ATPBD3
- Known as:
- ATPBD3
- Catalog number:
- 002279A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- ATPBD3
Related genes to: ATPBD3
- Gene:
- CTU1 NIH gene
- Name:
- cytosolic thiouridylase subunit 1
- Previous symbol:
- ATPBD3
- Synonyms:
- MGC17332, NCS6
- Chromosome:
- 19q13.41
- Locus Type:
- gene with protein product
- Date approved:
- 2005-10-24
- Date modifiied:
- 2014-11-19
Related products to: ATPBD3
Related articles to: ATPBD3
- Type-I photosensitizers (PSs) are considered to be efficient agents for overcoming the oxygen-dependent deficiency of traditional photodynamic therapy (PDT). However, it is still challenging to design type-I PSs that can be activated by the second near-infrared (NIR-II) irradiation. Herein, a series of organic heavy-atom-free molecules are designed (named as CTU1, CTU2, and CTU3) and exhibit strong absorption bands over the first near-infrared and NIR-II regions. Among them, water-dispersible CTU3 nanoparticles (NPs) show strong J-aggregate characteristics and a good NIR-II absorption band, resulting in highly efficient •O generation upon irradiation of 1064 nm light. In addition, the CTU3 NPs also exhibit a high photothermal conversion efficiency of 88.6%. In vitro and in vivo experiments show that CTU3 NPs have superior PDT and photothermal therapy (PTT) effects, which can further induce immunogenic cell death and activate immune cells in 4T1 tumor-bearing mice for combined PDT/PTT anti-tumor photoimmunotherapy against refractory tumors. This work presents a paradigm of de novo design of NIR-II light-activated type-I PS for combinational photoimmunotherapy of cancer. - Source: PubMed
Publication date: 2025/06/04
Chen HuanWang YuHe ZhangxinWan YingpengCao ChenLu ZiweiGao YijianCui XiaoLee Ka-WaiTan Ji-HuaXu WenchangYang YuliangLi XiliangWang YaliHou JianquanLi ShengliangLee Chun-Sing - Synthesizing the cellular proteome is a demanding process that is regulated by numerous signaling pathways and RNA modifications. How precisely these mechanisms control the protein synthesis machinery to generate specific proteome subsets remains unclear. Here, through genome-wide CRISPR screens we identify genes that enable mammalian cells to adapt to inactivation of the kinase mechanistic target of rapamycin complex 1 (mTORC1), the central driver of protein synthesis. When mTORC1 is inactive, enzymes that modify tRNAs at wobble uridines (U-enzymes), Elongator and Ctu1/2, become critically essential for cell growth in vitro and in tumors. By integrating quantitative nascent proteomics, steady-state proteomics and ribosome profiling, we demonstrate that the loss of U-enzymes particularly impairs the synthesis of ribosomal proteins. However, when mTORC1 is active, this biosynthetic defect only mildly affects steady-state protein abundance. By contrast, simultaneous suppression of mTORC1 and U-enzymes depletes cells of ribosomal proteins, globally inhibiting translation. Thus, mTORC1 cooperates with tRNA U-enzymes to sustain the protein synthesis machinery and support the high translational requirements of cell growth. - Source: PubMed
Publication date: 2025/05/06
Hermann JuliaBorteçen TomanKalis RobertKowar AlexanderPechincha CatarinaVogt VivienSchneider MartinHelm DominicKrijgsveld JeroenLoayza-Puch FabricioZuber JohannesPalm Wilhelm - JOURNAL/nrgr/04.03/01300535-202606000-00070/figure1/v/2026-02-11T151048Z/r/image-tiff Alzheimer's disease-associated transcriptomic landscapes have been defined in brain tissue. However, changes in blood RNA and their clinical relevance remain poorly understood. In this study, we developed an RNA profile based on 1468 blood samples from both human and mouse studies, which include bulk RNA sequencing (RNA-seq), microRNA-seq, and single-cell RNA-seq data. We developed a comprehensive analysis pipeline that conducted over 11 million comparisons and correlations to identify more than 20,000 blood features. With these findings, we established a blood RNA database related to Alzheimer's disease, RNAs in Blood of AD (RBAD, http://www.bioinform.cn/RBAD/ ). Using RBAD, we initially validated well-established Alzheimer's disease-related