ArticleNucleic acids research2003
Identification of novel co-repressor molecules for Interferon Regulatory Factor-2.
Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
84 citing papers in PubMed, 138 citations in OpenAlex.
- Article
- A 3'UTR polymorphism disrupts IRF2BP2 autoregulation through an eIF4H translational enhancer.Frontiers in genetics · 2026Article
- Development of compact transcriptional effectors using high-throughput measurements in diverse contexts.Nature biotechnology · 2025Article
- Advances in the Molecular Biology of Chondrosarcoma for Drug Discovery and Precision Medicine.Cancers · 2025Review
- The Multifaceted Roles ofNon-coding RNA · 2025Review
- Identification of coilin interactors reveals coordinated control of Cajal body number and structure.The Journal of cell biology · 2025Article
- Transcriptional regulation of adipocyte lipolysis by IRF2BP2.Science advances · 2025Article
- Super-Enhancer-Driven IRF2BP2 is Activated by Master Transcription Factors and Sustains T-ALL Cell Growth and Survival.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Case Report: NovelFrontiers in immunology · 2025Article
- Malate initiates a proton-sensing pathway essential for pH regulation of inflammation.Signal transduction and targeted therapy · 2024Article
- IRF2BP2 binds to a conserved RxSVI motif of protein partners and regulates megakaryocytic differentiation.Nature communications · 2024Article
- Astrocyte-induced Cdk5 expedites breast cancer brain metastasis by suppressing MHC-I expression to evade immune recognition.Nature cell biology · 2024Article
- CDYL loss promotes cervical cancer aggression by increasing PD-L1 expression via the suppression of IRF2BP2 transcription.Translational oncology · 2024Article
- AnJournal of virology · 2024Article
- IRF2BP2 counteracts the ATF7/JDP2 AP-1 heterodimer to prevent inflammatory overactivation in acute myeloid leukemia (AML) cells.Nucleic acids research · 2024Article
- SPOP point mutations regulate substrate preference and affect its function.Cell death & disease · 2024Article
- Genetic Discrimination of Grade 3 and Grade 4 Gliomas by Artificial Neural Network.Cellular and molecular neurobiology · 2023Article
- Genetic susceptibility to post-endoscopic retrograde cholangiopancreatography pancreatitis identified in propensity score-matched analysis.The Korean journal of internal medicine · 2023Article
- The integrated stress response protects against ER stress but is not required for altered translation and lifespan from dietary restriction inFrontiers in cell and developmental biology · 2023Article
- Novel frameshift variants expand the map of the genetic defects in IRF2BP2.Frontiers in immunology · 2023Article
24 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
We have identified two novel proteins that interact specifically with the C-terminal repression domain of Interferon Regulatory Factor-2 (IRF-2). These proteins, which we term IRF-2 binding proteins 1 and 2 (IRF-2BP1 and IRF-2BP2, the latter having two splicing isoforms, A and B), are nuclear proteins, and have the properties of IRF-2-dependent transcriptional co-repressors that can inhibit both enhancer-activated and basal transcription in a manner that is not dependent upon histone deacetylation. IRF-2BP1 and IRF-2BP2A/B contain an N-terminal zinc finger and a C-terminal RING finger domain of the C3HC4 subclass, but show no homology to other known transcriptional regulators; they therefore define a new family of co- repressor proteins. An alternatively spliced form of IRF-2 that lacks two amino acids (valines 177 and 178) in the central portion of the protein (IRF-2[S]) cannot bind to these co-repressors and cannot mediate repression despite having the same C- terminal repression domain as IRF-2, suggesting that the relative conformation of the DNA binding domain and the C-terminal region of IRF-2 is crucial for transcriptional repression.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.