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

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.

The high-resolution structure of a filamentous flexible plant virus shows that there is structural homology between its coat protein and the nucleoproteins of an unrelated group of enveloped RNA animal viruses.

Host protein kinase C family members regulate influenza virus genome replication by phosphorylating the viral nucleoprotein and controlling assembly of the viral replication machinery.

Hantaan virus nucleocapsid cryo-EM structure determined at 3.3 Å resolution reveals how nucleoproteins assemble into a metastable helix containing a continuous RNA-binding groove compatible with genome encapsidation and compaction.

Herpes simplex ICP4 preferentially binds to and delineates the viral genome, ultimately resulting in robust viral transcription at the expense of the host.

Extensive genetic diversity and novel genome structures in RNA viruses from arthropods shed important new light on the ancestry and evolutionary history of major classes of vertebrate and plant viruses.

Some of the mutations that occur during influenza evolution can only be tolerated in conjunction with other mutations that increase the stability of a viral protein.

Genetic, structural, and biochemical analyses of IS607-family transposons shows that the DNA translocation reaction proceeds very differently from other reactions promoted by serine recombinases.

As a Russian doll, mimivirus dsDNA genome is folded in a nucleocapsid-like structure enclosed in the nucleoid compartment, encased in the icosahedral capsid itself decorated by long glycosylated fibrils surprisingly made of the same protein as the genomic fiber.