ZBTB25 antibody - middle region (ARP33531_P050)
- Known as:
- ZBTB25 (anti-) - middle region (ARP33531_P050)
- Catalog number:
- arp33531_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- ZBTB25 antibody - middle region (ARP33531_P050)
Related genes to: ZBTB25 antibody - middle region (ARP33531_P050)
- Gene:
- ZBTB25 NIH gene
- Name:
- zinc finger and BTB domain containing 25
- Previous symbol:
- ZNF46, C14orf51
- Synonyms:
- KUP
- Chromosome:
- 14q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 1991-07-12
- Date modifiied:
- 2016-10-05
Related products to: ZBTB25 antibody - middle region (ARP33531_P050)
Related articles to: ZBTB25 antibody - middle region (ARP33531_P050)
- Rv1899c, a previously identified HDAC1-ZBTB25-interacting protein of , plays a crucial role in bacterial adaptation and immune modulation. Recombinant -expressing (MS_ ) showed enhanced survival under acidic and oxidative stress compared to vector controls, along with improved early intracellular growth in THP1-derived macrophages. This was accompanied by reduced reactive oxygen species (ROS), diminished cytokines associated with inflammation and downregulation of autophagy proteins ATG5, Beclin, and LC3, which ultimately skewed the immune response, suppressing the pro-inflammatory M1 macrophage population. Targeting Rv1899c with 3-aminobenzamide (3-AB) impaired intracellular bacterial survival and restored IL-12B expression, while its combination with the HDAC inhibitor C1994 significantly enhanced bacterial clearance. Structural modelling confirmed the high stereochemical quality of the Rv1899c macrodomain, and computational studies identified 3-AB as the strongest ligand (-5.75 kcal/mol), stabilized through hydrogen bonding and hydrophobic interactions with key residues. Molecular dynamics simulations conducted for 200 ns demonstrated stable protein-ligand interactions with consistent parameters, while MM/GBSA analysis indicated favourable binding energy (ΔG_bind = -6.6 kcal/mol), largely influenced by van der Waals and electrostatic forces. Together, these findings highlight as a mediator of stress resistance and immune evasion and propose it as a potential therapeutic target against . - Source: PubMed
Publication date: 2025/11/09
Menon Arjun MGopichand BoinapalliThomas Shwetha SusanAbhinand KuniyilNair Bipin GKumar Geetha BBabu PradeeshArun K BEdison Lekshmi KMadhavan Aravind - Rheumatoid arthritis (RA) is a systemic immune-mediated disease characterized by synovitis and joint cartilage destruction. Although many studies have shown that mitophagy is crucial in the development of bone metabolism disorders, its exact function in rheumatoid arthritis (RA) is still not well understood. This study analysed the GSE77298 dataset from the Gene Expression Omnibus (GEO) to identify differentially expressed genes (DEGs) between rheumatoid arthritis (RA) patients and healthy controls. Mitophagy-related genes (MRGs) were extracted from the literature and screened using bioinformatics techniques, resulting in differentially expressed MRGs (DE-MRGs). The diagnostic value of these genes was assessed using receiver operating characteristic (ROC) curves, and an ANN model was constructed. In the GSE77298 dataset, 267 differentially expressed genes (DEGs) were identified. Weighted gene co-expression network analysis (WGCNA) identified 2191 key module genes, leading to 63 DE-MRGs. Two MRGs, TMEM45A and ZBTB25, were identified as hub genes with areas under the curve (AUC) of 0.991 and 0.911, respectively. The nomogram model demonstrated high diagnostic value. Mitophagy plays a critical role in the progression of rheumatoid arthritis (RA). Identifying two genes associated with mitophagy may aid in the early diagnosis, mechanistic understanding, and treatment of RA. - Source: PubMed
Publication date: 2025/07/16
Chen JiayiHuang ZuhaiQin ChengyuPang ZixiangChen Yuanming - The main protease of severe acute respiratory syndrome coronavirus 2, Mpro, is a key viral protein essential for viral infection and replication. Mpro has been the target of many pharmacological efforts; however, the host-specific regulation of Mpro protein remains unclear. Here, we report the ubiquitin-proteasome-dependent degradation of Mpro protein in human cells, facilitated by the human E3 ubiquitin ligase ZBTB25. We demonstrate that Mpro has a short half-life that is prolonged via proteasomal inhibition, with its Lys-100 residue serving as a potential ubiquitin acceptor. Using in vitro binding assays, we observed ZBTB25 and Mpro bind to each other in vitro, and using progressive deletional mapping, we further uncovered the required domains for this interaction. Finally, we used an orthologous beta-coronavirus infection model and observed that genetic ablation of ZBTB25 resulted in a more highly infective virus, an effect lost upon reconstitution of ZBTB25 to deleted cells. In conclusion, these data suggest a new mechanism of Mpro protein regulation as well as identify ZBTB25 as an anticoronaviral E3 ubiquitin ligase. - Source: PubMed
