Biochemistry: Cells enforce an ion curtain. by Berks, B

The twin-arginine translocation (Tat) protein export pathway by Palmer, T, Berks, B

Intermediates in the Sox sulfur oxidation pathway are bound to a sulfane conjugate of the carrier protein SoxYZ by Grabarczyk, D, Berks, B

Analysis of Tat targeting function and twin-arginine signal peptide activity in Escherichia coli. by Palmer, T, Berks, B, Sargent, F

The DNA transporter ComEC has metal-dependent nuclease activity that is important for natural transformation by Silale, A, Lea, S, Berks, B

Type 9 secretion system structures reveal a new protein transport mechanism by Lauber, F, Deme, J, Lea, S, Berks, B

In vivo experiments do not support the charge zipper model for Tat translocase assembly by Alcock, F, Damen, M, Levring, J, Berks, B

Thiosulfate reduction in Salmonella enterica is driven by the proton motive force. by Stoffels, L, Krehenbrink, M, Berks, B, Unden, G

Processing by rhomboid protease is required for Providencia stuartii TatA to interact with TatC and to form functional homo-oligomeric complexes by Fritsch, M, Krehenbrink, M, Tarry, M, Berks, B, Palmer, T

Genetic evidence for a TatC dimer at the core of the Escherichia coli twin arginine (Tat) protein translocase. by Maldonado, B, Buchanan, G, Müller, M, Berks, B, Palmer, T

Precursor-receptor interactions in the twin arginine protein transport pathway probed with a new receptor complex preparation by Wojnowska, M, Gault, J, Yong, S, Robinson, C, Berks, B

Aberrant topologies of bacterial membrane proteins revealed by high sensitivity fluorescence labelling by Hickman, SJ, Miller, H, Bukys, A, Kapanidis, A, Berks, B

Crystal structure of the Bacillus subtilis phosphodiesterase PhoD reveals an iron and calcium-containing active site. by Rodriguez, F, Lillington, J, Johnson, S, Timmel, C, Lea, S, Berks, B

Single-molecule fluorescence microscopy of the twin-arginine translocation (Tat) system by Leake, M, Greene, N, Godun, R, Palmer, T, Berry, R, Berks, B

Reversible assembly of twin-arginine protein translocation sites by Baker, M, Alcock, F, Greene, N, Palmer, T, Wallace, M, Berks, B

Live cell imaging shows reversible assembly of the TatA component of the twin-arginine protein transport system. by Alcock, F, Baker, M, Greene, N, Palmer, T, Wallace, M, Berks, B

Core components of bacterial protein secretion systems revealed at high resolution by cryo-electron microscopy by Deme, J, Kuhlen, L, Abrusci, P, Johnson, S, Lauber, F, Berks, B, Lea, S

A covalent mechanism at an unusual reactive thiolate-ligated heme by Grabarczyk, D, Chappell, P, McPherson, I, Vincent, K, Lea, S, Berks, B

TatBC, TatB, and TatC form structurally autonomous units within the twin arginine protein transport system of Escherichia coli. by Orriss, G, Tarry, M, Ize, B, Sargent, F, Lea, S, Palmer, T, Berks, B

Characterisation of the membrane-extrinsic domain of the TatB component of the twin arginine protein translocase. by Maldonado, B, Kneuper, H, Buchanan, G, Hatzixanthis, K, Sargent, F, Berks, B, Palmer, T