ATP5D
- Known as:
- ATP5D
- Catalog number:
- 002194A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- ATP5D
Related genes to: ATP5D
- Gene:
- ATP5F1D NIH gene
- Name:
- ATP synthase F1 subunit delta
- Previous symbol:
- ATP5D
- Synonyms:
- -
- Chromosome:
- 19p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 1993-02-25
- Date modifiied:
- 2017-11-22
Related products to: ATP5D
Antigens ATP5D, 23-168aa, Human, His tag, E.coli, RecombinantATP5B Gene ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptideATP5D antibody Host rabbitATP5D antibody Host rabbitATP5D antibody Host rabbitATP5D antibody Ab host: RabbitATP5D antibody Ab host: RabbitATP5D (23-168, His-tag) antigenATP5D (23-168, His-tag) antigenATP5D (C-term) antibody Isotype Ig Host rabbitATP5D (C-term) antibody Host rabbitATP5D (C-term) Ig antibody Ab host: RabbitATP5D 3&_39;UTR Lenti-reporter-Luc VectorATP5D antibodyATP5D antibody Related articles to: ATP5D
- Post-traumatic stress disorder (PTSD) is highly prevalent among U.S. service members and veterans (SMV) and has lasting impacts on health and well-being. However, the biological underpinnings of PTSD remain poorly characterized. This study aimed to discover novel candidate proteins and protein pathways associated with PTSD using unbiased, high-throughput proteomics profiling. - Source: PubMed
Publication date: 2026/09/15
Lim ArumRobey ClaireKenney KimbraYun SijungYun JosephAlice JohnDark HeatherGill Jessica MLippa Sara M - Focal cortical dysplasia (FCD) is a prevalent cause of drug-resistant epilepsy, but a comprehensive understanding of its pathogenesis at a cellular resolution remains limited. Previous transcriptomic studies, often constrained by bulk tissue analysis, have been unable to dissect the cell-type-specific contributions to epileptogenesis. - Source: PubMed
Publication date: 2025/11/27
Jiang ChaoGao QingyaoZhao YanYou YimingWang ZhuojueWang JianYang GuangGuo ChuangCui Zhiqiang - Amyotrophic lateral sclerosis (ALS) is a terminal neurodegenerative disease, marked by considerable clinical and molecular heterogeneity. While several genetic drivers have been linked to familial ALS (fALS), the biology of sporadic ALS (sALS)-which accounts for the majority of ALS cases-remains poorly defined. To address this gap, we analyzed 247 bulk mRNA-sequenced post-mortem tissue samples from the lumbar spinal cord and motor cortex and compared expression profiles between fALS, sALS, and controls. Variance-stabilized DEGs from DESeq2 analysis were used as inputs for weighted gene co-expression network analysis (WGCNA). Finally, gene ontology was used to identify transcriptomic signatures and biological pathways unique to sALS and fALS. In the spinal cord, sALS samples exhibited specific downregulation of mitochondrial complex I subunits (e.g., NDUFS8 and NDUFB7) and regulatory genes (e.g., AURKAIP1 and ATP5F1D), suggesting compromised metabolic resilience. In the motor cortex, a co-expression module associated with adaptive immune function and leukocyte infiltration was downregulated in sALS yet upregulated in fALS, indicating distinct inflammatory pathways between these two forms of ALS. Together, our findings highlight that while sALS and fALS are largely the same disease, they exhibit distinct transcriptomic signatures. By accounting for mode of inheritance in study designs-particularly sALS, which represents ~90% of ALS cases-researchers may reveal deeper insights into ALS pathology. This perspective could enable more targeted therapeutic strategies, ultimately improving outcomes for all ALS patients. - Source: PubMed
Publication date: 2025/09/22
