ATF5 antibody - N-terminal region (P100653_P050)
- Known as:
- ATF5 (anti-) - N-terminal region (P100653_P050)
- Catalog number:
- p100653_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- ATF5 antibody - N-terminal region (P100653_P050)
Related genes to: ATF5 antibody - N-terminal region (P100653_P050)
- Gene:
- ATF5 NIH gene
- Name:
- activating transcription factor 5
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 19q13.33
- Locus Type:
- gene with protein product
- Date approved:
- 2000-03-22
- Date modifiied:
- 2014-11-19
Related products to: ATF5 antibody - N-terminal region (P100653_P050)
Related articles to: ATF5 antibody - N-terminal region (P100653_P050)
- Tumor-associated macrophages (TAMs) are key components of the tumor immune-suppressive microenvironment. However, studies focusing on the modulation of TAM-specific gene signatures to improve neuroblastoma (NB) prognosis are limited. MYCN amplification (MNA) is known to influence the immune landscape in neuroblastoma. - Source: PubMed
Publication date: 2026/08/01
Huang YanhuaGao ZiyangLiang WenqiangSu ZhenchaoMo YuemeiWu Huangjian - Multiple myeloma (MM) is a heterogeneous hematological malignancy characterized by the clonal proliferation of plasma cells in the bone marrow, with distinct subtypes including smoldering MM (SMM), newly diagnosed MM (NDMM), and relapsed/refractory MM (RRMM). Despite therapeutic advances, outcomes remain unsatisfactory, especially for RRMM, due to unclear heterogeneity, progression mechanisms, and crosstalk between tumor cells and the bone marrow microenvironment (BMME) via direct interactions or extracellular vesicles (EVs). - Source: PubMed
Publication date: 2026/07/15
Fan LuZhao HanCong MengyaZhang MengxiaoRouzi TuerxunayiXie BeibeiDai JifeiBao Weiying - This study aimed to explore the intra- and inter-tumoral heterogeneity, gene expression profiles, tumor microenvironment (TME) alterations and the potential of therapeutic marker discovery in endometrial cancer (EC). - Source: PubMed
Publication date: 2026/07/15
Zhong ShanliangLiu JianyaoXu HanziLv JuanLi HuixinHu HuanhuanXiao ShuyueXie XinyiLi YueWu YinanWu WangfeiGong Zhen - Mitochondrial dysfunction, impaired proteostasis, and reduced stress resistance and resilience are aging hallmarks. At the core of these hallmarks, the mitochondrial unfolded protein response (mtUPR) is a transcriptional pathway that restores mitochondrial proteostasis in response to proteotoxicity. Although the mtUPR is well studied in invertebrates and cell culture models, how the mtUPR is engaged in aged mammalian tissue is poorly defined. Here, we defined the extent to which repeated physical stress initiates mtUPR transcription in aged mouse skeletal muscle and assessed candidate regulatory mechanisms in vivo. Aged muscle exhibited reduced mitoprotective chaperone and protease availability and greater carbonylation of intermyofibrillar mitochondria relative to young muscle, suggesting diminished proteostatic reserve and increased oxidative burden. Short-term physical stress induced a greater initiation of mtUPR genes in aged muscle than young muscle, coinciding with reduced physiological reserve. Physical stress shifted ATF5 localization from the mitochondria to the nucleus in the muscle of both ages, whereas CHOP mRNA and nuclear localization were selectively elevated in aged muscle. Mechanistically, we show mitochondrial reactive oxygen species (mtROS) contribute to mtUPR initiation in aged skeletal muscle. Using in vivo ChIP-qPCR and in vitro knockdown/inhibition experiments, we provide support for CHOP as a redox-sensitive factor contributing in part to the enhanced mtUPR initiation in aged mouse muscle, potentially linked to JNK signaling. Collectively, these data suggest reduced mitochondrial proteostatic reserve and mtROS signaling in aged muscle contribute to an amplified mtUPR transcriptional response following repetitive physical stress, providing the foundation to explore the mtUPR in mammalian aging. - Source: PubMed
Laskin Grant RMazonson Baylah RThompson LaDora V - Mitochondrial proteotoxic stress activates the mammalian UPR through a multilayered mechanistic architecture rather than a linear pathway. At its core lies an import-gated sensing logic: reduced preprotein import and mito-nuclear stoichiometric imbalance activates the integrated stress response (ISR) toward the translation of ATF4, CHOP, and the mitochondria-targeted transcription factor ATF5. These factors cooperatively reprogram transcription to expand the chaperone-protease capacity while transiently reducing the nuclear-encoded OXPHOS load. Parallel translational mechanisms that include eIF2α-dependent repression, stress-granule triage, and miRNA-driven selective silencing reduce the mitochondrial precursor import and maintain proteostatic symmetry between the cytosol and mitochondria. Within the organelle, LONP1- and CLPP-dependent proteolysis, mitoribosome pausing, and tRNA-processing checkpoints further dampen nascent chain pressure. Epigenetic licensing by demethylases and acetyltransferases links metabolic and bioenergetic status to promoter accessibility at UPR loci. Together, these import-gated, translational, and epigenetic control layers form a coherent mechanistic circuit ensuring that mitochondrial recovery is matched to folding, assembly, and metabolic capacity. We propose a unified framework explaining how these layers cooperate to determine adaptive versus maladaptive outcomes. - Source: PubMed
Publication date: 2026/05/29
Czechowicz PaulinaWięch-Walów AnnaKozioł SylwiaDudzik JakubCollawn James FBartoszewski Rafal