The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Chemical Compound Review

Torpedo     N,N-bis(2-chloroethyl)-4- methyl-2,6...

Synonyms: CHLORNIDINE, AC1L1PQB, AI3-62692, 26389-78-6, Caswell No. 089A
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Torpedo


Psychiatry related information on Torpedo

  • Alzheimer's disease antibodies bind specifically to a neurofilament protein in Torpedo cholinergic neurons [6].
  • The common Id was detectable in sera of rats immunized with AChR of either Torpedo, eel or syngeneic muscle [7].
  • Production of such Abs in EAD rats by prolonged immunization with Torpedo cholinergic NF-H results in the accumulation of IgG in the septum and hippocampus of the immunized rats and in memory deficits [8].

High impact information on Torpedo


Chemical compound and disease context of Torpedo

  • We determined the 2.4 A crystal structure of hCE1 in complex with tacrine, the first drug approved for treating Alzheimer's disease, and compare this structure to the Torpedo californica acetylcholinesterase (AcChE)-tacrine complex [12].
  • Furthermore, the in vitro proliferative response of lymph node cells to Torpedo AChR and the purified protein derivative of Mycobacterium tuberculosis was significantly lower in the linomide-treated EAMG rats than in the controls [13].
  • Also, even though this Torpedo protein has higher affinity for insecticides, such as gamma-BHC, than does the GABAA receptor, it is the latter whose specificity correlates best with polychlorocycloalkane toxicity [14].
  • We found that some MAbs raised against the peptide were able to recognize both the virus glycoprotein and the snake neurotoxin alpha-bungarotoxin; moreover, they can inhibit the binding of rabies virus glycoprotein and alpha-bungarotoxin to the nicotinic acetylcholine receptor extracted from the electric organs of Torpedo marmorata [15].

Biological context of Torpedo

  • The nicotinic acetylcholine receptor (AChR) from the electroplax of the ray Torpedo californica is composed of five subunits present in a molar stoichiometry of alpha 2 beta gamma delta (refs 1-3) and contains both the binding site for the neurotransmitter and the cation gating unit (reviewed in refs 4-6) [16].
  • A consensus amino-acid sequence repeat in Torpedo and mammalian Ca2+-dependent membrane-binding proteins [17].
  • DNA sequences complementary to the Torpedo californica electroplax mRNA coding for the alpha-subunit precursor of the acetylcholine receptor were cloned [18].
  • Nucleotide sequence analysis of the cloned DNAs has revealed the primary structures of the calf and human AChR alpha-subunit precursors, which exhibit marked sequence homology with their Torpedo counterpart [19].
  • Previous work with chimaeras between the Torpedo californica and bovine AChR delta-subunits has shown that the region comprising the hydrophobic segment M2 and its vicinity contains an important determinant of the rate of ion transport through the AChR channel [20].

Anatomical context of Torpedo

  • Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes [21].
  • Basal lamina-rich extracts of Torpedo californica electric organ contain a factor that causes acetylcholine receptors (AChRs) on cultured myotubes to aggregate into patches [22].
  • The csp gene of Drosophila encodes proteins homologous to synaptic vesicle proteins in Torpedo [23].
  • The physiological and pharmacological profiles of Torpedo AChR's expressed in mouse fibroblast cells differ in some details from those described earlier, and may provide a more accurate reflection of the properties of this receptor in its natural environment [24].
  • This polyadenylate [poly(A)+]RNA from Torpedo californica directs, in a cell-free system, the synthesis of peptides 60,000, 51,000, 49,000 41,000, and 35,000 daltons which account for approximately 2 percent of the total synthesized proteins [25].

Associations of Torpedo with other chemical compounds


Gene context of Torpedo


Analytical, diagnostic and therapeutic context of Torpedo

  • The mouse acetylcholinesterase sequence shares approximately 88% and 61% amino acid identity with bovine and Torpedo acetylcholinesterases, respectively, but only 52% identity with mouse butyrylcholinesterase, the sequence of which we have also deduced by molecular cloning [34].
  • The biochemical information derived from analyses of ACHE and BCHE from human, Torpedo, mouse, and Drosophila, as well as that from the recombinant forms of their natural variants and site-directed mutants, can currently be re-examined in view of the recent X-ray crystallography data revealing the three-dimensional structure of Torpedo ACHE [35].
  • The Torpedo cDNA encodes a full-length protein, and on Northern blots recognizes a 3.5 kb mRNA [36].
  • Immunogold electron microscopy on isolated postsynaptic membranes from Torpedo showed that both mabs bind to intracellular epitopes on the receptor [37].
  • A bona fide MAGI-1c (150 kD) was detected by Western blotting in the postsynaptic membrane of Torpedo electrocytes, and in a high molecular mass cross-link product of MuSK [38].


