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Le Goffic Francois
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http://hub.abes.fr/acs/periodical/jmcmar/1986/volume_29/issue_1/101021jm00151a024/authorship/6
http://hub.abes.fr/acs/periodical/jacsat/1989/volume_111/issue_8/101021ja00190a042/authorship/2
http://hub.abes.fr/acs/periodical/jmcmar/1986/volume_29/issue_6/101021jm00156a021/authorship/5
http://hub.abes.fr/acs/periodical/bichaw/1987/volume_26/issue_7/101021bi00381a023/authorship/5
http://hub.abes.fr/acs/periodical/bichaw/1988/volume_27/issue_7/101021bi00407a006/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1990/volume_29/issue_15/101021bi00467a012/authorship/3
http://hub.abes.fr/acs/periodical/jmcmar/1986/volume_29/issue_4/101021jm00154a024/authorship/6
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(.beta.-Chloro-.alpha.-aminoethyl)phosphonic acids as inhibitors of alanine racemase and D-alanine-D-alanine ligase
The lysine pathway as a target for a new genera of synthetic antibacterial antibiotics?
Glucosamine-6-phosphate synthase from Escherichia coli: determination of the mechanism of inactivation by N3-fumaroyl-L-2,3-diaminopropionic derivatives
Glucosamine synthetase from Escherichia coli: purification, properties, and glutamine-utilizing site location
Glucosamine-6-phosphate synthase from Escherichia coli: mechanism of the reaction at the fructose 6-phosphate binding site
(1-Amino-2-propenyl)phosphonic acid, an inhibitor of alanine racemase and D-alanine:D-alanine ligase
Glucosamine synthetase from Escherichia coli: kinetic mechanism and inhibition by N3-fumaroyl-L-2,3-diaminopropionic derivatives
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