Ask about this productRelated genes to: HSP90B1 antibody
- Gene:
- HSP90B1 NIH gene
- Name:
- heat shock protein 90 beta family member 1
- Previous symbol:
- TRA1
- Synonyms:
- GP96, GRP94
- Chromosome:
- 12q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 1991-07-03
- Date modifiied:
- 2016-10-11
Related products to: HSP90B1 antibody
Related articles to: HSP90B1 antibody
- Usher syndrome type 3A (USH3A), caused by CLRN1 mutations, leads to progressive deaf-blindness. Although CLRN1 expression has been localized to Müller glia (MG), the pathogenic mechanisms linking glial CLRN1 deficiency to photoreceptor death remain undefined. We utilized a novel large-animal model to elucidate cell-type-specific pathogenesis at single-nucleus resolution. - Source: PubMed
Lee YeachanGao YuanyuanNguyen Van PhucLiang BoPrieskorn Diane MBeyer LisaWei ZhuyingKhan NaheedWeiland JamesIannuzzi MichaelBisgaier CharlesRaphael YehoashChen Y EugenePaulus Yannis MYang Dongshan - Using DIA quantitative proteomics technology to screen for coronary artery calcification (CAC)-associated differentially expressed proteins, this study explores the value of SMOC1, HSP90B1, and OPTN as potential serum biomarkers for CAC and constructs an individualized risk prediction model. - Source: PubMed
Publication date: 2026/06/01
Cui RuyanLiu Xiaoyu - Wooden Breast (WB) and White Striping (WS) are prevalent myopathies affecting the (PM) muscle of modern broiler chickens, with significant implications for animal welfare and meat quality. This pilot study aimed to characterize proteomic alterations associated with increasing severity of WB and WS in the PM of Hubbard × Ross 708 broilers. Muscle samples ( = 12) were previously categorized into four severity ranks based on established macroscopic criteria. Presently, proteins were extracted and analyzed using LC-MS/MS-based shotgun proteomics. Statistical comparisons between groups were performed using Generalized Linear Models. Fibronectin 1, fibrinogen alpha chain, musculoskeletal embryonic nuclear protein 1, glutathione S-transferase 2, calsequestrin-2, and endoplasmin emerged as potential biological markers and their prospective roles in the pathogenesis of these myopathies are discussed. Our findings suggest a progressive alteration of the muscle proteome with increasing disease severity, highlighting pathways related to muscle structure, metabolism, and stress response. These results aid in providing new insights into the molecular mechanisms underlying WB and WS and may inform future research on genetic and management strategies. As a pilot study, these findings warrant further investigation in larger cohorts and different commercial lines. - Source: PubMed
Publication date: 2026/06/03
Karolak Madeline CYaman AhmetZapata IsainCressman Michael DWick Macdonald P - Neuroinflammation is a pivotal pathological process underlying numerous neurological disorders. While the interplay between neuroinflammation and glycosylation is gaining increasing attention, it remains unclear whether modulating glycosylation can effectively inhibit neuroinflammation. To address this, our study employed a combined proteomic and glycoproteomic approach to investigate the role of protein glycosylation in lipopolysaccharide (LPS)-induced neuroinflammation models. There was a significant association between the changes we observed and pathways related to glycation and neuroinflammation. Moreover, during neuroinflammation, protein glycosylation levels exhibit fluctuations. Crucially, we demonstrated that the pan-glycosylation inhibitor NGI-1 effectively suppressed the inflammatory response. We subsequently screened Tanshinone IIA (STS), identifying it as a potent therapeutic candidate for neuroinflammatory disorders. Tanshinone IIA exerts its anti-inflammatory effects partially through the targeted inhibition of Hsp90b1 glycosylation at position 217, thereby attenuating the activation of the NF-κB pathway. Collectively, our findings offer novel insights into the therapeutic potential of targeting glycosylation modifications in neuroinflammation. - Source: PubMed
Publication date: 2026/05/20
Li YahuiDuan KunfengLiu GuangyuanYan JingwenWang QianZhang YuyuWang YuranGuo BowenZhang PanpanZhang WeiKong Dezhi - Efficient skeletal muscle repair remains a significant clinical challenge due to the lack of safe pharmacological interventions. Our work identifies Tamoxifen as a potent driver of muscle regeneration, operating through the GRP94. In C2C12 myoblasts, Tamoxifen treatment directly triggered myogenic differentiation and accelerated myotube formation in a dose-dependent manner, alongside the marked upregulation of MyoD, Myogenin (MyoG), and MYHC. These pro-myogenic effects were effectively abolished upon GRP94 inhibition, confirming its role as an essential mediator. In vivo, using a bupivacaine-induced injury model, we observed that 10 mg/kg Tamoxifen significantly expedited tissue repair and increased the cross-sectional area (CSA) of regenerating myofibers. Collectively, our findings demonstrate for the first time that Tamoxifen orchestrates muscle repair by modulating GRP94, offering a promising strategy for treating acute injury and chronic muscle wasting. - Source: PubMed
Publication date: 2026/05/23
Xing LeiZhang KunHan YiTeng HuaixinWang YuxiLi Shuang