RPL11 antibody
- Known as:
- RPL11 (anti-)
- Catalog number:
- orb128647
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- RPL11 antibody
Related genes to: RPL11 antibody
- Gene:
- RPL11 NIH gene
- Name:
- ribosomal protein L11
- Previous symbol:
- -
- Synonyms:
- L11, uL5
- Chromosome:
- 1p36.11
- Locus Type:
- gene with protein product
- Date approved:
- 1998-07-23
- Date modifiied:
- 2019-04-23
Related products to: RPL11 antibody
Related articles to: RPL11 antibody
- : Radioresistance is a critical challenge in the treatment of esophageal squamous cell carcinoma (ESCC). Histone lysine-specific demethylase 4D (KDM4D) has been implicated in DNA damage response; however, its role in regulating ESCC radiosensitivity remained unclear. We hypothesized KDM4D modulates radiosensitivity through the c-Myc/checkpoint kinase 1 (CHK1) pathway. : To investigate the role of KDM4D in ESCC radiosensitivity and to elucidate the underlying molecular mechanisms. : KDM4D expression was analyzed in tumor samples from 32 ESCC patients who received neoadjuvant radiotherapy. ESCC cell lines with KDM4D knockdown or overexpression were subjected to irradiation, and radiosensitivity was evaluated. Chromatin immunoprecipitation-polymerase chain reaction (ChIP-PCR), luciferase assay, and xenograft models were used to explore the underlying mechanisms. : Elevated KDM4D expression was associated with improved response to radiotherapy and prolonged progression-free survival (PFS). KDM4D knockdown significantly reduced radiation-induced apoptosis. Mechanistically, KDM4D promoted the demethylation of histone H3 lysine 9 trimethylation (H3K9me3), thereby activating S1 RNA-binding domain-containing protein 1 (SRBD1). SRBD1 subsequently upregulated ribosomal protein L11 (RPL11), which suppressed c-Myc expression, thereby downregulating wild-type p53-induced phosphatase 1 (WIP1) and CHK1. Rescue experiments and xenograft studies further verified this regulatory axis. : KDM4D enhances ESCC radiosensitivity through the SRBD1/RPL11/c-Myc/WIP1/CHK1 pathway, highlighting its potential as both a diagnostic biomarker and a therapeutic target. - Source: PubMed
Publication date: 2026/05/15
Gao ZhenhuaHan XiaoyunYuan Shuanghu - Prenatal e-cigarette (e-cig) exposure has been associated with adverse cardiovascular outcomes in offspring, yet the underlying molecular mechanisms remain poorly understood. Using a rat model of gestational e-cig aerosol exposure combined with quantitative LC-MS/MS proteomics and integrated KEGG, Gene Ontology (GO), protein-protein interaction (PPI), and EggNOG analyses, we identified profound and sexually dimorphic alterations in the neonatal cardiac proteome. There was extensive mitochondrial and metabolic dysregulation in the developing heart following prenatal e-cig exposure. In male offspring, enriched pathways included oxidative phosphorylation, tricarboxylic acid (TCA) cycle activity, and respiratory chain assembly, indicating disruption of mitochondrial energy metabolism. In contrast, female offspring exhibited prominent dysregulation of mitochondrial chaperones (Hspa9, Hspa4) and ribosomal proteins (Rps11, Rpl11, Rps3), suggesting impaired proteostasis and translational capacity. PPI and KEGG analyses further revealed sex-dependent perturbations of signaling and structural protein networks critical for cardiac contractility, cardiomyopathy progression, and myocardial stress resilience. Males primarily showed alterations in sarcomeric, structural, and metabolic proteins, whereas females exhibited widespread disruption of GPCR/cAMP/PKA-mediated regulatory pathways. These early-life proteomic alterations translated into functional deficits in adulthood, with males displaying impaired baseline cardiac function and exacerbated ischemia/reperfusion (I/R) injury, while females showed preserved baseline function but heightened susceptibility to I/R stress. Collectively, these findings demonstrate that prenatal e-cig exposure programs long-lasting, sex-specific cardiac vulnerability through early-life proteomic reorganization, providing mechanistic insight into developmental cardiotoxicity and informing risk assessment during pregnancy. - Source: PubMed
Publication date: 2026/06/16