Publication date: 2023/10/27
Lear Travis BBoudreau Áine NLockwood Karina CChu EliseCamarco Daniel PCao QingNguyen MatthewEvankovich John WFinkel TorenLiu YuanChen Bill B - Downregulation of host gene expression is a key strategy employed by intracellular pathogens for their survival in macrophages and subsequent pathogenesis. In a previous study, we have shown that histone deacetylase 1 (HDAC1) levels go up in macrophages infected with , and it hypoacetylates histone H3 at the promoter of gene, leading to its downregulation. We now show that after infection with , HDAC1 is phosphorylated, and the levels of phosphorylated HDAC1 (pHDAC1) increase significantly in macrophages. We found that transcriptional repressor protein zinc finger and BTB domain 25 (ZBTB25) and transcriptional corepressor Sin3a associate with the HDAC1 silencing complex, which is recruited to the promoter of to downregulate its expression in infected macrophages. Knocking down of enhanced release of IL-12p40 from infected macrophages. Inhibition of HDAC1 and ZBTB25 promoted colocalization of and LC3 (microtubule-associated protein 1A/1B-light chain 3) in autophagosomes. Induction of autophagy resulted in the killing of intracellular Enhanced phosphorylation of JAK2 and STAT4 was observed in macrophages upon treatment with HDAC1 and ZBTB inhibitors, and inhibition of JAK2/STAT4 negated the killing of the intracellular pathogen, suggesting their role in the autophagy-mediated killing of intracellular In view of the emergence of drug resistance in , host-directed therapy is an attractive alternative strategy to combat tuberculosis (TB). HDACs have been proposed to be host targets for TB treatment. Our study indicates that ZBTB25, a functional subunit of the HDAC1/Sin3a repressor complex involved in suppression, could be an alternative target for host-directed anti-TB therapy. Following infection with , levels of HDAC1 go up in macrophages, and it is recruited to the promoter of where it hypoacetylates histone H3, leading to the downregulation of the gene. Here, we show that host transcriptional repressor protein ZBTB25 and transcriptional corepressor Sin3a associate with HDAC1 in the silencing complex. Knocking down of prevented the recruitment of the complex to the promoter and consequently enhanced the gene expression and the release of IL-12p40 from infected macrophages. Pharmacological inhibition of ZBTB25 in infected macrophages resulted in the induction of autophagy and killing of intracellular Drug-resistant TB is a serious challenge to TB control programs all over the world which calls for finding alternative therapeutic methods. Host-directed therapy is gaining significant momentum in treating infectious diseases. We propose that ZBTB25 is a potential target for host-directed treatment of TB. - Source: PubMed
Publication date: 2021/02/24
Madhavan AravindArun K BPushparajan Akhil RajBalaji MKumar Ramakrishnan Ajay - Proteins that bind to DNA depending on its methylation status play an important role in methylation-mediated regulation of gene expression. Using a variety of genomics and proteomics approaches, we identify zinc finger and BTB domain-containing protein 2 (ZBTB2) as a reader of unmethylated DNA in mouse embryonic stem cells. ZBTB2 preferentially binds to CpG island promoters, where it acts as a transcriptional activator. The binding of ZBTB2 to its targets is direct and independent of two other zinc finger proteins, ZBTB25 and ZNF639, which we show to interact with ZBTB2. Our data suggest an anticorrelation between ZBTB2 DNA binding and DNA methylation, indicating that ZBTB2-binding dynamics are sensitive to differential DNA methylation. ZBTB2 is intricately interwoven with DNA methylation, as we find not only that its binding to DNA is methylation sensitive, but also that ZBTB2 regulates the turnover of methylated DNA In ZBTB2 knockout cells, several pluripotency factors are upregulated, inducing a delay in differentiation. We propose that ZBTB2 is a novel DNA methylation-sensitive transcription factor that regulates cellular differentiation. - Source: PubMed
Publication date: 2018/02/01
Karemaker Ino DVermeulen Michiel