Awai AlexandriaJohnson Erica LLeng TiandongPatrickson JohnZody Michael CLillard James WOn Behalf Of The Nygc Als Consortium - Atherosclerosis, a chronic inflammatory disorder, is pathophysiologically linked to endothelial cell (EC) pyroptosis. This study aims to elucidate the mechanisms by which succinate exacerbates EC pyroptosis through mitochondrial damage. Serum samples are collected from patients with coronary heart disease (CHD) and healthy controls (HCs), and the levels of succinate, interleukin (IL)-6, and IL-18 are quantified. To establish a succinate accumulation model, human umbilical vein endothelial cells (HUVECs) are treated with diethyl butyl malonate (DEBM), followed by analysis of inflammatory cytokines. The expression of pyroptosis-related proteins is assessed via western blot analysis. Morphological changes in pyroptotic vesicles and membrane pores are examined by scanning electron microscopy (SEM) and transmission electron microscopy (TEM). The mitochondrial membrane potential and reactive oxygen species (ROS) levels are evaluated via a JC-1 kit and MitoSOX, respectively. RNA sequencing (RNA-seq) is performed to identify potential target genes and regulatory pathways. To investigate the functional role of ATP5F1D, small interfering RNAs (siRNAs) are used to knockdown , while lentiviral vectors are used to overexpress ATP5F1D in HUVECs. The results reveal significantly elevated levels of succinate, IL-6, and IL-18 in both CHD patients and DEBM-treated HUVECs. Succinate accumulation induced by DEBM triggers pyroptosis and mitochondrial damage in HUVECs, as evidenced by the upregulation of pyroptosis-related proteins and the impairment of mitochondrial structure and function. RNA sequencing analysis identifies ATP5F1D as a key downstream target of succinate accumulation. Downregulation of ATP5F1D promotes pyroptosis and mitochondrial injury in HUVECs, whereas restoration of ATP5F1D expression effectively mitigates these detrimental effects. Succinate-induced downregulation of ATP5F1D drives mitochondrial dysfunction and pyroptosis in HUVECs. - Source: PubMed
Publication date: 2025/08/15
Huang HongCui JianTang DanXiang XingMao JieHe ZheHu HengjingHe ZhangxiuHe LuTang Huifang - Transmissible gastroenteritis virus (TGEV) infection can down-regulate circBIRC6-2 expression and induce mitochondrial permeability transition pore (mPTP) opening abnormally. BIRC6-236aa, encoded by circBIRC6-2, can suppress mPTP opening by interacting with VDAC1. However, the molecular mechanism of circBIRC6-2 downregulation by TGEV infection is unsuspected, and it is unclear that whether BIRC6-236aa can inhibit mPTP opening by post translational modifications (PTM) and downstream regulatory proteins. In this study, we found that TGEV membrane protein (TGEV-M) can suppress circBIRC6-2 expression by interacting with heterogeneous nuclear ribonucleoprotein A1 (hnRNPA1) and inhibiting the translocation of hnRNPA1, which can bind to baculoviral IAP repeat containing 6 (birc6) pre-mRNA to promote the formation of circBIRC6-2. In addition, glycogen synthase kinase-3 beta (GSK-3β) can phosphorylate Ser180 of BIRC6-236aa, and phosphorylated-BIRC6-236aa (p-BIRC6-236aa) can inhibit mPTP opening. 271 differential expression proteins (DEPs) were identified after overexpression of BIRC6-236aa. ATP synthase, H transporting, mitochondrial F1 complex, delta subunit (ATP5D, also named ATP5F1D), one of the DEPs was down-regulated in response to BIRC6-236aa, and ATP5D can promote mPTP opening induced by TGEV. In conclusion, TGEV-M can suppress the expression of circBIRC6-2 through targeting hnRNPA1. The Ser180 of BIRC6-236aa encoded by circBIRC6-2 can be phosphorylated by GSK-3β, and p-BIRC6-236aa can inhibit mPTP opening by down-regulating ATP5D expression. - Source: PubMed
Publication date: 2025/06/13
Guo JianxiongChang LinglingZhang FengxiDang XingyiZhang XiangyinZhang FenliZhao XiaominTong Dewen