Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Human Cytomegalovirus Infection Causes Degradation of Sp100 Proteins That Suppress Viral Gene Expression

1 Sept 2011

Abstract excerpt

The interferon-inducible Sp100 proteins are thought to play roles in the chromatin pathway and in transcriptional regulation. Sp100A, the smallest isoform, is one of the major components of PML nuclear bodies (NBs) that exhibit intrinsic antiviral activity against several viruses. Since PML NBs are disrupted by the immediate-early 1 (IE1) protein during human cytomegalovirus (HCMV) infection, the modulation of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cytomegalovirus and herpesvirus research
Share to Immune Cell Function and Interaction
Share to interferon and immune responses

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 21880768
DOI: 10.1128/jvi.00758-11

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Human Cytomegalovirus Infection Causes Degradation of Sp100 Proteins That Suppress Viral Gene ExpressionPMID 21880768Read ↗

Evidence 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 CycleSemantic proximity Read ↗

Human cytomegalovirus immediate-early gene expression is restricted by the nuclear domain 10 component Sp100Semantic proximity Read ↗

Characterization of Recombinant Human Cytomegaloviruses Encoding IE1 Mutants L174P and 1-382 Reveals that Viral Targeting of PML Bodies Perturbs both Intrinsic and Innate Immune ResponsesSemantic proximity Read ↗

Ability of the Human Cytomegalovirus IE1 Protein To Modulate Sumoylation of PML Correlates with Its Functional Activities in Transcriptional Regulation and Infectivity in Cultured Fibroblast CellsSemantic proximity Read ↗

The ND10 Component Promyelocytic Leukemia Protein Acts as an E3 Ligase for SUMOylation of the Major Immediate Early Protein IE1 of Human Cytomegalovirus.Semantic proximity Read ↗

Viral Immediate-Early Proteins Abrogate the Modification by SUMO-1 of PML and Sp100 Proteins, Correlating with Nuclear Body DisruptionSemantic proximity Read ↗

Human cytomegalovirus IE1 downregulates Hes1 in neural progenitor cells as a potential E3 ubiquitin ligaseSemantic proximity Read ↗

The Human Cytomegalovirus IE1 Protein Antagonizes PML Nuclear Body-Mediated Intrinsic Immunity via the Inhibition of PML De Novo SUMOylation.Semantic proximity Read ↗

Revisiting promyelocytic leukemia protein targeting by human cytomegalovirus immediate-early protein 1.Semantic proximity Read ↗

Differential Functions of Interferon-Upregulated Sp100 Isoforms: Herpes Simplex Virus Type 1 Promoter-Based Immediate-Early Gene Suppression and PML Protection from ICP0-Mediated DegradationSemantic proximity Read ↗

The Interferon-Inducible Human PLSCR1 Protein Is a Restriction Factor of Human CytomegalovirusSemantic proximity Read ↗

Positive Role of Promyelocytic Leukemia Protein in Type I Interferon Response and Its Regulation by Human CytomegalovirusSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.