ReviewJournal of molecular medicine (Berlin, Germany)2003
Regulation of distinct biological activities of the NF-kappaB transcription factor complex by acetylation.
Review in Journal of molecular medicine (Berlin, Germany), 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
105 citing papers in PubMed, 275 citations in OpenAlex.
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- The FcRn from gene to protein and function: comparison between species.Frontiers in immunology · 2025Review
- Post-translational modifications as a key mechanism for herpes simplex virus type I evasion of host innate immunity.Frontiers in microbiology · 2025Review
- Beneficial Effects ofNutrients · 2024Review
- A phenotypic screening platform for identifying chemical modulators of astrocyte reactivity.Nature neuroscience · 2024Article
- p38-mediated FOXN3 phosphorylation modulates lung inflammation and injury through the NF-κB signaling pathway.Nucleic acids research · 2023Article
- Review
- Diabetes and Its Cardiovascular Complications: Potential Role of the Acetyltransferase p300.Cells · 2023Review
- Protein Acetylation Going Viral: Implications in Antiviral Immunity and Viral Infection.International journal of molecular sciences · 2022Review
- Review
- The transcription factor activity gradient (TAG) model: contemplating a contact-independent mechanism for enhancer-promoter communication.Genes & development · 2022Review
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- Dual-Targeted Therapy Circumvents Non-Genetic Drug Resistance to Targeted Therapy.Frontiers in oncology · 2022Review
- HDAC4 Is Indispensable for Reduced Slow Myosin Expression at the Early Stage of Hindlimb Unloading in Rat Soleus Muscle.Pharmaceuticals (Basel, Switzerland) · 2021Article
- Dual Role of SIRT1 in Autophagy and Lipid Metabolism Regulation in Osteoarthritic Chondrocytes.Medicina (Kaunas, Lithuania) · 2021Article
- DNA methyltransferase inhibitors upregulate CD38 protein expression and enhance daratumumab efficacy in multiple myeloma.Leukemia · 2020Article
- Identification of BRMS1L as Metastasis Suppressing Gene in Esophageal Squamous Cell Carcinoma.Cancer management and research · 2020Article
- Exopolysaccharide from Paecilomyces lilacinus modulates macrophage activities through the TLR4/NF‑κB/MAPK pathway.Molecular medicine reports · 2019Article
- PI3K-AKT-mTOR and NFκB Pathways in Ovarian Cancer: Implications for Targeted Therapeutics.Cancers · 2019Review
45 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Although the proximal cytoplasmic signaling events that control the activation of the NF-kappaB transcription factor are understood in considerable detail, the subsequent intranuclear events that regulate the strength and duration of the NF-kappaB-mediated transcriptional response remain poorly defined. Recent studies have revealed that NF-kappaB is subject to reversible acetylation and that this posttranslational modification functions as an intranuclear molecular switch to control NF-kappaB action. In this review, we summarize this new and fascinating mechanism through which the pleiotropic effects of NF-kappaB are regulated within the cells. NF-kappaB is a heterodimer composed of p50 and RelA subunits. Both subunits are acetylated at multiple lysine residues with the p300/CBP acetyltransferases playing a major role in this process in vivo. Further, the acetylation of different lysines regulates different functions of NF-kappaB, including transcriptional activation, DNA binding affinity, IkappaBalpha assembly, and subcellular localization. Acetylated forms RelA are subject to deacetylation by histone deacetylase 3 (HDAC3). This selective action of HDAC3 promotes IkappaBalpha binding and rapid CRM1-dependent nuclear export of the deacetylated NF-kappaB complex, which terminates the NF-kappaB response and replenishes the cytoplasmic pool of latent NF-kappaB/IkappaBalpha complexes. This readies the cell for the next NF-kappaB-inducing stimulus. Thus, reversible acetylation of RelA serves as an important intranuclear regulatory mechanism that further provides for dynamic control of NF-kappaB action.
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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.