Ask about this productRelated genes to: HSP90AB1 antibody
- Gene:
- HSP90AB1 NIH gene
- Name:
- heat shock protein 90 alpha family class B member 1
- Previous symbol:
- HSPC2, HSPCB
- Synonyms:
- -
- Chromosome:
- 6p21.1
- Locus Type:
- gene with protein product
- Date approved:
- 1990-06-27
- Date modifiied:
- 2016-10-05
Related products to: HSP90AB1 antibody
Related articles to: HSP90AB1 antibody
- Chronic inflammation is a key driver of atherosclerotic cardiovascular disease. Notably, anti-inflammatory therapies have demonstrated efficacy in reducing cardiac events. We previously reported that TREM2 (triggering receptor expressed on myeloid cells 2) promotes foam cell formation in atherosclerosis. Elevated levels of soluble TREM2 (sTREM2) have been observed in the plasma of patients with atherosclerosis. This study sought to investigate the pathological role of sTREM2 in the progression of atherosclerosis, elucidate its underlying mechanistic pathways, and propose potential targeted therapeutic interventions. - Source: PubMed
Publication date: 2026/07/29
Guo XiaoqingLiu XiaomingYu JieQin MengtingWang ShengnanChen JiaojiaoJiang DailiangFeng YuhangYu JiangnanXu XiaojunMao Ling - This study aimed to use quantitative phosphoproteomics to explore phosphorylation characteristics in ()-induced liver abscess (KPLA) formation and liver injury. The strain LA- was phenotypically and genotypically characterized. A murine model of KPLA was established via intragastric inoculation. Phosphoproteomics and bioinformatic analyses were conducted to identify and quantify phosphosites and phosphoproteins. LA- displayed a hypermucoviscous phenotype, serotype K1, ST23 genotype, and harbored six major virulence genes. Inoculation induced liver colonization and typical histopathological abscess lesions. We quantified 3017 phosphoproteins covering 12,798 phosphosites (dominated by serine phosphorylation); 1723 proteins were upregulated and 425 downregulated. Bioinformatic analyses revealed remodeling in metabolism, stress response, signal transduction, and cytoskeleton organization. Upregulated proteins converged on fatty acid elongation, inositol phosphate metabolism, and the tricarboxylic acid cycle; downregulated proteins were enriched in PI3K-Akt, IL-17 signaling, and T-cell differentiation. Protein-protein interaction network analysis identified 10 key proteins (Src, Rac1, Actb, Hsp90aa1, Hsp90ab1, Egfr, Rps6, Pik3CA, Itgb1, and Fyn) that mediate inflammatory signaling, cytoskeleton remodeling, and immune infiltration. Dysregulated phosphorylation networks drive pathological metabolic adaptation, suppressed immune homeostasis, and cytoskeletal disorganization, collectively facilitating KPLA progression. The identified hub proteins and pathways represent high-value mechanistic targets and candidate therapeutic vulnerabilities for KPLA. - Source: PubMed
Publication date: 2026/07/14
Yan ChaoLiu XuanfengChen YujieSu AnRen XueZhang TingtingYuan Jing - Bisphenol A (BPA) is a potential risk factor for pancreatic ductal adenocarcinoma (PDAC). This study integrated network toxicology, molecular docking, molecular dynamics (MD) simulations, and TCGA clinical data analysis to explore the potential molecular mechanisms linking BPA exposure to PDAC risk. BPA-PDAC intersection targets were identified through multi-database screening, followed by protein-protein interaction (PPI) network construction to screen core hub genes. A total of 10 core hub genes were identified via PPI analysis combined with the Maximal Clique Centrality (MCC) algorithm. Molecular docking demonstrated that ESR1 exhibited one of the strongest binding affinities for BPA (-8.2 kcal/mol), and MD simulations confirmed favorable thermodynamic stability of the BPA-ESR1 complex. TCGA analysis revealed stage-dependent expression patterns: early stages showed downregulation of TP53 and BCL2, whereas advanced stages showed upregulation of BCL2L1, HSP90AA1, and HSP90AB1, while ESR1, HIF1A, and PARP1 remained consistently low. These findings suggest that BPA may promote PDAC progression by disrupting ERα-mediated endocrine signaling and impairing DNA repair through PARP1 interference, providing candidate molecular targets and a hypothesis-generating foundation for pancreatic cancer risk assessment, warranting further experimental validation. - Source: PubMed
