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- W2022136880 abstract "NFкB exists as a multi-gene family of proteins that can form stable homo- and heterodimeric complexes that vary in their DNA binding specificity and transcriptional activation potential. Five proteins belonging to the NFкB family have been identified in mammalian cells: RelA (p65), c-Rel, RelB, NFкB1 (p50 and its precursor p105), and NFкB2 (p52 and its precursor p100). NFкB/Rel proteins share a highly conserved 300 amino acid N-terminal Rel homology domain (RHD) responsible for DNA binding, dimerization, and association with the IкBB inhibitory proteins. The p50/p65 complex displays strong transcriptional activation, whereas the p50/p50 and p52/p52 homodimers function to repress transcription of NFкB target genes. The existence of a multi-gene family provides one tier of regulation by which the cell can fine-tune NFкB mediated gene expression. NFкB resides in the cytoplasm in an inactive form by virtue of its association with a class of inhibitory proteins termed IкBs. Seven IкBs have been identified that include IкBα, IкBβ, IкBɛ, IкBγ, Bcl3, NFкB1 precursor (p105), and the NFкB2 precursor (p100). The IкB family members, having in common ankyrin repeat domains, regulate the subcellular localization, and hence the DNA binding and transcriptional activity, of NFкB proteins. Activation of NFкB is achieved primarily through the signal induced proteolytic degradation of IкB that is mediated by the ubiquitin/proteasome system. The critical event that initiates the degradation of IкB is the stimulus dependent phosphorylation of IкB at specific N-terminal residues. Phosphorylation of IкBα on serines 32 and 36 is mediated by IкB kinases (IKKs), whose activity is induced by activators of the NFкB pathway." @default.
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- W2022136880 date "2006-11-01" @default.
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- W2022136880 title "594 POSTER Combined targeting of mTOR and ILK for maximal suppression of cancer cell growth, Akt activation and cell survival" @default.
- W2022136880 doi "https://doi.org/10.1016/s1359-6349(06)70599-7" @default.
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