tetano
Editor, Senior Moderator
J Virol. 2014 Apr 16. [Epub ahead of print]
Phosphorylation of highly conserved serine residues in the influenza A virus nuclear export protein NEP plays a minor role in viral growth in human cells and mice.
Reuther P1, Giese S, G?tz V, Riegger D, Schwemmle M.
Author information
Abstract
Phosphorylation at the highly conserved serine residues S23 to S25 in NEP of influenza A viruses was suspected to regulate its nuclear export activity or polymerase-activity enhancing function. Mutation of these phosphoacceptor sites to either alanine or aspartic acid showed only a minor effect on both activities, but revealed the presence of other phosphoacceptor sites that might be involved in regulating NEP activity.
PMID:
24741082
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24741082
Phosphorylation of highly conserved serine residues in the influenza A virus nuclear export protein NEP plays a minor role in viral growth in human cells and mice.
Reuther P1, Giese S, G?tz V, Riegger D, Schwemmle M.
Author information
Abstract
Phosphorylation at the highly conserved serine residues S23 to S25 in NEP of influenza A viruses was suspected to regulate its nuclear export activity or polymerase-activity enhancing function. Mutation of these phosphoacceptor sites to either alanine or aspartic acid showed only a minor effect on both activities, but revealed the presence of other phosphoacceptor sites that might be involved in regulating NEP activity.
PMID:
24741082
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24741082