Structure-based design of small molecule inhibitors of the cagT4SS ATPase Cagα of .

We here describe the structure-based design of small molecule inhibitors of the type IV secretion system of . The secretion system is encoded by the  pathogenicity island, and we chose Cagα, a hexameric ATPase and member of the family of VirB11-like proteins, as target for inhibitor design. We first solved the crystal structure of Cagα in a complex with the previously identified small molecule inhibitor 1G2.

Reproducibility of inverse gas chromatography under infinite dilution: Results and interpretations of an interlaboratory study.

Over the last years, inverse gas chromatography (IGC) proved to be a versatile and sensitive analytical technique for physicochemical properties. However, the comparability of results obtained by different users and devices remains a topic for debate. This is the first time, an interlaboratory study using different types of IGC instruments is reported.

A "Drug Sweeping" State of the TriABC Triclosan Efflux Pump from Pseudomonas aeruginosa.

The structure of the TriABC inner membrane component of the triclosan/SDS-specific efflux pump from Pseudomonas aeruginosa was determined by cryoelectron microscopy to 4.5 Å resolution. The complete structure of the inner membrane transporter TriC of the resistance-nodulation-division (RND) superfamily was solved, including a partial structure of the fused periplasmic membrane fusion subunits, TriA and TriB.

Multiscale Tomographic Analysis for Micron-Sized Particulate Samples.

The three-dimensional characterization of distributed particle properties in the micro- and nanometer range is essential to describe and understand highly specific separation processes in terms of selectivity and yield. Both performance measures play a decisive role in the development and improvement of modern functional materials. In this study, we mixed spherical glass particles (0.

Targeting a moonlighting function of aldolase induces apoptosis in cancer cells.

Muscle fructose-1,6-bisphosphate aldolase (ALDOA) is among the most abundant glycolytic enzymes in all cancer cells. Here, we show that the enzyme plays a previously unknown and critical role in a cancer cell survival. Simultaneous inhibition of ALDOA activity and interaction with F-actin cytoskeleton using ALDOA slow-binding inhibitor UM0112176 leads to a rapid cofilin-dependent loss of F-actin stress fibers which is associated with elevated ROS production, inhibition of ATP synthesis, increase in calcium levels, caspase activation and arrested cellular proliferation.