Publication for NFKB1 and NFKB2

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
hsa	NFKB1	nuclear factor kappa B subunit 1	4790			[link]
hsa	NFKB2	nuclear factor kappa B subunit 2	4791

Pubmed ID	Priority	Text
19524538	1.00	NF-kappaB signaling system consists of five NF-kappaB subunits:RelA, c-Rel, RelB, p50, and p52:and five proteins with inhibitory activity:IkappaBalpha, IkappaBbeta, IkappaBepsilon, p105, and p100.
	0.98	Nfkb1 and Nfkb2 proteins p105 and p100 serve both as NF-kappaB precursors and inhibitors of NF-kappaB dimers.
	0.98	p50 and RelB:p50 dimers to the nucleus and leaving p52:p100 cis-inhibited dimers.
	0.97	p52 preferentially partitioned to high-MW fractions, which also contained p105 and p100 (Figure 1C).
	0.97	p105 proteins self-associate upon synthesis, they may either be completely processed to give rise to p50 or p52 homodimers, or they may form stable high-MW assemblies via two intermediates, complex I and complex II.
	0.96	Nfkb1 and Nfkb2 Proteins p105 and p100 Function as the Core of High-Molecular-Weight Heterogeneous Complexes
	0.96	p105 and p100 trap at least 50% of cytoplasmic p50 and p52 in macrophages post-LPS stimulation, thus participating in terminating NF-kappaB signaling.
	0.95	p50 and p52, p105 and p100 can also inhibit preformed NF-kappaB dimers.
	0.94	Nfkb1/p105 and Nfkb2/p100 share sequence similarity with both classical IkappaBs (IkappaBalpha, IkappaBbeta, and IkappaBepsilon) and NF-kappaBs (RelA, c-Rel, and RelB) because of the presence of the RHD and ANK domains (Figure 1A and Figure S1 available online).
	0.94	p105 or p100 associate with RelA, c-Rel, or RelB, they may be processed to give rise to NF-kappaB heterodimers containing p50 or p52, as has been previously shown for p50:c-Rel and p50:RelA. The processing may be constitutive or stimulus inducible, but the partner NF-kappaB subunit is likely to influence its efficiency (Figure 7C).
	0.92	p50 dimer activity during LTbetaR signaling and RSV-induced signaling, and stimulus-responsive expression of the nfkb2 gene can provide negative feedback onto RelA:p50 dimer during prolonged TLR-mediate IKK signaling.
	0.91	p50 and p52 appear as two isoforms in western blots.
	0.87	nfkb1-/-nfkb2-/- MEF were analyzed by GF in the presence of 0.5% DOC.
	0.85	NF-kappaB signaling system consists of five NF-kappaB subunits:RelA, c-Rel, RelB, p50, and p52:and five proteins with inhibitory activity:IkappaBalpha, IkappaBbeta, IkappaBepsilon, p105, and p100.
	0.65	Nfkb1 and Nfkb2 proteins, p105 and p100, have dual functions in the NF-kappaB signaling system.
26988706	0.98	p50 and p52 is indicated in these cells.
	0.98	p50 or p52 alone.
	0.98	p50-selective motifs contained a higher conservation of a G in the first position compared to p52-selective motifs, indicating a putative contribution of highly symmetric binding sites for p50 homodimer recruitment.
	0.98	p50 and p52 are prevalent in HL cells.
	0.98	p50/RelA or p52/RelB (Additional file 9: Table S7) differed greatly in the enriched GO terms (Fig. 4b, Additional file 10: Table S8).
	0.98	p50/RelA and p52/RelB control genes that are involved in modulation of immune system responses as well as cell survival.
	0.98	p50-RelA or p52-RelB) was not significantly associated with gene regulation ('1010' and '0101' in Fig. 5a and Additional file 2: Figures S5B and C).
	0.98	p50 and p52 recruitment.
	0.98	p50-RelA and p52-RelB, both of which activated genes associated with cell death/apoptosis (Fig. 4a), on cell viability.
	0.98	NF-kappaB subunits, but a decrease in protein levels was only observed upon the KD of p52/RelB, which was concomitant to strong caspase 8 activation (see Fig. 6b).
	0.98	p52-RelB is essential for the survival of HL cells through the upregulation of proteins that block the intrinsic and especially the extrinsic apoptosis pathway (for example, c-Flip), whereas p50-RelA also contributes to survival by the upregulation of Bcl-XL and subsequent inhibition of the intrinsic apoptosis pathway.
	0.98	p50 and p52 in HL cells can be observed at late time points upon stimulation with TWEAK or CD40, suggesting that this might be a common feature of cells with stimulated NIK pathways.
	0.98	p50 and p52 and each of them is recruited to more than 10,000 binding regions.
	0.98	p50/RelA or p52/RelB. Several established NF-kappaB targets, which were previously identified, such as CCR7, CCND2, FAS, JUNB, or VCAM1, were bound by canonical and non-canonical subunits, but not regulated upon knockdown.
	0.98	p50/RelA and p52/RelB, revealing additive or synergistic regulation.
	0.98	p50 or p52 dimers that lack transactivation domains and do not interact with transcriptional co-activators, may prevent access of activating RelA or RelB containing heterodimers.
	0.98	p50-RelA and p52-RelB alone is significantly associated with gene regulation.
	0.97	p50-RelA. The non-canonical pathway depends on the activation of NF-kappaB-inducing kinase (NIK) and IkappaB kinase alpha (IKKalpha), resulting in the induction of NF-kappaB dimers containing p52 and/or RelB. Our recent work, however, has shown that non-canonical signaling is more complex.
	0.97	p50 and p52 production, NIK depletion had a similar effect on total NF-kappaB DNA-binding (Additional file 2: Figure S1A).
	0.97	p50 and p52 was also evident in primary HL samples.
	0.97	NF-kappaB activity in HL cells, which is strongly dominated by production of dimers that contain p50 or p52.
	0.97	p50, and p52 binding regions.
	0.97	p50 and p52 dimers recognize distinct DNA motifs, MEME de novo search was performed with ChIP-seq regions that selectively recruited p50 or p52.
	0.97	p50-RelA or p52-RelB are rare in both cell types, about 2 %.
	0.97	p50/RelA and p52/RelB. a, b Genes activated (a) or repressed (b) by p50/RelA or p52/RelB in L1236 cells, respectively, and functional enrichment analysis of using Gene Ontology for biological processes (GO) analysis.
	0.97	p52/RelB controls the majority of the NF-kappaB regulated genes and especially represses genes involved in differentiation processes.
	0.97	p50 and p52, either alone or in combination with RelB or RelB plus RelA was significantly associated with regulation (that is, activation or repression) of gene expression by canonical and non-canonical dimers.
	0.97	NF-kappaB subunit-selective gene regulation is not determined by the exclusive recruitment of the targeted prototypic dimers, but by more complex combinations of NF-kappaB subunits, involving a parallel contribution of p50 and p52.
	0.97	p50/RelA or p52/RelB KD efficiencies and expression of the initiator caspase 8 (p18), the initiator caspase 9 (p10), and the effector caspase 3 (p17) in the samples of L1236 cells treated with siRNAs as described above.
	0.97	p105 precursor processing to p52 and p50.
	0.97	p52/RelB that primarily affected the extrinsic apoptosis pathway, while p50/RelA contributed to cell death protection by interfering with the intrinsic pathway.
	0.96	p105 and p100, their products p50 and p52, as well as phospho-Ser-866/870-p100 and phospho-Ser-933-p105 were analyzed in whole extracts by western blot (WB).
	0.96	p50 and p52 but only a low amount of RelA was present in the nucleus.
	0.96	p50 and in 83 % for p52 (Fig. 1c and Additional file 3: Table S1).
	0.96	p50 and/or p52, in contrast to RelA and RelB in LCL.
	0.96	p50/RelA- and p52/RelB-dependent sets in each case partially overlapped, but also revealed genes that were only controlled by either p50/RelA or p52/RelB (Fig. 4a and b, top panels).
	0.96	p50 and p52.
	0.96	p50, p52, and RelB were distance independent.
	0.95	p50 and p52, which account for most NF-kappaB activity in HL cells.
	0.95	p50 (left panel) and p52 (right panel) in malignant Reed-Sternberg cells compared to surrounding benign cells.
	0.95	p50, p52, RelA, and RelB in L1236 cells.
	0.95	p50/p52 scored highest with repressed genes when in distal positions, but with activation, when at proximal positions (Additional file 2: Figure S5C and D).
