Dardel F - Search Results

1

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. Among authors: dardel f. FEBS Lett. 1996 Apr 29;385(1-2):91-5. doi: 10.1016/0014-5793(96)00357-2. FEBS Lett. 1996. PMID: 8641475 Free article.

2

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. Among authors: dardel f. J Mol Biol. 1996 Sep 27;262(3):375-86. doi: 10.1006/jmbi.1996.0521. J Mol Biol. 1996. PMID: 8845003

3

Solution structure of nickel-peptide deformylase.

Dardel F, Ragusa S, Lazennec C, Blanquet S, Meinnel T. Dardel F, et al. J Mol Biol. 1998 Jul 17;280(3):501-13. doi: 10.1006/jmbi.1998.1882. J Mol Biol. 1998. PMID: 9665852

4

1H and 15N resonance assignments and structure of the N-terminal domain of Escherichia coli initiation factor 3.

Garcia C, Fortier PL, Blanquet S, Lallemand JY, Dardel F. Garcia C, et al. Among authors: dardel f. Eur J Biochem. 1995 Mar 1;228(2):395-402. Eur J Biochem. 1995. PMID: 7705354 Free article.

5

Heteronuclear NMR studies of the interactions of 15N-labeled methionine-specific transfer RNAs with methionyl-tRNA transformylase.

Wallis NG, Dardel F, Blanquet S. Wallis NG, et al. Among authors: dardel f. Biochemistry. 1995 Jun 13;34(23):7668-77. doi: 10.1021/bi00023a013. Biochemistry. 1995. PMID: 7779813

6

The N-terminal half of initiation factor IF3 is folded as a stable independent domain.

Fortier PL, Schmitter JM, Garcia C, Dardel F. Fortier PL, et al. Among authors: dardel f. Biochimie. 1994;76(5):376-83. doi: 10.1016/0300-9084(94)90111-2. Biochimie. 1994. PMID: 7849101

7

Methionyl-tRNA synthetase zinc binding domain. Three-dimensional structure and homology with rubredoxin and gag retroviral proteins.

Fourmy D, Dardel F, Blanquet S. Fourmy D, et al. Among authors: dardel f. J Mol Biol. 1993 Jun 20;231(4):1078-89. doi: 10.1006/jmbi.1993.1353. J Mol Biol. 1993. PMID: 8515466

8

Molecular recognition governing the initiation of translation in Escherichia coli. A review.

Schmitt E, Guillon JM, Meinnel T, Mechulam Y, Dardel F, Blanquet S. Schmitt E, et al. Among authors: dardel f. Biochimie. 1996;78(7):543-54. doi: 10.1016/s0300-9084(96)80001-0. Biochimie. 1996. PMID: 8955898 Review.

9

Lysine 335, part of the KMSKS signature sequence, plays a crucial role in the amino acid activation catalysed by the methionyl-tRNA synthetase from Escherichia coli.

Mechulam Y, Dardel F, Le Corre D, Blanquet S, Fayat G. Mechulam Y, et al. Among authors: dardel f. J Mol Biol. 1991 Feb 5;217(3):465-75. doi: 10.1016/0022-2836(91)90750-z. J Mol Biol. 1991. PMID: 1847216

10

Methionyl-tRNA synthetase from E. coli--a review.

Meinnel T, Mechulam Y, Dardel F, Schmitter JM, Hountondji C, Brunie S, Dessen P, Fayat G, Blanquet S. Meinnel T, et al. Among authors: dardel f. Biochimie. 1990 Aug;72(8):625-32. doi: 10.1016/0300-9084(90)90126-2. Biochimie. 1990. PMID: 2126467

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