Duquesne S - Search Results

1

Microcins, gene-encoded antibacterial peptides from enterobacteria.

Duquesne S, Destoumieux-Garzón D, Peduzzi J, Rebuffat S. Duquesne S, et al. Nat Prod Rep. 2007 Aug;24(4):708-34. doi: 10.1039/b516237h. Epub 2007 Apr 18. Nat Prod Rep. 2007. PMID: 17653356 Review.

2

Two enzymes catalyze the maturation of a lasso peptide in Escherichia coli.

Duquesne S, Destoumieux-Garzón D, Zirah S, Goulard C, Peduzzi J, Rebuffat S. Duquesne S, et al. Chem Biol. 2007 Jul;14(7):793-803. doi: 10.1016/j.chembiol.2007.06.004. Chem Biol. 2007. PMID: 17656316

3

Structural and functional diversity of microcins, gene-encoded antibacterial peptides from enterobacteria.

Duquesne S, Petit V, Peduzzi J, Rebuffat S. Duquesne S, et al. J Mol Microbiol Biotechnol. 2007;13(4):200-9. doi: 10.1159/000104748. J Mol Microbiol Biotechnol. 2007. PMID: 17827970 Review.

4

The iron-siderophore transporter FhuA is the receptor for the antimicrobial peptide microcin J25: role of the microcin Val11-Pro16 beta-hairpin region in the recognition mechanism.

Destoumieux-Garzón D, Duquesne S, Peduzzi J, Goulard C, Desmadril M, Letellier L, Rebuffat S, Boulanger P. Destoumieux-Garzón D, et al. Among authors: duquesne s. Biochem J. 2005 Aug 1;389(Pt 3):869-76. doi: 10.1042/BJ20042107. Biochem J. 2005. PMID: 15862112 Free PMC article.

5

Post-translational modification and folding of a lasso-type gene-encoded antimicrobial peptide require two enzymes only in Escherichia coli.

Duquesne S, Destoumieux-Garzón D, Zirah S, Knappe TA, Goulard C, Peduzzi J, Marahiel MA, Rebuffat S. Duquesne S, et al. Adv Exp Med Biol. 2009;611:35-6. doi: 10.1007/978-0-387-73657-0_15. Adv Exp Med Biol. 2009. PMID: 19400082 No abstract available.

6

Characterization of a novel β-alanine biosynthetic pathway consisting of promiscuous metabolic enzymes.

Perchat N, Dubois C, Mor-Gautier R, Duquesne S, Lechaplais C, Roche D, Fouteau S, Darii E, Perret A. Perchat N, et al. Among authors: duquesne s. J Biol Chem. 2022 Jul;298(7):102067. doi: 10.1016/j.jbc.2022.102067. Epub 2022 May 24. J Biol Chem. 2022. PMID: 35623386 Free PMC article.

7

Yarrowia lipolytica lipase Lip2: an efficient enzyme for the production of concentrates of docosahexaenoic acid ethyl ester.

Casas-Godoy L, Meunchan M, Cot M, Duquesne S, Bordes F, Marty A. Casas-Godoy L, et al. Among authors: duquesne s. J Biotechnol. 2014 Jun 20;180:30-6. doi: 10.1016/j.jbiotec.2014.03.018. Epub 2014 Mar 18. J Biotechnol. 2014. PMID: 24657346

8

Metagenomics for the discovery of pollutant degrading enzymes.

Ufarté L, Laville É, Duquesne S, Potocki-Veronese G. Ufarté L, et al. Among authors: duquesne s. Biotechnol Adv. 2015 Dec;33(8):1845-54. doi: 10.1016/j.biotechadv.2015.10.009. Epub 2015 Oct 23. Biotechnol Adv. 2015. PMID: 26526541 Review.

9

Rationally engineered double substituted variants of Yarrowia lipolytica lipase with enhanced activity coupled with highly inverted enantioselectivity towards 2-bromo phenyl acetic acid esters.

Cambon E, Piamtongkam R, Bordes F, Duquesne S, André I, Marty A. Cambon E, et al. Among authors: duquesne s. Biotechnol Bioeng. 2010 Aug 15;106(6):852-9. doi: 10.1002/bit.22770. Biotechnol Bioeng. 2010. PMID: 20506522

10

Enantioselectivity of Candida rugosa lipases (Lip1, Lip3, and Lip4) towards 2-bromo phenylacetic acid octyl esters controlled by a single amino acid.

Piamtongkam R, Duquesne S, Bordes F, Barbe S, André I, Marty A, Chulalaksananukul W. Piamtongkam R, et al. Among authors: duquesne s. Biotechnol Bioeng. 2011 Aug;108(8):1749-56. doi: 10.1002/bit.23124. Epub 2011 Apr 5. Biotechnol Bioeng. 2011. PMID: 21391204

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