	0.95	p50 and p52 significantly correlated with gene expression.
	0.95	p50, p52, and RelB, we have found in this study very similar 11-bp motifs for each factor (p50, p52, RelA, and RelB).
	0.94	p50/RelA- and/or p52/RelB have a high biological significance for HL (for a selection, see Fig. 4c) and encode cytokines and chemokines responsible for clinical symptoms and TF networks implicated in this disease.
	0.94	p50/RelA and p52/RelB subunit combinations, reflecting canonical and non-canonical NF-kappaB signaling in HL cells in vitro, with primary human lymphoma, we performed a retrospective analysis of microarray datasets generated from micro-dissected Hodgkin/Reed Sternberg (HRS) cells of classical HL, other malignant B cell lymphomas, and normal B cells at various stages of differentiation.
	0.94	p50, p52, RelA, and RelB in HL cells by ChIP-sequencing and combined these data with the genes regulated by these subunits.
	0.93	p50, p52, RelA, and RelB subunits in binding regions that have been assigned to genes they regulate reveal a cross-contribution of p52 and p50 to canonical and non-canonical transcriptomes.
	0.93	p50 and p52, and both are important to assure the full range of signal-induced gene expression.
	0.93	NF-kappaB dimer composition, p50 and p52 were immunoprecipitated from nuclear extracts (Additional file 2: Figure S1C).
	0.93	NF-kappaB subunit recruitment can be grouped into eight clusters (Fig. 2b) with a most prominent contribution of p50 and p52, either alone or in combination.
	0.93	p50/p52 (binary code '1100' in Fig. 5a), the identified high confidence binding patterns did not simply correlate with their frequency of occurrence in the ChIP-seq datasets (Additional file 8: Table S6).
	0.92	p50 and p52 are formed through NIK-dependent p105 and p100 precursor processing in HL cells and are the predominant DNA binding subunits.
	0.92	p50/RelA and p52/RelB
	0.92	p50/RelA and p52/RelB were defined as bound by at least p50 and p52, respectively, by ChIP-sequencing and differentially regulated upon KD of the specific dimers (FDR <0.05), and at least 10 % expression difference between the knockdown and control experiment).
	0.91	p52 and p50.
	0.91	p50 and p52, rather than with p52 alone, while RelA occupancy is least frequent.
	0.91	NF-kappaB subunits is very similar and binding regions are shared, even though the enrichment for RelA is weaker than that for p50, p52 and RelB (for example, NFKBIA gene).
	0.90	NF-kappaB family of transcription factors (TFs) includes RelA (p65), RelB, c-Rel, and the precursor proteins p105 and p100, which are processed to p50 and p52, respectively.
	0.90	NF-kappaB subunits, their cistromes, and p50/RelA- and p52/RelB-specific transcriptomes and functions in HL cells.
	0.88	p50, p52, RelA, and RelB in the promoter and first intron.
	0.87	p50/RelA and/or p52/RelB according to their activation or repression status and grouped them by related biological processes, using Gene Ontology (GO) terms.
	0.87	p50/RelA and p52/RelB, as indicated and harvested 3 days after the end of the siRNA treatments.
	0.84	p50 and p52 overlapped by about 70 %.
0.81	p50/RelA KD and up to 95 % reduction in viability upon p52/RelB KD (Fig. 6a and Additional file 2: Figures S6A and B).
0.79	p52/RelB as well as of p50/RelA (Fig. 6b).
0.78	p105/p50 and p100/p52 in representative biopsies from HL patients.
0.78	p50-RelA and p52-RelB gene signatures distinguish classical Hodgkin lymphoma from other lymphomas and normal B cells
0.74	p50 and p52 may recruit repressor complexes, including histone deacetylases, in a context-dependent manner to suppress transcription.
0.69	p52-RelB and to a lesser extent p50-RelB dimers in all cell lines.
0.69	p50-p52 heterodimers were detected.
0.63	p52/RelB revealed a high preference for binding of p50 along with p52, with or without RelB and were independent of proximal or distal localization of the region relative to the TSS (Fig. 5a).
0.62	p105 phosphorylation, accumulation of the precursors, and decreased generation of their products p52 and p50 (Fig. 1a).
0.54	p50 and p52 in the constitutive NF-kappaB activity in HL cells.
0.50	p50 to gene regulation by non-canonical p52-containing dimers and vice versa.
31134075	0.98	Nfkb2 retains RelB and other NF-kappaB proteins in the cytoplasm.
	0.98	NF-kappaB heterodimers, namely RelA:p50, RelA:p52, RelB:p50, and RelB:p52.
	0.98	Nfkb2-/- MEFs a low level of basal RelB:p50 activity; targeting IkappaBalpha-bound complexes, TNFp further augmented this RelB activity at 0.5 h post-stimulation that was diminished to the basal level by 1 h (Figure S2B).
	0.98	NF-kappaB signaling transiently in WT cells, produced a similar late RelB:p50 activity in Nfkb2-/- MEFs (Figure 2D; Figure S2C).
	0.98	NF-kappaBn induced in a time-course in Nfkbia-/- and Nfkb2-/- MEFs upon TNFp treatment (top panel).
	0.98	p50 response to TNFp in the Nfkb2-deficient system.
	0.98	NF-kappaB responsive transgenic promoter in Relb-/-Nfkb2-/- MEFs.
	0.98	p50 for their expressions; they were induced in Nfkb2-/- or Rela-/-Nfkb2-/- MEFs, but not in WT or Relb-/- Nfkb2-/- cells.
	0.98	p50 activated by TNFc in Nfkb2-/- cells induced a distinct set of genes, which were not induced by RelA:p50 in WT cells and encoded functions unrelated to immune processes.
	0.98	Nfkb2-/- MEFs revealed both overlapping and distinct gene functions of RelA:p50 and RelB:p50.
	0.97	NF-kappaBn response in Nfkb2-/- MEFs that consisted of an early peak and a progressively strengthening second phase (Figure 2B).
	0.97	Nfkb2-/- MEFs induce an additional late NF-kappaB activity composed of RelB:p50 heterodimers.
	0.97	Nfkb2-/- cells expressing RelB from the NF-kappaB-driven, but not constitutive, promoter (Figure S3B).
	0.97	Nfkb2-/- MEFs, but not in NF-kappaB-deficient cells.
	0.97	Nfkb2-/- MEF possessing both RelA:p50 and RelB:p50 activities.
	0.97	Nfkb2-/- cells, but <1.3 fold average induction in NF-kappaB-deficient cells to arrive onto a list of 304 genes.
	0.97	NF-kappaB-driven RelB synthesis augmented the constitutive RelB:p50 activity present in Nfkb2-/- MEFs in response to TNFp stimulation.
	0.97	p50 heterodimers, which generated enduring NF-kappaB response to short-lived TNF signal in Nfkb2-/- MEFs.
	0.96	p50 and RelB:p50 in our microarray studies, not only in WT and Nfkb2-/- MEFs but also in Relb-/-Nfkb2-/- and Rela-/-Nfkb2-/- cells.
	0.96	p50 in Nfkb2-/- MEFs, we asked if TNFp triggered persistent expression of NF-kappaB-dependent genes in p100-deficient cells.
	0.96	p50 activity induced at 8 h by the preceding TNF pulse in the Nfkb2-/-deficient system.
	0.96	Nfkb2-/- cells strengthen late RelB:p50 signaling.
	0.95	NF-kappaB-mediated transcription of Relb promoted the late RelB:p50 response to TNFp in the Nfkb2-deficient system (Figure 3C).
	0.95	p50 in WT, Nfkb2-/- and Relb-/- Nfkb2-/- MEFs or in RelB:p50-containing Rela-/- Nfkb2-/- cells.
	0.95	p50, either alone (Gr-III) or in collaboration with RelA:p50 (Gr-IV), activated additional genes in Nfkb2-/- MEFs that were not normally induced in WT MEFs.
	0.95	NF-kappaB-dependent genes were sustained by RelB:p50 in TNFp-stimulated Nfkb2-/- MEFs.
	0.94	Nfkb2-deficient system produced a prolonged NF-kappaBn response, whose temporal profile was somewhat comparable to that of the TNFc-induced NF-kappaBn activity (Figure 1E).
	0.94	Nfkb2-/- MEFs, which activated exclusively RelA:p50 upon TNFc treatment, and Rela-/-Nfkb2-/- cells, which elicited solely RelB:p50 response (Figure 4A).
