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Journal Abstract Search

99 related items for PubMed ID: 212272

  • 1. Collagenase sensitivity and aggregation properties of Electrophorus acetylcholinesterase.
    Bon S, Massoulié J.
    Eur J Biochem; 1978 Aug 15; 89(1):89-94. PubMed ID: 212272
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  • 6. Torpedo marmorata acetylcholinesterase; a comparison with the Electrophorus electricus enzyme. Molecular forms, subunits, electron microscopy, immunological relationship.
    Rieger F, Bon S, Massoulié J, Cartauld J, Picard B, Benda P.
    Eur J Biochem; 1976 Sep 15; 68(2):513-21. PubMed ID: 61859
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  • 7. Electrophorus acetylcholinesterase. Biochemical and electron microscope characterization of low ionic strength aggregates.
    Cartaud J, Bon S, Massoulié J.
    J Cell Biol; 1978 May 15; 77(2):315-22. PubMed ID: 649654
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  • 9. Characterization of pepsin-resistant collagen-like tail subunit fragments of 18S and 14S acetylcholinesterase from Electrophorus electricus.
    Mays C, Rosenberry TL.
    Biochemistry; 1981 May 12; 20(10):2810-7. PubMed ID: 6788073
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  • 10. The dependence of acetylcholinesterase aggregation at low ionic strength upon a polyanionic component.
    Bon S, Cartaud J, Massoulié J.
    Eur J Biochem; 1978 Apr 12; 85(1):1-14. PubMed ID: 639808
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  • 16. Characterization of the association of Electrophorus electricus acetylcholinesterase with sphingomyelin liposomes. Relevance to collagen-sphingomyelin interactions.
    Cohen R, Barenholz Y.
    Biochim Biophys Acta; 1984 Nov 21; 778(1):94-104. PubMed ID: 6498189
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  • 18. Molecular forms of Electrophorus acetylcholinesterase the catalytic subunits: fragmentation, intra- and inter-subunit disulfide bonds.
    Bon S, Massoulié J.
    FEBS Lett; 1976 Dec 01; 71(2):273-8. PubMed ID: 1001444
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  • 20. Relationship of collagen-tailed acetylcholinesterase with basal lamina components. Absence of binding with laminin, fibronectin, and collagen types IV and V and lack of reactivity with different anti-collagen sera.
    Grassi J, Massoulié J, Timpl R.
    Eur J Biochem; 1983 Jun 01; 133(1):31-8. PubMed ID: 6852032
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