Sin1, a regulatory subunit of TOR protein kinase, has an evolutionarily conserved domain that specifically binds and recruits substrate for phosphorylation, and may represent a potential target for anti-cancer drugs.

The human Origin Replication Complex is shaped as a shallow corkscrew in a classic AAA+ organization reminiscent of clamp loader complexes with highly controlled ATPase activity as exemplified by Meier-Gorlin syndrome mutations.

Zinc metalloproteinase Papp-aa-mediated Igfbp5 proteolysis functions as a [Ca²⁺]-regulated molecular switch linking IGF signaling to epithelial cell proliferation and bone calcification.

A lipid acts to promote the development of nematode worm larvae through activation of an enzyme complex called TORC1.

Metformin extends C. elegans lifespan through lysosome-dependent coordination of TORC1 and AMPK pathways.

A domain called the 'Conserved region in the middle' is responsible for target recognition in the TORC2 complex in fission yeast and the mTORC2 complex in mammals.

A computer model of human cardiomyocyte was produced and validated on independent datasets, overcoming shortcomings of its predecessors, also yielding broadly relevant insights and results on major ionic currents.

Young defense metabolites are often believed to be solely outputs but evidence suggests that they can regulate ancient signaling pathways.

Despite BCAAs being de novo-synthesized in chloroplasts, TOR activation by BCAAs is conserved in plants and triggers a re-organization of actin and actin-associated endomembranes.

Human-based electromechanical simulations reveal electrocardiogram biomarkers are better indicators of pro-arrhythmic substrate after myocardial infarction than ejection fraction.