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Experientia|December 15, 1996
The mitochondrial processing peptidase: function and specificityP Luciano, V GéliJournal of Molecular Biology|September 23, 1997
Functional cooperation of the mitochondrial processing peptidase subunitsP Luciano, S Geoffroy, A Brandt, et al.Journal of Molecular Biology|July 9, 1998
The mitochondrial processing peptidase behaves as a zinc-metallopeptidaseP Luciano, K Tokatlidis, I Chambre, et al.Proceedings of the National Academy of Sciences of the United States of America|July 1, 1993
Functional reconstitution in Escherichia coli of the yeast mitochondrial matrix peptidase from its two inactive subunitsV GéliMolecular Microbiology|September 1, 1994
Immunity proteins to pore-forming colicins: structure-function relationshipsD Espesset, P Piet, C Lazdunski, et al.Journal of Molecular Biology|February 2, 1999
Integration of the colicin A pore-forming domain into the cytoplasmic membrane of Escherichia coliD Duché, Y Corda, V Géli, et al.The EMBO Journal|May 15, 1996
The channel domain of colicin A is inhibited by its immunity protein through direct interaction in the Escherichia coli inner membraneD Espesset, D Duché, D Baty, et al.Journal of Bacteriology|September 1, 1995
Quantification of group A colicin import sitesD Duché, L Letellier, V Géli, et al.Biochemistry|November 17, 1992
Acidic interaction of the colicin A pore-forming domain with model membranes of Escherichia coli lipids results in a large perturbation of acyl chain order and stabilization of the bilayerV Géli, M C Koorengevel, R A Demel, et al.Gene|February 17, 2001
The AprX protein of Pseudomonas aeruginosa: a new substrate for the Apr type I secretion systemF Duong, E Bonnet, V Géli, et al.Pageof 6