SHEEP ANTI ESTRONE GLUCURONIDE Antibody (0.1ml)
- Known as:
- SHEEP ANTI ESTRONE GLUCURONIDE Antibody (0.1ml)
- Catalog number:
- oasa09069
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- SHEEP ANTI ESTRONE GLUCURONIDE Antibody (0.1ml)
Related genes to: SHEEP ANTI ESTRONE GLUCURONIDE Antibody (0.1ml)
- Gene:
- GNL2 NIH gene
- Name:
- G protein nucleolar 2
- Previous symbol:
- -
- Synonyms:
- Ngp-1, HUMAUANTIG, Nog2, Nug2
- Chromosome:
- 1p34.3
- Locus Type:
- gene with protein product
- Date approved:
- 2004-09-06
- Date modifiied:
- 2019-02-08
Related products to: SHEEP ANTI ESTRONE GLUCURONIDE Antibody (0.1ml)
Related articles to: SHEEP ANTI ESTRONE GLUCURONIDE Antibody (0.1ml)
- To identify biomarkers and potential therapeutic targets related to angiogenesis and RNA modification in diabetic retinopathy (DR). - Source: PubMed
Publication date: 2026/10/18
Wang XueWu Dan-PingDu WeiLi RuiLou WeiChen Ran-RanLiao Yu-JieLi QianLi Xiao-MeiCui Hong-PingZhang Jin-Ling - Avian reovirus (ARV) is a major pathogen causing viral arthritis, tenosynovitis, malabsorption syndrome, and immunosuppression in chickens, leading to severe economic losses in the global poultry industry. The nonstructural protein p17 is vital for ARV replication and modulates diverse host signaling pathways by interacting with multiple host factors. In our previous work, nucleolar GTP‑binding protein 2 (GNL2), a conserved nucleolar GTPase governing 60S ribosomal subunit maturation and nucleocytoplasmic transport, was screened as a potential binding partner of ARV p17 using yeast two‑hybrid assay. In the present study, the physical interaction between p17 and GNL2 was validated by coimmunoprecipitation (Co‑IP), glutathione S‑transferase (GST) pull‑down, and laser confocal microscopy. Mechanistically, the central region of p17 (amino acids 19-61) directly binds to the GTPase domain of GNL2. Notably, ARV infection or ectopic expression of p17 significantly upregulates GNL2 expression. Functional assays revealed that GNL2 overexpression markedly promotes ARV replication at both RNA and protein levels, whereas GNL2 knockdown remarkably restricts viral proliferation. Furthermore, GNL2 enhances p17‑mediated cellular autophagosome formation, thereby constructing a favorable intracellular milieu for efficient ARV propagation. Collectively, these findings demonstrate that GNL2 serves as a key host dependency factor hijacked by ARV p17 to remodel host cellular functions. This study provides new insights into the molecular pathogenesis of ARV and offers potential targets for developing antiviral strategies against ARV infection. - Source: PubMed
Publication date: 2026/08/03
Tan XuechaoZhang XinzhuoJiang XiongOu YangyanLiu XinyuZhang Chengcheng - Liver hepatocellular carcinoma (LIHC) is a common malignancy, yet the core genes driving its progression and potential therapeutic targets remain insufficiently explored. Ribosome biogenesis (RB) is a critical biological process linked to various cancers; however, its systematic role in LIHC remains unclear. - Source: PubMed
Publication date: 2026/05/14
Qi YajieLi KunLi PinchengYan JianyuFeng ShuyueWan DanDu KeLiang XiaoYang FanZhou ErzhengHuang NaWang QianLiu Nanbin - Production of the eukaryotic ribosomal subunits (40S and 60S) is a highly dynamic process in which numerous assembly factors (AFs) coordinate structural rearrangements of pre-ribosomal complexes to achieve their mature, functional architectures. Across the domains of life, GTPases leverage their functions as molecular switches to induce conformational changes that drive key steps in subunit maturation. Three GTPases, GTPBP4, GNL2, and GNL3, have been detected in nucleolar/nucleoplasmic human pre-60S complexes. Here, we compositionally analyze the pre-ribosomal particles associated with each of these GTPases and demonstrate the requirement of these enzymes, and their abilities to bind and hydrolyze GTP, for distinct steps in pre-ribosomal RNA processing. We further reveal that the GNL3 paralog, GNL3L, also associates with pre-ribosomes, and we map GNL3L binding sites on pre-rRNAs as well as identifying RNA contact sites on GNL3L. Lack of GNL3L impairs synthesis of the 60S rRNAs and expression of GTPase-inactive GNL3L causes defects in early steps of pre-rRNA processing. Impaired GTP hydrolysis by GNL3L leads to its accumulation on pre-60S particles, together with other AFs with proximal binding sites. Our data further demonstrate that the GTPase activity of GNL3L is required for maintaining 60S subunit levels, protein synthesis, and cellular proliferation. - Source: PubMed
Thomé Chairini CLemus-Diaz NicolasBloch von Blottnitz Katja ITagnères SophieKlein Helmkamp MerleHonemann-Capito MonaHackert PhilippMoshkovskii SergeiLenz ChristofBohnsack Markus TUrlaub HenningBohnsack Katherine E - : Carfilzomib (CFZ) and bortezomib (BTZ) are proteasome inhibitors used as the first-line therapy for relapsed or refractory multiple myeloma (MM) but are associated with cardiovascular adverse events (CVAEs). This study aims to identify differentially methylated positions (DMPs) and regions (DMRs), and enriched pathways associated with CVAEs related to CFZ or BTZ-based treatment. : Baseline germline DNA methylation profiles from 79 MM patients (49 on CFZ and 30 on BTZ) in the Prospective Study of Cardiac Events During Proteasome Inhibitor Therapy (PROTECT) were analyzed. Epigenome-wide analyses were performed within each group, followed by meta-analyses to identify signals common to CVAEs associated with both medicines. : Four DMPs were significantly associated with CFZ-CVAEs, including cg15144237 within ( = 9.45 × 10), cg00927646 within ( = 9.78 × 10), and cg10965131 within ( = 1.00 × 10). One DMR was identified in the region ( = 5.46 × 10). There was no evidence of any DMPs in BTZ-treated patients, however two DMPs and one DMR reached a suggestive level of significance ( < 1.00 × 10): cg09666417 in ( = 3.41 × 10) and cg12987761 in ( = 5.00 × 10), and a DMR mapped to the region ( = 8.11 × 10). Meta-analysis did not find any significant DMPs, with the top CpG being cg17933807 in ( = 7.38 × 10). Pathway enrichment analyses identified peroxisome, MAPK, Rap1, adherens junction, phospholipase D, autophagy, and aldosterone-related pathways to be implicated in CVAEs. : Our study identified distinct DMPs, DMRs, and pathways enrichment associated with CVAE, suggesting epigenetic contributors to CVAEs and supporting the need for larger validation studies. - Source: PubMed
Publication date: 2026/02/03
Alshammari Raed AwadhRubinstein Samuel MFarber-Eger EricShaffer Lauren LeeTantawy MarwaAlomar Mohammed EWells Quinn SLenihan DanielCornell Robert FShain Kenneth HBaz Rachid CGong Yan