	0.93	p50 response to TNFp in the Nfkb2-deficient system.
	0.92	Nfkb2-/- and Rela-/-Nfkb2-/- MEFs, we cataloged these NF-kappaB-dependent genes into six distinct clusters, which were arranged further into four gene-groups (Gr-I to Gr-IV; Figure 4B; Supplementary Materials, Materials and Methods).
	0.92	p50 activity induced in p100-deficient cells by TNFc paralleled the signal-induced RelA:p50 activity; it consisted of an early 0.5 h peak followed by an attenuated activity at 1 h and a late-acting response prevailing between 3 and 8 h. Our brief TNF stimulation regime instead generated contrasting temporal profiles of these two NF-kappaB heterodimers in Nfkb2-/- cells; it induced a transient RelA:p50 activity but a prolonged RelB:p50 response (Figure 9).
	0.91	p50 activity induced by TNFp in the Nfkb2-deficient system for the individual parameter groups.
	0.90	NF-kappaB control in the Nfkb2-deficient system where even short-duration IKK2 inputs produced prolonged NF-kappaBn responses (Figure 1D).
	0.87	p50 activity present in Nfkb2-/- MEFs.
	0.86	:p50 Modify the TNF-Activated Gene-Expression Program in Nfkb2-/- MEFs
	0.82	p50 and RelB:p50, we focused on TNFc regime, which produced equivalent nuclear activity of these two heterodimers at 6 h post-stimulation in Nfkb2-/- MEFs (Figure 4A).
	0.80	Nfkb2-/- MEFs stably expressing RelB from a retroviral transgene (tg) either constitutively (const.) or from an NF-kappaB responsive promoter.
	0.66	NF-kappaBn activity consisted of mostly RelA:p50 in the WT system with only a minor amount of RelA:p52 and RelB:p50 heterodimers (Figure 1F).
	0.63	p50 Response in Nfkb2-/- Cells
	0.57	p50 heterodimers generated the late-acting NF-kappaBn response to TNFp in the Nfkb2-deficient system (Figure 1F).
	0.55	Nfkb2-/- cells subjected to brief TNF stimulation, RelB:p50 sustained the expression of a subset of immune response genes and also activated additional RelB-important genes, which encoded immune differentiation and metabolic functions.
27641334	0.98	p52 activity was shown both to promote and suppress NFkappaB-dependent gene expressions in HMCLs and patient-derived myeloma cells.
	0.98	p50 activity at 8 h post-TNF stimulation in Rela-/-Nfkb2-/- MEFs (Figure 4c) and ChIP analyses revealed recruitment of RelB to Relb promoter at this time point (Figure 4d and Supplementary Figure S4e).
	0.98	NFkappaB dimers to cFLIP and cIAP2 promoter upon TNF treatment of Nfkb2-/- MEFs.
	0.97	NFkappaB module, which induces partial proteolysis of p100 into p52 to promote RelB:p52/NFkappaB activation from p100-inhibited complex during immune cell differentiation.
	0.97	Nfkb2-/- MEFs (Figure 4e) that temporally coincided with TNF-induced RelB:p50 DNA-binding activity.
	0.97	Nfkb2-/- MEFs in three out of four NFkappaB-dependent clusters.
	0.97	NFkappaB target genes was mostly preserved, and if anything was subtly enhanced, in Nfkb2-/- cells, which stimulates both RelA:p50 and RelB:p50 activity (Figures 5b and c).
	0.97	NF-kappaB deficient (Rela-/-Relb-/-Rel-/-) and Rela-/-Nfkb2-/- MEFs were analyzed by k-median clustering.
	0.96	p52 NFkappaB complex, but completely degraded p100 to reposition RelB under IkappaBalpha control, whose degradation during TNF signaling induced an early RelB:p50 containing NFkappaB activity.
	0.96	Nfkb2 that produce dysfunctional p100 lacking the NFkappaB inhibitory domain has been reported.
	0.96	p50/NFkappaB activity within 30 min of TNF stimulation in Nfkb2-/- MEFs with only minor RelB:p50 induction in WT cells (Figures 3c and d and Supplementary Figure S3b).
	0.96	p50 activity was attenuated by 1 h, TNF additionally stimulated a late RelB:p50 NFkappaB DNA-binding activity, which gradually accumulated in the nucleus between 2 and 8 h in Nfkb2-/- MEFs (Figure 3c).
	0.96	NFkappaB independent manner, remained unaltered upon RelB knockdown in Rela-/-Nfkb2-/- MEFs (Figure 5d and Supplementary Figure S5b).
	0.96	p50 dimer in stimulating expression of these pro-survival factors, we asked if alternate RelB/NFkappaB activity suppresses apoptosis in Rela-/-Nfkb2-/- MEFs.
	0.96	Nfkb2-/- MEFs are indeed resistant to TNF-induced death, while Rela-/- Nfkb1-/- cells are extremely susceptible (Figure 6b).
	0.96	p50 response in Rela-/-Nfkb2-/- MEFs.
	0.96	p50/NFkappaB dimer protects Rela-/-Nfkb2-/- MEFs from apoptotic death.
	0.95	p50 activity, Rela-/-Nfkb2-/- cells, which exclusively activate RelB:p50, and control NFkappaB-deficient Rela-/-Relb-/-Rel-/- cells, which lack the expression of all three transcription-activating NFkappaB subunits RelA, RelB and cRel.
	0.95	Nfkb1-/- MEFs within 4 h of TNF treatment is essentially absent in Rela-/-Nfkb2-/- MEFs as in WT cells (Figure 6c and Supplementary Figure S6b).
	0.95	p50 induction by TNF in Relb-/-Nfkb2-/- MEFs stably expressing RelB from either a constitutive (const.) or an NF-kappaB inducible (ind.) promoter.
	0.95	p50 dimer in response to TNF in Nfkb2-/- MEFs upon implementing positive autoregulatory control in the mathematical model.
	0.94	p50 dimer in Nfkb2-/- MEFs in response to TNF (Figure 4b).
	0.94	NFkappaB dimers to Relb promoter in a TNF time course in Nfkb2-/- MEFs.
	0.93	p52 subunit, thereby liberating RelB:p52/NFkappaB activity into the nucleus.
	0.93	Nfkb1-/- or Rela-/-Nfkb2-/- MEFs upon TNF treatment.
	0.90	NFkappaB activity induced by TNF is responsible for the protracted drug-refractory state of HMCLs harboring non-canonical aberrations, and that this resistance is independent of RelA. These studies also raised a mechanistic conundrum as activating mutations in the non-canonical NFkappaB module do not appear to act through RelB:p52; rather they promote perpetuating RelB:p50/NFkappaB response to canonical TNF signal.
	0.80	NFkappaB pathway modified TNF signaling to impart drug resistance in myeloma cells independent of the principal NFkappaB subunit RelA. Interestingly, these mutations did not act through typical p52 NFkappaB complexes, but depleted p100 to reposition RelB under IkappaBalpha control.
	0.78	NFkappaB target genes, a recent investigation suggested that RelB:p52 suppresses expression of NFkappaB target pro-apoptotic gene Bim.
	0.75	p52/NFkappaB activity has been identified in myeloma cells.
	0.72	NFkappaB activity in a time course upon 1 ng/ml of TNF stimulation of WT or Nfkb2-/- MEFs.
	0.65	p50 induction, it failed to capture progressive nuclear accumulation of late-acting RelB:p50 dimer observed in TNF-stimulated Nfkb2-/- MEFs (Figure 3f).
	0.62	p52, functions as a transcriptional repressor in the basal state in HMCLs, our investigation indicated that TNF-induced RelB:p50 acts as a potent activator of pro-survival gene expressions.
	0.62	p50 dimer in WT (cyan) and Nfkb2-/- (black) MEFs.
	0.61	Nfkb2-/- MEFs expressing RelB from either a constitutive or a kappaB-driven retroviral promoter (Supplementary Figure S3d) confirmed that kappaB-dependent expression of RelB is necessary for late, but not early, RelB:p50 induction in the absence of p100 (Figure 3g).
	0.60	p50 response in Rela-/-Nfkb2-/- MEFs owing to autoregulatory control.
29874793	0.98	p50 and p52, but not RelA. p50 homodimers, which are normally considered to be transcriptionally inactive, activate the transcription of NF-kappaB target genes when associated with IkappaBzeta.
	0.98	p50 dimers and noncanonical RelB-p52 dimers.
	0.98	p50 and noncanonical RelB-p52 dimers are probably the most commonly observed because of binding stability.
