V. Dive

Publication List Details

Period

2002 - 2009

Number

16

Co-Authors

Crystal structure of the dinuclear zinc aminopeptidase PepV from Lactobacillus delbrueckii unravels its preference for dipeptides (2002)

Jozic,D., Bourenkow,G., Bartunik,H., Scholze,H., Dive,V., Henrich,B., ...

PepV from Lactobacillus delbrueckii, a dinuclear zinc peptidase, has been characterized as an unspecific amino dipeptidase. The crystal structure of PepV in complex with the phosphinic inhibitor...

Crystal structure of the dinuclear zinc aminopeptidase PepV from Lactobacillus delbrueckii unravels its preference for dipeptides (2002)

Jozic, D., Bourenkow, G., Bartunik, H., Scholze, H., Dive, V., Henrich, B., ...

PepV from Lactobacillus delbrueckii, a dinuclear zinc peptidase, has been characterized as an unspecific amino dipeptidase. The crystal structure of PepV in complex with the phosphinic inhibitor...

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....

Role of endopeptidase 3.4.24.16 in the catabolism of neurotensin, in vivo, in the vascularly perfused dog ileum.

Barelli, H., Fox-Threlkeld, J. E., Dive, V., Daniel, E. E., Vincent, J. P., Checler, F.

1. The degradation of tritiated and unlabelled neurotensin (NT) following close intra-arterial infusion of the peptides in ileal segments of anaesthetized dogs was examined. 2. Intact NT and its...