It is suggested that pUL16 interactions with pUL21 may regulate the isoform of PP1 that is bound to pUL21 and thereby regulate the specificity of substrate dephosphorylation and thereby regulate the specificity of substrate dephosphorylation.
In-cell cross-linking mass spectrometry maps protein contacts in influenza-infected human cells, revealing how the virus hijacks host membrane-trafficking factors and dismantles nuclear paraspeckles to enhance replication.
I. Kotova, Lars Mühlberg, Konstantin Gilep et al.· Nature Microbiology· 1 citation
This work observed that the NS5 protein of tick-borne encephalitis virus (TBEV) localized both in the cytoplasm and nucleoplasm of infected human cells and identified the specific residues responsible for its nuclear addressing and showed that it interacts with numerous nuclear proteins, including some involved in regu...
Maxime Chazal, A. Sow, Elodie le Seac'h et al.· Journal of Virology· 0 citations
Analysis of viral gene expression, protein abundance, and post-translational modifications (PTMs) during natural infection suggests that MDV CHPK orchestrates the subcellular localization of multiple viral proteins in epithelial skin cells via phosphorylation, thereby enabling efficient replication and horizontal trans...
H. Akbar, Nagendraprabhu Ponnuraj, B. F. Minhas et al.· bioRxiv· 0 citations
Current knowledge on the structural features of herpesvirus tegument proteins are summarized, highlighting the structure-based functional implications, including their potential as targets for antiviral drug development.
Huiping He, Shuang Liao, Dong-Dong Gu et al.· 0 citations
A virion-wide spatial and quantitative protein proximity map of herpes simplex virus 1 (HSV-1) is defined by combining cross-linking mass spectrometry with quantitative proteomics, showing how conserved organizational principles shape virus-specific virion interaction networks during herpesvirus maturation.
Lars Mühlberg, Yannick Jensen, Julia Ruta et al.· bioRxiv· 0 citations
This work reviews the current evidence on PTMs in orthoflavivirus C proteins and integrates insights from studies of other RNA viruses to propose mechanisms by which PTMs may regulate C protein function, and identifies conserved regulatory hotspots that represent promising targets for future experimental validation.
N. C. Mebus-Antunes, Dayane Henriques, A. D. Da Poian· Molecules· 0 citations
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