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Constitution and properties of axonal membranes of crustacean nerves.
Balerna M, Fosset M, Chicheportiche R, Romey G, Lazdunski M. Balerna M, et al. Among authors: lazdunski m. Biochemistry. 1975 Dec 16;14(25):5500-11. doi: 10.1021/bi00696a019. Biochemistry. 1975. PMID: 58
A cardiac tetrodotoxin binding component: biochemical identification, characterization, and properties.
Lombet A, Renaud JF, Chicheportiche R, Lazdunski M. Lombet A, et al. Among authors: lazdunski m. Biochemistry. 1981 Mar 3;20(5):1279-85. doi: 10.1021/bi00508a036. Biochemistry. 1981. PMID: 6261788 No abstract available.
Toxin-induced K+ efflux through the Na+ channel of neuroblastoma cells.
Jacques Y, Romey G, Lazdunski M. Jacques Y, et al. Among authors: lazdunski m. Eur J Biochem. 1980 Oct;111(1):265-73. doi: 10.1111/j.1432-1033.1980.tb06102.x. Eur J Biochem. 1980. PMID: 6108216
The specificity of the sodium channel for monovalent cations.
Frelin C, Vigne P, Lazdunski M. Frelin C, et al. Among authors: lazdunski m. Eur J Biochem. 1981 Oct;119(2):437-42. doi: 10.1111/j.1432-1033.1981.tb05627.x. Eur J Biochem. 1981. PMID: 6273156 No abstract available.
Properties of the interaction of the sodium channel with permeant monovalent cations.
Jacques Y, Romey G, Fosset M, Lazdunski M. Jacques Y, et al. Among authors: lazdunski m. Eur J Biochem. 1980 May;106(1):71-83. doi: 10.1111/j.1432-1033.1980.tb05998.x. Eur J Biochem. 1980. PMID: 6281000
Synthesis and mode of action on axonal membranes of photoactivable derivatives of tetrodotoxin.
Chicheportiche R, Balerna M, Lombet A, Romey G, Lazdunski M. Chicheportiche R, et al. Among authors: lazdunski m. J Biol Chem. 1979 Mar 10;254(5):1552-7. J Biol Chem. 1979. PMID: 762156
Solubilization of the nitrendipine receptor from skeletal muscle transverse tubule membranes. Interactions with specific inhibitors of the voltage-dependent Ca2+ channel.
Borsotto M, Norman RI, Fosset M, Lazdunski M. Borsotto M, et al. Among authors: lazdunski m. Eur J Biochem. 1984 Aug 1;142(3):449-55. doi: 10.1111/j.1432-1033.1984.tb08307.x. Eur J Biochem. 1984. PMID: 6088224
At 4 degrees C the equilibrium dissociation constant of the [3H]nitrendipine X receptor complex was 7 +/- 3 nM and was close to that determined from the rate constants of association (k1 = 1.3 10(5) M-1 s-1) and dissociation (k-1 = 1.10 X 10(-3) s-1) of 8.4nM. ...
At 4 degrees C the equilibrium dissociation constant of the [3H]nitrendipine X receptor complex was 7 +/- 3 nM and was close to that determi …
Monoclonal antibodies that coimmunoprecipitate the 1,4-dihydropyridine and phenylalkylamine receptors and reveal the Ca2+ channel structure.
Vandaele S, Fosset M, Galizzi JP, Lazdunski M. Vandaele S, et al. Among authors: lazdunski m. Biochemistry. 1987 Jan 13;26(1):5-9. doi: 10.1021/bi00375a002. Biochemistry. 1987. PMID: 2435317
Immunochemical analysis of subunit structures of 1,4-dihydropyridine receptors associated with voltage-dependent Ca2+ channels in skeletal, cardiac, and smooth muscles.
Schmid A, Barhanin J, Coppola T, Borsotto M, Lazdunski M. Schmid A, et al. Among authors: lazdunski m. Biochemistry. 1986 Jun 17;25(12):3492-5. doi: 10.1021/bi00360a002. Biochemistry. 1986. PMID: 2424495
Molecular properties of the apamin-binding component of the Ca2+-dependent K+ channel. Radiation-inactivation, affinity labelling and solubilization.
Schmid-Antomarchi H, Hugues M, Norman R, Ellory C, Borsotto M, Lazdunski M. Schmid-Antomarchi H, et al. Among authors: lazdunski m. Eur J Biochem. 1984 Jul 2;142(1):1-6. doi: 10.1111/j.1432-1033.1984.tb08242.x. Eur J Biochem. 1984. PMID: 6086337
The dissociation constant of the apamin-receptor complex is 40-150 pM, the rates constants of association and dissociation being 3.2 X 10(6) M-1s-1 and 1.4 X 10(-4)s-1 respectively. ...
The dissociation constant of the apamin-receptor complex is 40-150 pM, the rates constants of association and dissociation being 3.2 X 10(6) …
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