A pliable hydrophobic interface in the HIV-1 Rev protein enables assembly of diverse oligomeric structures, guided by the RRE scaffold present in HIV-1 mRNAs.

A mathematical model that combines stochasticity and spatial structure describes the dynamics of the viral population during an infection cycle, and fitting the model to RNA and virus abundances over time shows that poliovirus follows a geometric replication mode.

A conserved element in the flavivirus genomic 5′ terminus switches its conformation in response to long-range RNA interactions, and thereby regulates the dynamic recruitment of viral replicase for efficient viral RNA replication.

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.

A structural comparison of different states of the protein responsible for encapsidation of the viral RNA genome provides mechanistic insights into this process.

Mutations within the ATPase domain of RIG-I in patients with Singleton-Merten Syndrome prevent ATP-hydrolysis dependent dissociation of RIG-I from double-stranded RNA and lead to unintentional constitutive signaling through increased binding of endogenous RNA.

Structural and functional studies reveal how Newcastle disease virus nucleocapsid protects its viral genome through a self-capping mechanism, which is important for new antiviral drug design.

Combining ribosome profiling and RNA sequencing illuminates novel features of porcine reproductive and respiratory syndrome virus gene expression, including the regulation of polyprotein stoichiometry through temporal modulation of ribosomal frameshifting and the synthesis of non-canonical transcripts.

Cryo-electron tomography unveils striking new structural components of positive-strand virus RNA replication compartments, greatly advancing mechanistic insights into the structure, assembly, function and control of these critical complexes.

A combination of X-ray crystallography, molecular dynamics and small angle X-ray scattering shows that the transcription antiterminator M2-1 is a structurally dynamic homotetramer that undergoes large concerted conformational changes upon binding its target RNA.