Methamphetamine, Card
- Known as:
- Methamphetamine, Card
- Catalog number:
- BQ 041-RTDA
- Product Quantity:
- 1/kit (x30)
- Category:
- -
- Supplier:
- Bioquant
- Gene target:
- Methamphetamine Card
Related genes to: Methamphetamine, Card
- Gene:
- MAVS NIH gene
- Name:
- mitochondrial antiviral signaling protein
- Previous symbol:
- -
- Synonyms:
- VISA, KIAA1271, IPS-1, Cardif
- Chromosome:
- 20p13
- Locus Type:
- gene with protein product
- Date approved:
- 2009-04-01
- Date modifiied:
- 2017-09-22
Related products to: Methamphetamine, Card
Related articles to: Methamphetamine, Card
- Ovarian cancer remains a leading cause of gynecologic cancer mortality, largely due to high recurrence and frequent cisplatin resistance. This study investigates the role of ADAR1 lactylation-mediated RNA editing in ovarian cancer chemoresistance. Cisplatin-resistant cells exhibit significantly elevated global adenosine-to-inosine (A-to-I) RNA editing and ADAR1 expression. Genetic knockdown of ADAR1 enhances cisplatin sensitivity in vitro and in vivo, activates innate immune MAVS/PKR pathways, and promotes CD4⁺/CD8⁺ T cell infiltration. Mechanistically, Tip60 mediates ADAR1 lactylation, facilitating its interaction with deubiquitinase USP48 to stabilize ADAR1. Lactylation-dependent ADAR1 upregulation suppresses innate immunity and enhances protein translation, driving chemoresistance. Notably, inhibitor ZYS-1 targets ADAR1 lactylation, reducing ADAR1 expression, activating antitumor immunity, and synergizing with cisplatin to delay tumor growth in mice. These findings establish ADAR1 lactylation as a critical regulatory mechanism, supporting ZYS-1 plus cisplatin as a promising strategy for platinum-resistant ovarian cancer. - Source: PubMed
Publication date: 2026/05/25
Cui LinluYi QihuaTang ChunyanGu QiuyingLuo QingyaLuo XinLuo FataoLi LiLiu TaoYi Ping - PACT (PKR activating protein)/PRKRA is a quintessential double-stranded RNA (dsRNA) binding protein that has recently surfaced as a novel and compelling antiviral target, exhibiting resistance against a spectrum of respiratory viruses. Despite this, no antiviral ligand compounds targeting PACT have been identified to date. In this study, we conducted an extensive screening within natural products, leading to the development of an exceptional PACT-T78 site ligand, tubeimoside II (TBM II). TBM II effectively combats a spectrum of respiratory viruses, including the coronaviruses HCoV-OC43 and SARS-CoV-2, as well as the influenza A H1N1 virus (IAV-H1N1), by reducing viral loads and inhibiting viral replication and proliferation both and . Single-cell RNA sequencing demonstrated that TBM II significantly impacts the RIG-I signaling pathway associated with PACT. We found that when PACT was knocked down or when RIG-I, MAVS, or IFN- were knocked out, the ability of TBM II to activate the RIG-I signaling pathway was diminished, resulting in a corresponding attenuation of its antiviral efficacy. These findings indicated that TBM II targets PACT to activate the RIG-I signaling pathway, thereby increasing the secretion of type I interferon IFN-, ultimately promoting the innate immune response and achieving antiviral efficacy. In summary, our work identified TBM II as a new generation PACT ligand that activating the RIG-I signaling pathway, achieving broad-spectrum antiviral effects. - Source: PubMed
Publication date: 2026/03/14
Liu XianXie DanCui MengyaoLi ShuranYang XiaoweiZhang JuanZhang YuCao ShanBao LeiGeng ZihanSun JingZhao RonghuaGao ShuangrongCui XiaolanSun ChengpengGuo Shanshan - Melanoma differentiation-associated gene 5 (MDA5) is a prime member of the RIG-I-like receptor (RLR) family that recognises viral RNA in the cytoplasm and triggers antiviral innate immunity mainly via the MAVS-dependent signalling cascade. This study reports the molecular cloning and characterization of MDA5 in Labeo rohita (LrMDA5), a commercially important major carp in India and Southeast Asia. The LrMDA5 has 3000bp open reading frame (ORF) encoding a 1000-amino acid protein of molecular weight (mw) 240.764kDa and isoelectric point (pI) of ∼4.84. It's