Philippe Cuniasse

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

Life Sciences, Biochemistry, Pharmacology +15

Development of Selective Inhibitors and Substrate of Matrix Metalloproteinase-12

Laurent Devel, Vassilis Rogakos, Arnaud David et al. · Journal of Biological Chemistry · 2006 · 149 citations · Full text

Pharmacy, Medicinal Chemistry, Pharmacology +14

Phosphinic Pseudo-Tripeptides as Potent Inhibitors of Matrix Metalloproteinases:  A Structure−Activity Study

Stamatia Vassiliou, Artur Mucha, Philippe Cuniasse et al. · Journal of Medicinal Chemistry · 1999 · 111 citations · Full text

Pharmacy, Biochemistry, Medicinal Chemistry +12

Residues Determining the Binding Specificity of Uncompetitive Inhibitors to Tissue-Nonspecific Alkaline Phosphatase

Alexey Kozlenkov, Marie‐Hélène Le Du, Philippe Cuniasse et al. · Journal of Bone and Mineral Research · 2004 · 97 citations

Medicine, Molecular Biology, Pharmacology +13

Crystal structure of the stromelysin-3 (MMP-11) catalytic domain complexed with a phosphinic inhibitor mimicking the transition-state11Edited by R. Huber

Anne-Laure Gall, Marc Ruff, Rama Kannan et al. · Journal of Molecular Biology · 2001 · 95 citations

Life Sciences, Biology, Molecular Biology +10