Proteasome-independent disruption of PML oncogenic domains (PODs), but not covalent modification by SUMO-1, is required for human cytomegalovirus immediate-early protein IE1 to inhibit PML-mediated transcriptional repression.
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Activation of nucleotide oligomerization domain 2 (NOD2) by human cytomegalovirus initiates innate immune responses and restricts virus replicationAbility of the human cytomegalovirus IE1 protein to modulate sumoylation of PML correlates with its functional activities in transcriptional regulation and infectivity in cultured fibroblast cellsAnalysis of human cytomegalovirus-encoded SUMO targets and temporal regulation of SUMOylation of the immediate-early proteins IE1 and IE2 during infectionIntrinsic host restriction factors of human cytomegalovirus replication and mechanisms of viral escapeThe carboxy terminal region of the human cytomegalovirus immediate early 1 (IE1) protein disrupts type II inteferon signaling.Kaposi's sarcoma-associated herpesvirus K-bZIP represses gene transcription via SUMO modification.Role of noncovalent SUMO binding by the human cytomegalovirus IE2 transactivator in lytic growth.Lytic replication-associated protein (RAP) encoded by Kaposi sarcoma-associated herpesvirus causes p21CIP-1-mediated G1 cell cycle arrest through CCAAT/enhancer-binding protein-alpha.The human cytomegalovirus DNA polymerase processivity factor UL44 is modified by SUMO in a DNA-dependent manner.Crystal structure of cytomegalovirus IE1 protein reveals targeting of TRIM family member PML via coiled-coil interactions.Versatile protein tag, SUMO: its enzymology and biological function.SUMOylation of the human cytomegalovirus 72-kilodalton IE1 protein facilitates expression of the 86-kilodalton IE2 protein and promotes viral replicationEvidence for a dual antiviral role of the major nuclear domain 10 component Sp100 during the immediate-early and late phases of the human cytomegalovirus replication cycleTranscriptional activation of endoplasmic reticulum chaperone GRP78 by HCMV IE1-72 proteinOncolytic vesicular stomatitis virus induces apoptosis via signaling through PKR, Fas, and Daxx.Regulation and function of SUMO modification.Human Cytomegalovirus Immediate-Early 1 Protein Rewires Upstream STAT3 to Downstream STAT1 Signaling Switching an IL6-Type to an IFNγ-Like ResponseCharacterization of Recombinant Human Cytomegaloviruses Encoding IE1 Mutants L174P and 1-382 Reveals that Viral Targeting of PML Bodies Perturbs both Intrinsic and Innate Immune ResponsesThe replication defect of ICP0-null mutant herpes simplex virus 1 can be largely complemented by the combined activities of human cytomegalovirus proteins IE1 and pp71Binding STAT2 by the acidic domain of human cytomegalovirus IE1 promotes viral growth and is negatively regulated by SUMO.Physical requirements and functional consequences of complex formation between the cytomegalovirus IE1 protein and human STAT2.Interplay between Herpesvirus Infection and Host Defense by PML Nuclear BodiesSumoylation at the host-pathogen interface.Deletion of the rat cytomegalovirus immediate-early 1 gene results in a virus capable of establishing latency, but with lower levels of acute virus replication and latency that compromise reactivation efficiency.The Human Cytomegalovirus IE1 Protein Antagonizes PML Nuclear Body-Mediated Intrinsic Immunity via the Inhibition of PML De Novo SUMOylationStimulation of the Replication of ICP0-Null Mutant Herpes Simplex Virus 1 and pp71-Deficient Human Cytomegalovirus by Epstein-Barr Virus Tegument Protein BNRF1.Analysis of the functional interchange between the IE1 and pp71 proteins of human cytomegalovirus and ICP0 of herpes simplex virus 1.The Human CMV IE1 Protein: An Offender of PML Nuclear Bodies.H2B homology region of major immediate-early protein 1 is essential for murine cytomegalovirus to disrupt nuclear domain 10, but is not important for viral replication in cell culture.Arsenic mediated disruption of promyelocytic leukemia protein nuclear bodies induces ganciclovir susceptibility in Epstein-Barr positive epithelial cells.Human cytomegalovirus IE72 protein interacts with the transcriptional repressor hDaxx to regulate LUNA gene expression during lytic infection.Human cytomegalovirus protein pp71 displaces the chromatin-associated factor ATRX from nuclear domain 10 at early stages of infection.The ND10 Component Promyelocytic Leukemia Protein Acts as an E3 Ligase for SUMOylation of the Major Immediate Early Protein IE1 of Human Cytomegalovirus.Viral Interplay with the Host Sumoylation System.Comparison of the SUMO1 and ubiquitin conjugation pathways during the inhibition of proteasome activity with evidence of SUMO1 recycling.Post-translational modification of Rta of Epstein-Barr virus by SUMO-1.PIAS1 enhances SUMO-1 modification and the transactivation activity of the major immediate-early IE2 protein of human cytomegalovirus.The carboxyl-terminal region of human cytomegalovirus IE1491aa contains an acidic domain that plays a regulatory role and a chromatin-tethering domain that is dispensable during viral replication.Adenovirus E4 ORF3 protein inhibits the interferon-mediated antiviral responseHuman Herpesvirus 6 immediate-early 1 protein is a sumoylated nuclear phosphoprotein colocalizing with promyelocytic leukemia protein-associated nuclear bodies.
P2860
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P2860
Proteasome-independent disruption of PML oncogenic domains (PODs), but not covalent modification by SUMO-1, is required for human cytomegalovirus immediate-early protein IE1 to inhibit PML-mediated transcriptional repression.
description
2001 nî lūn-bûn
@nan
2001 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Proteasome-independent disrupt ...... ted transcriptional repression
@nl
Proteasome-independent disrupt ...... ed transcriptional repression.
@ast
Proteasome-independent disrupt ...... ed transcriptional repression.
@en
Proteasome-independent disrupt ...... ed transcriptional repression.
@en-gb
type
label
Proteasome-independent disrupt ...... ted transcriptional repression
@nl
Proteasome-independent disrupt ...... ed transcriptional repression.
@ast
Proteasome-independent disrupt ...... ed transcriptional repression.
@en
Proteasome-independent disrupt ...... ed transcriptional repression.
@en-gb
prefLabel
Proteasome-independent disrupt ...... ted transcriptional repression
@nl
Proteasome-independent disrupt ...... ed transcriptional repression.
@ast
Proteasome-independent disrupt ...... ed transcriptional repression.
@en
Proteasome-independent disrupt ...... ed transcriptional repression.
@en-gb
P2093
P2860
P3181
P1433
P1476
Proteasome-independent disrupt ...... ted transcriptional repression
@en
P2093
C M apRhys
G S Hayward
P2860
P304
10683-10695
P3181
P356
10.1128/JVI.75.22.10683-10695.2001
P407
P577
2001-11-01T00:00:00Z