gG Antibody, Biotin conjugated

1. HSV-1 Us3 is a multifunctional protein that plays various roles in the viral life cycle by phosphorylating a number of viral and cellular substrates. [review] PMID:29896662
2. It regulates the pathogenicity of herpes simplex virus type-1 PMID:28484184
3. This study identifies the alphaherpesvirus-specific Us3 kinase as an mTORC1 activator that subverts the host cell energy-sensing program to support viral productive growth irrespective of physiological stress. PMID:28468873
4. findings show that Us8A is a virulence factor for HSV-1 infection in mice, and the function of Us8A for viral invasion into the central nervous system from peripheral sites is regulated by Us3-mediated phosphorylation of the protein at Ser-61. PMID:27030266
5. The difference between HSV-1 and HSV-2 Us3 kinases appeared to be due to the fact that some Us3 phosphorylation sites in HSV-1 proteins are not conserved in the corresponding HSV-2 proteins. PMID:26491159
6. Us3 enables the nucleus to cytoplasm capsid translocation. Nevertheless, Us3 is not essential for the production of infective progeny viruses. PMID:25588052
7. HSV-1-encoded Us3 protein interrupted TCR signaling and interleukin-2 production by inactivation of the linker for activation of T cells. PMID:25907557
8. Ablation of this phosphorylation abolished herpes simplex virus 1 US3-mediated downregulation of CD1d expression, suggesting that phosphorylation of KIF3A is the primary mechanism of viral suppression of CD1d expression. PMID:25878107
9. This study demonstrated that herpes simplex virus 1 protein kinase US3 significantly inhibited NF-kappaB activation via hyperphosphorylation of p65 and decreased the expression of inflammatory chemokine interleukin-8 (IL-8). PMID:24807716
10. Sufficient dUTPase activity was required for efficient herpes simplex virus 1 replication and Us3 phosphorylation of viral dUTPase Ser-187 upregulated dUTPase activity in host cells with low cellular dUTPase activity. PMID:24760895
11. STING is stable in cancer-derived HEp-2 or HeLa cells infected with wild-type HSV-1 but is degraded in cells infected with mutants lacking the genes encoding functional infected cell protein 0 (ICP0), ICP4, or the US3 protein kinase PMID:24449861
12. Herpes simplex virus 1 US3 hyperphosphorylates IRF3 and inhibits beta interferon production. PMID:24049179
13. Human herpesvirus 1 US3 is necessary and sufficient for inhibiting TLR2 signaling at or before the stage of TRAF6 ubiquitination. PMID:23478027
14. US3 plays a significant role in down-regulation of membrane biosynthesis. PMID:22789738
15. These results suggested that Us3 phosphorylation of UL47 Ser-77 promoted the nuclear localization of UL47 in cell cultures and played a critical role in viral replication and pathogenesis in vivo. PMID:21734045
16. identified gB and US3 as two viral factors that together downregulate CD1d surface expression; results suggest that HSV-1 uses gB and US3 to rapidly inhibit NKT cell function in the initial antiviral response PMID:21653669
17. The authors demonstrated that Us3 phosphorylation of glycoprotein B Thr-887 upregulated the accumulation of endocytosed of glycoprotein B from the surfaces of infected cells. PMID:21389132
18. Us3 is an Akt surrogate with overlapping substrate specificity to activate mTORC1, stimulating translation and virus replication PMID:21123650
19. Us3 phosphorylation of gB Thr-887 played a critical role in viral replication in vivo and in HSV-1 pathogenesis PMID:19846518
20. This prostein accumulates in cells infected with the mutant lacking the gene encoding ICP22 mediated the phosphorylation of histone deacetylase. PMID:15956590
21. U(S)3 and U(S)3.5 protein kinases of herpes simplex virus 1 differ with respect to their functions in blocking apoptosis and in virion maturation and egress. PMID:16571792
22. U(S)3 protein kinase blocks histone deacetylation by a mechanism distinct from that of ICP0. PMID:16785443
23. It was concluded that US3 was mediating the suppression of mitochondrial respiration following HHV-1 infection. PMID:16847111
24. Us3, Us5, and Us12 viral genes each have unique inhibitory effects on the different T lymphocyte cytotoxic effects PMID:16987059
25. US3 blocks the proteolytic cleavage that generates active caspase 3 from the transfected zymogen procaspase 3, concomitant with inhibition of apoptosis. PMID:17634220
26. These results supported the hypothesis that Us3 phosphorylates gB and downregulates the cell surface expression of gB in HSV-1-infected cells. PMID:18945776
27. The majority of the US3-dependent phosphorylation of gB involved the CT domain and amino acid T887, a residue present in a motif similar to that recognized by US3 in other proteins. PMID:19158241
28. US3-mediated phosphorylation of UL31 is critical to regulate nuclear egress. PMID:19279109
29. regulation of Us3 activity by autophosphorylation appeared to play a critical role in viral replication in vivo and in HSV-1 pathogenesis PMID:19297494
30. regulatory and functional effects differ from Us3 protein kinase in herpes simplex virus 2 PMID:19740999

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KEGG: vg:2703404