SND1 antibody
- Known as:
- SND1 (anti-)
- Catalog number:
- 38700
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Signalway
- Gene target:
- SND1 antibody
Related genes to: SND1 antibody
- Gene:
- SND1 NIH gene
- Name:
- staphylococcal nuclease and tudor domain containing 1
- Previous symbol:
- -
- Synonyms:
- TDRD11, p100
- Chromosome:
- 7q32.1
- Locus Type:
- gene with protein product
- Date approved:
- 2006-12-19
- Date modifiied:
- 2016-10-05
Related products to: SND1 antibody
Related articles to: SND1 antibody
- Alterations of BRAF, most commonly the V600E point mutation, are uncommon in salivary gland tumors, while BRAF fusions are exceptionally rare. We report four salivary gland tumors harboring BRAF fusions. The cohort included three males and one female aged 30-67 years (median, 46 years), all with tumors arising in the parotid gland. Two tumors were classified as intraductal carcinoma of oncocytic and mixed oncocytic-intercalated duct subtype, harboring AGK::BRAF and PAPSS1::BRAF fusions. In both cases, tumor cells were positive for S100, SOX10, and mammaglobin, and negative for androgen receptor. One tumor was diagnosed as low-grade acinic cell carcinoma with an SND1::BRAF fusion; tumor cells expressed SOX10, DOG1, and NR4A2 (Nurr1), but were negative for S100 and NOR1. The fourth tumor, classified as high-grade salivary adenocarcinoma, not otherwise specified, harbored an AGK::BRAF fusion and showed unusual morphology, including monolayered tubules and trabeculae, and focal papillary formations. Tumor cells were columnar with enlarged, overlapping vesicular nuclei and pale cytoplasm, expressing GATA3, S100, SOX10, and DOG1, while lacking mammaglobin expression. Focal p63/p40 positivity suggested a possible preexisting in situ component. BRAF fusions are exceedingly rare in salivary gland tumors and may occur across different histologic types. Given their potential sensitivity to MEK or next-generation RAF inhibitors, comprehensive molecular testing is essential for identifying patients who may benefit from targeted therapies. - Source: PubMed
Publication date: 2026/05/22
Laco JanBradová MartinaMauramo MattiVaněček TomášKohout AlešHájek JosefHácová MáriaLeivo IlmoMolony PeterJirásek TomášAgaimy AbbasSkálová Alena - Staphylococcal nuclease and Tudor domain‑containing protein 1 (SND1) is a multifunctional RNA‑binding protein implicated in transcriptional regulation, post‑transcriptional RNA control, oncogenesis, and viral infection. Initially identified as a transcriptional coactivator, SND1 was later established as a component of the RNA‑induced silencing complex, where it contributes to RNA turnover and microRNA regulation. SND1's diverse activities stem from its modular architecture, comprising four staphylococcal nuclease‑like domains, capable of direct RNA binding, and an extended Tudor domain that together form an integrated RNA‑binding and catalytic platform. This versatility also underlies its role in viral infection: SND1 acts as an m⁶A reader and is exploited by RNA viruses, such as SARS‑CoV‑2. Recent work showed that SND1 depletion, particularly loss of its third structured domain (SN3), reduces recruitment of the viral protein Nsp9 to the 3' untranslated region of the SARS‑CoV‑2 genome, impairing viral RNA synthesis through a direct SN3-Nsp9 interaction. Here, we report expression, purification, and near‑complete backbone NMR assignments of the SN3 domain of SND1. Secondary structure elements calculated by TALOS-N based on these assignments are in good agreement with the existing crystal structure of SN3. Our data provide an excellent foundation for future structural studies of SND1-RNA complexes and their roles in viral RNA priming in SARS-CoV-2. - Source: PubMed
Publication date: 2026/05/16
Ajith ShradhaCubeddu LizaGamsjaeger Roland - - Source: PubMed
Publication date: 2026/04/16
Li YingYang ChengruCui GuoliGui ShiliangJia LinlinChen YuNiu HonglinXin Hua - - Source: PubMed
Publication date: 2026/04/10
Zhan FuliangZhong YanyingQin YunnaLi LiangWu WenwenYao Meizhen - The protein-protein interaction (PPI) between metadherin (MTDH) and Staphylococcal nuclease domain-containing protein 1 (SND1) is a pivotal oncogenic driver in various cancers, yet the atomic-level details of their binding mechanism remain elusive, hindering targeted drug discovery. This study employs integrated computational approaches, including molecular dynamics (MD) simulations, binding free energy calculations, and residue interaction network analysis, to identify hotspot residues at the MTDH-SND1 interface and elucidate the binding mechanism. The results demonstrate that the MTDH-SND1 complex exhibits strong binding affinity, primarily driven by electrostatic and hydrophobic interactions. Structural stability analysis confirmed the complex's integrity during simulations, while dynamic cross-correlation and mutual information analyses revealed a key interaction region (R1) with correlated motions, which was further proved by contact probability analysis. Hydrogen bond analysis identified a stable network involving residues Arg239, Arg243, and Hie263, which were confirmed as hotspot residues by the alanine scanning mutagenesis method. Furthermore, the binding and interaction mechanisms between SND1 and 12 activity-known small molecule inhibitors were investigated and compared with that in the MTDH-SND1 complex. Energy decomposition highlighted that the conserved triad-Arg239, Arg243, and Hie263-is crucial across all systems. This work provides unprecedented atomic-level insights into the MTDH-SND1 interaction and offers a robust structural foundation for the rational design of high-affinity inhibitors against this oncogenic PPI. - Source: PubMed
Publication date: 2026/04/30
Zhu XiChang JiaruiFang MinWu XinyuYin ZhixiangZhang John Z HQi FenghuaZhu TongGao Ya