FEN1, 1_380aa, Human, E.coli
- Known as:
- FEN1, 1_380aa, Human, E.coli
- Catalog number:
- ATGP0442
- Product Quantity:
- 0.5mg
- Category:
- -
- Supplier:
- ATGen
- Gene target:
- FEN1 1_380aa Human .coli
Related genes to: FEN1, 1_380aa, Human, E.coli
- Gene:
- FCN2 NIH gene
- Name:
- ficolin 2
- Previous symbol:
- -
- Synonyms:
- P35, FCNL, EBP-37, ficolin-2
- Chromosome:
- 9q34.3
- Locus Type:
- gene with protein product
- Date approved:
- 1996-07-11
- Date modifiied:
- 2016-10-05
- Gene:
- FEN1 NIH gene
- Name:
- flap structure-specific endonuclease 1
- Previous symbol:
- RAD2
- Synonyms:
- FEN-1, MF1
- Chromosome:
- 11q12.2
- Locus Type:
- gene with protein product
- Date approved:
- 1995-02-03
- Date modifiied:
- 2016-10-05
Related products to: FEN1, 1_380aa, Human, E.coli
Related articles to: FEN1, 1_380aa, Human, E.coli
- Rolling circle amplification (RCA) is a powerful isothermal nucleic acid amplification technique, yet its specificity is often compromised because padlock probes can be circularized even with imperfectly matched targets, leading to false-positive signals. Herein, we report a strand displacement-assisted FEN1 cleavage strategy to substantially improve the specificity of RCA. A dumbbell-shaped padlock probe is designed to generate dual 5' flaps only upon perfect hybridization with the target. Flap endonuclease 1 (FEN1) specifically recognizes the three-base overlap structure and cleaves the 5' flaps, enabling stringent single-base mismatch discrimination over a recognition length exceeding 23 base pairs. After FEN1 cleavage, the padlock is circularized by T4 DNA ligase, followed by RCA triggered by primer-conjugated magnetic beads. The RCA products form G-quadruplex structures that bind thioflavin T (ThT) for fluorescence readout. The method achieves excellent sensitivity for breast cancer-related biomarkers, with detection limits of 0.61 fM for hsa-miR-2682 and 1.13 fM for hsa_circ_0131242, along with high specificity (single-base resolution), good reproducibility (CV < 5%), and satisfactory recovery (95.1-101.5%) in serum. Clinical validation using 15 breast cancer patient samples and 15 healthy controls shows that the method reliably recapitulates differential expression of hsa_circ_0131242, with results highly consistent with RT-qPCR. By overcoming the inherent specificity limitation of conventional RCA, this FEN1-assisted, strand displacement-enhanced strategy provides a sensitive, reliable, and versatile platform for RNA biomarker analysis, holding great promise for early diagnosis of breast cancer and other diseases. - Source: PubMed
Publication date: 2026/06/17
Li YuetingShi Pengxu - Synthetic lethality (SL) underlies the success of PARP1 inhibitors (PARPi) in treating homologous recombination (HR)-deficient cancers, yet their broader applicability beyond HR deficiency remains poorly defined. Here, we performed an in vivo CRISPR screen that identifies FANCA deficiency as a driver of tumor progression and PARPi SL, validated across diverse human cancer models. Notably, FANCA loss does not impair HR but instead disrupts FEN1 recruitment to replication forks, leading to defective Okazaki fragment maturation, lagging-strand single-strand DNA gap accumulation, and RPA exhaustion upon PARPi treatment. Additionally, FANCA loss in oncogene-expressing cells promotes transcription-replication conflict (TRC) accumulation selectively on the lagging strand and sensitizes HR-proficient cells to PARPi, a phenotype reversible by RNA polymerase II inhibition or RNase H overexpression. Together, these findings identify FANCA deficiency as a context-specific PARPi vulnerability and establish FANCA as a key suppressor of TRCs required for genomic stability under oncogenic replication stress. - Source: PubMed
Publication date: 2026/06/16
Wang QinhongEllington Simon WGuerra PaoloGharibpoor FaezeSimpson Dennis ACho Min-GukBeltran AdrianaGupta Gaorav P - Non-alcoholic fatty liver disease (NAFLD) is one of the most common chronic liver disorders and has been linked to oxidative stress. Therefore, it can be hypothesized that NAFLD may be associated with genes encoding proteins involved in the base-excision repair (BER) pathway. Moreover, mitochondrial dysfunction plays a significant role in the development of NAFLD. In light of these observations, we suggested that fatty liver may be associated with genes that encode proteins responsible for mitochondrial DNA (mtDNA) degradation. This study evaluates single-nucleotide polymorphisms (SNPs) within the , , , , , and genes in 99 patients and 104 controls. SNP genotyping was performed using TaqMan probes and the findings were presented as odds ratios with corresponding 95% confidence intervals. Each of the eight investigated SNPs was found to modulate the risk of NAFLD occurrence. The analysis revealed that the studied haplotypes of and significantly affected the frequency of NAFLD in patients. The findings allow us to assume that there is a link between , , , , , and and liver steatosis. We believe that the impaired repair and degradation of damaged mtDNA may have a significant impact on the development of NAFLD. - Source: PubMed
