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André MATAGNE
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Articles

Three factors that modulate the activity of class D β-lactamases and interfere with the post-translational carboxylation of Lys 70

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Lionel Vercheval, Cédric Bauvois, Alexandre di Paolo, Franck Borel, Jean-Luc Ferrer, Eric Sauvage, André Matagne, Jean-Marie Frère, Paulette Charlier, Moreno Galleni, Frédéric Kerff
Journal: Biochemical Journal
Biochem J (2010) 432 (3): 495–506.
https://doi.org/10.1042/BJ20101122
Published: 25 November 2010
View articletitled, Three factors that modulate the activity of class D β-lactamases and interfere with the post-translational carboxylation of Lys 70
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Includes: Supplementary data
Articles

Guanidinium chloride denaturation of the dimeric Bacillus licheniformis BlaI repressor highlights an independent domain unfolding pathway

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Christelle VREULS, Patrice FILÉE, Hélène VAN MELCKEBEKE, Tony AERTS, Peter DE DEYN, Gabriel LLABRÈS, André MATAGNE, Jean-Pierre SIMORRE, Jean-Marie FRÈRE, Bernard JORIS
Journal: Biochemical Journal
Biochem J (2004) 384 (1): 179–190.
https://doi.org/10.1042/BJ20040658
Published: 09 November 2004
View articletitled, Guanidinium chloride denaturation of the dimeric Bacillus licheniformis BlaI repressor highlights an independent domain unfolding pathway
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Articles

Secondary-structure characterization by far-UV CD of highly purified uncoupling protein 1 expressed in yeast

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Pierre DOUETTE, Rachel NAVET, Fabrice BOUILLENNE, Alain BRANS, Claudine SLUSE-GOFFART, André MATAGNE, Francis E. SLUSE
Journal: Biochemical Journal
Biochem J (2004) 380 (1): 139–145.
https://doi.org/10.1042/bj20031957
Published: 15 May 2004
View articletitled, Secondary-structure characterization by far-UV CD of highly purified uncoupling protein 1 expressed in yeast
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Articles

Catalytic properties of class A β-lactamases: efficiency and diversity

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André MATAGNE, Josette LAMOTTE-BRASSEUR, Jean-Marie FRÈRE
Journal: Biochemical Journal
Biochem J (1998) 330 (2): 581–598.
https://doi.org/10.1042/bj3300581
Published: 01 March 1998
View articletitled, Catalytic properties of class A β-lactamases: efficiency and diversity
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