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increased expression of NF-YA may promote a malignant phenotype in OS cells via modulation of FASN (show FASN Proteins) expression.
The findings indicate that overexpression of NF-YA contributes to tumor angiogenesis through EZH2 (show EZH2 Proteins)-STAT3 (show STAT3 Proteins) signaling in human melanoma cells, highlighting NF-YA as a potential therapeutic target in human melanoma.
Data indicate that specific cancer-driving nodes are generally under NF-YA/B control.
our results indicate that NF-YA alternative splicing is an influential muscle cell determinant, through direct regulation of selected cell cycle blocking genes, and, directly and indirectly, of muscle-specific (show EIF3K Proteins) transcription factors
enhanced CDCA8 (show CDCA8 Proteins) promoter activities by NF-Y overexpression and reduced CDCA8 (show CDCA8 Proteins) transcription by NF-Y knockdown further verified that NF-Y is a positive regulator of CDCA8 (show CDCA8 Proteins) transcription.
Data show that Zinc-fingers and homeoboxes 2 (ZHX2 (show ZHX2 Proteins)) represses nuclear transcription factor Y alpha (NF-Y)-mediated activation of multidrug resistance 1 (MDR1) transcription.
NF-Y inhibits NT2/D1 cell growth in p53 (show TP53 Proteins)-independent manner and decreases SOX2 (show SOX2 Proteins) expression.
Stimulation of the lymphocytes with phytohemagglutinin, restores normal OGG1 (show OGG1 Proteins) levels and repair rates. MAP kinase (show MAPK1 Proteins) c-Jun N-terminal kinase (JNK) and the recruitment of the transcription factor NFYA to the promoter region of OGG1 (show OGG1 Proteins) are shown to be involved.
Association of p21 with NF-YA suppresses the expression of PLK1 and prevents mitotic death in response to DNA damage.
NF-YA binds directly over the CCAAT sequence.
Interaction of C/EBP-beta and NF-Y factors constrains activity levels of the nutritionally controlled promoter IA expressing the acetyl-CoA carboxylase-alpha gene in cattle.
Data show that nuclear factor Y (NF-Y) binds to the inverted CCAAT element (ICE) in the Fatty acid synthase (Fasn (show FASN Proteins)) promoter specifically in refeeding states.
findings may point to a possible role of NF-YA in stress conditions that occur in chronic obesity, ER stress might be involved in the pathogenesis of obesity through NF-YA depletion.
we conclude that NF-Y and YY1 (show YY1 Proteins) are important for the basal transcription of Pcyt2 (show PCYT2 Proteins) and that NF-Y is involved in the inhibitory effects of 25-HC on Pcyt2 (show PCYT2 Proteins) transcription.
these results indicate that the transcription factor NF-Y regulates the proximal promoter activity of mouse Col11a1 (show COL11A1 Proteins) gene in chondrocytes
these results raise an exciting possibility that targeting CDK1 (show CDK1 Proteins) or NF-Y in the diseased heart may inhibit fibrosis and subsequently confer cardioprotection.
NF-Ya is a functional activator of Bmal1 (show ARNTL Proteins) transcription and it cooperates with Sp1 (show SP1 Proteins) and Rev-Erbalpha (show NR1D1 Proteins) to generate the daily cycle of Bmal1 (show ARNTL Proteins) expression.
Sp1 (show SP1 Proteins), CREB (show CREB1 Proteins), HNF-1 (show HNF1A Proteins), and NF-Y, known to be responsive to hormones and diet, regulate NAGS (show NAGS Proteins) transcription
results indicate nuclear transcription factor NF-Y as a pivotal upstream participant in a regulatory network necessary for the preservation of cycling hematopoietic stem cell.
Findings establish that NF-Y acts upstream of E2F1 (show E2F1 Proteins) in p53 (show TP53 Proteins)-mediated apoptosis.
Transcriptional regulation of myeloid differentiation primary response (MyD) genes during myeloid differentiation is mediated by nuclear factor Y.
The protein encoded by this gene is one subunit of a trimeric complex, forming a highly conserved transcription factor that binds to CCAAT motifs in the promoter regions in a variety of genes. Subunit A associates with a tight dimer composed of the B and C subunits, resulting in a trimer that binds to DNA with high specificity and affinity. The sequence specific interactions of the complex are made by the A subunit, suggesting a role as the regulatory subunit. In addition, there is evidence of post-transcriptional regulation in this gene product, either by protein degradation or control of translation. Further regulation is represented by alternative splicing in the glutamine-rich activation domain, with clear tissue-specific preferences for the two isoforms.
, nuclear transcription factor Y, alpha
, CAAT box DNA-binding protein subunit A
, CAAT-box DNA binding protein subunit A
, CCAAT-binding transcription factor subunit B
, HAP2 CCAAT-binding protein
, Transcription factor NF-Y, A subunit
, nuclear transcription factor Y subunit A
, nuclear transcription factor Y subunit alpha
, CAAT-box DNA-binding protein subunit A
, NF-Y protein chain A
, nuclear transcription factor-Y alpha