Characterization of the novel E3 ubiquitin ligase encoded in exon 3 of herpes simplex virus-1-infected cell protein 0.
about
TRIM family proteins: retroviral restriction and antiviral defenceThe degradation of promyelocytic leukemia and Sp100 proteins by herpes simplex virus 1 is mediated by the ubiquitin-conjugating enzyme UbcH5aReplication-initiator protein (UL9) of the herpes simplex virus 1 binds NFB42 and is degraded via the ubiquitin-proteasome pathwayThe potential link between PML NBs and ICP0 in regulating lytic and latent infection of HSV-1HSV-1 ICP0: An E3 Ubiquitin Ligase That Counteracts Host Intrinsic and Innate ImmunityHerpes simplex virus 1 mutant in which the ICP0 HUL-1 E3 ubiquitin ligase site is disrupted stabilizes cdc34 but degrades D-type cyclins and exhibits diminished neurotoxicityRole of ICP0 in the strategy of conquest of the host cell by herpes simplex virus 1HSV-2 inhibits type-I interferon signaling via multiple complementary and compensatory STAT2-associated mechanismsSpecificity of the E1-E2-E3 enzymatic cascade for ubiquitin C-terminal sequences identified by phage displayHerpes simplex virus 1 gene expression is accelerated by inhibitors of histone deacetylases in rabbit skin cells infected with a mutant carrying a cDNA copy of the infected-cell protein no. 0.Components of nuclear domain 10 bodies regulate varicella-zoster virus replicationViral avoidance and exploitation of the ubiquitin system.The multifaceted roles of USP7: new therapeutic opportunities.Ubiquitin ligase activities of Bombyx mori nucleopolyhedrovirus RING finger proteins.Activities of ICP0 involved in the reversal of silencing of quiescent herpes simplex virus 1.Analysis of the functions of herpes simplex virus type 1 regulatory protein ICP0 that are critical for lytic infection and derepression of quiescent viral genomes.Herpes simplex virus type 1 ICP0 protein mediates activation of adeno-associated virus type 2 rep gene expression from a latent integrated form.Synthetic biology approach to reconstituting the ubiquitylation cascade in bacteria.MORC3, a Component of PML Nuclear Bodies, Has a Role in Restricting Herpes Simplex Virus 1 and Human Cytomegalovirus.Functional characterization of residues required for the herpes simplex virus 1 E3 ubiquitin ligase ICP0 to interact with the cellular E2 ubiquitin-conjugating enzyme UBE2D1 (UbcH5a)Structural model of ubiquitin transfer onto an artificial RING finger as an E3 ligase.The herpes simplex virus type 1 (HSV-1) regulatory protein ICP0 interacts with and Ubiquitinates p53.In silico analysis identifies a C3HC4-RING finger domain of a putative E3 ubiquitin-protein ligase located at the C-terminus of a polyglutamine-containing protein.
P2860
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P2860
Characterization of the novel E3 ubiquitin ligase encoded in exon 3 of herpes simplex virus-1-infected cell protein 0.
description
2002 nî lūn-bûn
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2002 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Characterization of the novel ...... rus-1-infected cell protein 0.
@ast
Characterization of the novel ...... rus-1-infected cell protein 0.
@en
Characterization of the novel ...... rus-1-infected cell protein 0.
@nl
type
label
Characterization of the novel ...... rus-1-infected cell protein 0.
@ast
Characterization of the novel ...... rus-1-infected cell protein 0.
@en
Characterization of the novel ...... rus-1-infected cell protein 0.
@nl
prefLabel
Characterization of the novel ...... rus-1-infected cell protein 0.
@ast
Characterization of the novel ...... rus-1-infected cell protein 0.
@en
Characterization of the novel ...... rus-1-infected cell protein 0.
@nl
P2860
P356
P1476
Characterization of the novel ...... rus-1-infected cell protein 0.
@en
P2093
Ryan Hagglund
P2860
P304
P356
10.1073/PNAS.122246999
P407
P577
2002-06-01T00:00:00Z