Frederic Berthiaume

Molecular composition of staufen2-containing ribonucleoproteins in embryonic rat brain.

Conformation change in a self-recognizing autotransporter modulates bacterial cell-cell interaction.

Influence of environmental cues on transcriptional regulation of foo and clp coding for F165(1) and CS31A adhesins in Escherichia coli.

Influence of L-leucine and L-alanine on Lrp regulation of foo, coding for F1651, a Pap homologue.

Waterborne pathogen detection by use of oligonucleotide-based microarrays.

The periplasmic folding of a cysteineless autotransporter passenger domain interferes with its outer membrane translocation.

Proteolytic processing is not essential for multiple functions of the Escherichia coli autotransporter adhesin involved in diffuse adherence (AIDA-I).

Contribution of AIDA-I to the pathogenicity of a porcine diarrheagenic Escherichia coli and to intestinal colonization through biofilm formation in pigs.

Mutations affecting the biogenesis of the AIDA-I autotransporter.

O-linked glycosylation ensures the normal conformation of the autotransporter adhesin involved in diffuse adherence.

Escherichia coli STb toxin binding to sulfatide and its inhibition by carragenan.

Growth-phase-dependent expression of the operon coding for the glycosylated autotransporter adhesin AIDA-I of pathogenic Escherichia coli.

A structural motif is the recognition site for a new family of bacterial protein O-glycosyltransferases.