Wei-Chieh Cheng

TL;DR: It is proposed that NN-DNJ chaperones β-Glu folding at neutral pH allows the stabilized enzyme to transit from the endoplasmic reticulum to the Golgi, enabling proper trafficking to the lysosome.

TL;DR: Chemical modulation reveals differences in S1P-S1P1 'set points' among tissues and highlights both mechanistic advantages (lymphocyte sequestration) and risks (pulmonary edema) of therapeutic intervention.

TL;DR: It is demonstrated that G202R, a glucocerebrosidase variant that is known to be retained in the endoplasmic reticulum, is also amenable to chemical chaperoning, and the L444P variant is not chaperoned by any of the active site-directed molecules tested, likely because this mutation destabilizes a domain distinct from the catalytic domain.

TL;DR: The X-ray crystal structure of the bifunctional transglycosylase penicillin-binding protein 1b from Escherichia coli in complex with its inhibitor moenomycin is determined to 2.16-Å resolution and reveals a domain for protein–protein interaction and a transmembrane helix domain essential for substrate binding, enzymatic activity, and membrane orientation.

TL;DR: In this paper, the authors used a cell-based infection assay to screen more than 3,000 agents used in humans and animals, including 2,855 small molecules and 190 traditional herbal medicines, and identified 15 active small molecules in concentrations ranging from 0.1 nM to 50 μM.