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.

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.

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

A simulation study is used to demonstrate how mistakes in identifying the experimental unit and the unit of analysis can lead to incorrect analyses and inappropriate inferences when reporting research studies.

A region of the brain called the putamen has a central role in our ability to keep a beat in our head.

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