Frédérique Pompeo

PknB kinase activity is regulated by phosphorylation in two Thr residues and dephosphorylation by PstP, the cognate phospho‐Ser/Thr phosphatase, in <i>Mycobacterium tuberculosis</i>

Brigitte Boitel, M. Ortiz-Lombardı́a, Rosario Durán et al. · Molecular Microbiology · 2003 · 168 citations · Full text

Life Sciences, Biochemistry, Molecular Biology +14

Crystal Structure of the Catalytic Domain of the PknB Serine/Threonine Kinase from Mycobacterium tuberculosis

M. Ortiz-Lombardı́a, Frédérique Pompeo, Brigitte Boitel et al. · Journal of Biological Chemistry · 2003 · 155 citations · Full text

Life Sciences, Biochemistry, Molecular Biology +11

An approach to identifying novel substrates of bacterial arylamine N-acetyltransferases

Edward W. Brooke, Stephen G. Davies, Andrew W. Mulvaney et al. · Bioorganic & Medicinal Chemistry · 2003 · 85 citations

Life Sciences, Biochemistry, Microbiology +4

Phosphorylation of the cell division protein <scp>GpsB</scp> regulates <scp>PrkC</scp> kinase activity through a negative feedback loop in <scp><i>B</i></scp><i>acillus subtilis</i>

Frédérique Pompeo, Elodie Foulquier, Christophe Grangeasse et al. · Molecular Microbiology · 2015 · 84 citations · Full text

Life Sciences, Microbiology, Molecular Biology +13

Probing the Role of Cysteine Residues in Glucosamine-1-Phosphate Acetyltransferase Activity of the Bifunctional GlmU Protein from <i>Escherichia coli</i> : Site-Directed Mutagenesis and Characterization of the Mutant Enzymes

Frédérique Pompeo, Jean van Heijenoort, Dominique Mengin‐Lecreulx · Journal of Bacteriology · 1998 · 74 citations · Full text

Life Sciences, Biochemistry, Microbiology +13