Melissa G. Chambers

TL;DR: The mitochondrial adenosine triphosphate (ATP) synthase is the enzyme responsible for the synthesis of more than 90% of the ATP produced by mammalian cells under aerobic conditions and the chemiosmotic mechanism, proposed by Peter Mitchell, states that the enzyme transduces the energy of a proton gradient into the major energy currency of the cell, ATP.

TL;DR: The results suggest that Hrd1 forms a retro-translocation channel for the movement of misfolded polypeptides through the endoplasmic reticulum membrane.

TL;DR: A second structure, obtained at the acidic pH of an endosome, reveals a significant structural change in the delivery and glucosyltransferase domains, and thus provides a framework for understanding the molecular mechanism of LCT cellular intoxication.

TL;DR: Cryo-electron microscopy structures of synaptic RAG complexes at up to 3.4 Å resolution reveal a closed conformation with base flipping and base-specific recognition of RSSs, and uncovers the two-metal-ion catalytic mechanism.

TL;DR: X-ray and cryo-electron microscopy structures of fungal mitochondrial calcium uniporter proteins reveal a tetrameric architecture and shed light on the function of the channel, providing insights into calcium coordination, selectivity and conduction.