Ask about this productRelated 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
- SND1 is an oncoprotein found to be overexpressed in breast cancer, especially in triple-negative breast cancer(TNBC). In our previous study, a novel SND1-interacting peptide 4-2 was identified, exhibiting cytotoxicity to TNBC cells by inducing SND1 degradation. This study for the first time demonstrated the degradation of SND1 was proteasome-dependent. A series of peptide 4-2 derivatives were constructed using PROTAC technology. Among these, 4-2 VHL-recruiting PROTAC showed significantly increased SND1 degradation efficiency and higher anticancer activity to TNBC cells. The in vivo efficacy study suggested the D-isoform of 4-2VHL PROTAC suppressed the growth of TNBC cells in xenograft mouse model more effectively than peptide 4-2. Mechanistically, 4-2 VHL-recruiting PROTAC was demonstrated to induce pyroptosis of TNBC cells through Fas-mediated IL-17signaling. This study provides a new lead compound for the development of theSND1-targeted therapy via the proteolysis-targeting system. - Source: PubMed
Wang QiqiHuang QiufengOu HuipingHuang TingtingHe YunjiaoLi Peng - Xylem development involves a series of coordinated processes, including cell differentiation, expansion, secondary cell wall (SCW) deposition, and programmed cell death (PCD). Here, we characterize a subtilisin-like serine protease gene, SBT4.1, which exhibits specific expression in stem xylem. Loss of SBT4.1 function results in reduced xylem cell number, smaller cell size, thinner secondary walls, and delayed organelle degradation during PCD. In contrast, SBT4.1 overexpression accelerates cellular clearance and increases xylem cell number, size, and wall thickness, indicating its critical roles in differentiation, SCW synthesis, and PCD. Consistent with a positive regulatory function, pectinase activity and the expression of pectin-related genes are decreased in the mutant but increased in overexpressors. Accordingly, SBT4.1 promotes cell expansion, at least partly, by modulating pectinase activity, as evidenced by enhanced pectin methylesterase (PME) activity upon co-expression with specific PME genes in Nicotiana benthamiana. Molecular analyses revealed that SBT4.1 is a direct transcriptional target of the key SCW regulators SND1, VND6, and MYB46. Furthermore, the expression of SCW synthesis-related genes and PCD-associated protease genes is downregulated in the mutant and upregulated in overexpressing plants. Taken together, our findings demonstrate that SBT4.1, transcriptionally activated by SND1/VND6/MYB46, coordinates xylem cell differentiation, SCW deposition, and PCD, while also promoting cell expansion through modulation of pectin metabolism. - Source: PubMed
Publication date: 2026/08/06
Zhang ChongXu YaomingGe ZiyueSun YuSun LeiqianLi HuiLu Hai - Hepatocellular carcinoma (HCC) is undergoing a profound epidemiological shift from viral etiologies toward metabolic dysfunction-associated steatohepatitis (MASH). Current targeted therapies often fail to provide effective responses due to the complex, interconnected nature of the tumor microenvironment. This review aims to explain the molecular axis linking chronic metabolic injury to carcinogenesis, focusing specifically on the oncoproteins Astrocyte elevated gene-1/metadherin (AEG-1/MTDH) and staphylococcal nuclease and tudor domain-containing 1 (SND1) as cooperating regulators of this disease network. This article represents a narrative review of the published literature and does not follow a systematic or exhaustive search protocol. A structured literature search using specific search terms was conducted across PubMed, Scopus, and Web of Science databases, with a last search date of May 2026. Available preclinical data indicate that AEG-1 mediates early preneoplastic injury via dysregulation of hepatic lipid metabolism leading to lipotoxicity and survival of genetically unstable hepatocytes. As the disease progresses, AEG-1 amplifies NF-κB-driven inflammation and, as tumors emerge, recruits SND1 as a cooperating partner to form a gene-silencing complex that suppresses tumor suppressor proteins. Furthermore, AEG-1 and SND1 reprogram surrounding macrophages into an immunosuppressive state and drive tumor resistance to standard anti-angiogenic and chemotherapeutic drugs. The evidence reviewed supports a model in which HCC is driven by an interconnected metabolic-inflammatory-oncogenic cycle. AEG-1 functions as an upstream metabolic and inflammatory driver that cooperates with SND1 in a subset of oncogenic silencing events within this pathogenic network. Therefore, utilizing advanced nanomedicine platforms to simultaneously target these proteins represents a mechanistically rational therapeutic strategy that warrants further preclinical evaluation in advanced HCC. - Source: PubMed
