Ask about this productRelated genes to: CDC45L antibody
- Gene:
- CDC45 NIH gene
- Name:
- cell division cycle 45
- Previous symbol:
- CDC45L2, CDC45L
- Synonyms:
- -
- Chromosome:
- 22q11.21
- Locus Type:
- gene with protein product
- Date approved:
- 1998-09-08
- Date modifiied:
- 2014-11-19
Related products to: CDC45L antibody
Related articles to: CDC45L antibody
- Non-small cell lung cancer (NSCLC) remains a leading cause of cancer-related mortality worldwide, with limited therapeutic efficacy due to tumor heterogeneity in conventional treatments. In the present study, an integrative, network pharmacology approach was employed to elucidate the multi-target mechanism of action of phytochemicals derived from Glossocardia bosvallia against NSCLC. Among 38 phytocompounds identified, 31 compounds that satisfied pharmacokinetic properties were selected for subsequent analysis. Ligand-based target prediction identified 429 potential protein targets, which are integrated with the top 250 differentially expressed genes obtained from the GSE33532 dataset. Intersection analysis identified eight therapeutic targets: PTGES, SRD5A1, CDK1, KIF11, TOP2A, CDC45, MB, and CHEK1. Protein-protein interaction and enrichment analyses demonstrated that these targets are predominantly involved in cell cycle regulation, mitotic cell cycle, and DNA replication pathways. Gene expression analysis demonstrated significant overexpression of the prioritized targets in NSCLC tissues, while survival analysis identified CHEK1 as the gene significantly associated with survival (p < 0.05). Molecular docking identified TOP2A_quinic acid as the most favorable complex, exhibiting a binding affinity of -12.27 kcal/mol, KIF11_linoleic acid as -12.10 kcal/mol and CHEK1_2,3-dihydro-3,5-dihydroxy-6-methyl-4h-pyran-4-one as -6.75 kcal/mol, which was further validated by dynamic simulations, principal component analysis based free energy landscape, and DSSP analysis, confirming the stability of the protein. This integrative framework provides a robust strategy for identifying biologically relevant and therapeutically actionable targets supporting the potential of G. bosvallia-derived phytochemicals as promising candidates for NSCLC. - Source: PubMed
Publication date: 2026/08/04
Kulandhaivel Soundar RajanStalin AntonyMuthuramalingam PandiyanSivaprakasam BalasubramanianJesudass Joseph Sahayarayan - Cervical cancer remains a major global health challenge, particularly in low-resource settings where treatment efficacy is limited by drug resistance and toxicity. Although (Sanqi) has demonstrated anticancer activity, its molecular mechanisms against cervical cancer remain insufficiently understood. - Source: PubMed
Publication date: 2026/07/10
Kamal ShahQin ChenWang YanjuanHe RuilinAmjad Kamal MohammadLi Wenji - We describe the anatomy of replication forks by detecting proteins associated with DNA replication (Cdc45 and RPA), DNA damage (H2A.X), and DNA repair (Rad51) relative to tracts of synthesized, 5'-bromodeoxyuridine (BrdU)-labeled DNA on chromatin fiber images. These fibers track pixel intensity and positional data, which are analyzed using our program: R-ODD-BLOBS (One Dimensional Data Boolean Logic Operations Binning System in the programming language R). We studied the effect of threshold and signal smoothing for BrdU and protein tracts following hydroxyurea in wild type fission yeast (), compared to DNA replication checkpoint mutants and . We show that R-ODD-BLOBS allows robust analysis of BrdU lengths and that Rad51, Cdc45, RPA, and H2A.X show distinctive, checkpoint-dependent locations around replicated tract ends. Rad51 was found at 22% more replicated areas in than in wild type, suggesting that homologous recombination repair may be more common at forks. Helicase detachment in post-HU was indicated by Cdc45 enrichment in unreplicated chromatin close to putative forks. Similarly, fibers show that Rad51, RPA, and H2A.X are distributed upstream of replicated areas more than in wild type. Excitingly, we find that H2A.X is distributed asymmetrically around replication forks, suggesting that the fork complex is a barrier for DNA damage signal extension into replicated areas. Together, R-ODD-BLOBS analysis shows a rigorous, iterative computational analysis tool to assess large chromatin spread datasets. R-ODD-BLOBS finds patterns of DNA replication length and protein components at replication forks that describe the anatomy of a fork and how structures change after replication checkpoint loss. - Source: PubMed
Publication date: 2026/07/22
Cheng KerenzaAliar KazeeraManshaei RoozbehForsburg Susan LMazalek AliSabatinos Sarah A - Wilms tumor (WT) is a prevalent pediatric renal malignancy, yet its molecular mechanisms remain poorly defined. Identifying key prognostic genes and understanding their functional roles is critical for improving clinical management. This study aimed to identify prognostic genes in WT and to investigate whether ATP5F1A functions as a candidate downstream effector in a CDCA8-associated regulatory axis. - Source: PubMed
Publication date: 2026/07/21
Zeng QiangTao JunfengPeng GuangbeiQin LiluWu ShuzhenWang ChenLiu ZhongZeng Linshan - Mammalian cells frequently enter mitosis before DNA replication has finished, necessitating the rapid processing of unreplicated loci to facilitate chromosome segregation. The TRAIP ubiquitin ligase induces replisome disassembly during mitosis, triggering the cleavage of DNA replication forks. Until now, the mechanisms that regulate TRAIP and process cleaved DNA replication forks were unclear. In this study, we show that the transcription termination factor 2 (TTF2) adenosine triphosphatase is a new type of phosphoreceptor that binds a conserved phosphorylation site on TRAIP during mitosis. TTF2 couples phosphorylated TRAIP to DNA polymerase ε (Pol ε) in the replisome, leading TRAIP to ubiquitylate the CDC45-MCM-GINS (CMG) helicase. This triggers mitotic replisome disassembly and a repair pathway that produces sister-chromatid exchanges, supporting a model for how fork cleavage promotes the segregation of underreplicated loci in mammalian cells. - Source: PubMed
Publication date: 2026/08/13
Fujisawa RyoLabib Karim P M