Ask about this productRelated genes to: DDX3X antibody
- Gene:
- DDX3X NIH gene
- Name:
- DEAD-box helicase 3 X-linked
- Previous symbol:
- DDX3
- Synonyms:
- DBX, HLP2, DDX14
- Chromosome:
- Xp11.4
- Locus Type:
- gene with protein product
- Date approved:
- 1998-04-29
- Date modifiied:
- 2018-04-26
Related products to: DDX3X antibody
Related articles to: DDX3X antibody
- Antiretroviral therapy (ART) effectively suppresses HIV-1 replication but does not purge the latent HIV-1 reservoir. Strategies aimed at HIV-1 latency reversal and subsequent elimination of infected cells are being explored. Targeting the inhibitor of apoptosis proteins (IAP) and DEAD-box polypeptide 3 (DDX3) RNA helicase reduces the HIV-1 reservoir ex vivo. However, the mechanisms driving apoptosis of HIV-1 infected cells remain unclear. Here, we uncovered the mechanism regarding HIV-1 transcriptional activation and induction of apoptosis specific for HIV-1 infected cells using an acute in vitro infection model. Inhibition of IAP by second mitochondrial-derived activator of caspases mimetic (SMACm; AZD5582) resulted in activation of non-canonical NF-κB pathway (RelB/p52) that induced HIV-1 transcription, confirming previous reports, whereas inhibition of DDX3 sensitized HIV-1 infected cells for apoptosis (DDX3i; FH1321). Transcriptome analysis revealed that HIV-1 actively suppressed apoptosis-related genes in HIV-1 infected cells. SMACm treatment resulted in a broad induction of these genes irrespective of infection. Notably, DDX3 inhibition specifically restored the expression of the majority of HIV-1 suppressed genes, and when combined with SMACm, restored almost all HIV-1 downregulated genes, thereby rendering HIV-1 infected cells sensitive to apoptosis. Thus, our data strongly suggest that inhibition of host factors IAP and DDX3 not only induces activation of HIV-1 transcription but also restores HIV-1 suppressed apoptotic processes in infected cells. - Source: PubMed
Publication date: 2026/05/27
Jansen JadeMan ShirleyKootstra Fennavan Nuenen Ad Cvan Dort Karel AZamperini ClaudioHouck Conraed WillemKootstra Neeltje AGeijtenbeek Teunis B H - Spring viremia of carp virus (SVCV) is one of the most devastating viral pathogens threatening the aquaculture of grass carp (Ctenopharyngodon idellus), and its outbreaks frequently result in severe economic losses worldwide. DEAD-box RNA helicase DDX3X has been established as a critical regulator of innate immune responses in mammals; however, its functional role and underlying mechanism in fish against SVCV infection remain largely unexplored. In this study, the coding sequence of grass carp DDX3X (gcDDX3X) was cloned and characterized. Sequence analysis revealed that gcDDX3X possesses conserved DEXDc and HELICc domains and shares high sequence similarity with DDX3X orthologs from other cyprinid fish species. Tissue expression profiling demonstrated that SVCV infection significantly upregulated gcDDX3X mRNA levels in multiple immune-related tissues, including the eye, intestine, liver, spleen, and gill. Consistently, poly(I:C) stimulation induced gcDDX3X expression in both GCO and EPC cells in a time- and dose-dependent manner. Subcellular localization analysis showed that gcDDX3X is predominantly distributed in the cytoplasm. Functional assays revealed that gcDDX3X overexpression markedly attenuated SVCV-induced cytopathic effects and plaque formation and significantly reduced viral titers, with more pronounced antiviral activity observed in GCO cells. Mechanistically, gcDDX3X overexpression substantially upregulated the transcriptional and protein levels of IRF3, IRF7, and type I interferon. Furthermore, co-immunoprecipitation and immunofluorescence co-localization assays demonstrated that gcDDX3X specifically interacts with gcTRAF6 in the cytoplasm. Collectively, these findings provide the first evidence that grass carp DDX3X functions as a positive regulator of the IRF3/7-IFN signaling axis via TRAF6-mediated pathways to restrict SVCV replication. This study expands our understanding of the regulatory network of DDX3X in teleost innate immunity and offers a potential molecular target for developing therapeutic strategies against SVCV infection in grass carp aquaculture. - Source: PubMed
