Marie‐Thérèse Chauvet

The Hemoregulatory Peptide N-Acetyl-Ser-Asp-Lys-Pro Is a Natural and Specific Substrate of the N-terminal Active Site of Human Angiotensin-converting Enzyme

Anne Rousseau, Annie Michaud, Marie‐Thérèse Chauvet et al. · Journal of Biological Chemistry · 1995 · 311 citations · Full text

RXP 407, a phosphinic peptide, is a potent inhibitor of angiotensin I converting enzyme able to differentiate between its two active sites

Vincent Dive, Jöel Cotton, Athanasios Yiotakis et al. · Proceedings of the National Academy of Sciences · 1999 · 177 citations · Full text

Bioorganic Chemistry, Active Sites, Chemical Biology +18

Phylogeny of the Neurohypophysial Hormones

Roger Acher, Jacqueline Chauvet, Marie‐Thérèse Chauvet · European Journal of Biochemistry · 1970 · 104 citations · Full text

Comparative Endocrinology, Mammalian Physiology, Synapsida +17

<i>Drosophila melanogaster</i> angiotensin I-converting enzyme expressed in Pichia pastoris resembles the C domain of the mammalian homologue and does not require glycosylation for secretion and enzymic activity

Tracy Ann Williams, Annie Michaud, Xavier Houard et al. · Biochemical Journal · 1996 · 75 citations · Full text

Substrate Dependence of Angiotensin I-Converting Enzyme Inhibition: Captopril Displays a Partial Selectivity for Inhibition ofN-Acetyl-Seryl-Aspartyl-Lysyl-Proline Hydrolysis Compared with That of Angiotensin I·

Annie Michaud, Tracy Ann Williams, Marie‐Thérèse Chauvet et al. · Molecular Pharmacology · 1997 · 72 citations