Catherine S. Chan

Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli.

The TatA subunit of Escherichia coli twin-arginine translocase has an N-in topology.

Investigating protein-protein interactions by far-Westerns.

Identification of residues in DmsD for twin-arginine leader peptide binding, defined through random and bioinformatics-directed mutagenesis.

Copper and quaternary ammonium cations exert synergistic bactericidal and antibiofilm activity against Pseudomonas aeruginosa.

Differential Interactions between Tat-specific redox enzyme peptides and their chaperones.

Chromosomal antioxidant genes have metal ion-specific roles as determinants of bacterial metal tolerance.

Comparing system-specific chaperone interactions with their Tat dependent redox enzyme substrates.

Towards understanding the Tat translocation mechanism through structural and biophysical studies of the amphipathic region of TatA from Escherichia coli.

Nanodiscs and SILAC-Based Mass Spectrometry to Identify a Membrane Protein Interactome.

Two copies of the SecY channel and acidic lipids are necessary to activate the SecA translocation ATPase.