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.
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.
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.
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.