MCM7 Antibody
- Known as:
- MCM7 Antibody
- Catalog number:
- 32176
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Signalway
- Gene target:
- MCM7 Antibody
Related genes to: MCM7 Antibody
- Gene:
- MCM7 NIH gene
- Name:
- minichromosome maintenance complex component 7
- Previous symbol:
- MCM2
- Synonyms:
- CDC47, PPP1R104
- Chromosome:
- 7q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 1994-12-13
- Date modifiied:
- 2016-10-05
Related products to: MCM7 Antibody
Related articles to: MCM7 Antibody
- During eukaryotic DNA replication initiation, inactive MCM2-7 double-hexamers assembled at replication origins must be converted into two active CMG helicases, yet how this transition is coupled to origin DNA unwinding in vivo remains unclear. Here, we identify a DNA-bound intermediate with an extended genomic footprint that forms during helicase activation. Genome-wide mapping of initial strand separation reveals that DNA unwinding initiates near the N-terminal interface of opposing MCM2-7 hexamers. At these sites, the origin DNA exhibits a conserved AT-rich/GC-rich/AT-rich sequence architecture centred under the helicase complex, which is associated with an elevated DNA melting probability. We further show that restricting hexamer splitting delays release of the Cdc45-loading factor Sld3, demonstrating that mechanical transitions during helicase activation are tightly coupled to complex disassembly. Finally, we provide in vivo evidence that single-stranded DNA is ejected through a specialised DNA exit gate at the Mcm2/5 interface during helicase activation, which is dispensable for ongoing DNA synthesis. Together, these findings establish a mechanistic framework for how replication origins are remodelled to initiate DNA replication and reveal key intermediates and DNA transactions during helicase activation. - Source: PubMed
Publication date: 2026/07/23
Weekes ChristopherWillerding LiaKhadayate Sanjay PLiebl KorbinianMossler AudreyMontoya AlexRauthe VanessaKarimi Mohammad MZacharias MartinUlrich Helle DSpeck ChristianReuter L Maximilian - Hepatocellular Carcinoma (HCC) represents a significant health challenge globally, characterized by its high incidence and mortality rates. The exact relationship between ovarian-tumor-domain-containing deubiquitinase 3 (OTUD3) expression and HCC remains inadequately explored, presenting a significant gap in our understanding. - Source: PubMed
Publication date: 2026/08/10
Lu LuLu QifengZhang JialinZhou Na - Chemoresistance remains a critical barrier to the efficacy of oxaliplatin in colon cancer treatment. While the deubiquitinating enzyme USP46 is implicated in multiple tumor progression pathways, its specific role in oxaliplatin resistance remains undetermined. Our analysis reveals that USP46 is significantly overexpressed in colon cancer tissues, with its elevated expression correlating with poor clinical outcomes in colon cancer patients. Silencing USP46 suppresses both the proliferation and metastatic potential of colon cancer cells while simultaneously enhancing cellular sensitivity to the DNA-damaging agent oxaliplatin. Mechanistically, overexpression of USP46 leads to upregulation of nuclear RAD51 expression and facilitates the assembly of RAD51 foci, thereby increasing homologous recombination repair (HRR) capacity and contributing to oxaliplatin resistance in colon cancer cells. MCM7 is identified as a bona fide substrate of USP46 by LC-MS/MS profiling. Subsequent experiments confirm that USP46 specifically removes K48-linked polyubiquitin chains from MCM7, thereby stabilizing its protein expression. Rescue assays validate that USP46 modulates RAD51 expression and HRR function in an MCM7-dependent manner. Collectively, our study uncovers a novel USP46-MCM7-RAD51 signaling cascade that confers oxaliplatin resistance in colon cancer via augmentation of HRR-dependent DNA repair, thereby establishing this axis as a promising therapeutic target for overcoming oxaliplatin resistance. - Source: PubMed
Publication date: 2026/06/25
Wu ChangleiZhu WenjieLiu ZitaoXiao TaifuZuo ChengZhu ZhengmingHuang Jun - - Source: PubMed
Publication date: 2026/07/25
Hu XiaosongYang LiCui Hongjuan - This study re-evaluates the classification of the Halosphaeriaceae (Microascales, Hypocreomycetidae) based on phylogenetic analyses of 18S and 28S regions of rDNA and protein coding genes (rDNA, RPB1, RPB2, TEF1-ɑ, MCM7) along with comprehensive morphological comparisons. Halosphaeriaceae are worldwide in distribution and commonly found in marine habitats. A natural classification was not possible when the family was introduced, since it predated molecular phylogenetic studies; therefore, morphology-based descriptions only were provided. This study recognises 77 genera with 202 species which includes seven new genera (, , , , , , ), and one new species . The new taxonomic combinations include , , , , , , , , , , , , and . Divergent time estimation of Halosphaeriaceae, based on combined 18S, 28S rDNA, RPB1, RPB2, TEF1-ɑ, MCM7 sequences, indicates that the family originated in the Paleozoic at ~545 MYA. Ecologically, Halosphaeriaceae species occur widely on different substrates and play an important role in the recycling of complex organic material. They are often early colonizers of wood in the marine environment and are the source of a wide range of enzymes and antimicrobials. - Source: PubMed
Publication date: 2026/06/25
Dayarathne Monika CJones E B GarethBahkali Ali HDevadatha BandarupalliHyde Kevin DAbdel-Wahab Mohamed ACalabon Mark SCorreia PedroAbdel-Aziz Faten ABakhit Mahmoud SSakayaroj JariyaPrematunga ChasikaCaeiro Maria FAzevedo EgídiaAsghari RahelehApurillo Carlo Chris SBhagya Amuhenage TharinduAumentado Herbert DustinMukhopadhyay SamhitaPhukhamsakda ChayanardChen YanpengMaharachchikumbura Sajeewa SGuo Sheng-YuPang Ka-Lai