Foucault, G., Vacher, M., Cribier, S., & Arrio-Dupont, M. (2000). Interactions between beta-enolase and creatine kinase in the cytosol of skeletal muscle cells. The Biochemical Journal, 346 Pt 1, 127-31. (Original work published 2000)

Dereuddre-Bosquet, N., Roy, B., Routledge, K., Clayette, P., Foucault, G., & Lepoivre, M. (2004). Inhibitors of CTP biosynthesis potentiate the anti-human immunodeficiency virus type 1 activity of 3TC in activated peripheral blood mononuclear cells. Antiviral Research, 61(1), 67-70. https://doi.org/10.1016/j.antiviral.2003.08.002

Capilla-Geay, E., Poyet, R., Brocq, F., Pons, F., Kerebel, S., Foucault, G., … Cellarier, G. (2016). Acute anterior myocardial infarction as presenting feature of antiphospholipid syndrome related lupus arthritis . La Revue de Medecine Interne, 37(5), 371-4. https://doi.org/10.1016/j.revmed.2015.08.010

Foucault, G., & COLLET, A. (1955). Not Available . Comptes Rendus Des Seances de la Societe de Biologie et de Ses Filiales, 149(5-6), 507-9.

Foucault, G., Kellershohn, N., Seydoux, F., Yon, J., Parquet, C., & Arrio, B. Comparative study of some conformational properties of alpha, beta and psi bovine trypsins. Biochimie, 56(10), 1343-50. https://doi.org/10.1016/s0300-9084(75)80020-4 (Original work published 1974)

Foucault, G., Traore, F., Levilliers, J., & Pudles, J. (1974). Structure-function relationship in rabbit muscle glyceraldehyde-3-phosphate dehydrogenase. Trinitrophenylation of the lysine residues. European Journal of Biochemistry, 46(1), 43-57. https://doi.org/10.1111/j.1432-1033.1974.tb03595.x (Original work published 1974)

Foucault, G., Duval, G., Simon, R., Beauchet, O., Dinomais, M., Annweiler, C., & SOCOS, group. Serum Vitamin D and Cingulate Cortex Thickness in Older Adults: Quantitative MRI of the Brain. Current Alzheimer Research, 16(11), 1063-1071. https://doi.org/10.2174/1567205016666191113124356 (Original work published 2019)

Nakano, M., Foucault, G., & Pudles, J. (1976). Relationship between structure and chemical reactivity in D-glyceraldehyde 3-phosphate dehydrogenase. Trinitrophenylation of the lysine residues in yeast, sturgeon and rabbit muscle enzyme. Journal of Molecular Biology, 105(2), 275-91. https://doi.org/10.1016/0022-2836(76)90112-1 (Original work published 1976)

Foucault, G., Nakano, M., & Pudles, J. (1978). Role of lysine-183 in D-glyceraldehyde-3-phosphate dehydrogenases. Properties of the N-acetylated yeast, sturgeon muscle and rabbit muscle enzymes. European Journal of Biochemistry, 83(1), 113-23. https://doi.org/10.1111/j.1432-1033.1978.tb12074.x (Original work published 1978)

Foucault, G., Bodo, J., & Nakano, M. (1981). Structure and reactivity relationship in glyceraldehyde-3-phosphate dehydrogenase. Dinitrophenylation of cysteine residues of yeast and rabbit muscle enzymes. European Journal of Biochemistry, 119(3), 625-32. https://doi.org/10.1111/j.1432-1033.1981.tb05653.x