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Protein N-terminal methionine excision.
Giglione C, Boularot A, Meinnel T. Giglione C, et al. Among authors: meinnel t. Cell Mol Life Sci. 2004 Jun;61(12):1455-74. doi: 10.1007/s00018-004-3466-8. Cell Mol Life Sci. 2004. PMID: 15197470 Review.
Mapping of the active site zinc ligands of peptide deformylase.
Meinnel T, Lazennec C, Blanquet S. Meinnel T, et al. J Mol Biol. 1995 Nov 24;254(2):175-83. doi: 10.1006/jmbi.1995.0609. J Mol Biol. 1995. PMID: 7490741
Mapping of the zinc binding domain of Escherichia coli methionyl-tRNA synthetase.
Fourmy D, Meinnel T, Mechulam Y, Blanquet S. Fourmy D, et al. Among authors: meinnel t. J Mol Biol. 1993 Jun 20;231(4):1068-77. doi: 10.1006/jmbi.1993.1352. J Mol Biol. 1993. PMID: 8515465
The C-terminal domain of peptide deformylase is disordered and dispensable for activity.
Meinnel T, Lazennec C, Dardel F, Schmitter JM, Blanquet S. Meinnel T, et al. FEBS Lett. 1996 Apr 29;385(1-2):91-5. doi: 10.1016/0014-5793(96)00357-2. FEBS Lett. 1996. PMID: 8641475
A new subclass of the zinc metalloproteases superfamily revealed by the solution structure of peptide deformylase.
Meinnel T, Blanquet S, Dardel F. Meinnel T, et al. J Mol Biol. 1996 Sep 27;262(3):375-86. doi: 10.1006/jmbi.1996.0521. J Mol Biol. 1996. PMID: 8845003
Formate dehydrogenase-coupled spectrophotometric assay of peptide deformylase.
Lazennec C, Meinnel T. Lazennec C, et al. Among authors: meinnel t. Anal Biochem. 1997 Jan 1;244(1):180-2. doi: 10.1006/abio.1996.9910. Anal Biochem. 1997. PMID: 9025929 No abstract available.
Structure-function relationships within the peptide deformylase family. Evidence for a conserved architecture of the active site involving three conserved motifs and a metal ion.
Meinnel T, Lazennec C, Villoing S, Blanquet S. Meinnel T, et al. J Mol Biol. 1997 Apr 4;267(3):749-61. doi: 10.1006/jmbi.1997.0904. J Mol Biol. 1997. PMID: 9126850
Solution structure of nickel-peptide deformylase.
Dardel F, Ragusa S, Lazennec C, Blanquet S, Meinnel T. Dardel F, et al. Among authors: meinnel t. J Mol Biol. 1998 Jul 17;280(3):501-13. doi: 10.1006/jmbi.1998.1882. J Mol Biol. 1998. PMID: 9665852
Control of peptide deformylase activity by metal cations.
Ragusa S, Blanquet S, Meinnel T. Ragusa S, et al. Among authors: meinnel t. J Mol Biol. 1998 Jul 17;280(3):515-23. doi: 10.1006/jmbi.1998.1883. J Mol Biol. 1998. PMID: 9665853
Using the model substrate N-formyl-Met-Ala-Ser, kcat/Km values of 5.4, 1.2 and 25 10(4)M-1s-1 could be obtained for the E. coli, T. thermophilus and B. stearothermophilus enzymes, respectively. ...
Using the model substrate N-formyl-Met-Ala-Ser, kcat/Km values of 5.4, 1.2 and 25 10(4)M-1s-1 could be obtained for the E. coli, T. t …
Substrate recognition and selectivity of peptide deformylase. Similarities and differences with metzincins and thermolysin.
Ragusa S, Mouchet P, Lazennec C, Dive V, Meinnel T. Ragusa S, et al. Among authors: meinnel t. J Mol Biol. 1999 Jun 25;289(5):1445-57. doi: 10.1006/jmbi.1999.2832. J Mol Biol. 1999. PMID: 10373378
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