ICP27 phosphorylation site mutants are defective in herpes simplex virus 1 replication and gene expression.
about
Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through Nup62, inhibiting host nucleocytoplasmic transport pathwaysICP27 phosphorylation site mutants display altered functional interactions with cellular export factors Aly/REF and TAP/NXF1 but are able to bind herpes simplex virus 1 RNAHerpes simplex virus 1 regulatory protein ICP27 undergoes a head-to-tail intramolecular interaction.Three arginine residues within the RGG box are crucial for ICP27 binding to herpes simplex virus 1 GC-rich sequences and for efficient viral RNA export.Head-to-tail intramolecular interaction of herpes simplex virus type 1 regulatory protein ICP27 is important for its interaction with cellular mRNA export receptor TAP/NXF1.Stability of structured Kaposi's sarcoma-associated herpesvirus ORF57 protein is regulated by protein phosphorylation and homodimerization.CK2 inhibitors increase the sensitivity of HSV-1 to interferon-β.Structure of the C-Terminal Domain of the Multifunctional ICP27 Protein from Herpes Simplex Virus 1N-terminal phosphorylation sites of herpes simplex virus 1 ICP0 differentially regulate its activities and enhance viral replication.The many roles of the highly interactive HSV protein ICP27, a key regulator of infection.The human adenovirus type 5 E1B 55-kilodalton protein is phosphorylated by protein kinase CK2.Herpes simplex virus requires poly(ADP-ribose) polymerase activity for efficient replication and induces extracellular signal-related kinase-dependent phosphorylation and ICP0-dependent nuclear localization of tankyrase 1.Human Antiviral Protein IFIX Suppresses Viral Gene Expression during Herpes Simplex Virus 1 (HSV-1) Infection and Is Counteracted by Virus-induced Proteasomal Degradation.pUL69 of Human Cytomegalovirus Recruits the Cellular Protein Arginine Methyltransferase 6 via a Domain That Is Crucial for mRNA Export and Efficient Viral Replication
P2860
Q24305296-F66D7126-7640-41AB-950D-8B90BFBF349DQ33648948-C85F8223-3AC6-4DC8-9140-8768C38874B3Q33826787-2A662EA4-02C8-4D1C-90F5-93FA8548B5C1Q33990699-D20449A2-04A1-4A46-9879-4108526B74FEQ34285978-D9BE67AF-145B-40B3-AEB9-5ABE6FC39EF7Q35111060-77D51948-0ADE-4E93-AC57-DCDAC41DF86CQ35175764-CFBF02E0-C91F-4EE7-BCEA-0B7E70DA5D74Q35913888-012EFEFB-9491-4E9A-969F-E29ECBDA6899Q36607356-11607162-33E2-4AB1-9040-9D4DDD797488Q37955947-1E19D039-0C79-4EAC-BC4B-E1C3E2D5C3A4Q39424095-EA428E19-8F1C-4296-804D-CFBC9D3CC8DFQ39455618-8CA13614-3FE4-43A0-A7D1-253653C468A0Q40376097-039DFEEC-8B6E-4EF2-BC81-C141D3617D45Q41583100-4DA7CB31-21F6-44D5-9299-B76C5AD43D73
P2860
ICP27 phosphorylation site mutants are defective in herpes simplex virus 1 replication and gene expression.
description
2009 nî lūn-bûn
@nan
2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
ICP27 phosphorylation site mut ...... plication and gene expression.
@ast
ICP27 phosphorylation site mut ...... plication and gene expression.
@en
type
label
ICP27 phosphorylation site mut ...... plication and gene expression.
@ast
ICP27 phosphorylation site mut ...... plication and gene expression.
@en
prefLabel
ICP27 phosphorylation site mut ...... plication and gene expression.
@ast
ICP27 phosphorylation site mut ...... plication and gene expression.
@en
P2093
P2860
P356
P1433
P1476
ICP27 phosphorylation site mut ...... plication and gene expression.
@en
P2093
Kara A Corbin-Lickfett
Laurimar Escudero-Paunetto
Santos Rojas
P2860
P304
P356
10.1128/JVI.00917-09
P577
2009-12-16T00:00:00Z