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MiR (show MLXIP Proteins)-22 over-expression attenuated lung cancer cell EMT (show ITK Proteins) and invasion via targeted inhibiting Snail.
High glucose enhances the formation of EZH2 (show EZH2 Proteins)/Snail/HDAC1 (show HDAC1 Proteins) complex in the nucleus, which in turn causes E-cadherin (show CDH1 Proteins) repression.
Neutrophils and Snail orchestrate the establishment of a pro-tumor microenvironment in lung cancer.
Snail-1 plays a major role in the progression and migration of urinary bladder cancer.
In patients with gastric cancer, the positive-to-negative conversion of the Snail status-between primary tumors and lymph node metastasis may be important for confirming epithelial-mesenchymal transition and mesenchymal-epithelial transition.
Inhibition of cell migration, invasion, and metastasis in esophageal carcinoma requires CBX8 (show CBX8 Proteins)-mediated repression of Snail.
Dermal fibroblast-to-myofibroblast transition sustained by alphavss3 integrin-ILK-Snail1/Slug signaling is a common feature for hypermobile Ehlers-Danlos syndrome and hypermobility spectrum disorders.
increased abundance of Snail and Axin2 (show AXIN2 Proteins) is highly correlated to malignant transformation of OL, making them novel biomarker(s) predicting oral cancer development
FoxM1 (show FOXM1 Proteins) may enhance the invasion and migration of cancer cells, and thus promotes their Epithelialmesenchymal transition, in a mechanism that may involve the regulation of Snai1.
High SNAIL expression is associated with invasion, metastasis, and epithelial-to-mesenchymal transition of gastric cancer.
Nrf2 (show NFE2L2 Proteins) attenuates Epithelial-mesenchymal transition and fibrosis process by regulating the expression of snail in pulmonary fibrosis.
Pbx-dependent Epithelial-mesenchymal transition programs mediate murine upper lip/primary palate morphogenesis and fusion via regulation of Snail1.
a Snail1-ATGL (show PNPLA2 Proteins) axis that regulates adipose lipolysis and fatty acid release, is reported.
A20 (show TNFAIP3 Proteins) promotes metastasis of aggressive basal-like breast cancers through multi-monoubiquitylation of Snail1.
Metagenomic analysis revealed direct correlation between PPARGC1A, SNAI1, and metastatic lung disease.
both Snail and Slug are able to form binary complexes with either YAP (show YAP1 Proteins) or TAZ (show TAZ Proteins) that, together, control YAP (show YAP1 Proteins)/TAZ (show TAZ Proteins) transcriptional activity and function throughout mouse development.
results demonstrate that skeletal stem/stromal cell mobilize Snail/Slug-YAP (show YAP1 Proteins)/TAZ (show TAZ Proteins) complexes to control stem cell function
these results might suggest that calcineurin inhibitor (show RCAN1 Proteins)-induced tubular SNAI1 protein cytoplasmic accumulation, possibly because of impaired SNAI1 proteasomal degradation and nuclear translocation, might be a sign of a diseased profibrotic epithelial phenotype.
Snail1 as a molecular bypass that suppresses the anti-proliferative and pro-apoptotic effects exerted by wild-type p53 (show TP53 Proteins) in breast cancer
While either Snail or Serpent induced a profound loss of epithelial polarity and tissue organisation, Serpent but not Snail also induced an increase in the size of wing discs. Furthermore, the Serpent-induced tumour-like tissues were able to grow extensively when transplanted into the abdomen of adult hosts.
Disruption of Snail expression in follicle stem cells compromises proliferation, but not maintenance. FSCs with excessive Snail expression had increased proliferation and lifespan, accompanied by a moderate decrease inE-cadherin expression (required for adhesion of FSCs to their niche) at the junction between their adjacent cells, indicating a conserved role of Snail in E-cadherin (show CDH1 Proteins) inhibition.
during gastrulation of Drosophila embryos, Sna expression downregulates polarity protein Baz which in turn results in junction disassembly at protein levels.
evidence for mechanosensitivity of cell-cell junctions and implications that myosin-mediated tension can prevent Snail-driven Eepithelial-mesenchymal transitions
Snail can potentiate enhancer activation by collaborating with different activators, providing a new mechanism by which Snail regulates development.
Rapid transcription kinetics and negative autoregulation are responsible for the remarkable homogeneity of snail expression and the coordination of mesoderm invagination.
Study shows that Sna represses transcription of pbl in the mesoderm primordium of D. melanogaster via one or more Sna-binding sites, which are conserved among species of the Drosophila genus, but not in the mosquito, correlating with the different modes of gastrulation in the different genuses.
Complex interactions between cis (show CISH Proteins)-regulatory modules in native conformation are critical for Drosophila snail expression.
The Snail repressor positions Notch (show NOTCH1 Proteins) signaling in the Drosophila embryo.
results show that Sna has a positive regulatory function on sim (show SIM2 Proteins) expression in the presumptive mesectoderm; this positive effect of Sna depends on the Su(H (show RBPJ Proteins))-binding sites within the sim (show SIM2 Proteins) promoter, suggesting that Sna regulates Notch (show NOTCH1 Proteins) signaling
The transcription factor Snail1 is essential for tissue separation, enabling paraxial protocadherin (PAPC (show PCDH8 Proteins)) to promote tissue separation through novel functions.
Interaction with Snail1/2, and Twist function more generally, is regulated by GSK-3-beta-mediated phosphorylation of conserved sites in the WR domain.
the same E3 ubiquitin ligase (show MUL1 Proteins) known to regulate Snail family proteins, Partner of paired (Ppa (show FBXL14 Proteins)), also controlled Twist stability and did so in a manner dependent on the Twist WR-rich domain
The Drosophila embryonic protein snail is a zinc finger transcriptional repressor which downregulates the expression of ectodermal genes within the mesoderm. The nuclear protein encoded by this gene is structurally similar to the Drosophila snail protein, and is also thought to be critical for mesoderm formation in the developing embryo. At least two variants of a similar processed pseudogene have been found on chromosome 2.
, protein snail homolog 1
, snail 1 homolog
, snail 1 zinc finger protein
, snail 1, zinc finger protein
, snail homolog 1
, zinc finger protein SNAI1
, snail like protein
, Protein snail-like protein 1
, snail homolog 1 (Drosophila)
, zinc-finger transcription factor Snail
, protein Xsnail
, protein snail homolog Sna
, protein xSna
, snail protein
, zinc finger protein with snail domain similar to escargot
, transcription factor protein
, snail zinc finger protein
, snail-like protein 1