Publication date: 2026/06/23
Chen YuGuo XinYou ShiqiLi FangLi YunxuanZhang YingshuoYuan WuzhouLi YongqingWang YuequnZhu PingFan XiongweiWu XiushanJiang Zhigang - NBO therapy has demonstrated a neuroprotective effect on ischemic stroke. This study investigated the role of HIF-1α in regulating SG formation and NLRP3 inflammasome activation following I/R injury in NBO-induced neuroprotection. - Source: PubMed
Publication date: 2026/06/19
Guo SichaoCheng ZheAl Tekreeti AbdullahLi FengwuDing YuchuanGeng Xiaokun - G-quadruplexes (G4s) are four-stranded nucleic acid structures that regulate virtually all nucleic acid-dependent cellular processes. At present, most functional studies involving G4s have focused on cancer cells. This study investigated how neurons respond to genotoxic stress induced by quarfloxin (CX-3543), a small molecule that stabilizes G4s. We found that quarfloxin treatment induced DNA damage in neurons, with double-strand breaks enriched in the nucleolus. Proteomic analysis revealed that quarfloxin promoted substantial protein changes, affecting networks associated with Alzheimer's, Parkinson's, and Huntington's diseases, and amyotrophic lateral sclerosis. Among the affected proteins, the G4 helicase DDX3X, encoded on the X chromosome, was upregulated, prompting further investigation of DDX3X and its Y-linked homolog DDX3Y in male and female neurons, respectively. RNA sequencing identified DDX3X- and DDX3Y-regulated gene networks involved in DNA damage responses, inflammation, cell cycle regulation, and stress-associated pathways, with notable sex-dependent differences. In human brain tissue, DDX3X expression and nuclear enrichment were increased in neurons from older females compared to younger individuals, with further elevation observed in Alzheimer's disease. Taken together, these findings identify DDX3X and DDX3Y as modulators of neuronal stress responses downstream of G4 stabilization and indicate that their induction is accompanied by activation of DNA damage response genes, as well as cell cycle- and inflammation-associated pathways, suggesting that sustained activation of these pathways may disrupt neuronal homeostasis. Our study provides insight into G4-dependent stress mechanisms in neurons and highlights sex-linked pathways that may contribute to brain aging and neurodegenerative disease vulnerability. - Source: PubMed
Publication date: 2026/06/18
Diaz Escarcega RocioM J Vijay KumarArizmendez AshleeTan ChunfengUrayama AkihikoMarrelli Sean PMorales RodrigoWefel Jeffrey SZhang ChunchaoMcCullough Louise DKim NayunMonchaud DavidJung Sung YunTsvetkov Andrey S - ADAR1 converts adenosine to inosine in endogenous double-stranded RNAs (dsRNAs) to prevent excessive MDA5-driven interferon-stimulated gene expression. The source of endogenous immunogenic dsRNAs remains enigmatic because only a small fraction of ADAR1 substrates activate MDA5, and cellular MDA5 filaments have not been isolated. Here, we couple affinity purification of cellular MDA5 filaments with RNA sequencing to define immunogenic endogenous dsRNAs. Greater than 84% of dsRNAs suppressed by combined DDX3X RNA helicase and ADAR1 base-editing activities were present in MDA5 filaments, compared to less than 1% of dsRNA substrates acted on by ADAR1 alone. Dual substrate dsRNAs consisted of inverted repeats embedded in 3'-UTRs with high base-pair complementarity and longer intervening sequences between repeats, with a minor contribution coming from intermolecular dsRNAs formed by sense and antisense transcripts. Moreover, the majority of dual substrate immunogenic dsRNAs were hyperedited in DDX3X mutant cancers. This reveals the identity of endogenous immunogenic dsRNAs and quality control mechanisms underlying their suppression. - Source: PubMed
Publication date: 2026/06/08
Chen JieMo ZongChaoChen SixingWang XiHsu TiffanyTorres CeliaLiu Kathy FangeHur SunLi QinGreenberg Roger A