Tu JiazichaoJian JieLi YongChavez JacobZhang QuanqingYu RongjunYu WansuZhang LuboXiao Daliao - A complex cyclic polypeptide antibiotic, thiostrepton, is made by two large macrocyclic rings: a 26-membered ring associated with a thiazoline moiety and a 27-membered ring accompanied by a quinaldic acid unit, a dehydropiperidine ring, and a flexible bis-dehydroalanine tail. The site-specific local structure and nuclear-spin dynamics of this polypeptide antibiotic is determined by using 2D solution NMR (H-C HSQC, H-C HMBC, H-H COSY, H-H TOCSY, and H-H NOESY) and solid-state NMR methods (C CP-MAS 2D PASS, H-C HETCOR, and site-specific C spin-lattice relaxation measurements). The combined H-C HETCOR and H-H NOESY data demonstrate that the quinaldic acid residue is positioned in close spatial proximity to multiple structural elements, including the thiazoline and piperidine rings, isoleucine-valine chain, butyrine, thiostreptin residue, dehydroalanine units, threonine, and thiazole. These interactions generate a compact hydrophobic core that stabilizes the conformation of the bis-dehydroalanine tail. The flexible side chains of both macrocyclic rings, together with the tail region, accommodate themselves within the interface of ribosomal protein L11 and the 23S rRNA, thereby perturbing the 70S ribosomal subunit. The dynamics of these flexible segments are quantified by employing NMR relaxometry. Therefore, although functional activity is not examined directly, the integrated solution- and solid-state NMR results deliver site-specific structural information and local nuclear spin dynamics at individual carbon sites of this cyclic polypeptide antibiotic. These characteristics are associated with the functional state of thiostrepton and offer a foundation for the rational design of next-generation polypeptide antibiotics. - Source: PubMed
Publication date: 2026/06/16
Pradhan Bijay LaxmiSen PrinceGhosh PoulomiDey Krishna KishorGhosh Manasi - Systemic lupus erythematosus (SLE) is a multifactorial autoimmune disease characterised by loss of immune tolerance and chronic inflammation, but its molecular pathogenesis remains incompletely understood. In this work we examine whether immune regulatory transcripts and pathways are recurrently detectable across heterogeneous publicly available SLE transcriptomic datasets, and we explore one of the recurrent pathways with a kinetic systems-biology model. We analyzed one microarray dataset (E-GEOD-46923, profiled on Affymetrix HG-U133A and HG-U133B), two bulk RNA-seq datasets (E-MTAB-7145, E-MTAB-11919), and two single-cell RNA-seq datasets (GSE135779, GSE163121) using a unified differential-expression criterion (|log2 fold change|≥ 1, Benjamini-Hochberg adjusted p-value < 0.05). KEGG pathway enrichment was performed with a per-dataset background gene universe. A mass-action kinetic model of Th1/Th2 differentiation was constructed in MATLAB SimBiology, and global sensitivity analysis was performed using the variance-based Sobol method. Across the heterogeneous datasets, CD53, IFITM1, and RPL11 were recurrently identified as differentially expressed transcripts, and the Th1/Th2 cell differentiation pathway, together with related cytokine-cytokine receptor and JAK-STAT pathways, emerged as a recurrent immune-regulatory signal. Systems-biology simulation under SLE-derived initial conditions predicted atypical IL-2 and GATA3 expression dynamics, which is consistent with, but does not by itself prove, the cytokine-signalling dysregulation reported in SLE. Sobol sensitivity analysis identified IL-4 and the modelled co-stimulatory and Notch ligand species (CDN1-6 and Jagged1/2) as the largest non-additive regulators of IL-2 in the model. Overall, this work integrates transcriptomic recurrence analysis with kinetic modelling to generate testable hypotheses regarding immune regulatory dysfunction in SLE. - Source: PubMed
Publication date: 2026/06/15
Saleem KashifParacha Rehan ZafarKhalid LintaManzoor AyeshaNisar MaryumMurad DidarDin Nazar MuhammadAmir Afreenish - Ribosomes are central to protein synthesis but also serve as dynamic hubs that integrate cellular stress responses. Here, we investigate how ribosomal protein L11 regulates ribosome conformational dynamics and long-distance coupling. Long-timescale molecular dynamics simulations of wild-type and L11-deleted (ΔL11) ribosomes reveal that L11 functions as a global allosteric regulator coordinating communication between the ribosomal stalk and the peptidyl transferase center. The absence of L11 disrupts long-distance couplings involving RelA and Obg and rigidifies the hibernation-promoting factor site, suggesting altered hibernation dynamics that could affect ribosome persistence under stress. To examine the physiological implications of these computational predictions, we construct a ΔL11 Bacillus subtilis strain and quantify its sporulation behavior. The ΔL11 variant exhibits delayed entry into and exit from dormancy, consistent with a breakdown in stress-adaptive ribosomal regulation. Overall, these results highlight the role of L11 in ribosomal allostery, suggesting how local perturbations propagate through the ribosome to influence global physiological outcomes and bacterial survival under environmental stress. - Source: PubMed
Publication date: 2026/06/12
Yangaliev DanisMoon Eun ChaeSüel Gürol MOzkan S Banu