Publication date: 2026/05/28
Ziółkowska SylwiaKosmalski MarcinKołodziej ŁukaszJarmusz KingaEjsmont MagdalenaPietras TadeuszJabłkowska AleksandraJabłkowski MaciejSzemraj JanuszCzarny Piotr - Flap endonuclease 1 (FEN1) removes 5'-flaps from double-flap DNA junction intermediates during replication and repair. Substrate recognition and reaction site selection depend on two intrinsically disordered regions: the α4-α5 helical arch, through which the 5'-flap threads prior to catalysis, and the adjacent 3'-flap binding pocket, which allosterically signals disorder-to-order transition of the arch upon sensing a 3'-flap, committing the enzyme-DNA complex towards reaction. The phosphate steering hypothesis proposes that conserved, positively charged amino acids in α4/α5 facilitate passage of 5'-flap DNA through the arch during threading and position the target phosphate diester for hydrolysis; however, supporting evidence is limited and mechanistic details are currently lacking. We investigated functional roles for these residues using kinetic and spectroscopic methods, finding that alanine substitutions of Arg103, Arg104, Arg129 and Lys132 modestly reduce the catalytic rate and the stability of 5'-flap threading. Following arch ordering, distortion of the reacting DNA duplex is necessary for active site transfer of the target cut site, and we identified key roles in this process for two substrate-facing residues from α5, Lys125 and Arg129. Concurrently, 'back-of-arch' residues Arg104 and Lys132 contact the +1 phosphate to precisely position the target phosphodiester for hydrolysis. Helicity-disrupting mutations in α4/α5, designed to impair ordering, reduced the catalytic rate and severely inhibited allosteric signalling of 3'-flap recognition to the active site. These findings define critical functional roles for phosphate steering residues in the FEN1 mechanism, and inform a deeper understanding of how coordinated substrate verification optimises targeting specificity to preserve genome integrity. - Source: PubMed
Publication date: 2026/06/04
Thompson Mark JShahari Nur Nazihah B MdOuanounou Reuben JGittens NathanCiani BarbaraFinger L DavidGrasby Jane A - Arsenic poisoning significantly elevates the risk of cancer and other chronic illnesses. The goal of this research is to identify important genes whose expression changes in response to arsenic toxicity, and the molecular pathways affected by arsenic, using computational analysis of arsenic toxicity profiles. This approach will computationally identify and analyze genes whose expression changes in response to arsenic, thereby elucidating the heightened risk of carcinogenesis in arsenic-exposed individuals. This work employed high-throughput arsenic toxicity profiles to computationally identify and analyze expressed genes (DEGs) differentially in Affymetrix microarray datasets from the Gene Expression Omnibus (GEO) database, which were screened using the GEO2R program. A protein-protein interaction (PPI) network was constructed using STRING to elucidate the functional links between these DEGs and DNA repair genes. Interactions between the seven central genes (E2F1, EXO1, EZH2, FEN1, HIST1H3A, POLA1, and TIMELESS) and the repair genes PARP1, NBN, PMS1, MSH3, XRCC5, XRCC6, MGMT, and MLH1 were discovered. We employed the DAVID and Enrichr-KG platforms to investigate the functions of these genes and their associations with cellular and molecular processes in greater detail. Two hundred eighty-one non-synonymous single-nucleotide polymorphisms (nsSNPs) in the 07 genes linked to arsenic toxicity were found using the COSMIC database. Based on our analysis, mutations in E2F1, EXO1, EZH2, FEN1, HIST1H3A, POLA1, and TIMELESS can hinder DNA repair mechanisms, ultimately leading to cancer. Our computational analysis demonstrated that these non-synonymous SNPs can affect gene function, potentially altering protein stability and activity. Furthermore, according to Metal-Protein docking and protein-protein docking, these genes and their mutations appear to affect interactions with repair proteins substantially. Specific dietary consumption may lessen the detrimental effects of arsenic poisoning on protein function. We hypothesized that the mutations might be reversed by attaching particular molecules to these mutants. The protective effects of six curcumin compounds were examined using molecular docking with AutoDock 4.2.6 to assess protein dynamics and binding interactions. Optimal complexes were selected for dynamics simulation using GROMACS, and potential strategies for long-term cancer prevention related to arsenic exposure were identified. - Source: PubMed
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