Phosphorylation of the herpes simplex virus tegument protein VP22 has no effect on incorporation of VP22 into the virus but is involved in optimal expression and virion packaging of ICP0.
about
Novel roles of cytoplasmic ICP0: proteasome-independent functions of the RING finger are required to block interferon-stimulated gene production but not to promote viral replication.Characterization of a UL49-null mutant: VP22 of herpes simplex virus type 1 facilitates viral spread in cultured cells and the mouse corneaCK2 inhibitors increase the sensitivity of HSV-1 to interferon-β.Replication-competent herpes simplex virus 1 isolates selected from cells transfected with a bacterial artificial chromosome DNA lacking only the UL49 gene vary with respect to the defect in the UL41 gene encoding host shutoff RNase.VP22 core domain from Herpes simplex virus 1 reveals a surprising structural conservation in both the Alpha- and Gammaherpesvirinae subfamiliesPhosphorylation of Bovine Herpesvirus 1 VP8 Plays a Role in Viral DNA Encapsidation and Is Essential for Its Cytoplasmic Localization and Optimal Virion Incorporation.VP22 of herpes simplex virus 1 promotes protein synthesis at late times in infection and accumulation of a subset of viral mRNAs at early times in infection.Kaposi's Sarcoma-Associated Herpesvirus Inhibitor of cGAS (KicGAS), Encoded by ORF52, Is an Abundant Tegument Protein and Is Required for Production of Infectious Progeny VirusesElucidation of the block to herpes simplex virus egress in the absence of tegument protein UL16 reveals a novel interaction with VP22.A Conserved Leucine Zipper Motif in Gammaherpesvirus ORF52 Is Critical for Distinct Microtubule Rearrangements.The varicella-zoster virus (VZV) ORF9 protein interacts with the IE62 major VZV transactivator.Recruitment of herpes simplex virus type 1 immediate-early protein ICP0 to the virus particle.A VP22-Null HSV-1 Is Impaired in Inhibiting CD1d-Mediated Antigen Presentation.Regulation and function of phosphorylation on VP8, the major tegument protein of bovine herpesvirus 1.A network of protein interactions around the herpes simplex virus tegument protein VP22.Virion incorporation of the herpes simplex virus type 1 tegument protein VP22 occurs via glycoprotein E-specific recruitment to the late secretory pathway.
P2860
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P2860
Phosphorylation of the herpes simplex virus tegument protein VP22 has no effect on incorporation of VP22 into the virus but is involved in optimal expression and virion packaging of ICP0.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
Phosphorylation of the herpes ...... and virion packaging of ICP0.
@en
Phosphorylation of the herpes ...... and virion packaging of ICP0.
@nl
type
label
Phosphorylation of the herpes ...... and virion packaging of ICP0.
@en
Phosphorylation of the herpes ...... and virion packaging of ICP0.
@nl
prefLabel
Phosphorylation of the herpes ...... and virion packaging of ICP0.
@en
Phosphorylation of the herpes ...... and virion packaging of ICP0.
@nl
P2860
P1433
P1476
Phosphorylation of the herpes ...... and virion packaging of ICP0.
@en
P2093
Corinne Potel
Gillian Elliott
P2860
P304
14057-14068
P356
10.1128/JVI.79.22.14057-14068.2005
P407
P577
2005-11-01T00:00:00Z