Franck Duong

The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure.

Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase.

Break on through to the other side--the Sec translocon.

The bacterial protein-translocation complex: SecYEG dimers associate with one or two SecA molecules.

Investigating the SecY plug movement at the SecYEG translocation channel.

Deregulation of the SecYEG translocation channel upon removal of the plug domain.

Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA.

Cell biology: fraternal twins.

Structure and function of the bacterial Sec translocon.

Structure, binding, and activity of Syd, a SecY-interacting protein.

The SecY complex forms a channel capable of ionic discrimination.

Modulation of the SecY channel permeability by pore mutations and trivalent cations.

Reconstitution of the SecY translocon in nanodiscs.

The action of cardiolipin on the bacterial translocon.

The SecY complex: conducting the orchestra of protein translocation.

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.

Structure-activity analysis of niclosamide reveals potential role for cytoplasmic pH in control of mammalian target of rapamycin complex 1 (mTORC1) signaling.

Discovery of an auto-regulation mechanism for the maltose ABC transporter MalFGK2.