	0.97	NFKB1/p105 is thought to be constitutively processed into the active p50 subunit concurrent with translation, whereas NFKB2/p100 remains unprocessed until noncanonical pathway activation induces its proteasome-dependent processing into the active p52 subunit (Figure 1).
	0.97	p50 dimer, which is primarily activated by canonical NF-kappaB signaling, and the RelB-p52 dimer, which is activated by noncanonical NF-kappaB signaling.
	0.97	NF-kappaB requires the degradation of the IkappaB proteins to release the RelA-p50 dimers, whereas noncanonical NF-kappaB requires the proteasome for p100 processing to p52.
	0.97	NF-kappaB transcription factors RelB and p100/p52 (NFKB2) have been implicated in promoting breast cancer.
	0.97	p52 bind to the EZH2 promoter, indicating direct transcriptional regulation of EZH2 by noncanonical NF-kappaB. A supporting study in melanoma cells suggests that noncanonical NF-kappaB upregulation of EZH2 may be a general mechanism to bypass p53-induced senescence.
	0.97	p50 and p52, rather than the transcriptionally active RelA, RelB, or c-Rel.
	0.97	NF-kappaB activation, Bcl-3 binds p50 and p52 and acts as a transcriptional activator, promoting the transcription of anti-apoptotic and proliferation genes, such as cyclin D1.
	0.97	p50 and p52 (see below).
	0.97	p50 and RelB-p52 heterodimers appear to be the most abundant within cells, other important dimer combinations have been studied.
	0.96	p52 has generally been shown to promote noncanonical NF-kappaB and oncogenic functions, its precursor, p100, has been demonstrated to act as a tumor suppressor in an NF-kappaB-independent mechanism.
	0.95	NF-kappaB pathway activation leads to transcription regulation by dimers of 5 related transcription factors (RelA/p65, RelB, c-Rel, NFKB1/p105, and NFKB2/p100).
	0.95	NFKB1/p105 and NFKB2/p100 subunits require posttranslational proteolytic processing before they can support transcription activation.
	0.95	p52 and hyperactive noncanonical NF-kappaB.
	0.95	NF-kappaB transcription factors RelB and p52 were recently shown to induce APOBEC3B expression in some cancer cells.
	0.94	NF-kappaB is activated in C250T mutant cells, p52 can recruit Ets transcription factors to the mutated TERT promoter and drive transcription.
	0.91	NF-kappaB pathway, in order to generate the functional p52 transcription factor.
	0.85	p52 in order to induce TERT expression (Figure 2), and reversion of the C250T promoter mutation blocked p52 binding, and noncanonical NF-kappaB-induced TERT expression.
	0.84	NF-kappaB transcription factors, namely RelB and p52, can support the growth of several cancer types.
	0.79	NFKB1/p105, and NFKB2/p100 have been observed, with TRAF3 inactivation being the most frequent alteration.
19860880	0.98	NF-kappaB (p52/p65) and heterodimeric AP-1 (c-Jun/c-Fos) transcription factors with the human iEkappa enhancer region are important for the upregulation of kappa light chain in LMP1-positive nasopharyngeal carcinoma cells.
	0.98	NF-kappaB complex, we performed super-EMSA with antibodies specific for NF-kappaB family members p50, p52, p65, c-Rel and RelB to analyze the nuclear extracts of HNE2-LMP1 cells.
	0.98	p52 and p65 transcription factors to kappaNF-kappaB motif in vitro.
	0.97	NF-kappaB subunits p52 and p65 as well as AP-1 family members c-Jun and c-Fos binding to the kappaNF-kappaB and the kappaAP-1 motifs in vitro, respectively.
	0.97	p52 and p65 binding to the kappaB motif as well as c-Jun and c-Fos binding to the AP-1 motif of Ig kappa gene in vivo.
	0.97	NF-kappaB family members p50, p52, p65, c-Rel and RelB as well as AP-1 family members c-Jun and c-Fos.
	0.97	NF-kappaB binding site produced 159-bp amplicons that could be observed with the positive control (input chromatin) and when the chromatin was precipitated with antibodies specific for p52 and p65.
	0.97	NF-kappaB/DNA complex containing p52 and p65 subunits by Gel Super-shift assay (Fig. 4C, lanes 5 and 6).
	0.97	p52 forms heterodimers with other NF-kappaB subunits, such as p65 and RelB, or as a homodimer has also been found.
	0.96	NF-kappaB subunits p52 and p65 as well as AP-1 family members c-Jun and c-Fos binding to the kappaNF-kappaB and the kappaAP-1 motifs in vitro, respectively.
	0.96	p52 and p65 binding to the kappaB motif as well as c-Jun and c-Fos binding to the AP-1 motif of Ig kappa gene in vivo.
	0.96	p52 and p65 binding to the kappaNF-kappaB motif as well as c-Jun and c-Fos binding to the kappaAP-1 motif in vitro
	0.96	p52 subunit binding to kappaB site within the iEkappa may play an important role in upregulating the activity of iEkappa and kappa light chain production in HNE2-LMP1 NPC cells.
	0.95	p50, c-Rel and RelB antibody did not influence the mobility or intensity of the NF-kappaB binding complex (lanes 4, 7 and 8), whereas the addition of antibodies for p52 and p65 resulted in a significant diminishment or supershift of the specific complex (lanes 5 and 6).
	0.95	p52 and p65 proteins in the complex with the kappa NF-kappaB binding site.
	0.86	p52/p65 preferentially activates HIV-1 gene expression relative to the p50/p65 heterodimers, which is similar to our results.
	0.85	p52/p65 and c-Jun/c-Fos heterodimers can bind to the kappaB and the AP-1 site of human Ig kappa gene in vitro, respectively, which may be the key events in upregulating the activity of iEkappa by LMP1 in NPC cells.
	0.68	kappaB oligonucleotide probe in the absence (lane 2) or presence of antibodies directed against different NF-kappaB subunits p50, p52, p65, c-Rel, RelB or control antibody (IgG) (indicated above each lane) and then supershift assays were performed.
	0.60	p52/p65 binding to the kappaNF-kappaB motif as well as c-Jun/c-Fos binding to the kappaAP-1 motif in vivo
	0.59	p52/p65 and c-Jun/c-Fos heterodimers in the regulation of the human iEkappa in vivo, we analyzed the fragments that span the NF-kappaB and the AP-1 binding regions within and downstream the iEkappa using a chromatin immunoprecipitation assay (ChIP), respectively.
29678621	0.98	NF-kappaB/p52 levels in a dose-dependent manner.
	0.98	NF-kappaB/p52 and NF-kappaB/Phospho-p65 levels, with maximal activation achieved at just 5 ng/ml RANKL (Fig. 2A,B), whilst treatment with TRAIL (5 ng/ml, 72 h) was seen to significantly increase NF-kappaB/Phospho-p65 levels (Fig. 2B).
	0.97	NF-kappaB/p52 induction (Fig. 1A).
	0.97	NF-kappaB/p52 pathway to alter endothelial paracrine signalling and elicit pro-calcific responses within underlying vascular smooth muscle cells.
	0.96	NF-kappaB as follows: (A) p52/p100 ratio; and (B) Phospho- p65/p65 ratio.
	0.95	NF-kappaB/p52 and canonical NF-kappaB/p65 pathways in both cell types.
	0.95	NF-kappaB/p52 pathway in HAECs.
	0.95	NF-kappaB as follows: (A) p52/p100 ratio; and (B) Phosphop65/ p65 ratio.
	0.93	NF-kappaB/p52 pathway in HAECs is essential for eliciting pro-calcific activation within co-cultured HASMCs.
	0.93	NF-kappaB/p52 (and canonical NF-kappaB/p65) pathway in these cells.
	0.93	NF-kappaB as follows: (A) p52/p100 ratio; and (B) Phospho-p65/p65 ratio.
	0.88	p52 (Fig. 3A) and NF-kappaB/Phospho-p65 (Fig. 3B) in underlying HASMCs.
	0.87	p52) and canonical (p65) NF-kappaB signalling pathways was investigated.
	0.83	NF-kappaB/p52 in HAECs, clearly pointing to the mechanistic relevance of this specific pathway to RANKL function within the endothelium.
	0.79	NF-kappaB/p52 pathway in vascular endothelial cells by RANKL elicits pro-calcific signalling in co-cultured smooth muscle cells
	0.79	NF-kappaB/p52) exhibited strongly attenuated pro-calcific activation of underlying HASMCs relative to scrambled siRNA controls.
