Breast cancer resistant to either doxorubicin or epirubicin relies on distinct primary metabolic processes, which can be targeted to reduce cancer progression.

The accumulation of its product, cytidine triphosphate, encourages the enzyme CTP synthetase (CtpS) to form large-scale polymers and inhibits the enzyme's activity.

MgADP binding to the high-affinity 'consensus' ATPase active site of SUR1 and remodeling of the L0-loop (lasso region) overrides tonic ATP inhibition of KATP channels.

A structural and biochemical approach shows that CTP binding and hydrolysis regulate nucleation, spreading, and recycling of a chromosome segregation protein ParB.

Bacteria release ATP as part of their attack in sepsis.

Biochemical analysis on hetero-mutated c₁₀ subunits ring and molecular dynamics simulations demonstrate the cooperation among c-subunits of F_oF₁-ATP synthase in rotation-coupled proton translocation.

A molecular model that provides a framework for interpreting the wealth of functional information obtained on the E. coli F-ATP synthase has been generated using cryo-electron microscopy.

The equilibrium between solubility and aggregation of proteins in the nucleus is controlled by co-aggregates like RNA and the action of ATP as both an energy source and a destabilizing chemical agent.

Structural analysis of the ATP synthase – in combination with evolutionary covariance analysis – reveals the fold of the a subunit and shows that the enzyme can adopt several different conformations, which support the Brownian ratchet model for generating rotation.

The first structural and biochemical study of the role of the ATP-cone in anaerobic ribonucleotide reductases shows that dATP allosterically prevents transfer of a glycyl radical to the substrate.