The MIDAS domain of Mdn1, an ATP-driven mechanoenzyme involved in ribosome biogenesis, forms catch bonds with two different ubiquitin-like domain-containing ribosomal assembly factors.

A molecular mechanism for force-dependent binding of the cell adhesion proteins αE-catenin and vinculin to actin is derived from the structure of the αE-catenin actin-binding domain bound to F-actin.

Deleting the first helix of the α-catenin actin-binding domain results in a slip bond interaction between the cadherin–catenin complex and F-actin, such that the binding interaction is stable at low force.

All-atom molecular dynamics simulations of an αβ T-cell receptor complexed with the major histocompatibility complex molecule presenting wild-type or mutant antigenic peptides reveal how it uses conserved framework motion to discriminate antigens by leveraging physiological force applied during immune surveillance.

Directed mechanical stresses can trigger active T1 events that lead to tissue elongation perpendicular to the main direction of tissue stress.

The entry glycoproteins of hepatitis C virus, E1E2, possess a novel regulatory mechanism in which protein disorder is harnessed to control their activity and their ability to evade antibodies.

Computer simulations considering actions of the intranuclear enzyme, Topoisomerase-II, in a mechanistic scheme elucidated a capability of enzymes to contribute to controlling chromatin spatial organizations and discovered new characteristic features in eu- and heterochromatin organization caused by the enzymatic activity.

The spatial organization of pathogenic bacteria into microcolonies can be shaped by the stiffness of the substrate that they colonize, via modifications of the bacterial motility.

Atomic force microscopy based single-molecule force spectroscopy of smooth muscle myosin light chain kinase strongly indicates the existence of a mechanically triggerable activation pathway analogous to its well-established biochemical regulation pathway via calcium-loaded calmodulin.

Biophysical and structural studies reveal how low piconewton forces across actin enhance binding by the critical cell-cell adhesion protein α-catenin versus its force insensitive homolog vinculin.