31, 35-60.
    • (1993) Toxicon , vol.31 , pp. 35-60
    • Yeo, M.S.L.1    Jeyaseelan, K.2    Chung, M.C.M.3    Gopalakrishnakone, P.4    Tan, C.H.5    Wong, H.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.