Ask about this productRelated genes to: ETFA antibody
- Gene:
- ETFA NIH gene
- Name:
- electron transfer flavoprotein subunit alpha
- Previous symbol:
- -
- Synonyms:
- GA2, EMA, MADD
- Chromosome:
- 15q24.2-q24.3
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2018-04-23
Related products to: ETFA antibody
Related articles to: ETFA antibody
- The goal of this study is to explore the genetic predictive associations between plasma proteomics and bladder cancer using the Mendelian randomization (MR) method, and to investigate whether plasma lipidomics characteristics mediate these associations. - Source: PubMed
Publication date: 2026/08/29
Cao QianLiu HongyanXu YangyangWang YouzhiAn LiLi JunboRen HaitaoZhou DianshengLiang JiamingGuan ZhaokaiWang WeiweiWu ChangliYang YangWang JianmeiJiang Ning - Fluorinated carboxylate ester solvents are promising electrolyte components for lithium metal batteries because they can improve oxidative stability and promote LiF-rich solid electrolyte interphase (SEI) formation. However, how fluorination position and degree regulate their intrinsic decomposition behavior on lithium metal remains unclear. Herein, density functional theory (DFT) calculations and ab initio molecular dynamics (AIMD) simulations were employed to systematically investigate six pure fluorinated ethyl acetate solvents on the Li(001) surface, including α-fluorinated ethyl fluoroacetate (EFA), ethyl difluoroacetate (EDFA), and ethyl trifluoroacetate (ETFA), as well as β-fluorinated 2-fluoroethyl acetate (FEA), 2,2-difluoroethyl acetate (DFEA), and 2,2,2-trifluoroethyl acetate (TFEA). Electronic-structure analysis shows that although the lowest unoccupied molecular orbitals (LUMOs) of all six solvents are mainly distributed around the carbonyl and adjacent regions, the dominant electron-accepting center strongly depends on the fluorination position. In α-fluorinated solvents, the LUMO is highly localized on the α-C atom directly bonded to fluorine, whereas in β-fluorinated solvents, it remains concentrated around the carbonyl C atom. Real-time Bader charge and bond-evolution analyses reveal that fluorination position is the primary factor governing the initial decomposition pathway. The α-fluorinated series preferentially undergoes C-F bond cleavage, and increasing fluorination degree induces deeper cascade decomposition; fully fluorinated ETFA even exhibits C=O double bond cleavage. In contrast, β-fluorinated solvents preferentially undergo carbonyl-side C-O bond cleavage, while C-F bond cleavage occurs only in subsequent steps or is completely suppressed. Notably, β-fluorinated solvents retain high chemical stability even with α-H atoms because the LUMO electron density on α-H is negligible. Meanwhile, limited deep decomposition can still provide F species for SEI formation. These findings establish an atomic-level structure-reactivity relationship for fluorinated carboxylate ester solvents and provide theoretical guidance for designing stable electrolyte solvents for lithium metal batteries. - Source: PubMed
Publication date: 2026/06/30
Du FumingHu ShutingWang XiaoGu XinLiu JianjunHu Hailong - Based on the magnetic bead "fishing" technology, this study explored the direct targets of the active ingredients of Shuangshen Ningxin Capsules in preventing and treating myocardial ischemia-reperfusion injury. Three active ingredients of Shuangshen Ningxin Capsules, namely dehydrocorydaline, salvianolic acid B, and ginsenoside Rg_1, were selected based on previous work. Firstly, three complexes of magnetic bead-single active ingredient of Shuangshen Ningxin Capsules were synthesized. Then, they were incubated with the protein solutions of SD rat heart tissue, mouse myocardial microvascular endothelial cells, and rat H9c2 cardiomyocytes separately to form magnetic bead-active ingredient-target protein complexes. The target proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE), and then in-gel digestion was performed. The proteins were identified by high-resolution mass spectrometry. Potential target proteins were screened by bioinformatics analysis and molecular docking. A rat model of myocardial ischemia-reperfusion injury was established, and the biological function was verified preliminarily through Western blot experiments. The results showed that three complexes of magnetic bead-TCM monomer were successfully prepared, and the potential direct targets of the three active ingredients of Shuangshen Ningxin Capsules were obtained through the "fishing" method. Through mass spectrometry identification and Kyoto Encyclopedia of Genes and Genomes(KEGG) pathway enrichment analysis, it was found that most of the target proteins were involved in metabolic pathways related to glucose, fatty acids, amino acids, and energy. After Venn analysis and molecular docking, proteins such as electron transfer flavoprotein subunit alpha(ETFA), pyruvate kinase M1/M2(PKM), acyl-CoA dehydrogenase medium chain(ACADM), ATP synthase F1 subunit alpha(ATP5F1A), isocitrate dehydrogenase(NADP~+) 2(IDH2), and aspartyl-tRNA synthetase(DARS) were finally screened out. Through the rat myocardial ischemia-reperfusion injury model, it was found that Shuangshen Ningxin Capsules significantly up-regulated the expression of ATP energy production-related proteins such as ATP5F1A, ETFA, 3-oxoacid CoA-transferase 1(OXCT1), and succinate-CoA ligase GDP-forming subunit beta(SUCLG2). This suggested that restoring mitochondrial energy supply was an important aspect for Shuangshen Ningxin Capsules to exert myocardial protective effects. In conclusion, ATP5F1A, ETFA, OXCT1, SUCLG2, etc. may be the direct targets of the active ingredients of Shuangshen Ningxin Capsules in preventing and treating myocardial ischemia-reperfusion injury. - Source: PubMed
Chen Xiao-XiaoSun Ming-QianGao Yun-XiaoLin LiPeng QingLiu Jian-XunMiao LanRen Jun-Guo - Current therapies for multiple sclerosis (MS) primarily reduce relapse rates and delay disability by targeting inflammation, while have limited efficacy against disease progression driven by neurodegenerative processes. We sought to identify and validate proteins for MS progression by integrating a large genome-wide association study (GWAS) of MS progression with large-scale protein quantitative trait loci data from blood and brain. - Source: PubMed
Publication date: 2026/06/02
Jiang YuanXiao JinyuKockum IngridStridh PernillaLiu QianwenOlsson TomasAlfredsson LarsJiang Xia - Multiple acyl-Coenzyme A dehydrogenase deficiency (MADD) is an inborn error of metabolism affecting fatty acid, amino acid and choline oxidation and is included in newborn screening in Australia. Recent reports describe adults with clinical and biochemical features of MADD, but negative genetic findings, associated with sertraline use. - Source: PubMed
Publication date: 2026/05/17
Barbetti RebeccaColeman KateFraser LouiseDemetriou KalliopeJayadiwangsa ElaineBratkovic DragoSiu Carol Wai-Kwan