Computational and theoretical models reveal mechanisms by which protein compartments assemble around enzymes and reagents to facilitate reactions in bacteria, allowing the identification of strategies for reengineering such compartments as customizable nanoreactors.
A homopolymer-sphere model is shown to accurately reproduce the interactions that underpin selective gating of macromolecular transport into and out of the cell nucleus.
Simple biophysical considerations explain the collective behavior of molecularly diverse complex protein assemblies that regulate transport between the nucleus and the cytoplasm in eukaryotic organisms.
A new approach measures the respective participations of elementary cell behaviors – such as cell division, intercalation, shape change and death – in the shaping of animal tissues.
Time-lapse recording and theoretical analysis of individual cells isolated from the zebrafish segmentation clock reveal that they behave as self-sustained, autonomous oscillators with distinctive noisy dynamics.
The Munc18-1 protein promotes formation of the t-SNARE complex and the half-zippered SNARE complex, two rate-limiting steps of SNARE assembly, to enhance membrane fusion.
Tension is the activating stimulus of Piezo1 mechanosensitive ion channels and resting membrane tension modulates overall channel sensitivity to mechanical stimulation.
