DDX23 antibody - C-terminal region (ARP36377_P050)
- Known as:
- DDX23 (anti-) - C-terminal region (ARP36377_P050)
- Catalog number:
- arp36377_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- DDX23 antibody - C-terminal region (ARP36377_P050)
Related genes to: DDX23 antibody - C-terminal region (ARP36377_P050)
- Gene:
- DDX23 NIH gene
- Name:
- DEAD-box helicase 23
- Previous symbol:
- -
- Synonyms:
- prp28, U5-100K, PRPF28, SNRNP100
- Chromosome:
- 12q13.12
- Locus Type:
- gene with protein product
- Date approved:
- 2003-06-13
- Date modifiied:
- 2016-10-05
Related products to: DDX23 antibody - C-terminal region (ARP36377_P050)
Related articles to: DDX23 antibody - C-terminal region (ARP36377_P050)
- - Source: PubMed
Publication date: 2026/04/15
Ma HaotianAimaiti XiyidanWang YiyangLi YongxiangZhao JiaweiHou JiayueLi JiaqiGuo Chenming - Genome stability is constantly threatened by DNA damage and noncanonical nucleic acid structures, e.g., R-loops. Translesion synthesis (TLS) constitutes a major pathway for cells to cope with unrepaired DNA lesions. In this vein, polymerase κ (Pol κ) was shown to maintain genome stability by promoting error-free bypass of minor-groove -modified 2'-deoxyguanosine adducts and by participating in DNA repair. To explore functions of Pol κ, we employed two independent approaches, proximity labeling and affinity pull-down, followed by liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis, to profile the Pol κ-interaction proteome. We found that Pol κ interacts with DDX23 and the polymerase is enriched at R-loop loci in chromatin. In addition, Pol κ recruits DDX23 to R-loop sites to promote DDX23-mediated R-loop resolution, where individual ablation of Pol κ and DDX23 led to augmented accumulation of R-loops in cells. Together, we discovered an interaction between Pol κ and DDX23 and revealed the functions of this interaction in R-loop resolution. - Source: PubMed
Publication date: 2026/04/08
Tang FengWang YinanYuan JunHe XiaomeiZhang QuanqingGuo ShiyuanDai XiaoxiaLi LinYuan Bi-FengWang Yinsheng - - Source: PubMed
Publication date: 2026/02/25
Lin ChengjieLi TingWang YanLai ShihuiHuang YueGuo ZhenyunZhang XiangWeng Shangeng - SR proteins are RNA-binding proteins with one or two RNA recognition motif (RRM)-type RNA-binding domains and a C-terminal region rich in arginine-serine dipeptides. They function in cellular processes ranging from transcription to translation. The best-known SR protein, SRSF1, modulates RNA splicing by stabilizing the binding of constitutive splicing factors, but there is also evidence that it participates in constitutive splicing reactions and is present in spliceosomal complexes. It has been shown recently that it interacts with DDX23, an RNA helicase that triggers the transition from complex pre-B to complex B during activation of the spliceosome. To identify in which other steps of spliceosome assembly and reaction it might be present, we have used split-APEX with SRSF1 and a number of helicases, each of the latter being involved in a particular step. Peroxidase activity should only be reconstituted if SRSF1 and the helicase were in contact, and the consequent biotinylation should reveal proteins in the vicinity. Our results show that all the helicases tested can complement SRSF1, but that the proximal proteins are very similar in all cases. Moreover, the proteins identified fall into two major classes: splicing-related proteins and ribosomal proteins. The results raise the possibility that SRSF1 and the canonical helicases have hitherto unsuspected collaborative roles in ribosomal assembly or translation. - Source: PubMed
Publication date: 2025/12/19
Paschalis VasileiosWills Max F KDe Gusmao Araujo PhilippeLucas ChristianTubasum SumeraCui ShijieKara HesnaBueno-Alejo CarlosSantana-Vega MarinaTaladriz-Sender AndreaZhao ZhengyunAxer AlexanderDominguez CyrilClark Alasdair WBurley Glenn AHudson Andrew JEperon Ian C - Upper tract urothelial carcinoma (UTUC) is a rare malignancy with a significantly poorer prognosis than bladder cancer (BC). One distinguishing feature of UTUC is its enhanced resistance to reactive oxygen species (ROS)-induced lipid peroxidation, a phenomenon closely associated with adverse clinical outcomes. However, the molecular mechanisms underlying this resistance remain largely unexplored. In this study, we identify LncPEDS1-AS, an ultra-long (>6900 nt) antisense lncRNA, as a key regulator of ROS resistance in UTUC. Mechanistically, LncPEDS1-AS interacts with the splicing factor DDX23, forming a nuclear RNA-protein complex that facilitates the splicing and maturation of PEDS1 pre-mRNA. PEDS1 encodes plasmanylethanolamine desaturase, which plays a protective role against lipid peroxidation. Based on these findings, we developed an antisense oligonucleotide (ASO) therapy strategy targeting LncPEDS1-AS, which effectively suppressed tumour growth and enhanced tumour cells' ROS sensitivity both in vitro and in vivo. Moreover, our findings also highlight the distinctive molecular features and regulatory capacity of ultra-long antisense lncRNAs such as LncPEDS1-AS, which merit further comprehensive exploration in cancer biology. The LncPEDS1-AS-DDX23-PEDS1 axis is involved in resistance to lipid peroxidation and plays a critical role in the prognosis of UTUC (Created with BioRender.com). - Source: PubMed
Publication date: 2025/12/08
Li GuanruZhang ErweiWang ZhiyuZhang ZhijinZhang YukeDi ShichenLu JingyiCao ShunXie GuoqingZhang YuLi Keqiang