CCNB1 Antibody (Center) Blocking Peptides
- Known as:
- CCNB1 Antibody (Center) Blocking Peptides
- Catalog number:
- BP11096c
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- CCNB1 Antibody (Center) Blocking Peptides
Related genes to: CCNB1 Antibody (Center) Blocking Peptides
- Gene:
- CCNB1 NIH gene
- Name:
- cyclin B1
- Previous symbol:
- CCNB
- Synonyms:
- -
- Chromosome:
- 5q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1991-12-10
- Date modifiied:
- 2016-10-05
Related products to: CCNB1 Antibody (Center) Blocking Peptides
Related articles to: CCNB1 Antibody (Center) Blocking Peptides
- Polypropylene nanoplastics (PP-NPs) are emerging environmental contaminants, but their gestational toxicity and underlying mechanisms remain poorly understood. In this study, we integrated maternal exposure mouse models, HTR8/SVneo trophoblast assays, quantitative proteomics, and phosphoproteomics to delineate the pathogenic basis of PP-NP-induced placental injury. PP-NPs accumulated prominently in the placenta, eliciting placental structural disruption, reduced placental efficiency, impaired fetal growth, and increased embryo loss. In trophoblasts, PP-NPs were readily internalized and impaired viability, proliferation, migration, invasion, and tube formation, accompanied by mitochondrial damage. To decipher the underlying molecular mechanisms, we performed integrated quantitative proteomic and phosphoproteomic analyses. These multi-omics landscapes revealed that cellular senescence is the dominant pathogenic program triggered by PP-NPs, accompanied by extensive phosphorylation remodeling. CDK1 emerged as the top predicted upstream kinase within this senescence-associated network. Notably, although CDK1 abundance was increased after PP-NPs exposure, its canonical cell-cycle-driving activity was not effectively engaged, as evidenced by reduced Thr161 phosphorylation, weakened CDK1-CCNB1 complex formation, and G1-phase arrest. Instead, PP-NPs were associated with increased phosphorylation of senescence-related substrates linked to CDK1-predicted signaling, including RBL2 at Thr, SQSTM1 at Ser, and FOXO3 at Ser, together with activation of DNA damage signaling, the P53-P21/P16 axis, and a SASP-like inflammatory response. Pharmacological inhibition of CDK1 with Ro-3306 attenuated trophoblast senescence, restored trophoblast function, alleviated placental injury, and improved fetal outcomes in vivo, while siRNA-mediated CDK1 knockdown similarly suppressed CDK1-linked phosphorylation and rescued senescence-associated functional defects in trophoblasts. In conclusion, our study demonstrates that PP-NPs drive premature placental ageing through global proteomic and phosphoproteomic reprogramming, providing a new theoretical basis and potential therapeutic targets for environmental pollutant-induced adverse pregnancy outcomes. - Source: PubMed
Publication date: 2026/07/10
Li ShuxianWang KaiLi LingbingLi ZihanZhou MeijuanGuo JunjunGong PihaiZhang Meihua - To identify baseline gene expression programs associated with recurrence timing in estrogen receptorpositive (ER+) breast cancer (BC) using a multi-state modeling framework. - Source: PubMed
Publication date: 2026/06/30
Wang YongzheQuinones ChristineKang IreneRugo HopeMartinez ErnestSeewaldt VictoriaMortimer JoanneNath AritroJones Veronica - Maintenance of genome integrity is essential for cellular homeostasis, and its perturbation leads to tumorigenesis. Here, we uncover an unanticipated somatic role for the synaptonemal complex protein SYCP1, previously regarded as strictly meiosis specific, in a broad spectrum of human cancers including breast cancer. Through integrative genomic, proteomic, and functional analyses, we demonstrate that SYCP1 is aberrantly reexpressed in tumor cells, where it actively promotes DNA damage repair, cell cycle progression, and malignant growth. SYCP1 binds chromatin at regulatory elements and directly controls transcriptional programs governing genome maintenance, including key effectors such as , , , and . Loss of SYCP1 impairs DNA repair kinetics, attenuates tumor cell proliferation and migration, and increases sensitivity to chemotherapeutics cisplatin and gemcitabine. Mechanistically, SYCP1 coimmunoprecipitates with chromatin remodeling complexes and transcription factors SP1 and SP2 and modulates their genomic occupancy and oncogenic transcriptional outputs. Clinically, high SYCP1 expression stratifies patients with poor prognosis and therapy resistance across multiple cancer types. Our findings illuminate a previously unrecognized moonlighting function of SYCP1 in somatic cancer cells and position it as a critical chromatin-associated regulator of genome stability, with implications for biomarker development and therapeutic targeting. - Source: PubMed
Publication date: 2026/07/08
Brennan Louise CGrinchuk Oleg VPachon-Penalba MiguelSou Ieng FFawcett Conor JNogueira Claudia GGuthrie MeganBates Andrew DHine MeganThomaz AmandaFielding Andew BDavies Owen RTee Wee-WeiMcClurg Urszula L - Pyroptosis is a major contributor to the pathophysiology of acute liver failure (ALF), a condition with high mortality. Although N‑acetylcysteine (NAC) is used clinically for ALF, its mechanisms of regulating pyroptosis and multiple signaling pathways to achieve hepatoprotection remain incompletely understood. We integrated public transcriptomic data (GSE14668, GSE96851, GSE38941) and performed differential expression analysis, weighted gene co‑expression network analysis, protein-protein interaction network construction, and machine learning to identify ALF‑related pyroptosis signature genes. Network pharmacology and molecular docking were used to predict the core therapeutic targets and mechanisms of NAC. An in vitro cellular inflammation model (LPS/D‑GalN‑treated L02 hepatocytes) was established, and the effects of NAC on target proteins and signaling pathways were validated by CCK‑8, LDH release, Western blot, ELISA, and qPCR. Six core targets-IL18, BCL2, TLR4, CASP1, CCNB1, and CAV1-were identified. Molecular docking predicted binding affinities between NAC and these targets in the moderate range (- 4.2 to - 5.3 kcal/mol). In vitro, NAC (10 mM) significantly reduced total CASP1 and GSDMD protein levels. More importantly, we further assessed NLRP3 expression, cleaved caspase‑1 (p20 subunit), and the N‑terminal cleavage fragment of GSDMD (GSDMD‑NT); NAC markedly suppressed all three markers, providing direct evidence that it inhibits the canonical NLRP3/caspase‑1/GSDMD pyroptotic axis. NAC also restored BCL2, CCNB1, and CAV1 expression, reversed TLR4 overexpression, and normalized the LC3B‑II/I ratio and p62 levels, indicating restoration of autophagic flux. Compared with a pyroptosis inhibitor (Ac‑YVAD‑CMK), NAC showed superior efficacy in reversing TLR4 upregulation and cell‑cycle‑related protein abnormalities. NAC exerts a comprehensive hepatoprotective effect that surpasses that of a simple pyroptosis inhibitor by synergistically modulating pyroptosis, apoptosis, cell cycle, inflammatory recognition, and endocytosis pathways through multiple targets. These findings provide a theoretical foundation for expanding the clinical application of NAC in ALF. - Source: PubMed
Publication date: 2026/07/08
Wei HuazhuYuan ShubingLiang ZiyuanShi Qinglan - [This corrects the article DOI: 10.1371/journal.pone.0254283.]. - Source: PubMed
Publication date: 2026/07/06