Mouse polyclonal to MYBBP1A, Host Mouse
- Known as:
- Mouse pab MYBBP1A, Host Mouse
- Catalog number:
- YF-PA17012
- Product Quantity:
- 50 ug
- Category:
- -
- Supplier:
- Abfron
- Gene target:
- Mouse polyclonal MYBBP1A Host
Related genes to: Mouse polyclonal to MYBBP1A, Host Mouse
- Gene:
- MYBBP1A NIH gene
- Name:
- MYB binding protein 1a
- Previous symbol:
- -
- Synonyms:
- P160, PAP2, FLJ37886, Pol5
- Chromosome:
- 17p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1999-06-25
- Date modifiied:
- 2017-05-26
Related products to: Mouse polyclonal to MYBBP1A, Host Mouse
Related articles to: Mouse polyclonal to MYBBP1A, Host Mouse
- Mitochondrial dynamics and autophagy are associated with esophageal squamous cell carcinoma (ESCC) progression, but their combined mechanisms are unclear. This study aimed to evaluate the prognostic significance of mitochondrial dynamics-related genes (MDRGs) and mitochondrial autophagy-related genes (MARGs) in ESCC by constructing a risk model. - Source: PubMed
Publication date: 2026/04/27
Lin HuiZhuang Feng-NianChen Wei-JieWei Wen-WeiGao Peng-QiangWang Pei-YuanWang FengShi Shan - N-methyladenosine (mA) represents the most abundant internal RNA modification and a key regulator of gene expression. Although individual mA regulators and sites have been linked to cancer, their transcriptome-wide functional landscape remains undefined. Here we developed an epitranscriptomic screening platform based on targeted mA deposition to identify functional modifications in prostate and lung cancer models. The unbiased screens uncovered 222 mA sites that modulate cell proliferation, predominantly in a cell-type-specific manner. Among them, an mA site within CHD9 emerged as a potent tumor-suppressive modification in prostate cancer. Deposition of mA at this site increased CHD9 protein abundance, suppressed cell proliferation and attenuated xenograft growth. Mechanistically, mA at CHD9 enhances translation through YTHDF1 and YTHDF3, promoting CHD9-MYBBP1A interaction in the nucleoplasm, sequestrating MYBBP1A from the nucleolus and activating CDKN1A (p21)-associated tumor-suppressive signaling. Collectively, our study establishes a scalable framework for functional mapping of the mA epitranscriptome and uncovers a mechanistic link between CHD9 mA modification and tumor suppression, paving the way for systematic exploration of other RNA modifications in cancer. - Source: PubMed
Publication date: 2026/02/06
Xu XinWang YujuanZhu HelenLam MagnusLuo WenqinTeng MonaLiu YinGuo Wang YuanAastha AasthaXu XiChen SujunCi XinpeiWang ShiyanZeng YongZhu GuanghuiKislinger ThomasLupien MathieuTsao Ming-SoundHe Housheng Hansen - RNA modification recognition proteins are crucial in cancer development and progression. Among all RNA modification-related proteins (RMRPs), Weighted Gene Co-expression Network Analysis (WGCNA), combined with comprehensive bioinformatic analysis, suggests that NAT10-the sole known writer of N4-acetylcytidine (ac4C)-is a critical regulatory protein in colorectal cancer (CRC) progression. NAT10 facilitates the malignancy phenotypes and DNA damage repair in CRC cells via its ac4C transferase activity and regulation of PPAN. Specifically, NAT10 enhances the translation efficiency of PPAN via acetylation at the C744 and C747 sites. In addition, NAT10 promotes the translation of ac4C-modified MYC mRNA. MYC protein then enhances PPAN transcription through binding to the PPAN promoter. The newly identified ac4C reader protein MYBBP1A mediates NAT10-induced translation of both PPAN and MYC. We further found that VDR binds to the NAT10 promoter to activate its transcription, resulting in the high expression of NAT10 in CRC. Xenograft studies and clinical data confirmed the role of the NAT10-PPAN axis in promoting CRC development and DNA damage repair. Collectively, our study reveals the role and underlying mechanism of mRNA ac4C modification in CRC progression, providing critical potential targets for CRC drug development. - Source: PubMed
Publication date: 2025/12/27
Wang HaoranGe LichenLi JianingZhong KeLi ShanzhiMa NingjingTao LijunZhou JiawangWang ZhaotongChang XingLu YunqingRui YalanXie GuoyouYang WeifengXu ZuanzongSaad Abdulaziz Ahmed AWang XiansongChen ZhuojiaLi WanglinYi ChengWang HongshengZhang Kun - Acute lymphoblastic leukemia (ALL) is the most common pediatric cancer. Although PEG-asparaginase (PEG-ASNase) is a key drug in treatment, hypersensitivity reactions, pancreatitis, and silent inactivation remain major challenges. Interindividual genetic variability influences drug metabolism and toxicity, and pharmacogenetic research aims to identify these variants early to predict specific responses effectively. - Source: PubMed
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Cecconello Daiane Kellerde Souza Silva Klerize Anecelyde Senna Evelin Cristine MendonçaCarlotto Lucas Alfeude Souza Amanda MásculoLins Mecneide MendesMagalhães Isis Maria Quezado Soaresde Sousa Ana Virgínia LopesEpelman SidneiCristofani LilianBarros Tais TerezianoPianovski MaraMoreira Larissa PolisRechenmacher CilianaDaudt Liane EstevesMichalowski Mariana Bohns - Porcine reproductive and respiratory syndrome virus (PRRSV) is a major swine pathogen that causes significant economic losses worldwide. The nucleocapsid (N) protein, the most abundant viral protein in infected cells, plays roles beyond its structural function, influencing various host cellular processes. Here, we report the identification of 301 cellular protein candidates interacting with PRRSV N using EGFP immunoprecipitation combined with label-free quantitative mass spectrometry. The analysis underscores the versatile nature of the N protein in targeting a wide range of cellular proteins and processes across multiple subcellular compartments. We observed strong enrichment of ribosomal proteins, nucleolar proteins involved in ribosome biogenesis, splicing factors, RNA helicases, and DNA-binding proteins involved in chromatin remodeling and DNA damage response. Additionally, we identified proteins involved in viral RNA sensing and intrinsic antiviral mechanisms that may contribute to the immunosuppressive properties of the viral protein. Several interactions were validated and further characterized for RNA dependence, including MYBBP1A, NCL, IGF2BP1, UPF3B, G3BP1, EIF2S1, RFC4, ABCF1, PPM1G, NSUN2, and NOP2. Notably, RTCB and MYBBP1A were identified as host dependency factors for PRRSV infection. Our findings expand the current understanding of PRRSV-host interactions and reveal novel N-interacting proteins that may contribute to viral pathogenesis and immune evasion. - Source: PubMed
Publication date: 2025/09/25
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