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Herpes Simplex Virus 1 Induces Phosphorylation and Reorganization of Lamin A/C through the γ134.5 Protein That Facilitates Nuclear Egress
Journal article   Open access   Peer reviewed

Herpes Simplex Virus 1 Induces Phosphorylation and Reorganization of Lamin A/C through the γ134.5 Protein That Facilitates Nuclear Egress

Songfang Wu, Shuang Pan, Liming Zhang, Joel Baines, Richard Roller, Joshua Ames, Mengmeng Yang, Jiyan Wang, Da Chen, Yaohui Liu, …
Journal of virology, Vol.90(22), pp.10414-10422
11/15/2016
DOI: 10.1128/JVI.01392-16
PMCID: PMC5105674
PMID: 27630226
url
https://doi.org/10.1128/JVI.01392-16View
Published (Version of record) Open Access

Abstract

Herpes simplex virus 1 (HSV-1) remodels nuclear membranes during virus egress. Although the UL31 and UL34 proteins control nucleocapsid transit in infected cells, the molecular interactions required for their function are unclear. Here we report that the γ
Phosphorylation - physiology Herpesvirus 1, Human - metabolism Nuclear Lamina - virology Humans Cytoplasm - virology Cercopithecus aethiops Cytoplasm - metabolism Nuclear Envelope - virology Nuclear Proteins - metabolism Virus Assembly - physiology Lamin Type A - metabolism Viral Proteins - metabolism Nuclear Envelope - metabolism Animals Cell Nucleus - metabolism Nuclear Lamina - metabolism Nucleocapsid - metabolism Protein Kinase C - metabolism Cell Nucleus - virology Virus Release - physiology Cell Line, Tumor HeLa Cells Capsid - metabolism Vero Cells

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