pathways, including olfactory transduction. We then observed a decrease in both the proportion and functionality of erythroid cells, likely attributed to their elevated CD45 levels and interactions with GZMK+CD8+ T cells. Furthermore, we identified 449 blood RNAs linked to patients' overall survival, along with two mRNAs ( H4C3 and CTU1 ) associated with cognitive decline. In summary, RBAD is the first web-based analysis platform dedicated to investigating blood RNA changes in Alzheimer's disease, and provides valuable insights into potential peripheral biomarkers and pathogenic mechanisms related to Alzheimer's disease. - Source: PubMed
Publication date: 2025/03/25
Duan TingtingChu JinyuLi JinquanPan ShiyaoLiu DanCheng GuirongLuo YuZhou WenWang ZhimingTan WeiWu QiongZeng YanHu Feifei - Cytosolic thiouridylase is a conserved cytoplasmic tRNA thiolase composed of two different subunits, CTU1 and CTU2. CTU2 serves as a scaffold protein, while CTU1 catalyzes the 2-thiolation at the 34th wobble uridine of the anticodon loop. tRNAGlnUUG, tRNAGluUUC, and tRNALysUUU are the tRNA substrates that are modified with a thiol group at the C2 positions (s2) by CTU1, and also with a methoxycarbonylmethyl group at the C5 positions (mcm5) by Elongator and ALKBH8. mcm5s2U34 modification of the three tRNAs, and their modifying enzymes are involved in human disease and development. Elongator mutant animals exhibit severe phenotypes, while the biological function of Ctu1 in vertebrate animal models remains poorly characterized. Here, we applied antisense morpholino oligonucleotides targeting cytosolic thiouridylase subunit1 (ctu1) transcripts in a zebrafish model and small interfereing RNA against CTU1 transcript in human endothelial cells to define the phenotypes. We found that deficiency of ctu1 causes impaired angiogenesis and development in zebrafish embryos, and CTU1 is involved in proliferation, migration, and tube formation of human endothelial cells. We employed single-cell RNA sequencing to acquire the transcriptomic atlas from ctu1 and control morphant zebrafish. Comprehensive bioinformatics analysis, including pseudo-time, RNA velocity, cell-cell communication, and gene regulatory network inference revealed that ctu1 deficiency leads to the arrest of cell cycle, and the defects of nerve development and erythrocyte differentiation and the attenuation of several pro-angiogenic signaling pathways, e.g., angpt-tek and dll4-notch. Our findings show for the first time that CTU1 is essential for angiogenesis and embryonic development in vertebrates. - Source: PubMed
Publication date: 2024/12/20
Yu YangziweiWang ChuqiaoWang YanShi HengHu HuiyuanDu YibinZhou Zhaoli - Thiolation of uridine 34 in the anticodon loop of several tRNAs is conserved in the three domains of life and guarantees fidelity of protein translation. U34-tRNA thiolation is catalyzed by a complex of two proteins in the eukaryotic cytosol (named Ctu1/Ctu2 in humans), but by a single NcsA enzyme in archaea. We report here spectroscopic and biochemical experiments showing that NcsA from Methanococcus maripaludis (MmNcsA) is a dimer that binds a [4Fe-4S] cluster, which is required for catalysis. Moreover, the crystal structure of MmNcsA at 2.8 Å resolution shows that the [4Fe-4S] cluster is coordinated by three conserved cysteines only, in each monomer. Extra electron density on the fourth nonprotein-bonded iron most likely locates the binding site for a hydrogenosulfide ligand, in agreement with the [4Fe-4S] cluster being used to bind and activate the sulfur atom of the sulfur donor. Comparison of the crystal structure of MmNcsA with the AlphaFold model of the human Ctu1/Ctu2 complex shows a very close superposition of the catalytic site residues, including the cysteines that coordinate the [4Fe-4S] cluster in MmNcsA. We thus propose that the same mechanism for U34-tRNA thiolation, mediated by a [4Fe-4S]-dependent enzyme, operates in archaea and eukaryotes. - Source: PubMed
Publication date: 2023/04/01
Bimai OrnellaLegrand PierreRavanat Jean-LucTouati NadiaZhou JingjingHe NishaLénon MarineBarras FrédéricFontecave MarcGolinelli-Pimpaneau Béatrice