Computer simulations reveal that viral nucleic acids have an ideal structure for being packaged into outer protein shells called capsids.

A robust method to quantitatively visualize HIV-1 replication complexes in infected cells shows that these complexes remain associated with the viral capsid beyond nuclear import in primary macrophages.

Comprehensive analyses of how mutations in a picornavirus capsid affect viral fitness provide novel insights into viral biology, evolution, and host interactions.

Duck Hepatitis B core protein forms capsids with a slowly folding extension domain which folding competence is important for viral replication.

Nucleation, elasticity theory, and simulations were combined to construct a general phase diagram that elucidates the conditions for successful viral assembly and the key factors to prevent it.

To protect mammals against retroviral infections, TRIM5 restriction factors recognize viral capsids by forming complementary hexagonal nets that can adapt to the patterns of capsid protein subunits on the viral capsid surface.

Internal DNA pressure of tens of atmospheres inside a herpesvirus capsid powers ejection of the viral genome into a cell nucleus, causing infection.

Tertiary folding of the Rev-response element (RRE) in HIV RNA ensures the rapid formation of the Rev-RRE viral ribonucleoprotein particle via a two-step process.

Disassembly of the HIV-1 capsid is a catastrophic process, whereby initiation and propagation can be controlled independently by molecules that bind to different features of the capsid lattice.

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.