Dag1 Blocking Peptide, Blocking Peptides
- Known as:
- Dag1 Blocking Peptide, Blocking Peptides
- Catalog number:
- 33R-7277
- Product Quantity:
- 100 ug
- Category:
- -
- Supplier:
- Fitzgerald
- Gene target:
- Dag1 Blocking Peptide Peptides
Related genes to: Dag1 Blocking Peptide, Blocking Peptides
- Gene:
- DAG1 NIH gene
- Name:
- dystroglycan 1
- Previous symbol:
- -
- Synonyms:
- A3a, 156DAG, AGRNR, DAG
- Chromosome:
- 3p21.31
- Locus Type:
- gene with protein product
- Date approved:
- 1997-07-22
- Date modifiied:
- 2019-04-23
Related products to: Dag1 Blocking Peptide, Blocking Peptides
Related articles to: Dag1 Blocking Peptide, Blocking Peptides
- Bacteria are frequently attacked by viruses, known as phages, and rely on diverse defence systems to survive. While phages can evade defences by covalently modifying their DNA, these non-canonical nucleobases create molecular signatures that bacteria can exploit. Here, using structure-guided discovery, we identified two widespread families of anti-phage DNA glycosylases, Dag1 and Dag2. Although DNA glycosylases are classically associated with DNA repair, Dag1 and Dag2 act as antiviral effectors that selectively target phages carrying modified guanine bases. Guided by the conserved glycosylase fold, we uncovered numerous defence-associated glycosylases that collectively form a diverse repertoire of enzymes targeting chemically modified phage DNA. We further identified a distinct glycosylase superfamily that protects against phages carrying modified thymidine bases. Together, these findings establish DNA glycosylases as a versatile class of bacterial immune proteins and highlight structure-guided discovery as a powerful strategy for uncovering hidden antiviral defences. - Source: PubMed
Publication date: 2026/08/06
Getz Landon JQian Amy LVivian Liu YFairburn Sam RButt Mahnoor SLee Yan-JiunWeigele Peter RMaxwell Karen L - Ischemic stroke (IS) is a cerebrovascular disease with high mortality and disability rates, currently lacking effective therapeutic targets. The STING inhibitor SN-011 shows potential in IS treatment, but its mechanism of action remains unclear. This study aims to explore the key molecular mechanisms of SN-011 in treating IS through bioinformatics approaches. IS transcriptome datasets were analyzed to identify differentially expressed genes. Mendelian randomization using brain eQTL and IS-GWAS data identified genes with causal relationships to IS. Single-cell transcriptome, pseudo-time trajectory, intercellular communication, and transcription factor regulatory network analyzes were performed. Molecular docking and DARTS-WB assay validated SN-011 binding to transcription factors. Transcriptomic analysis identified 77 intersecting genes. Mendelian randomization revealed ADGRE5 as a protective gene for IS (OR < 1), significantly downregulated in venous endothelial cells (vECs) during disease progression. Cell communication analysis showed ADGRE5-high vECs interact with immune, glial, and stromal cells via LAMININ (Lamb2-CD44, Lamb2-Itga6+Itgb1, Lamb2-Dag1 pair) and JAM signaling pathways. Transcription factor analysis identified JUNB as a negative regulator of ADGRE5. Molecular docking (-6.8 kcal/mol) combined with an in vitro DARTS-WB assay confirmed the interaction between SN-011 and JUNB. In OGD-induced endothelial cell injury models, SN-011 suppressed JUNB expression, restored ADGRE5 expression inhibited by JUNB overexpression, reversed the downregulation of LAMB2 and CD44, and reduced the expression of the pro-inflammatory cytokines IL-6 and IL-1β. Notably, blockade of LAMB2 largely abolished these protective effects, indicating that the anti-inflammatory and endothelial-protective activities of SN-011 are mediated, at least in part, through restoration of the LAMB2-CD44 signaling axis. ADGRE5 downregulation in vECs may impair vascular repair by disrupting LAMININ-mediated intercellular communication. SN-011 may exert neuroprotective effects by targeting JUNB to upregulate ADGRE5 expression and restore the vEC-centered cellular communication network, providing a theoretical basis for SN-011 as a potential IS therapeutic. - Source: PubMed
Ou XiangLingGong ZunKe - Limb-girdle muscular dystrophies (LGMDs) are disorders with an important clinical heterogeneity, usually involving proximal limb muscles. One subtype, LGMD R16 (LGMD 2P), is an autosomal recessive condition caused by pathogenic variants in , with clinical presentations ranging from mild to extremely severe forms. is responsible for producing dystroglycan, an essential complex in the muscular protein network. Following translation, dystroglycan is cleaved into alpha-dystroglycan, which undergoes glycosylation and acts as a sarcolemmal receptor for extracellular proteins, and beta-dystroglycan, which connects to dystrophin. In recent years, heterozygous nonsense or frameshift variants have been linked with asymptomatic hyperCKemia (increased serum creatine kinase levels) or mild muscular phenotypes characterized by fatigability and myalgia. Here, we describe a Romanian family comprising four affected individuals (one father and three sons) carrying the heterozygous missense variant NM_004393.6:c.887G>A, NP_004384.5:p.(Gly296Asp) and showing a mild-moderate muscular phenotype similar to previous cases of haploinsufficiency. Three of the affected individuals exhibit myopathic changes in muscle biopsies (increased fiber size variability, internalized nuclei, and regenerating fibers), while two demonstrate reduced alpha-dystroglycan glycosylation in muscle tissue. Atomic force microscopy findings in myoblasts from one patient showed a significantly lower stiffness compared to controls. These findings align with prior reports and further support the pathogenicity of this variant. - Source: PubMed
Publication date: 2026/07/04
Malfatti EdoardoCaramizaru AlexandruTrentin FedericaDumitrescu AndreeaSali LucaBastian AlexandraLee HaneTajsharghi HomaVerebi CamilleNectoux JulietteLeturcq FrancePhadke RahulSarkozy AnnaManzur AdnanFodil RedouaneDobrescu Amelia - Heart failure (HF) and body mass index (BMI) share substantial genetic architecture, which may lead genetically informed target discovery to preferentially identify adiposity-related pathways. We sought to identify circulating proteins associated with HF beyond this shared genetic component. - Source: PubMed
Publication date: 2026/06/22
Su Chen-YangLu Tianyuan - Idiopathic nephrotic syndrome (iNS) is clinically classified by treatment response; however, the molecular basis of multidrug resistance remains poorly defined. We hypothesized that multidrug-resistant disease represents a distinct biological state rather than a more severe form of active disease. - Source: PubMed
Publication date: 2026/05/26
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