	0.77	NF-kappaB/p52 and NF-kappaB/p65 pathways in endothelial cells and; (ii) the ability of TRAIL to robustly counteract RANKL- mediated activation of the non-canonical NF-kappaB/p52 pathway in HAECs.
	0.76	NF-kappaB/p52 pathway in mediating the pro-calcific actions of RANKL acting across the endothelium in a paracrine manner to the underlying smooth muscle cells.
	0.57	NF-kappaB/p52 (non-canonical/alternative) and NF-kappaB/p65 (canonical) pathways and importantly, to test whether or not the TRAIL-dependent blockade of RANKL actions recently demonstrated by our group can be mediated through one of these pathways.
	0.52	NF-kappaB/p52, clearly pointing to the mechanistic relevance of this specific pathway to RANKL function within endothelial cells.
25159142	0.98	p50- and p52-containing heterodimers are prototypical canonical and non-canonical pathway dimers, respectively, RelA, RelB and/or cRel predominated at clusters P5, P9, E4, E7, E8, and E10.
	0.98	NF-kappaB binding in LCLs, including by p50 and p52, occurred at highly active enhancers or promoters.
	0.98	NF-kappaB pathway components, including IKK-beta, RelA, p105/p50, and p100/p52.
	0.97	p52, which enables the p52-containing complexes RelB:p52, p52:p52, and p50:p52 to enter the nucleus.
	0.97	p50, and 2.8% for p52.
	0.97	NF-kappaB binding sites that lack kappaB motifs: E-boxes at cRel-occupied promoters, ZNF143 motifs at promoters occupied by all NF-kappaB subunits except p50, CTCF sites at p52-occupied promoters, and Ets/ISRE elements p52-occupied enhancers.
	0.97	p50 signals are significantly higher at NFKB2 locus binding sites that contain the 11 bp motif.
	0.96	NF-kappaB) subunits RelA, RelB, cRel, p50 and p52 are each critical for B-cell development and function.
	0.96	p50 and p52, and at a lower level, to each other.
	0.95	p50 and with p52 in LCL nuclei (Figure S1), as well as NF-kappaB homodimers, likely contributed to these patterns.
	0.94	NF-kappaB subunits: p105/p50, p100/p52, RelA (p65), RelB and cRel.
	0.93	p52 recruitment to EICE sites may thereby enable cross-talk between the non-canonical NF-kappaB, PU.1 and IRF4 pathways, each of which are important for B-cell development and activation.
	0.90	p52, to a lower level with p50, and to a substantially lower level with RelA. Both p50 and p52 associate with all NF-kappaB subunits (Figure S1).
	0.90	NF-kappaB subunit ChIP peak summit heights were correlated (Spearman R = 0.5 for p52).
	0.89	NF-kappaB dimers form, including canonical/non-canonical hybrids such as RelA:p52.
28689659	0.98	p52(or p50):DNA ternary complexes.
	0.98	NF-kappaB p52 and p50 homodimers, we investigated whether Bcl3 phosphorylation affected its ability to interact with p52.
	0.98	p52 and p50 homodimers: in one mode only Bcl3:p52(or p50) binary complex is allowed and in the other mode the binary complex can accommodate specific kappaB DNA forming ternary complexes.
	0.97	p50 and p52 from bound DNA.
	0.97	p52(or p50):DNA ternary complex formation.
	0.97	p52(or p50):DNA complexes in vitro, it is not known if Bcl3 ever exists in an unphosphorylated form in cells.
	0.96	p50 and p52 homodimers from active promoters just like the removal of p50:RelA heterodimer by IkappaBalpha.
	0.95	NF-kappaB RelA, cRel, and RelB dimers; the atypical IkappaB protein Bcl3 is primarily a transcriptional coregulator of p52 and p50 homodimers.
	0.95	p52(or p50):DNA binary complexes forming ternary compplexes.
	0.95	NF-kappaB p52 and p50 homodimers.
	0.91	NF-kappaB p50 and p52 homodimers.
	0.91	NF-kappaB p52.
	0.52	p52 and p50 homodimers from kappaB DNAs.
25873381	0.98	NF-kappaB activity, and expression of LMP1 in C33 cells revealed that LMP1 induced multiple distinct NF-kappaB forms using electrophoretic mobility shift assays (EMSA) including abundant p50 dimers, p50/p52 dimers, and p65.
	0.98	NF-kappaB pathway, and also, both p52 and relB expression were increased by LMP1-CTAR1 (Fig. 5).
	0.97	NF-kappaB activation properties in reporter assays, while CTAR1 uniquely activates noncanonical NF-kappaB signaling and strongly induces the processing of p100 to p52.
	0.97	NF-kappaB pathway were bound by bcl3 in the CTAR1-expressing cells, including the IkappaB kinase (NEMO), the NF-kappaB inhibitors IkappaBalpha, IkappaBbeta, IkappaBdelta, IkappaBepsilon, IkappaBzeta, TBK, NFKB1 (p50), NFKB2 (p52), and RelA. Even though the peaks called for some of these genes had FDRs greater than 10, the peaks for IkappaBalpha, IkappaBbeta, IkappaBdelta, IkappaBzeta, NFKB1, and NFKB2 overlapped bcl3 sites identified in ENCODE.
	0.97	NF-kappaB, represented by p52/relB dimers.
	0.96	NFKB1, and NFKB2 were identified in the bcl3 ChIP, confirming that some of the unique effects of CTAR1 on cellular gene expression are mediated by this important NF-kappaB member.
	0.96	NF-kappaB family members, NFKB1 p105, MAP3K14 (NIK), NFKBIA (IkappaBalpha), and NFKB2 p100 were also identified as possible upstream regulators with less significant z scores.
	0.96	p105 to p50 and its subsequent translocation to the nucleus where it can bind with bcl3 to turn on transcription or when bound as homodimers or heterodimers with p52, suppress transcription.
	0.93	p50 and p52.
	0.90	p50 homodimers or p50 with relB or p52, both of which were increased by CTAR1 expression (Table 3).
	0.90	p50/p52 or homodimers of p50/p50 which can bind DNA yet lack a transcriptional transactivation domain and are thought to inhibit transcription (Fig. 5).
	0.71	p50/p50- and p50/p52-mediated repression (Fig. 5).
26622945	0.98	p52 NF-kappaB subunit and androgen receptor (AR) interaction reduces growth of human prostate cancer cells by abrogating nuclear translocation of p52 and phosphorylated ARser81
	0.96	NF-kappaB family of proteins, which consists of RelA/p65, NF-kappaB1/p50, c-Rel, RelB, and NF-kappaB2/p52 (p52 NF-kappaB subunit), have been shown to be aberrantly activated in prosate cancer cells and tissues.
	0.95	p52 NF-kappaB subunit.
	0.93	p52 NF-kappaB subunit, and/or an increase in its stability by phosphorylation that delays its degradation.
	0.88	p52 NF-kappaB subunit translocates to the nucleus in LNCaP cells treated with R1881 after 72h.
	0.86	p52-02 does not bind to the ligand binding domain (LBD) of AR, which is consistent with our prior study, we may conclude that AR/p52-02 binds to either the N-terminal domain (NTD) or DNA binding domain (DBD) of AR, or interferes at the interface between AR and p52 NF-kappaB subunit and/or JunD.
	0.84	NF-kappaB that may sustain ROS production and p52 activation in low androgen environment in prostate cancer cells, contributing to castration-resistant prostate cancer progression.
	0.84	p52 NF-kappaB subunit, AR/p52-02, represses castration-resistant prostate cancer cell growth by blocking both AR and p52 pathways, and shows promise for development of a new therapeutic agent for castration-resistant prostate cancer.
	0.77	p52-02 inhibitor of AR/p52 interaction was further examined by assessing the level of other proteins in canonical and non-canonical NF-kappaB pathways eg, p65/p50, IkappaB-alpha and beta and IKKalpha/beta.
	0.73	p52 NF-kappaB subunit with C-terminal domain of Gaussia Luciferase and establishment of AR/p52 interaction via Gaussia Luciferase reconstitution assay
	0.71	p52 NF-kappaB subunit protein.
	0.66	p52 NF-kappaB subunit, AR/p52-02, represses the castration-resistant prostate cancer cell growth by blocking both AR and p52 pathways and may thereby prevent the transition of androgen-dependent growth of prostate cancer cells to castration-resistant growth.