Publication date: 2026/07/20
Li XueruWu FanZhang ZunhanAn JiayiZhou GuoqiangWang YangZhao DandanChen Xiaolu - Perfluorooctane sulfonamide (PFOSA) is an environmentally persistent compound that poses a threat to human health, but its hepatotoxicity mechanism remains unclear. This study integrated the National Health and Nutrition Examination Survey (NHANES) epidemiological data, network toxicology, bioinformatics analysis, and molecular docking simulation to systematically explore the hepatotoxicity mechanism of PFOSA from multiple levels. Potential targets of PFOSA and disease targets related to liver injury were screened through multiple databases, a protein-protein interaction (PPI) network was constructed, core targets were identified, and Gene Ontology (GO)/Kyoto Encyclopedia of Genes and Genomes (KEGG) functional enrichment analysis was conducted. Meanwhile, external validation was conducted through the Gene Expression Omnibus (GEO) dataset, and molecular docking was used to evaluate the affinity between PFOSA and key targets. Data from 2,476 NHANES participants (1999-2012) showed that there was a significant association between PFOSA exposure and liver function markers (aspartate aminotransferase (AST), alkaline phosphatase (ALP), total bilirubin (TBIL), etc.), establishing an association between the population level and liver injury. Through multi-database screening (CHEMBL, Search Tool for Interactions of Chemicals (STITCH), GeneCards, etc.), 623 intersection targets were identified, and 37 core targets were screened out. Among them, the top five were MDM2, HSP90AB1, HIF1A, MMP9, and TP53. The Gene Ontology (GO) and KEGG analyses highlighted the enrichment of cancer-related pathways, oxidative phosphorylation, and non-alcoholic fatty liver disease (NAFLD). The molecular docking of PFOSA with the core target shows a strong binding affinity. Overall, PFOSA may induce liver steatosis, fibrosis, and carcinogenic risks by disrupting the apoptosis regulation of MDM2-TP53, HIF1A-mediated oxidative stress, and MMP9-driven extracellular matrix degradation. These findings emphasize the necessity of stricter PFOSA regulations and enhanced environmental monitoring in areas where NAFLD is prevalent, providing a framework for toxicity assessment and intervention strategies. - Source: PubMed
Publication date: 2026/07/24
Yang YanYuan YeDing RenzhongHe PeilingWu WenjunSong YiHu Yijie - Myotonic dystrophy type 1 (DM1) and type 2 (DM2) are multisystemic diseases caused by the expression of toxic expansion RNAs that sequester muscleblind-like (MBNL) proteins, resulting in extensive alternative splicing dysregulation. Given that there are no current disease-modifying treatments for DM, we sought to identify compounds that rescue the underlying splicing dysregulation. A medium throughput splicing screen utilizing DM1 patient-derived fibroblasts was developed and used to screen 1584 compounds from the NIH NCI Diversity Set VI, leading to the identification of macbecin II, an HSP90 inhibitor. Macbecin II-mediated HSP90 inhibition corrects several MBNL-regulated splicing events in DM1 myotubes, and a structurally distinct HSP90 inhibitor, CCT018159, produces similar effects. Using RT-PCR splicing analysis, siRNA knockdown, RT-qPCR, immunoblotting, and RNA fluorescence in situ hybridization we examined the effects of HSP90 inhibition in DM models. HSP90 inhibition increases MBNL1 and MBNL2 transcript levels, increases MBNL2 protein, and reduces toxic CUG RNA and nuclear foci in DM1 cell models. An analysis of individual HSP90 isoforms reveals that knocking down HSP90AA1, HSP90AB1, and TRAP1 partially improves splicing defects, whereas HSP90B1 knockdown exacerbates mis-splicing. We also show that treatment with HSP90 inhibitors corrects mis-splicing in DM2 myotubes. Together, these data identify HSP90 as a modifier of RNA toxicity and alternative splicing in DM and support further evaluation of HSP90-directed therapeutic strategies. - Source: PubMed
Publication date: 2026/07/22
Zhang JingMascorro AmyOishi HumayraAliyeva AsmarShaughnessy SharonSheng JiaReddy KaalakCleary John DouglasBerglund J Andrew