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R Ménard

Showing results (11-20 of 69) with videos related to

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Methods in Enzymology|January 1, 1994
Catalytic mechanism in papain family of cysteine peptidasesA C Storer, R Ménard
FEBS Letters|September 17, 1998
Human cathepsin X: a novel cysteine protease of the papain family with a very short proregion and unique insertionsD K Nägler, R Ménard
Methods in Enzymology|January 1, 1994
Shigella flexneri: isolation of noninvasive mutants of gram-negative pathogensR Ménard, P J Sansonetti
Biophysical Chemistry|August 1, 1984
Interaction of (dien)Pd(II) with cytidine and cytidine 5'-monophosphate. Influence of the phosphate group on the kinetics and mechanismR Ménard, M Lachapelle, M Zador
The EMBO Journal|November 15, 1994
The secretion of the Shigella flexneri Ipa invasins is activated by epithelial cells and controlled by IpaB and IpaDR Ménard, P Sansonetti, C Parsot
Biochemical and Biophysical Research Communications|April 13, 1999
Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogenD K Nägler, T Sulea, R Ménard
Biochemistry|December 19, 1995
Engineering nitrile hydratase activity into a cysteine protease by a single mutationE Dufour, A C Storer, R Ménard
Biochemistry|July 18, 1995
Peptide aldehydes and nitriles as transition state analog inhibitors of cysteine proteasesE Dufour, A C Storer, R Ménard
Trends in Microbiology|June 1, 1996
Bacterial entry into epithelial cells: the paradigm of ShigellaR Ménard, C Dehio, P J Sansonetti
Journal of Bacteriology|September 1, 1993
Nonpolar mutagenesis of the ipa genes defines IpaB, IpaC, and IpaD as effectors of Shigella flexneri entry into epithelial cellsR Ménard, P J Sansonetti, C Parsot
Pageof 7

Showing results (11-20 of 69) with videos related to

Sort By:
Pageof 7
Methods in Enzymology|January 1, 1994
Catalytic mechanism in papain family of cysteine peptidasesA C Storer, R Ménard
FEBS Letters|September 17, 1998
Human cathepsin X: a novel cysteine protease of the papain family with a very short proregion and unique insertionsD K Nägler, R Ménard
Methods in Enzymology|January 1, 1994
Shigella flexneri: isolation of noninvasive mutants of gram-negative pathogensR Ménard, P J Sansonetti
Biophysical Chemistry|August 1, 1984
Interaction of (dien)Pd(II) with cytidine and cytidine 5'-monophosphate. Influence of the phosphate group on the kinetics and mechanismR Ménard, M Lachapelle, M Zador
The EMBO Journal|November 15, 1994
The secretion of the Shigella flexneri Ipa invasins is activated by epithelial cells and controlled by IpaB and IpaDR Ménard, P Sansonetti, C Parsot
Biochemical and Biophysical Research Communications|April 13, 1999
Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogenD K Nägler, T Sulea, R Ménard
Biochemistry|December 19, 1995
Engineering nitrile hydratase activity into a cysteine protease by a single mutationE Dufour, A C Storer, R Ménard
Biochemistry|July 18, 1995
Peptide aldehydes and nitriles as transition state analog inhibitors of cysteine proteasesE Dufour, A C Storer, R Ménard
Trends in Microbiology|June 1, 1996
Bacterial entry into epithelial cells: the paradigm of ShigellaR Ménard, C Dehio, P J Sansonetti
Journal of Bacteriology|September 1, 1993
Nonpolar mutagenesis of the ipa genes defines IpaB, IpaC, and IpaD as effectors of Shigella flexneri entry into epithelial cellsR Ménard, P J Sansonetti, C Parsot
Pageof 7