Vassiliou S - Search Results

1

Cyclic peptides with a phosphinic bond as potent inhibitors of a zinc bacterial collagenase.

Yiotakis A, Lecoq A, Vassiliou S, Raynal I, Cuniasse P, Dive V. Yiotakis A, et al. Among authors: vassiliou s. J Med Chem. 1994 Aug 19;37(17):2713-20. doi: 10.1021/jm00043a011. J Med Chem. 1994. PMID: 8064799

2

Phosphinic pseudo-tripeptides as potent inhibitors of matrix metalloproteinases: a structure-activity study.

Vassiliou S, Mucha A, Cuniasse P, Georgiadis D, Lucet-Levannier K, Beau F, Kannan R, Murphy G, Knäuper V, Rio MC, Basset P, Yiotakis A, Dive V. Vassiliou S, et al. J Med Chem. 1999 Jul 15;42(14):2610-20. doi: 10.1021/jm9900164. J Med Chem. 1999. PMID: 10411481

3

Protection of the Hydroxyphosphinyl Function of Phosphinic Dipeptides by Adamantyl. Application to the Solid-Phase Synthesis of Phosphinic Peptides.

Yiotakis A, Vassiliou S, Jirácek J, Dive V. Yiotakis A, et al. Among authors: vassiliou s. J Org Chem. 1996 Sep 20;61(19):6601-6605. doi: 10.1021/jo9603439. J Org Chem. 1996. PMID: 11667528

4

A synthetic method for diversification of the P1' substituent in phosphinic dipeptides as a tool for exploration of the specificity of the S1' binding pockets of leucine aminopeptidases.

Vassiliou S, Xeilari M, Yiotakis A, Grembecka J, Pawełczak M, Kafarski P, Mucha A. Vassiliou S, et al. Bioorg Med Chem. 2007 May 1;15(9):3187-200. doi: 10.1016/j.bmc.2007.02.042. Epub 2007 Feb 22. Bioorg Med Chem. 2007. PMID: 17337192

5

Design, synthesis, and evaluation of novel organophosphorus inhibitors of bacterial ureases.

Vassiliou S, Grabowiecka A, Kosikowska P, Yiotakis A, Kafarski P, Berlicki Ł. Vassiliou S, et al. J Med Chem. 2008 Sep 25;51(18):5736-44. doi: 10.1021/jm800570q. Epub 2008 Aug 22. J Med Chem. 2008. PMID: 18717581

6

Computer-aided optimization of phosphinic inhibitors of bacterial ureases.

Vassiliou S, Kosikowska P, Grabowiecka A, Yiotakis A, Kafarski P, Berlicki L. Vassiliou S, et al. J Med Chem. 2010 Aug 12;53(15):5597-606. doi: 10.1021/jm100340m. J Med Chem. 2010. PMID: 20684601

7

Phosphinic peptides, the first potent inhibitors of astacin, behave as extremely slow-binding inhibitors.

Yiallouros I, Vassiliou S, Yiotakis A, Zwilling R, Stöcker W, Dive V. Yiallouros I, et al. Among authors: vassiliou s. Biochem J. 1998 Apr 15;331 ( Pt 2)(Pt 2):375-9. doi: 10.1042/bj3310375. Biochem J. 1998. PMID: 9531473 Free PMC article.

The most efficient phosphinic peptide, fluorenylmethyloxycarbonyl-Pro-Lys-PhePsi(PO2CH2)Ala-P ro-Leu-Val, binds to astacin with a Ki value of 42 nM, which is about three orders of magnitude below the corresponding values for previously used hydroxamic acid derivatives. However, t …

The most efficient phosphinic peptide, fluorenylmethyloxycarbonyl-Pro-Lys-PhePsi(PO2CH2)Ala-P ro-Leu-Val, binds to astacin with a Ki value o …

8

Phosphinic peptide inhibitors as tools in the study of the function of zinc metallopeptidases.

Dive V, Lucet-Levannier K, Georgiadis D, Cotton J, Vassiliou S, Cuniasse P, Yiotakis A. Dive V, et al. Among authors: vassiliou s. Biochem Soc Trans. 2000;28(4):455-60. Biochem Soc Trans. 2000. PMID: 10961939 Review.

9

Structure-guided, single-point modifications in the phosphinic dipeptide structure yield highly potent and selective inhibitors of neutral aminopeptidases.

Vassiliou S, Węglarz-Tomczak E, Berlicki Ł, Pawełczak M, Nocek B, Mulligan R, Joachimiak A, Mucha A. Vassiliou S, et al. J Med Chem. 2014 Oct 9;57(19):8140-51. doi: 10.1021/jm501071f. Epub 2014 Sep 22. J Med Chem. 2014. PMID: 25192493 Free PMC article.

10

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

Dive V, Cotton J, Yiotakis A, Michaud A, Vassiliou S, Jiracek J, Vazeux G, Chauvet MT, Cuniasse P, Corvol P. Dive V, et al. Among authors: vassiliou s. Proc Natl Acad Sci U S A. 1999 Apr 13;96(8):4330-5. doi: 10.1073/pnas.96.8.4330. Proc Natl Acad Sci U S A. 1999. PMID: 10200262 Free PMC article.

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