SKIP, a CBF1-associated protein, interacts with the ankyrin repeat domain of NotchIC to facilitate NotchIC function

Biochemistry, Genetics and Molecular Biology

• Ankyrin 100%
• Ankyrin Repeat 100%
• Silencing Mediator of Retinoid and Thyroid Hormone Receptor 100%
• Protein-Protein Interaction 50%
• Promoter Region 50%
• Cell Fate 50%
• Biological Activity 50%
• Cellular Differentiation 50%
• Binding Protein 50%
• Binding Competition 50%
• Transmembrane Receptors 50%
• Corepressor 50%
• Caenorhabditis Elegans 50%
• Drosophila Melanogaster 50%
• Antisense 50%
• Yeast Two-Hybrid Screening 50%
• Notch 50%
• Notch Signaling Pathway 50%
• Histone Deacetylase 50%
• Notch Proteins 50%
• DNA-binding Protein 50%

Immunology and Microbiology

• Notch 100%
• Silencing Mediator of Retinoid and Thyroid Hormone Receptor 100%
• Cell Differentiation 50%
• Protein Protein Interaction 50%
• Cell Fate 50%
• Biological Activity 50%
• Protein Binding 50%
• Promoter Region 50%
• DNA Binding Protein 50%
• Caenorhabditis Elegans 50%
• Muscle Cell 50%
• Antisense 50%
• Binding Competition 50%
• Drosophila Melanogaster 50%
• Notch Signaling 50%
• Myoblast 50%

Keyphrases

• Associated Proteins 100%
• CBF1 100%
• Ankyrin Repeat 100%
• Ski-interacting Protein 100%
• Transcriptional Repression 16%
• Co-repressor Complex 16%
• Cell Fate Decision 8%
• Biological Activity 8%
• Translocated 8%
• Caenorhabditis Elegans 8%
• Membrane Receptors 8%
• Binding Experiment 8%
• DNA-binding Proteins 8%
• Binding Protein 8%
• Corepressor 8%
• Drosophila Melanogaster 8%
• Antisense 8%
• Competition Binding 8%
• Histone Deacetylase 1 (HDAC1) 8%
• Individual Cells 8%
• Mutually Exclusive 8%
• Myoblast 8%
• Yeast Two-hybrid Screen 8%
• Protein-protein Interaction Assay 8%
• Notch Proteins 8%
• Notch Signal Transduction 8%
• Inter-cell 8%
• Muscle Cell Differentiation 8%