To investigate why bats are long-lived and cancer-resistant, multi-omic data from bat and human cells was analyzed using computational flux modeling, suggesting dysregulation of succinate-fumarate dynamics and an ischemic-like basal metabolism in bat cells.

Revisiting limitations in time-resolved X-ray free-electron laser structures of the bacterial photosynthetic reaction center uncovers their irrelevance to proposed structural changes in electron transfer dynamics.

Investigations of the reaction center (RC)-light harvesting (LH) complex from an ancient chlorosome-less anoxygenic phototroph Roseiflexus castenholzii reveal the structural basis by which carotenoids assembly regulates the architecture and quinone exchange of bacterial RC-LH complex.

The structure of the photosystem I (PSI) supercomplex in Ostreococcus tauri has revealed a unique hybrid of both plant-type and green algal-type PSI supercomplexes with three Lhcp trimers located at the ‘state 2’ position.

The intracellular network that distributes iron-sulfur clusters in bacteria is surprisingly 'plug and play' with iron-sulfur enzymes acquired from distantly related species, whereas the intracellular electron transfer network often needs plug adapters to connect with foreign enzymes.

Under starvation conditions, anti-carD antisense RNA and Clp protease work together to decrease the CarD level to mediate the adaptation and survival of mycobacterial cells.

The three-dimensional structures of Mycobacterium tuberculosis cytochrome bcc in complex with the antituberculosis agents, Q203 and TB47, explain how these inhibitors suppress activity of the complex.

A CRISPR-based method enables targeted knockouts and genetic screens in human dendritic cells.

In the PomX/Y/Z cell division regulatory system, PomX is a PomZ ATPase activating protein, a scaffold for PomX/Y/Z complex formation, and important for fission of the PomX/Y/Z complex during division.

Bacterial small RNAs derived from the 3' untranslated region of an mRNA can serve as autoregulatory elements.