  1. Expression of functional acetylcholine receptor from cloned cDNAs. Mishina, M., Kurosaki, T., Tobimatsu, T., Morimoto, Y., Noda, M., Yamamoto, T., Terao, M., Lindstrom, J., Takahashi, T., Kuno, M. Nature (1984) [Pubmed]
  2. Linkage between the frequency of muscular weakness and loci that regulate immune responsiveness in murine experimental myasthenia gravis. Berman, P.W., Patrick, J. J. Exp. Med. (1980) [Pubmed]
  3. The 87K postsynaptic membrane protein from Torpedo is a protein-tyrosine kinase substrate homologous to dystrophin. Wagner, K.R., Cohen, J.B., Huganir, R.L. Neuron (1993) [Pubmed]
  4. Purification and characterization of an alpha-bungarotoxin receptor that forms a functional nicotinic channel. Gotti, C., Ogando, A.E., Hanke, W., Schlue, R., Moretti, M., Clementi, F. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  5. Binding of alpha-bungarotoxin to proteolytic fragments of the alpha subunit of Torpedo acetylcholine receptor analyzed by protein transfer on positively charged membrane filters. Wilson, P.T., Gershoni, J.M., Hawrot, E., Lentz, T.L. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
  6. Alzheimer's disease antibodies bind specifically to a neurofilament protein in Torpedo cholinergic neurons. Chapman, J., Bachar, O., Korczyn, A.D., Wertman, E., Michaelson, D.M. J. Neurosci. (1989) [Pubmed]
  7. Monoclonal autoantibodies to acetylcholine receptors: evidence for a dominant idiotype and requirement of complement for pathogenicity. Lennon, V.A., Lambert, E.H. Ann. N. Y. Acad. Sci. (1981) [Pubmed]
  8. Decreased density of forebrain cholinergic neurons and disintegration of the spatial organization of behavior in experimental autoimmune dementia (EAD). Michaelson, D.M., Dubovik, V., Faigon, M., Eilam, D., Feldon, J. Ann. N. Y. Acad. Sci. (1993) [Pubmed]
  9. Crosslinking of proteins in acetylcholine receptor-rich membranes: association between the beta-subunit and the 43 kd subsynaptic protein. Burden, S.J., DePalma, R.L., Gottesman, G.S. Cell (1983) [Pubmed]
  10. Pore stoichiometry of a voltage-gated chloride channel. Fahlke, C., Rhodes, T.H., Desai, R.R., George, A.L. Nature (1998) [Pubmed]
  11. Primary structure and functional expression of a developmentally regulated skeletal muscle chloride channel. Steinmeyer, K., Ortland, C., Jentsch, T.J. Nature (1991) [Pubmed]
  12. Crystal structure of human carboxylesterase 1 complexed with the Alzheimer's drug tacrine: from binding promiscuity to selective inhibition. Bencharit, S., Morton, C.L., Hyatt, J.L., Kuhn, P., Danks, M.K., Potter, P.M., Redinbo, M.R. Chem. Biol. (2003) [Pubmed]
  13. Immunomodulation of experimental autoimmune myasthenia gravis with linomide. Karussis, D.M., Lehmann, D., Brenner, T., Wirguin, I., Mizrachi-Koll, R., Sicsic, C., Abramsky, O. J. Neuroimmunol. (1994) [Pubmed]
  14. Action of polychlorocycloalkane insecticides on binding of [35S]t-butylbicyclophosphorothionate to Torpedo electric organ membranes and stereospecificity of the binding site. Matsumoto, K., Eldefrawi, M.E., Eldefrawi, A.T. Toxicol. Appl. Pharmacol. (1988) [Pubmed]
  15. Antipeptide monoclonal antibodies inhibit the binding of rabies virus glycoprotein and alpha-bungarotoxin to the nicotinic acetylcholine receptor. Bracci, L., Antoni, G., Cusi, M.G., Lozzi, L., Niccolai, N., Petreni, S., Rustici, M., Santucci, A., Soldani, P., Valensin, P.E. Mol. Immunol. (1988) [Pubmed]
  16. Structural homology of Torpedo californica acetylcholine receptor subunits. Noda, M., Takahashi, H., Tanabe, T., Toyosato, M., Kikyotani, S., Furutani, Y., Hirose, T., Takashima, H., Inayama, S., Miyata, T., Numa, S. Nature (1983) [Pubmed]
  17. A consensus amino-acid sequence repeat in Torpedo and mammalian Ca2+-dependent membrane-binding proteins. Geisow, M.J., Fritsche, U., Hexham, J.M., Dash, B., Johnson, T. Nature (1986) [Pubmed]
  18. Primary structure of alpha-subunit precursor of Torpedo californica acetylcholine receptor deduced from cDNA sequence. Noda, M., Takahashi, H., Tanabe, T., Toyosato, M., Furutani, Y., Hirose, T., Asai, M., Inayama, S., Miyata, T., Numa, S. Nature (1982) [Pubmed]