Publication date: 2026/07/20
Azzam ShadyStraus AlexandraSenkal CanSarkar Devanand - The protein-protein interaction (PPI) between metadherin (MTDH) and staphylococcal nuclease and tudor domain-containing 1 (SND1) drives oncogenic signaling and tumor progression in multiple cancer types, yet remains an underexploited therapeutic target. Here, we report an integrated computational-experimental strategy to identify small-molecule disruptors of the MTDH-SND1 interface. A focused PubChem library of 4149 2-arylbenzothiazoles was screened using a tiered workflow combining drug-likeness/PAINS filtering, hierarchical docking into the MTDH-binding groove on SND1 (PDB 4QMG), and MM/PBSA-based refinement. Top-ranked candidates were further evaluated by 1-μs molecular dynamics (MD) simulations and prioritized based on pose stability and interfacial engagement metrics. Four representative hits-L1 (2-(4-aminophenyl)benzothiazole), L2 (2-(4-amino-3-methylphenyl)-5-fluorobenzothiazole), L3 (YL-109), and L4 (2-(3,4,5-trimethoxyphenyl)benzothiazole)-were advanced for experimental validation. MD analyses indicated ligand-dependent modulation of PPI stability and conformational landscapes, while MM/PBSA decomposition suggested binding was driven predominantly by short-range hydrophobic packing within the interfacial groove. A quantitative split-luciferase complementation assay confirmed dose-dependent disruption of MTDH-SND1 in a cell-free format with low-micromolar potency (IC: L1 10.72 ± 1.12 μM, L2 5.72 ± 0.92 μM, L3 11.77 ± 1.42 μM, L4 7.41 ± 1.01 μM) and in a cell-based reporter (IC: L1 35.71 ± 2.80 μM, L2 16.44 ± 0.24 μM, L3 32.96 ± 2.58 μM, L4 21.93 ± 0.9 μM). Importantly, a linked-luciferase counterscreen (IC > 1000 μM) supported minimal luciferase interference. MST analysis further confirmed direct binding of L1-L4 to purified SND1, yielding low-micromolar K values. Together, these results establish 2-arylbenzothiazoles as a promising chemotype for MTDH-SND1 PPI inhibition and provide a validated computational-to-experimental framework for discovering and optimizing MTDH-directed therapeutics. - Source: PubMed
Publication date: 2026/07/24
Kamel Emadeldin MKhadrawy Sally MostafaAllam Ahmed AOthman Sarah IAbalkhail AdilAlkhayl Faris F AbaLamsabhi Al Mokhtar - Immunotherapy has revolutionized the treatment landscape of breast cancer, particularly for triple-negative breast cancer (TNBC), yet primary and acquired resistance remain formidable obstacles limiting durable clinical benefit. This review provides a comprehensive update on recent advances in breast cancer immunotherapy, with a focused emphasis on the molecular and cellular mechanisms driving treatment resistance and emerging strategies to overcome them. We dissect tumor-intrinsic resistance pathways, including loss of tumor antigens, defects in antigen processing and presentation machinery, insensitivity to interferon-γ signaling, metabolic reprogramming, and epigenetic dysregulation. Tumor-extrinsic mechanisms, such as infiltration of immunosuppressive cells, abnormal angiogenesis, extracellular matrix remodeling, and FGF/FGFR genomic amplification, are highlighted as key barriers to effective immune checkpoint blockade. Emerging evidence implicates novel resistance mediators, including the DUSP22-LGALS1 axis, THSD4-driven T cell exclusion, and the MTDH-SND1 complex impairing antigen presentation, etc. We critically evaluate current strategies to surmount resistance, encompassing combination regimens with chemotherapy, targeted therapies, radiotherapy, and novel immunomodulators. The review also addresses challenges in managing immune-related adverse events, controversies surrounding patient selection biomarkers, and the urgent need for optimized efficacy evaluation systems beyond RECIST criteria. Finally, we discuss future directions, including novel immune checkpoints, microbiome modulation, artificial intelligence-assisted decision-making, and innovative trial designs. By integrating mechanistic insights with clinical evidence, this review provides a framework for understanding and overcoming immunotherapy resistance, advancing the paradigm from "effective" to "precise" immuno-oncology in breast cancer. - Source: PubMed
Publication date: 2026/07/21
Wang Jia-MeiZhou YiLi FeiDing Yu