An unbiased mutational screen decodes the molecular basis of phage receptor interactions, identifies key functional regions determining activity and host range, and demonstrates the potential for engineering therapeutic phages.

Effective antiestrogens engage a new structural interaction to improve therapeutic antagonism in hormone-resistant breast cancer cells expressing Y537S estrogen receptor alpha.

The recruitment of SH2-containing proteins to Epidermal Growth Factor in cells happens more slowly than predicted by in vitro techniques.

Anti-inflammatory effects of resveratrol are mediated by the estrogen receptor to coordinate a complex array of transcriptional coregulators, suggesting that estrogenic effects must be considered in the complex polypharmacology of resveratrol.

Computer simulations explore the experimentally unknown S-protein structures, revealing novel drug binding sites.

Synthetic PPARγ ligands push and cobind with natural endogenous ligands, instead of compete and displace, which synergistically affects the structure and function of PPARγ.

Structures of the death domain of the p75 neurotrophin receptor in complex with downstream effectors show how competitive protein-protein interactions orchestrate the hierarchical activation of downstream pathways in non-catalytic receptors.

Comparative structural studies reveal how the cytoplasmic tails of Eph receptors can differentiate different downstream target proteins via highly specific SAM–SAM domain interactions.

Conformational changes occur within extracellular domain of BCR upon antigen engagement, and these conformational changes are related with the strength of BCR activation and are distinct in IgM- and IgG-BCR.

L-amino acids are agonists of calcium-sensing receptor, and act jointly with calcium and phosphate ions to control receptor function.