Tuning the strength of inter- and intra-subunit hydrogen bonds can control potassium flux across biological membranes.

Fluorescent sensors can track the movement and distribution of the plant hormone abscisic acid in roots and leaves in Arabidopsis.

Smurf1 and Smurf2 have essential functions in the mammalian Shh signaling pathway, binding to and ubiquitylating Patched1, leading to its endocytosis and subsequent degradation in lysosomes.

The dynein light intermediate chain is a member of the G protein superfamily and links the motor to several intracellular cargo adaptors.

A drug-like molecule called ISRIB, which activates the translation initiation factor eIF2B, antagonizes stress responses as diverse as protein misfolding and nutrient deprivation, and restores protein synthesis, enhancing memory.

An inorganic tin oxochloride cluster specifically binds to an intrinsically disordered, histidine-rich, low complexity protein region and arrests de novo transcription initiation without affecting reinitiation.

Interdomain linker-mediated oligomerization of the endoplasmic reticulum chaperone protein BiP responds to the unfolded protein burden

Plasticity arising from autocatalytic receptor activation coexists with robustness in ligand responsiveness only by differential endosomal sorting of spontaneous and ligand-activated EGFR as distinct molecular states.

The I_Ks potassium channel complex displays functional flexibility that depends on the ratio of its constituent KCNQ1 and KCNE1 protein subunits.

Molecular engineering can generate light-sensitive NMDA receptors with specific subunit combinations.