Ask about this productRelated genes to: CDCA5 Blocking Peptide
- Gene:
- CDCA5 NIH gene
- Name:
- cell division cycle associated 5
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 11q13.1
- Locus Type:
- gene with protein product
- Date approved:
- 2002-04-03
- Date modifiied:
- 2014-11-19
Related products to: CDCA5 Blocking Peptide
Related articles to: CDCA5 Blocking Peptide
- Intrauterine adhesions (IUA) are fibrotic scars that impair endometrial regeneration, and compromise fertility. Emerging evidence implicates circular RNAs (circRNAs) in fibrotic remodeling, but it remains unclear how the circRNA landscape and circRNA-associated splicing programs coordinately link uterine contractility, endometrial cell-cycle control, and immune activation in IUA. - Source: PubMed
Publication date: 2026/05/07
Chen YingqingJin JingXiang YingWang YanpingWu ShuangZhan NiXiong MengxinDeng Ali - The synaptonemal complex (SC) is a highly ordered proteinaceous structure that assembles between homologous chromosomes during the prophase I of meiosis. Conserved as a tripartite architecture across species, the SC plays a central role in chromosome synapsis, meiotic recombination, and faithful chromosome segregation. This review marks the 70th anniversary of the discovery of the synaptonemal complex by Montrose Moses in 1956. In mammals, the SC is composed of eight core (canonical) structural proteins: SYCP1, SYCP2, SYCP3, SYCE1, SYCE2, SYCE3, SIX6OS1, and TEX12. The archetypal SC consists of two lateral elements (SYCP2 and SYCP3), a central element (SYCE1/2/3, SIX6OS1, and TEX12), and numerous transverse filaments (SYCP1). A shared structural feature of SC components is the presence of coiled-coil domains. Although the tripartite organization of the SC is evolutionarily conserved, its constituent proteins exhibit little to no sequence homology across species. In addition to these core components, a number of proteins, including HORMAD1, HORMAD2, TRIP13, SKP1, CDCA5 (Sororin), UBE2I (UBC9), SYCP2L, HSPA2, PSMA8, and FKBP6, associate with the SC. Beyond serving as a structural scaffold essential for homolog synapsis, SC proteins interact with key recombination factors such as DMC1, RAD51, and TEX11, thereby regulating recombination progression and crossover formation. Genetic, biochemical, and structural analyses of SC components have provided important mechanistic insights into SC assembly and function, as well as their clinical relevance to non-obstructive azoospermia (NOA) and premature ovarian insufficiency (POI) in humans. - Source: PubMed
Publication date: 2026/04/30
Yang FangWang P Jeremy - The cohesin complex mediates sister-chromatid cohesion by topologically entrapping DNA within an SMC1-SMC3-RAD21 ring, yet how Sororin preserves cohesion beyond its known role of antagonizing Pds5 binding to the release factor Wapl has remained unclear. Here, we show that the extreme C-terminal region (CTR) of Sororin functions as a direct structural lock for cohesin's DNA-exit gate by engaging the RAD21-SMC3 interface. Centromere-tethered Sororin-CTR fully restores cohesion after Sororin depletion, whereas constitutive chromatin tethering prevents cohesin removal, recapitulating Wapl-loss phenotypes, including impaired mitotic chromosome condensation, decatenation and segregation. Through biochemical reconstitution, AlphaFold3-guided modeling, and targeted mutagenesis, we define conserved hydrophobic and electrostatic contacts between Sororin-CTR and the RAD21-SMC3 gate, the disruption of which abolishes cohesion in a Wapl-dependent manner. Furthermore, mitotic phosphorylation of Sororin selectively disrupts Pds5 binding while leaving gate engagement intact, providing a regulated molecular switch for cohesin release. Together, these findings redefine Sororin as a dual-function regulator that both antagonizes Wapl-Pds5 and directly locks the RAD21-SMC3 exit gate to stabilize sister-chromatid cohesion while permitting its timely dissolution. - Source: PubMed
Publication date: 2026/03/10
Chen QinfuYuan XueyingShi MiaoZhou XinyuZhu ShukaiLu WeiguoYan HaiyanWang Fangwei - Lapatinib is a dual EGFR/HER2 tyrosine kinase inhibitor used in HER2-positive breast cancer (BC). Here, we identified prognostic genes modulated by lapatinib and evaluated whether glucose-functionalized, lapatinib-conjugated silver nanoparticles could enhance its anticancer efficacy. - Source: PubMed
Publication date: 2026/02/26
Dolatabadi BehnazPeymani MaryamHashemi MehrdadRouhi LeilaSalehzadeh AliZarrabi Ali - Pancreatic ductal adenocarcinoma (PDAC) is a lethal cancer with five years survival rate less than 5%. In Pakistan, transcriptomic profiling of pancreatic cancer is limited, with most evidence derived from in silico and isolated NGS analyses, highlighting the need for RNA-sequencing-based expression profiling in Pakistani PDAC cohorts. The purpose of this study is to report hub genes that are involved in progression of cancer and can be used as diagnostic and therapeutic markers. Pakistani PDAC RNA-seq dataset was pooled with seven publicly available NCBI-GEO datasets (GSE136569, GSE119794, GSE164665, GSE119224, GSE211398, GSE196009, and GSE40174) to probe common hub genes. The expression of these hub genes in tumor samples was evaluated using Reverse Transcription Quantitative Polymerase Chain Reaction (RT-qPCR) and validated through Whole Exome Sequencing. CDC20, PLK1, BUB1, CDC45, and CDCA5 were concordantly present in seven NCI-GEO Datasets along with Pakistani RNA-seq dataset. These hub genes were upregulated at the initial stages of PDAC. RT-qPCR revealed significant upregulation in Pakistani tumor samples (*P < 0.05, **P < 0.001). WES analysis demonstrates non synonymous pathogenic variants in BUB1. The consistent dysregulated expression of the hub genes across independent NCBI-GEO datasets and the Pakistani RNA-seq cohort suggests their possible robustness across diverse populations and potential utility as broadly applicable biomarkers. These findings offer population-specific insights that may inform future biomarker-guided diagnostic and prognostic stratification of PDAC in Pakistan. - Source: PubMed
Publication date: 2026/02/17
Naeem MaryamQadeer KainatJabeen IshratAhmed IbrarMurtaza IramFarooq JaveriaSultan Aneesa