A. Yiotakis

Crystal Structures of MMP-9 Complexes with Five Inhibitors: Contribution of the Flexible Arg424 Side Chain to Selectivity (vol 371, pg 989, 2007) (2009)

Tochowicz, A., Maskos, K., Huber, R., Oltenfreiter, R., Dive, V., Yiotakis, A., ...

Crystal structures of MMP-9 complexes with five inhibitors: Contribution of the flexible arg424 side-chain to selectivity (2007)

Tochowicz, A., Maskos, K., Huber, R., Oltenfreiter, R., Dive, V., Yiotakis, A., ...

Crystal structures of MMP-9 complexes with five inhibitors: Contribution of the flexible arg424 side-chain to selectivity (2007)

Tochowicz, A., Maskos, K., Huber, R., Oltenfreiter, R., Dive, V., Yiotakis, A., ...

Crystal structures of MMP-9 complexes with five inhibitors: Contribution of the flexible arg424 side-chain to selectivity (2007)

TOCHOWICZ, A, MASKOS, K, HUBER, R, OLTENFREITER, RUTH, DIVE, V, YIOTAKIS, A, ...

Potent inhibition of endopeptidase 24.16 and endopeptidase 24.15 by the phosphonamide peptide N-(phenylethylphosphonyl)-Gly-L-Pro-L-aminohexanoic acid.

Barelli, H, Dive, V, Yiotakis, A, Vincent, J P, Checler, F

A phosphonamide peptide, N-(phenylethylphosphonyl)-Gly-L-Pro-L-aminohexanoic acid, previously shown to block Clostridium histolyticum collagenases, was examined as a putative inhibitor of...

Phosphinic peptide analogues as potent inhibitors of Corynebacterium rathayii bacterial collagenase.

Yiotakis, A, Lecoq, A, Nicolaou, A, Labadie, J, Dive, V

Pseudo-substrate analogues of collagenase from Corynebacterium rathayii, in which the scissile peptide bond is replaced by a phosphinic moiety, were synthesized and evaluated as inhibitors of this...

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

A series of phosphinic pseudo-peptides varying in length and composition have been designed as inhibitors of the crayfish zinc endopeptidase astacin, the prototype of the astacin family and of the...

Potent inhibition of endopeptidase 24.16 and endopeptidase 24.15 by the phosphonamide peptide N-(phenylethylphosphonyl)-Gly-L-Pro-L-aminohexanoic acid.

Barelli, H, Dive, V, Yiotakis, A, Vincent, J P, Checler, F

A phosphonamide peptide, N-(phenylethylphosphonyl)-Gly-L-Pro-L-aminohexanoic acid, previously shown to block Clostridium histolyticum collagenases, was examined as a putative inhibitor of...

Phosphinic peptide analogues as potent inhibitors of Corynebacterium rathayii bacterial collagenase.

Yiotakis, A, Lecoq, A, Nicolaou, A, Labadie, J, Dive, V

Pseudo-substrate analogues of collagenase from Corynebacterium rathayii, in which the scissile peptide bond is replaced by a phosphinic moiety, were synthesized and evaluated as inhibitors of this...

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

A series of phosphinic pseudo-peptides varying in length and composition have been designed as inhibitors of the crayfish zinc endopeptidase astacin, the prototype of the astacin family and of the...

Phosphorus-containing peptides as mixed inhibitors of endopeptidase 3.4.24.15 and 3.4.24.16: effect on neurotensin degradation in vitro and in vivo.

Vincent, B., Dive, V., Yiotakis, A., Smadja, C., Maldonado, R., Vincent, J. P., ...

1. We have examined several phosphorus-containing peptides as potential mixed inhibitors of two neurotensin-degrading zinc metallopeptidases, endopeptidase 3.4.24.15 and endopeptidase 3.4.24.16. 2....