Identification of a human respiratory syncytial virus phosphoprotein domain required for virus-like-particle formation
Author:
Funder
National Institute of General Medical Sciences
National Institutes of Health
Publisher
Elsevier BV
Subject
Virology
Reference45 articles.
1. Regulated but not constitutive human respiratory syncytial virus (HRSV) P protein phosphorylation is essential for oligomerization;Asenjo;FEBS Lett.,2000
2. Determination of phosphorylated residues from human respiratory syncytial virus P protein that are dynamically dephosphorylated by cellular phosphatases: a possible role for serine 54;Asenjo;J. Gen. Virol.,2005
3. Phosphorylation of human respiratory syncytial virus P protein at threonine 108 controls its interaction with the M2-1 protein in the viral RNA polymerase complex;Asenjo;J. Gen. Virol.,2006
4. Residues in human respiratory syncytial virus P protein that are essential for its activity on RNA viral synthesis;Asenjo;Virus Res.,2008
5. Phosphorylation of human respiratory syncytial virus P protein at serine 54 regulates viral uncoating;Asenjo;Virology,2008
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