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FEMS Microbiology Letters|February 15, 1995
Overproduction and properties of the mannuronate alginate lyase AlxMBM Malissard, F Chavagnat, C Duez, et al.
European Journal of Biochemistry|July 15, 1996
Recombinant soluble beta-1,4-galactosyltransferases expressed in Saccharomyces cerevisiae. Purification, characterization and comparison with human enzymeM Malissard, L Borsig, S Di Marco, et al.
Glycoconjugate Journal|May 18, 2000
Complete enzymic synthesis of the mucin-type sialyl Lewis x epitope, involved in the interaction between PSGL-1 and P-selectinS Zeng, R G Gallego, A Dinter, et al.
Carbohydrate Research|December 23, 1998
Antibody recognition of epitopes on wild-type and mutant beta-(1-->4)-galactosyltransferase-1J Keusch, G Panayotou, M Malissard, et al.
Bioorganic & Medicinal Chemistry Letters|September 11, 2001
Chemo-enzymatic synthesis of the Galili epitope Gal(alpha)(1-->3)Galbeta(1-->4)GlcNAc on a homogeneously soluble PEG polymer by a multi-enzyme systemN Brinkmann, M Malissard, M Ramuz, et al.
The Journal of Biological Chemistry|March 30, 2001
Exploring the acceptor substrate recognition of the human beta-galactoside alpha 2,6-sialyltransferaseP Legaigneur, C Breton, A El Battari, et al.
FEMS Microbiology Letters|June 1, 1993
Sequence of a gene encoding a (poly ManA) alginate lyase active on Pseudomonas aeruginosa alginateM Malissard, C Duez, M Guinand, et al.
Glycoconjugate Journal|January 5, 2000
UDP-N-Acetyl-alpha-D-glucosamine as acceptor substrate of beta-1,4-galactosyltransferase. Enzymatic synthesis of UDP-N-acetyllactosamineL Elling, A Zervosen, R G Gallego, et al.
Protein Expression and Purification|February 1, 1995
Large-scale production of a soluble human beta-1,4-galactosyltransferase using a Saccharomyces cerevisiae expression systemG F Herrmann, C Krezdorn, M Malissard, et al.
Bioorganic & Medicinal Chemistry|October 13, 2001
Immobilisation on polystyrene of diazirine derivatives of mono- and disaccharides: biological activities of modified surfacesY Chevolot, J Martins, N Milosevic, et al.
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