Mutations along the signaling pathway of the E. coli sensor histidine kinase PhoQ alter signal gain and ligand-sensitivity by altering thermodynamic allosteric coupling between domains.

The molecular mechanism of switching between phosphotransferase- and phosphatase-competent states in histidine-kinases has been uncovered, through direct crystallographic observation of bona fide complexes between a histidine-kinase and its response regulator from Bacillus subtilise.

An atomic model of the bacterial chemosensory array obtained through the synthesis of cryo-electron tomography and large-scale molecular-dynamics simulations reveals a new kinase conformation during signaling events.

Co-evolving residue pairs in the different components of a protein complex almost always make contact across the protein–protein interface, thus providing powerful restraints for the modeling of protein complexes.

The ISR kinase GCN2 is critical for maintaining tumor amino acid levels to facilitate growth, suggesting a novel therapeutic strategy for the treatment of prostate cancer by inducing starvation for essential amino acids.

The circadian clock of Synechococcus elongatus PCC7942 schedules the activity of the transcription factor RpaA, which controls key events in carbon metabolism that contribute to cell fitness in conditions mimicking the natural environment.

Interactions in protein complexes can be predicted from evolutionary information from genomic sequences.

The Ras activator RasGRP1 that impacts Ras signals in immune cells, leukemias, and colorectal cancer, switches to an active conformation aided by a pH-sensitive histidine residue in a central location of the RasGRP1 molecule.

The V600E mutation in BRAF is a cancer hot spot because it opens the activation segment through destabilization of autoinhibitory interactions, but it does not significantly impair folding of the inactive or active kinase domain.

The mammalian potassium channel KCa3.1, which is important for T- and B-cell activation, is inhibited by cytoplasmic copper, mediated by a histidine residue (His358) that is phosphorylated to activate the channel.