Showing results (1-10 of 211) with videos related to
Sort By:
Pageof 22
Journal of Molecular Biology|July 17, 1998
Solution structure of nickel-peptide deformylaseF Dardel, S Ragusa, C Lazennec, et al.FEBS Letters|April 29, 1996
The C-terminal domain of peptide deformylase is disordered and dispensable for activityT Meinnel, C Lazennec, F Dardel, et al.Journal of Molecular Biology|September 27, 1996
A new subclass of the zinc metalloproteases superfamily revealed by the solution structure of peptide deformylaseT Meinnel, S Blanquet, F DardelJournal of Molecular Biology|November 24, 1995
Mapping of the active site zinc ligands of peptide deformylaseT Meinnel, C Lazennec, S BlanquetJournal of Molecular Biology|July 17, 1998
Control of peptide deformylase activity by metal cationsS Ragusa, S Blanquet, T MeinnelJournal of Molecular Biology|April 4, 1997
Structure-function relationships within the peptide deformylase family. Evidence for a conserved architecture of the active site involving three conserved motifs and a metal ionT Meinnel, C Lazennec, S Villoing, et al.Biochemistry|April 9, 1999
Design and synthesis of substrate analogue inhibitors of peptide deformylaseT Meinnel, L Patiny, S Ragusa, et al.Journal of Molecular Biology|January 5, 1993
Critical role of the acceptor stem of tRNAs(Met) in their aminoacylation by Escherichia coli methionyl-tRNA synthetaseT Meinnel, Y Mechulam, C Lazennec, et al.Nucleic Acids Research|August 25, 1993
Role of the 1-72 base pair in tRNAs for the activity of Escherichia coli peptidyl-tRNA hydrolaseS Dutka, T Meinnel, C Lazennec, et al.Journal of Molecular Biology|June 22, 1999
Substrate recognition and selectivity of peptide deformylase. Similarities and differences with metzincins and thermolysinS Ragusa, P Mouchet, C Lazennec, et al.Pageof 22