This definition appears rarely
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Nuclear export protein (NEP) (Non-structural protein.
Its nucleocapsid is an icosahedron, and the viral capsid consists of 60 copies of capsid proteins arranged into 12 pentamers. The genome of this virus family contains a single-stranded positive-sense RNA with 7500 to 8000 nucleotides and a single open reading frame. RNA encodes a peptide chain with approximately 2200 amino acid residues. This peptide chain is divided factitiously into three regions, P1, P2, and P3, based on the differences in its structure and function. P1 constitutes the capsid protein fraction of the virus, whereas P2 and P3 comprise the non-structural proteins.
Protein-protein interactions play a central role in various aspects of the structural and functional organization of the cell, and their elucidation is crucial for a better understanding of process
Structural proteins linking the viral envelope with the virus core. They play a crucial role in virus assembly, and interact with the RNP complex as well as with the viral membrane. They are found in many enveloped viruses including paramyxoviruses, orthomyxoviruses, herpesviruses, retroviruses, filoviruses and other groups.
Start and stop codons of the ORF are indicated. The 5′ NTR contains an internal ribosome entry site (IRES). The structural core (C) protein and the two envelope glycoproteins (E1 and E2), together with p7 and NS2, are required for virus assembly (the so-called assembly module). The remainder of the non-structural proteins are required for RNA replication (the so-called replication module).
They have a hemagglutinin-neuraminidase attachment protein and do not produce a non-structural protein.
Suppressor of RNA-mediated gene silencing (Non-structural protein.