structural domain analysis identified two CARDs, a DEXDc, a helicase, and a C-terminal domain. Phylogenetically, LrMDA5 is closest to the Cyprinus carpio, and the ontogenic expression profiling revealed maximal expression at neurula stage {12hours post-fertilization (h.p.f)}. It was ubiquitously expressed across all tested organs/tissues, and in specialised cells such as mucosal RBCs (red blood cells) and PBLs (peripheral blood leukocytes). LrMDA5 gene transcripts along with its adaptor molecule, MAVS, and the cytokines (IL-8 and IL-1β) gene expression were significantly upregulated both in-vivo and in-vitro against poly I:C and LPS-stimulations, and infections with Aeromonas hydrophila and Edwardsiella tarda. These data together highlight the important immune role of MDA5 in fish. - Source: PubMed
Publication date: 2026/05/23
Pani SaswatiGanguly BristySamanta Mrinal - Chemotherapy-induced neuropathic pain (CINP) can be triggered by microtubule-targeting agents, including plant-derived vinca alkaloids such as vincristine (VCR). In a male mouse model of VCR-induced neuropathic pain (VINP), mitochondrial antiviral signaling protein (MAVS) expression was upregulated in the spinal cord. Suppression of MAVS significantly increased the pain threshold, alleviated persistent vincristine-induced hyperalgesia, and ameliorated mitochondrial damage in the spinal cord. Through bioinformatic analysis, transcription factor 12 (TCF12) was identified as a transcription factor with high binding potential to the MAVS gene promoter. Dual-luciferase reporter and electrophoretic mobility shift assays (EMSA) confirmed that TCF12 binds to the MAVS promoter region and promotes its transcriptional activation. Furthermore, immunofluorescence double staining demonstrated TCF12 localization in spinal astrocytes of VCR-treated male mice. Knockdown of TCF12 via siRNA attenuated chemotherapy-induced mechanical allodynia and thermal hyperalgesia, and reduced MAVS expression. Notably, in VCR-treated primary astrocytes, GFAP fluorescence intensity was increased and showed enhanced co-localization with TCF12. Silencing either TCF12 or MAVS elevated the mitochondrial membrane potential in primary mouse astrocytes and reduced the levels of pro-inflammatory cytokines such as TNF-α, IL-1β, and CXCL1. In summary, our study reveals that the TCF12-MAVS signaling axis plays a critical role in the development of VINP. Inhibition of this pathway alleviates neuropathic pain and mitochondrial injury caused by chemotherapeutic agents, providing new potential targets and molecular insights for the prevention and treatment of VINP. - Source: PubMed
Publication date: 2026/05/20
Zhou LinLi XiaoLiu HangLi YihengQian MingYang Hui - The matrix protein 2 (M2) is one of the most representative and widely studied ion channel proteins, which plays broad biological roles in the life cycle of the influenza A virus. The M2 protein affects the function of host cells and the regulation of cellular homeostasis in an ion channel activity-dependent or-independent manner and it is also the target for anti-influenza virus drugs, such as amantadine and rimantadine. The focus of this review is to summarize the research progress on the M2 protein, such as structure and function, vaccine and drug development as well as antagonist of host innate immune responses. A particular emphasis is placed on the multifaceted roles of M2 beyond canonical ion conduction. Specifically, M2 modulates the MAVS pathway through direct interaction with MAVS and by inducing ROS production, which amplifies interferon-mediated inflammation while paradoxically disrupting autophagic degradation of MAVS aggregation. Concurrently, the M2 protein orchestrates autophagy regulation by inhibiting autophagosome-lysosome fusion and initiating AKT-mTOR signaling, thus stabilizing the viral polymerase to enhance viral replication. A comprehensive understanding of these mechanisms is essential for advancing universal M2-based vaccine strategies and novel host-directed antiviral therapies. - Source: PubMed
Publication date: 2026/05/20
Ren WeigangWang QinYi YongxiangLi Junwei