28346502	0.98	p50, p52, RelA, and RelB in EBV-positive cell lines (Fig 4A).
	0.96	NF-kappaB protein expression and localization were examined by immunofluorescent staining using anti-p50, p52, RelA, and RelB antibodies as indicated.
	0.95	P50, p52, RelA, and RelB was detected (Fig 3B).
	0.94	p50, p52, RelA, and RelB antibodies as indicated.
	0.92	p50, p52, RelA, and RelB antibodies was performed as indicated.
	0.91	NF-kappaB. NF-kappaB is a dimeric transcription factor of the REL family members, RelA, RelB, c-Rel, p50, and p52 that mediates inflammatory and anti-apoptotic molecular signals.
	0.91	p50, p52, RelA, and RelB existed in the nucleus under maintenance conditions, while KHYG1, Jurkat and MOLT4 cells, which were EBV-negative NK and T cell lines, did not show or showed a little nuclear localization of these molecules under these conditions (Fig 1A).
	0.91	p50 and p52 protein localization in EBV-positive T or NK cells purified from patient peripheral blood mononuclear cells (PBMCs) using antibody-conjugated magnetic beads and immediately used in the assay.
	0.84	p50 and p52 was detected in these samples.
	0.79	p50, p52, RelA, and RelB were detected in the nucleus in the EBV-positive cell lines, whereas not or very weak in the EBV-negative cell lines.
	0.63	p50 staining, and the other for p52, RelA, and RelB antibody staining.
	0.58	NF-kappaB. Supershifted bands demonstrated that NF-kappaB-DNA binding complexes involved p50, p52, RelA, and RelB. These results indicated that NF-kappaB was activated not only the cell lines, but also in the EBV-positive T- or NK-cells from CAEBV patients.
29695914	0.98	NFkappaB-inducing kinase and activate an IKKalpha homodimer at the same time, ultimately leading to heterodimerization of the p100 precursor with RelB and processing into the active p52 subunit.
	0.98	p52, causing constitutive activation of the canonical NFkappaB pathway (p65/p50) and noncanonical NFkappaB pathway (p100/p52) and promoting the nuclear translocation and accumulationof p52/RelB, which can enhance proliferation of MCF1 cells.
	0.97	p105 contains ankyrin repeats that function as a p52 and p50 inhibitor.
	0.97	p105/IkappaBgamma and p100/IkappaBdelta play a dual role, ie, precursors of the NFkappaB proteins p50 and p52 and inhibitors of NFkappaB signaling.
	0.97	p105 are phosphorylated and cleaved into maturated p52 and p50 upon IKK activation.
	0.96	NFkappaB is an important transcription-factor family of five subunits: Rel (cRel), p65 (RelA, NFkappaB3), RelB, p105/p50 (NFkappaB1), and p100/p52 (NFkappaB2).
	0.96	p50 and p52 have only an RHD, but not a TAD.
	0.96	NFkappaB p100 to the p52-active form and translocation of p52 from the cytoplasm to the nucleus.
	0.95	NFkappaB family consists of three proteins with a transactivation domain (RelA [p65], cRel, and RelB) and two proteins lacking a transactivation domain (p105/p50 and p100/p52).
	0.94	p105/p50 and p100/p52 have ankyrin repeats that function as p52 and p50 inhibitors.
	0.85	NFkappaB from IkappaBs in the canonical pathway and processing of p100/102 into p52/50 in the noncanonical pathway to activate the NFkappaB pathway in inflammatory diseases, autoimmune diseases, and cancers.
	0.66	p50 and p52 are usually present in cells in the form of their precursors.
16205698	0.98	p50 and its precursor p105) and NF-kappaB2 (p52 and its precursor p100) form the second class; p105 and p100 contain inhibitory C-terminal ankyrin repeats that are cleaved to create transcriptionally active p50 and p52 proteins.
	0.98	Nuclear factor-kappaB nuclear expression was usually not detected in benign tissues with the exception of a few cores in which RelB (two out of 40) and p52 (one out of 39) were localised in the nucleus of secretory cells.
	0.97	NF-kappaB subunits, we analysed the expression and subcellular localisation of RelA, RelB, c-Rel, p50, and p52 on tissue array sections containing respectively 344, 346, 369, 343, and 344 cores from 75 patients.
	0.97	p52, and p50 was seen in 26.6, 15.6, 10.7, and 10.5% of cores, respectively.
	0.97	p50 and p52 should also be analysed to assess their potential as prognostic markers.
	0.96	p50 canonical pathway proteins were less frequently observed than cores expressing other subunit combinations such as RelB-p52 and RelA-RelB. In addition, the nuclear localisation of RelB correlated with patient's Gleason scores (Spearman correlation: 0.167; P=0.018).
	0.96	p50, RelB, p52, and c-Rel.
	0.95	p50 (G-I), RelB (J-L), and p52 (M-O) in normal, PIN, and cancerous prostate tissues (x 400).
	0.94	p52 combination is more frequent than the canonical RelA-p50 pair (Figure 2).
	0.89	p50) and noncanonical (RelB/p52) NF-kappaB complexes.
	0.85	p50) and the noncanonical (e.g., RelB, p52) NF-kappaB subunits can be activated in prostate cancer cells, whereas c-Rel remains inactive.
30158439	0.98	p50 and p52 NF-kappaB (class I) subunits are DNA binding, but do not have trans-activation activity by themselves.
	0.98	p50 or p52.
	0.98	NF-kappaB (RelA/p50)-driven expression, but seems to positively induce non-canonical NF-kappaB activation (processing to mature p52).
	0.97	p105 is that they can be processed into the p52 and p50 subunits, respectively, removing their 'inhibitory' ankyrin repeat domain.
	0.97	p50/RelA and p52/RelB, the regulation of c-Rel is less clear, but transcriptionally active complexes can occur as homodimers or as c-Rel/p50, c-Rel/RelA and c-Rel/p52 heterodimers.
	0.97	NF-kappaB subunits do not exclusively interact with each other, and other "hybrid" active transcription complexes can also occur where DNA binding is provided by p50 or p52, but with transactivation by a different kind of protein.
	0.97	p52 or p50 to promote specific NF-kappaB-driven transcription.
	0.97	NF-kappaB family subunits, especially p52 has been shown to be important, but the transactivating subunits RelA, RelB and c-Rel have all also been implicated in prostate cancer.
	0.97	p50/RelA and p52/RelB can drive AR expression, and p52/RelB can also drive expression of an androgen-independent AR splice variant (AR-V7).
	0.95	p52 primarily activates NF-kappaB transcription, together with the transactivating RelB subunit (Figure 1b).
	0.95	p50/RelA) but promotes non-canonical (p52/RelB) NF-kappaB signaling.
30501627	0.98	NF-kappaB pathway, and several lines of evidence propose that NFKB2 p100/p52 is a negative regulator of the canonical NF-kappaB pathway.
	0.96	NFKB1 p105 and NFKB2 p100 processing and the nuclear translocation of the RelA subunit upon exposure to TNF, IL-1beta, and LPS.
	0.96	NF-kappaB (NFKB2) signaling.
	0.95	NFKB1 p105/p50 (b) and NFKB2 p100/p52 (c) following a 1-h exposure to TNF, IL-1beta, and LPS.
	0.92	p50/RelA heterodimers and regulates a potent inflammatory response, whereas the non-canonical pathway involves the processing of NFKB2 p100 and the nuclear translocation of the p52/RelB heterodimer and is thought to regulate immune cell differentiation, attenuate apoptosis, and be associated with less acute and chronic inflammation.
	0.91	NF-kappaB family exist: RelA (p65), RelB, c-Rel, NFKB1 p50/p105, and NFKB2 p52/p100.
	0.87	NFKB1 p50 and NFKB2 p52 targets.
	0.87	NFKB2 was found significantly more abundant while NFKB1 was not.
	0.79	NFKB1, and NFKB2.
	0.78	NFKB2 and several other proteins, such as STAT1, ICAM1, FLOT1, TAPBP, and HLA-B, which are targets of NFKB2 p52 (Fig. 4a), suggesting that LPS-induced activation of NF-kappaB may be mediated predominantly via the non-canonical pathway.
	0.61	NF-kappaB via the non-canonical pathway, and we hypothesized that this activation could be responsible for regulating the abundance of proteins such as STAT1, ICAM1, and TAPBP, which are NFKB2 p52 targets.
