Rad51 Protein (Human) Rad51 Protein (Human)
- Known as:
- Rad51 Protein (Human) Rad51 Protein (Human)
- Catalog number:
- 10-001
- Product Quantity:
- 20 ug
- Category:
- -
- Supplier:
- BBridge
- Gene target:
- Rad51 Protein (Human)
Related genes to: Rad51 Protein (Human) Rad51 Protein (Human)
- Gene:
- RAD51 NIH gene
- Name:
- RAD51 recombinase
- Previous symbol:
- RAD51A, RECA
- Synonyms:
- HsRad51, HsT16930, BRCC5, FANCR
- Chromosome:
- 15q15.1
- Locus Type:
- gene with protein product
- Date approved:
- 1993-05-26
- Date modifiied:
- 2017-05-02
Related products to: Rad51 Protein (Human) Rad51 Protein (Human)
Related articles to: Rad51 Protein (Human) Rad51 Protein (Human)
- Glioblastoma (GBM) is the most common adult primary brain malignancy. Recent studies demonstrate that temozolomide (TMZ) facilitates the persistence of quiescent glioma stem cells (GSCs), which are responsible for GBM recurrence. An ideal therapy should eradicate both proliferating cells and GSCs. Abexinostat (Abx), a histone deacetylase inhibitor, was identified through connectivity mapping to target the specific GBM signature. Here, we demonstrate the anti-proliferative effect of Abx on both differentiated cells and GSCs. - Source: PubMed
Publication date: 2026/08/19
Perumalsamy BalajiVengoji RaghupathyThiraviyam AnandRamireddy IndumatiYadav PoonamShah AshuMallya KavitaSalehi AfshinKumar SushilJain ManeeshPonnusamy Moorthy PBatra Surinder KShonka Nicole - Poly(ADP-ribose) polymerase 1 (PARP1) is a key factor responsible for repairing DNA single-strand breaks and maintaining genomic stability. PARP1 inhibitors have achieved remarkable therapeutic efficacy in the treatment of BRCA-mutant breast cancer. However, only a small proportion of breast cancer patients carry BRCA mutations, which limits the indication scope of such agents. Recent studies have demonstrated that protein arginine methyltransferase 5 (PRMT5) inhibitors can enhance the sensitivity of BRCA wild-type tumor cells to PARP1 inhibitors by suppressing the DNA homologous recombination (HR) pathway. In this study, a series of novel PARP1/PRMT5 dual inhibitors were designed and synthesized for the first time. Among them, compound 8I exerted potent inhibitory activity against both PARP1 and PRMT5, and displayed excellent antiproliferative effects on both BRCA wild-type and BRCA-mutant breast cancer cells. Further mechanistic studies verified that 8I could inhibit HR function by down-regulating the expression of BRCA1, BRCA2 and RAD51, thereby triggering enhanced DNA damage and cell apoptosis. Notably, in the BRCA wild-type MDA-MB-231 xenograft tumor model, compound 8I exhibited more potent in vivo antitumor activity than single-agent treatment with the PARP1 inhibitor Olaparib or the PRMT5 inhibitor GSK3326595, and displayed efficacy comparable to the combination of the two agents. In conclusion, this study established a new class of PARP1/PRMT5 dual inhibitors with prominent synergistic antitumor effects, which hold potential for the treatment of breast cancer. - Source: PubMed
Publication date: 2026/08/16
Xu YingLei QianYang ShuguangZhang YanxinLuo XiangchaoSong XiaopingWang NingyuLiu Qingchao - DNA double-stranded breaks (DSBs) are toxic events that can be reversed without genetic information loss by homology-directed repair (HDR), wherein information is copied from an intact template molecule. Finding a correct template within millions to billions of other DNA bases is termed homology search and is mediated by the protein RAD51. To monitor transient search in cellulo, we develop RAD51 proximity identification sequencing (RaPID-seq), a highly sensitive method marking all DNA searched regardless of whether it is chosen as the final template. We find that HDR in human cells is hierarchical with DSB proximity constraining the search space from which sequence homology determines the chosen template. Exogenously introduced DNA templates, such as those used during genome editing, are unconstrained and efficiently searched by the DSB, thereby competing with endogenous template search. Our data reveal the invisible process of homology search and shed new light on fundamental mechanisms underlying genome editing. - Source: PubMed
Publication date: 2026/08/17
Yeh Charles Dvan de Venn LillyKreutzer SusanneZheng XinheCantos Naomi CBechter Luca VMailänder DominicSchröder MarkusHofmann RobinGerbaldo Felix EClemens AlexandraWienert BeekeRichardson Christopher DKontarakis ZachariasCorn Jacob E - - Source: PubMed
Publication date: 2026/08/08
Zhang CuicuiWu YufengZhao JiuzhouChen HaiyangWang Qiming - DNA double-strand breaks, including those arising from DNA interstrand crosslinks, are highly cytotoxic forms of DNA damage. Their precise repair by homologous recombination (HR) is essential for maintaining genomic stability. During HR, timely disassembly of the core machinery, RAD51 nucleoprotein filaments, is critical. The FIGNL1-FIRRM (also known as C1orf112) AAA+ ATPase has recently been identified by us and others as a novel anti-recombinase that facilitates RAD51 disassembly via an ATPase-driven unfolding mechanism distinct from all previously characterized pathways. In this study, we identify MACIR/C5orf30 as an adaptor for FIGNL1-FIRRM unfoldase. MACIR directly binds FIRRM, forming a ternary complex that promotes RAD51 filament disassembly and facilitates repair of DNA damage induced by agents including aldehydes and platinum drugs. MACIR loss leads to DNA damage accumulation and genome instability, activates inflammatory signaling, linking MACIR deficiency to autoimmune and tumor-related pathologies. We further show that MACIR's direct interactions with FIRRM and DNA are both required for DNA repair, indicating that MACIR functionally links these components. High expression of MACIR-FIRRM-FIGNL1 correlates with poor prognosis in ovarian cancer patients, and pharmacological targeting of this complex with the inhibitors (small-molecule compound 8 and 10) we identified sensitizes ovarian cancer cells to platinum drugs. Therefore, our findings reveal MACIR as a critical regulatory adaptor within this RAD51-unfolding complex, which functions in an additional layer of control over DNA repair and genome stability, and suggest that its inhibition could enhance chemotherapeutic efficacy in cancer treatment. - Source: PubMed
Publication date: 2026/08/13
Zhou TaoPang MingLiang XinxinZhou ZenanYang HanCui YilinYu ShangLiang LingWang PanChen YifanWang JiadongWang Weibin