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Junot, C
Gonzales, MF
Ezan, E
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Michaud, A
Azizi, M
Vassiliou, S
Yiotakis, A
Corvol, P
Dive, V
Citation: C. Junot et al., RXP 407, a selective inhibitor of the N-domain of angiotensin I-convertingenzyme, blocks in vivo the degradation of hemoregulatory peptide acetyl-Ser-Asp-Lys-Pro with no effect on angiotensin I hydrolysis, J PHARM EXP, 297(2), 2001, pp. 606-611
Authors:
Garcon, S
Vassiliou, S
Cavicchioli, M
Hartmann, B
Monteiro, N
Balme, G
Citation: S. Garcon et al., An effective one-pot synthesis of 3-benzylfurans and their potential utility as versatile precursors of 3,4-dibenzyltetrahydrofuran lignans. Formal synthesis of (+/-)-burseran, J ORG CHEM, 66(11), 2001, pp. 4069-4073
Authors:
Dive, V
Lucet-Levannier, K
Georgiadis, D
Cotton, J
Vassiliou, S
Cuniasse, P
Yiotakis, A
Citation: V. Dive et al., Phosphinic peptide inhibitors as tools in the study of the function of zinc metallopeptidases, BIOCH SOC T, 28, 2000, pp. 455-460
Authors:
Georgiadis, D
Matziari, M
Vassiliou, S
Dive, V
Yiotakis, A
Citation: D. Georgiadis et al., A convenient method to synthesize phosphinic peptides containing an aspartyl or glutamyl aminophosphinic acid. Use of the phenyl group as the carboxyl synthon (vol 55, pg 14635, 1999), TETRAHEDRON, 56(20), 2000, pp. 3261-3261
Authors:
Georgiadis, D
Matziari, M
Vassiliou, S
Dive, V
Yiotakis, A
Citation: D. Georgiadis et al., A convenient method to synthesize phosphinic peptides containing an aspartyl or glutamyl aminophosphinic acid. Use of the phenyl group as the carboxyl synthon., TETRAHEDRON, 55(51), 1999, pp. 14635-14648
Authors:
Dive, V
Cotton, J
Yiotakis, A
Michaud, A
Vassiliou, S
Jiracek, J
Vazeux, G
Chauvet, MT
Cuniasse, P
Corvol, P
Citation: V. Dive et al., RXP 407, a phosphinic peptide, is a potent inhibitor of angiotensin I converting enzyme able to differentiate between its two active sites, P NAS US, 96(8), 1999, pp. 4330-4335
Authors:
Vassiliou, S
Mucha, A
Cuniasse, P
Georgiadis, D
Lucet-Levannier, K
Beau, F
Kannan, R
Murphy, G
Knauper, V
Rio, MC
Basset, P
Yiotakis, A
Dive, V
Citation: S. Vassiliou et al., Phosphinic pseudo-tripeptides as potent inhibitors of matrix metalloproteinases: A structure-activity study, J MED CHEM, 42(14), 1999, pp. 2610-2620