31602271	0.98	NF-kappaB pathway (IKKbeta, p50/NFKB1, p65/RELA, NIK, p52, RELB, and IL-6) are associated with a better prognosis in breast cancer patients regardless of their classification (molecular, grade or LN status).
	0.98	p50, and p65 from the canonical, and NIK, p52 and RELB from the alternative NF-kappaB pathway were associated with better RFS of breast cancer patients.
	0.97	p50/NFKB1, p65/RELA, NIK (MAP4K4), p52 (NFKB2), RELB, IL-8 (CXCL8), IL6, and MMP-1.
	0.97	NF-kappaB pathway (IKKalpha (CHUK), IKBKB, p50/NFKB1, p65/RELA, NIK (MAP4K4), p52 (NFKB2), and RELB) have close interactions with TNF and cAMP-response element-binding protein (CREBBP), and regulate IL-8 (CXCL8), IL-6 and MMP-1.
	0.96	p50/p105), NFkappaB2 (p52/p100), RelA (p65), RelB, and c-Rel; which can homo or hetero-dimerize to allow DNA binding and activate transcription.
	0.95	p50 (LN-positive: HR = 0.75, P = 0.004; LN-negative: HR = 0.73, P = 0.00019), NIK (LN-positive: HR = 0.7, P = 0.00032; LN-negative: HR = 0.78, P = 0.0048), p52 (LN-positive: HR = 0.67, P = 6.8e-05; LN-negative: HR = 0.83, P = 0.028), and RELB (LN-positive: HR = 0.77, P = 0.0092; LN-negative: HR = 0.83, P = 0.029) correlated with better RFS in all patients independent of their LN status (Figure 3A-D, Table 4).
	0.95	p50, NIK, p52, and RELB correlated with better RFS (Table S4).
	0.95	p50, and p65 from the canonical, and NIK, p52 and RELB from the alternative NF-kappaB pathway were associated with better RFS of breast cancer patients.
	0.89	p50 and p65 from the canonical pathway; NIK, p52, and RELB from the alternative pathway; IKKalpha which is common to both canonical and non-canonical pathways, and IL-8, IL-6, MMP-1 as downstream targets controlled by these pathways.
	0.88	NF-kappaB dimers represent canonical and non-canonical pathways, for instance, p50:p65 are common to classical activation and p52:RelB to the alternative pathway.
	0.63	p50, p65, p52, NIK, RELB and, IL-6 were associated with better RFS in all patients regardless of their ER status (Figure 2B, C, and D, Table 3).
25255445	0.98	p52 and RelB are frequently found in the same NF-kappaB complex, removal of either subunit will not have the same effect.
	0.98	p52 can only be potentially compensated for by the activity of p50/RelB heterodimers or other NF-kappaB complexes.
	0.96	NF-kappaB and p53 that controls a gene regulatory network through which p52 and RelB act to suppress p53 and Rb mediated cellular senescence.
	0.95	NF-kappaB pathway, p52 and RelB can affect p53 dependent senescence.
	0.95	p52 and RelB. This result was confirmed by mining of ChIP-Seq data from GM12878 B-cells, where binding of all NF-kappaB subunits to the EZH2 promoter was seen (Fig. 10C).
	0.90	NF-kappaB pathway subunit p52 and p53, involving p53 modulation of p52 homodimer transcriptional activity, by inducing a change from p52/Bcl3 to p52/HDAC complexes, in addition to direct recruitment of p52 to p53 target gene promoters.
	0.90	NF-kappaB pathway subunits p52/p100 (encoded by the NFKB2 gene) and RelB in the NHD fibroblasts.
	0.88	NF-kappaB subunit to p52 as well as a basal level of the p53 tumor suppressor (Fig. 1A).
	0.69	p105 can also function as IkappaBs, prior to their processing to p52 and p50, which function as nuclear regulatory subunits.
	0.56	NF-kappaB family of transcription factors consists of five subunits, RelA (p65), c-Rel, RelB, NF-kappaB1 (p105/p50) and NF-kappaB2 (p100/p52), which form a wide variety of homodimeric and heterodimeric complexes.
26324762	0.98	p50, p52 and RelB (Table 1).
	0.98	p50-, p65-, p52-, RelB-, p50+, p65+, p52+ and RelB+.
	0.98	p50 dimers have significantly distinctive activities compared to other p65 or p50 dimers (mainly p50/p65 and p50/p50 dimers, potentially also p65/p65, p50/p52, p50/RelB dimers).
	0.98	NF-kappaB members significantly, because no c-Rel signatures were identified within p50+, p65+ p52+ or RelB+ GCB-DLBCL, whereas 16 differentially expressed genes (DEGs) were identified within the RelB- GCB-DLBCL subset by a high false discovery rate (FDR < 0.30) threshold.
	0.97	p52 in GCB-DLBCL, and p50, p52 and RelB in ABC-DLBCL (Fig. 1E-H).
	0.97	NFKB1 and RELA (but not NFKB2 or RELB) in ABC-DLBCL (Supplementary Fig. S1D-E).
	0.96	NF-kappaB activation and function, whereas MUT-p53 induces p52/NFKB2 gene expression.
	0.95	p50+, p65+, p52- and RelB- DLBCL subsets (Supplementary Fig. S2M-2N; Supplementary Table S2), but not in p50-, p65-, p52+ or RelB+ DLBCL.
	0.80	NF-kappaB subunits, we compared the GEP of c-Rel+ and c-Rel- within p50-, p65-, p52-, RelB-, p50+, p65+ p52+ and RelB+ DLBCL subsets individually.
	0.68	NF-kappaB subunits (significant for p52 and RelB by Spearman rank correlation): p50 (r = 0.12, P = 0.12), p52 (r = 0.26, P = 0.724E-8), p65 (r = 0.085, P = 0.073), and RelB (r = 0.12, P = 0.013).
21754991	0.98	NFKB2, NFKB1 and NFKBIA, which respectively encode NF-kappaB2 (p52/p100), NF-kappaB1 (p50/p105) and NF-kappaBIA/inhibitor IkappaBalpha were more moderately up-regulated (10 to 20-fold).
	0.98	p50 or anti-NF-kappaB2/p52 antibodies, as indicated in Materials and Methods .
	0.98	NF-kappaB, as well as selective expression of NF-kappaB components (RELB, NFKB1 and NFKB2).
	0.98	p52 and RelB/p50 dimers.
	0.98	NF-kappaB subunits (c-Rel, RelB, p50/ NF-kappaB1, p52/ NF-kappaB2, and Ikappa-Balpha), as well as the absence (or low level) of nuclear p65/RelA has also been previously described in breast tumors, as compared to normal adjacent tissue.
	0.96	NF-kappaB may also occur through alternative pathway involving the activation of IKKalpha (IKK1) and the activation of RelB/p52 and RelB/p50 dimers.
	0.96	NFKB1 and NFKB2/p52, Rel/NF-kappaB family members, but not RelA and c-rel, which is demonstrated for the first time in TNFalpha-stimulated endothelial cells, is unknown.
	0.86	p50 and NF-kappaB2/p52 proteins in TNF-alpha stimulated HMEC.
	0.59	NF-kappaB factors are homo- and heterodimeric transcription factors that belong to the Rel family; this family is composed of five homologous subunits in mammals: NF-kappaB1 (p50 and its precursor p105), NF-kappaB2 (p52 and its precursor p100), RelA/p65, RelB and c-Rel.
23538445	0.98	NF-kappaB DNA-binding complexes on stimulation with BV6 were mainly composed of p50, p52 and RelB subunits, because the addition of p50, p52 and/or RelB antibodies to nuclear extracts resulted in a supershift (for p50 antibody) or immunodepletion (for p52 and/or RelB antibodies) of DNA-binding complexes (Figure 3f).
	0.98	NF-kappaB pathway as demonstrated by accumulation of NIK protein, proteolytic processing of p100 to p52, translocation of p52 from the cytosol into the nucleus, binding of the NF-kappaB subunits p52, p50 and RelB to the DNA, transcriptional activation of NF-kappaB and increased mRNA expression of NF-kappaB target genes including TNFalpha.
	0.97	NF-kappaB DNA-binding subunits consist of p50, p52 and RelB further confirming the activation of the non-canonical NF-kappaB pathway.
	0.97	p52 and p50 and slightly that of p65, whereas TNFalpha primarily triggered p65 translocation (Figure 3d).
	0.96	NF-kappaB activation, we assessed accumulation of NIK protein and proteolytic processing of p100 to p52.
	0.96	p52, indicating that it stimulates non-canonical NF-kappaB signaling in primary GBM cells (Figure 8c).