  19. Cloning and sequence analysis of calf cDNA and human genomic DNA encoding alpha-subunit precursor of muscle acetylcholine receptor. Noda, M., Furutani, Y., Takahashi, H., Toyosato, M., Tanabe, T., Shimizu, S., Kikyotani, S., Kayano, T., Hirose, T., Inayama, S. Nature (1983) [Pubmed]
  20. Rings of negatively charged amino acids determine the acetylcholine receptor channel conductance. Imoto, K., Busch, C., Sakmann, B., Mishina, M., Konno, T., Nakai, J., Bujo, H., Mori, Y., Fukuda, K., Numa, S. Nature (1988) [Pubmed]
  21. Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes. Jentsch, T.J., Steinmeyer, K., Schwarz, G. Nature (1990) [Pubmed]
  22. Aggregates of acetylcholinesterase induced by acetylcholine receptor-aggregating factor. Wallace, B.G., Nitkin, R.M., Reist, N.E., Fallon, J.R., Moayeri, N.N., McMahan, U.J. Nature (1985) [Pubmed]
  23. Paralysis and early death in cysteine string protein mutants of Drosophila. Zinsmaier, K.E., Eberle, K.K., Buchner, E., Walter, N., Benzer, S. Science (1994) [Pubmed]
  24. Genetic reconstitution of functional acetylcholine receptor channels in mouse fibroblasts. Claudio, T., Green, W.N., Hartman, D.S., Hayden, D., Paulson, H.L., Sigworth, F.J., Sine, S.M., Swedlund, A. Science (1987) [Pubmed]
  25. Cell-free synthesis of acetylcholine receptor polypeptides. Mendez, B., Valenzuela, P., Martial, J.A., Baxter, J.D. Science (1980) [Pubmed]
  26. Dystroglycan binds nerve and muscle agrin. Sugiyama, J., Bowen, D.C., Hall, Z.W. Neuron (1994) [Pubmed]
  27. Subcellular localization of creatine kinase in Torpedo electrocytes: association with acetylcholine receptor-rich membranes. Wallimann, T., Walzthöny, D., Wegmann, G., Moser, H., Eppenberger, H.M., Barrantes, F.J. J. Cell Biol. (1985) [Pubmed]
  28. The tyrosine phosphorylation site of the acetylcholine receptor beta subunit is located in a highly immunogenic epitope implicated in channel function: antibody probes for beta subunit phosphorylation and function. Tzartos, S.J., Valcana, C., Kouvatsou, R., Kokla, A. EMBO J. (1993) [Pubmed]
  29. Svp25, a synaptic vesicle membrane glycoprotein from Torpedo electric organ that binds calcium and forms a homo-oligomeric complex. Volknandt, W., Schläfer, M., Bonzelius, F., Zimmermann, H. EMBO J. (1990) [Pubmed]
  30. The small leucine-rich repeat proteoglycan biglycan binds to alpha-dystroglycan and is upregulated in dystrophic muscle. Bowe, M.A., Mendis, D.B., Fallon, J.R. J. Cell Biol. (2000) [Pubmed]
  31. Human endplate acetylcholinesterase deficiency caused by mutations in the collagen-like tail subunit (ColQ) of the asymmetric enzyme. Ohno, K., Brengman, J., Tsujino, A., Engel, A.G. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  32. The yeast CLC chloride channel functions in cation homeostasis. Gaxiola, R.A., Yuan, D.S., Klausner, R.D., Fink, G.R. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  33. Cloning and characterization of the human homologue of a dystrophin related phosphoprotein found at the Torpedo electric organ post-synaptic membrane. Sadoulet-Puccio, H.M., Khurana, T.S., Cohen, J.B., Kunkel, L.M. Hum. Mol. Genet. (1996) [Pubmed]
  34. Molecular cloning of mouse acetylcholinesterase: tissue distribution of alternatively spliced mRNA species. Rachinsky, T.L., Camp, S., Li, Y., Ekström, T.J., Newton, M., Taylor, P. Neuron (1990) [Pubmed]
  35. Excavations into the active-site gorge of cholinesterases. Soreq, H., Gnatt, A., Loewenstein, Y., Neville, L.F. Trends Biochem. Sci. (1992) [Pubmed]
  36. Two forms of mouse syntrophin, a 58 kd dystrophin-associated protein, differ in primary structure and tissue distribution. Adams, M.E., Butler, M.H., Dwyer, T.M., Peters, M.F., Murnane, A.A., Froehner, S.C. Neuron (1993) [Pubmed]
  37. Immunochemical demonstration that amino acids 360-377 of the acetylcholine receptor gamma-subunit are cytoplasmic. LaRochelle, W.J., Wray, B.E., Sealock, R., Froehner, S.C. J. Cell Biol. (1985) [Pubmed]
  38. MAGI-1c: a synaptic MAGUK interacting with muSK at the vertebrate neuromuscular junction. Strochlic, L., Cartaud, A., Labas, V., Hoch, W., Rossier, J., Cartaud, J. J. Cell Biol. (2001) [Pubmed]
WikiGenes - Universities