ER-stress sensing mechanism of the unfolded protein response sensor/transducer IRE1 is conserved from yeast to mammals, where in mammals, unfolded protein binding to IRE1's ER lumenal domain is coupled to its oligomerization and activation through an allosteric conformational change.

NMR spectroscopy has been used to explain a central unresolved issue of nuclear transport, namely how it can be both fast and specific.

Structural and biochemical analysis reveals that two intrinsically disordered domains of the transcription factor FoxM1 co-fold to form an autoinhibited conformation, which is disrupted by a specific activating phosphorylation event.

Nuclear magnetic resonance analysis revealed the structural and dynamical changes in MgtE during the channel closure caused by the cooperative Mg²⁺-binding, which had remained undescribed only by a static crystal structure.

¹H-Magnetic resonance spectroscopy at 14T reveals a metabolic signature for anti-depressant-like effects of acetyl-L-carnitine in nucleus accumbens of susceptible mouse.

Molecular simulations can capture key aspects of the conformational exchange in a protein.

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

Low-field single-sided magnetic resonance diffusion methods detect and measure permeability of sub-micron compartments which likely include cell processes, organelles, and cellular vesicles within ex vivo mouse spinal cords.

The brain stores information that is needed immediately and information that will be needed in the future in different ways.

Understanding the structure of an antigen can guide the design of improved antigen-based vaccines.