Empirical energy landscape allows simulating the structural dynamics of the proteasomal ATPase complex, which yields predictions that are widely consistent with experimental observations and reveals the functional mechanism of the proteasome in substrate degradation.

Lactate is preferred to glucose as an energy substrate and exacerbates spiking activity in most neuron types of juvenile somatosensory cortex by closing ATP-sensitive potassium channels.

Mathematical analyses explore the impact of co-substrate cycling on the dynamics of cellular metabolism, and demonstrate that these dynamics can limit cellular fluxes and that co-substrate pool dynamics can be regulated to regulate fluxes.

A multiscale modeling approach reveals how the energy from ATP hydrolysis is used by Hsp70 chaperones to remodel the conformation of their substrates through a novel force-generating mechanism.

Mechanical instabilities are shown to underlie the development of bacterial biofilm morphology, suggesting an ancient origin for mechano-morphogenesis, which is known to drive developmental processes in tissues in higher organisms.

Theoretical study shows how enzymes can achieve substrate proofreading by taking advantage of existing molecular gradients in the cell while not being endowed with structural features typically required for proofreading.

SGLT2 inhibitors reduce podocyte lipotoxicity and improve kidney function in experimental Alport syndrome through a mechanism that involves a switch from the utilization of glucose to fatty acids as an energy substrate in podocytes.

ATP consumption enables chaperones to exploit the different kinetic properties of their conformational states to exhibit a non-equilibrium affinity for their substrates that is orders of magnitude higher than its equilibrium value.

Biophysical experiments, pulse-chase assays, and molecular dynamics simulations reveal how the proteasome targeting signal Fat10 can modulate the structure of substrate proteins to potentially regulate their degradation by the proteasome.

The DNA flanks on either side of an R-loop differ in stability, and CRISPR-Cas12 enzymes form double-strand breaks by targeting the more unstable flank with their single DNase active site.