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Results indicated that DLL3 expression was silenced in hepatocellular carcinoma (HCC (show FAM126A Proteins)) cells by DNA methylation (show HELLS Proteins) and was more readily affected by histone acetylation than histone methylation (H3K9me2 or H3K27me3).
our results indicated epidermal growth factor-like domain multiple 7 protein participates in growth hormone-secreting pituitary adenoma proliferation and invasion regulation via Notch2/DLL3 signaling pathway. These findings raised the possibility that epidermal growth factor-like domain multiple 7 protein might serve as a useful biomarker to assess growth hormone-secreting pituitary adenoma invasion and prognosis
The Dll3 was rarely detectable in (show PIK3CA Proteins) the (show AKT1 Proteins) para-carcinoma tissues, but positi (show NOTCH1 Proteins)ve in 82.1% of non-small cell cancer tissues.
Both global haplotype and individual haplotype analyses showed that the haplotypes of SNP1/SNP2/SNP3/SNP4/SNP5 did not correlate with the disease (P >0.05). Together, these data suggest that genetic variants of the DLL3 gene are not associated with CS in the Chinese Han population.
DLL3 was silenced by methylation in human human hepatocellular carcinoma and it negatively regulates the growth of human hepatocellular carcinoma cells.
We suggest that the three human DLL3 mutations associated with spondylocostal dysplasia are also functionally equivalent to the Dll3(neo) null allele in mice.
mutations in DLL3 cause a consistent pattern of abnormal vertebral segmentation in spondylocostal dysostosis
no novel or previously described mutations are present in our cohort, indicating that DLL3 mutations may not be a major cause of congenital scoliosis.
The intracellular region of Notch (show NOTCH1 Proteins) ligands Dll1 (show DLL1 Proteins) and Dll3 regulates their trafficking and signaling activity
Structural deformities of the vertebral column and adjacent ribs in the pudgy mouse are caused by mutations in Dll3. Review.
Dll3 overexpression promoted PI3K/Akt (show AKT1 Proteins) signaling through inhibiting Notch (show NOTCH1 Proteins) signaling in lung cancer.
O-fucosylation of DLL3 is required for its function during somitogenesis.
Intriguing changes are observed in the cranio-caudal borders of multifidus muscle in mutant Dll3 and Lfng (show LFNG Proteins) models of idiopathic scoliosis.
Dll3 has a unique function during T-cell development that is distinct from the role played by the other DSL ligands of Notch (show NOTCH1 Proteins).
Dll3 targets Notch1 (show NOTCH1 Proteins) for lysosomal degradation preventing Notch1 (show NOTCH1 Proteins) from undergoing post-translational processing.
Axial skeletal defects caused by mutation in the spondylocostal dysplasia/pudgy gene Dll3 are associated with disruption of the segmentation clock within the presomitic mesoderm.
DLL3 knockout mice have segmentation and neural defects
Notch (show NOTCH1 Proteins) ligands, including Delta-like1 and 3 and Jagged1 (show JAG1 Proteins) and Jagged2 (show JAG2 Proteins), show distinct expression patterns in the developing and adult brain overlapping that of Notch1 (show NOTCH1 Proteins)
Data describe the genetic interactions between Dll1 (show DLL1 Proteins), Dll3, Mesp2 (show Mesp2 Proteins) and Psen1 (show PSEN1 Proteins), and the roles of Dll1 (show DLL1 Proteins)- and Dll3-Notch (show NOTCH1 Proteins) pathways, with or without Psen1 (show PSEN1 Proteins), in rostrocaudal patterning.
This gene encodes a member of the delta protein ligand family. This family functions as Notch ligands that are characterized by a DSL domain, EGF repeats, and a transmembrane domain. Mutations in this gene cause autosomal recessive spondylocostal dysostosis 1. Two transcript variants encoding distinct isoforms have been identified for this gene.
delta-like protein 3
, drosophila Delta homolog 3