	0.95	p52, nuclear translocation of p52 and NF-kappaB activation.
	0.95	p52, p50, phospho-p65 (p-p65) and p65 were analyzed in cytoplasmic (C) and nuclear (N) fractions by western blotting.
	0.89	p52 and NF-kappaB DNA-binding compared with non-silencing control cells (Figures 7a and b).
24529193	0.98	p50, p52 and p65 are the major NF-kappaB subunits binding to the human Mcl-1-kappaB probe in vitro.
	0.98	NF-kappaB subunits p50, p52, p65, c-Rel, RelB or control antibody (IgG) (indicated above each lane) and then gel shift assays were performed.
	0.98	NF-kappaB subunit p50, p52, p65, c-Rel or RelB. The positive control is represented by the input fraction.
	0.98	NF-kappaB subunits p50, p52, p65, c-Rel and RelB. An IgG antibody was used as a nonspecific control.
	0.98	NF-kappaB family members p50, p52, p65, c-Rel, RelB or with a nonspecific antisera prior to interaction with the Mcl-1-kappaB site probe.
	0.98	p50 and p65 but not p52 were revealed directly binding to the kappaB site of human Mcl-1 promoter in intact cells by ChIP assays.
	0.93	NF-kappaB subunits p50, p52, p65, c-Rel, and RelB, the results revealed that the addition of an antibody against p50, p52 or p65 caused a substantial reduction in binding (lanes 7, 8 and 9).
	0.88	NF-kappaB family members p50, p52 and p65 were able to bind to the same probe in vitro.
	0.73	NF-kappaB subunit p50 and p52.
24530305	0.98	NF-kappaB family of transcription regulators consists of five related proteins: RelA/p65, RelB, c-Rel, p50 and p52.
	0.98	NF-kappaB proteins can be subdivided based on transactivation potential: only RelA, RelB and c-Rel contain a transactivation domain (TAD) required to recruit transcriptional machinery, the p50 and p52 subunits do not.
	0.98	p50, p52 and BCL3 are themselves regulated by NF-kappaB and we found that nuclear densities of p50 and BCL3 correlate with that of RelA.
	0.98	p50, p52 and BCL3).
	0.96	p50-p50 and p52-p52 homodimers lack a TAD, they do not have the intrinsic ability to drive transcription and can instead repress transcription when bound to kappaB sites of target genes.
	0.93	p50 knockdown may affect RelA-p50 heterodimer abundance, and that it may be difficult to isolate the influence of BCL3, p50 or p52 on transcription of a gene that is regulated by multiple competitors because knockdown of one candidate competitor affects the transcript abundance of the others (Figure S6E).
	0.91	p50 knockdown, transcription increased only in the absence of TNF (~6-fold, p = 0.08; Figure 6B), and for p52 knockdown, transcription increased only in the presence of TNF (~5-fold, p = 0.03; Figure 6B).
	0.59	p50, p52, and BCL3 as proteins that participate in competitor complexes and suggest that others exist.
	0.55	NF-kappaB-driven transcription should fulfill three conditions to establish a 'memory' of baseline nuclear RelA. It should: 1) prevent RelA from binding to target kappaB sites or reduce the transcription-inducing ability of bound RelA, 2) have no, or low, transcriptional activity on kappaB sites compared to RelA, and 3) be expressed in a RelA-dependent manner at levels that scale with baseline nuclear RelA. Homodimers of p50 or p52, the mature products of the NFKB1 and NFKB2 genes, and BCL3, a protein that stabilizes repressive homodimer complexes on a subset of kappaB sites, all satisfy these conditions and are plausible candidate competitors.
26147201	0.98	NF-kappaB activation were unveiled, including but not limited to inducible processing of P100 to P52 regulated by IKKalpha homodimers, further increasing the complexity of the system.
	0.98	NF-kappaB subunit, finding that only P100/P52 expression in tumor and the related stroma were concordant and correlated (Fig 2F and 2G).
	0.98	NF-kappaB subunits in prostate cancer tissue arrays; they found nuclear subunit combinations such as RelB-P100/P52 and RelA-RelB, introducing for the first time a different NF-kappaB pattern associated with the progression of the disease.
	0.97	P50), and NF-kappaB2 (P100/P52).
	0.97	P50 immunoreactivity was stronger compared with P100/P52 (Fig 1A and 1B).
	0.97	NF-kappaB subunit scores were subdivided into low (0-4), intermediate (5-6), or high (7-18) and compared within each tumor, RelB and P100/P52 showed significant concordance, with 49/77 tumors displaying simultaneously low scores for both subunits, likely reflecting the low expression levels of both proteins (Fig 2E).
	0.97	NF-kappaB activation, since RelA-P50 and RelB-P100/P52 complexes bind to NF-kappaB binding sites of different promoters.
	0.96	NF-kappaB activation pathways, the canonical (or classical) and non-canonical (or alternative), which are mediated by RelA/P50 or c-Rel/P50 and RelB/P52 dimers, respectively.
	0.89	P50 were expressed at higher levels compared with P52/P100.
29801480	0.98	NF-kappaB target genes CD44 and CXCL1 by p52 in TNBC cells was verified using siRNA knockdown and qRT-PCR.
	0.98	p52 (Fig. 4a) led to a significant increase in RELB, NFKB2 and CXCL1 in the MDA 468 cells (Fig. 4c) suggesting negative transcriptional regulation of alternative NF-kappaB transcription factors by IKKepsilon.
	0.98	p52 and non-canonical NF-kappaB activation in breast cancer cells is unclear.
	0.98	NF-kappaB signaling through p52 is important for survival in anchorage-resistant LA environments.
	0.97	NF-kappaB p52 signaling in anchorage-resistant conditions.
	0.95	p52 had no effect on the levels of IotaKappaKappaepsilon or MEK, suggesting their expression or activation are not regulated by non-canonical NF-kappaB signaling (Fig. 5a).
	0.93	NF-kappaB p52 transcription factor was significantly decreased in the presence of IKKepsilon.
	0.92	NF-kappaB p52 levels are inversely proportional to IotaKappaKappaepsilon, and growth of TNBC cells in anchorage supportive, high-attachment conditions requires IKKepsilon and activated MEK.
	0.89	NF-kappaB binding activity, invasion, anoikis, and spheroid formation were examined in cells expressing high or low levels of IKKepsilon, in conjunction with p52 RNA interference or MEK inhibition.
26579219	0.98	p50 and p52 lack a transactivation domain and functions to modulate the DNA-binding activity of NF-kappaB by forming Rel/p50 and Rel/p52 heterodimers.
	0.97	p50 and p52 homodimers may also acquire transactivation function by associating with non-Rel coactivator proteins.
	0.96	p52 but also leads to nuclear translocation of its sequestered NF-kappaB members, predominantly RelB. A central signaling component of the noncanonical NF-kappaB pathway is NF-kappaB inducing kinase (NIK), which functions together with a downstream kinase, IKKalpha, to induce phosphorylation-dependent p100 processing.
	0.95	p50 precursor protein p105, the p52 precursor protein p100, IkappaBalpha, IkappaBbeta, IkappaBepsilon, and several atyipical IkappaB members that are not shown in the figure.
	0.85	p50 and p52 are transcriptional repressors that play an important role to prevent aberrant expression of NF-kappaB target genes, including those involved in inflammation.
	0.72	p50) and NF-kappaB2 (p52) involves proteasome-mediated degradation of the IkappaB-like sequence of p105 and p100.
	0.69	NF-kappaB represents a family of structurally related proteins, including RelA (also called p65), RelB, c-Rel, p50 (also called NF-kappaB1), and p52 (also called NF-kappaB2), which share extensive homology in a region known as Rel homology domain (Fig. 1).
	0.67	NF-kappaB signaling relies on NF-kappaB inducing kinase (NIK), which together with IKKalpha mediate phosphorylation and processing of p100, causing generation of p52 and nuclear translocation of p52/RelB complex.
29084252	0.98	NF-kappaB family is constituted of 3 proteins with a transactivation domain (TAD): RelA (p65), cRel and RelB and 3 proteins lacking a TAD: p105/p50 (NF-kappaB1), p100/p52 (NF-kappaB2) and RelAp43, a sixth member of the NF-kappaB family and splicing variant of RelA. All these proteins share a Rel Homology Domain (RHD) involved in dimerization, DNA- and IkappaB binding.
	0.98	p52, and p105/p50 were quantified as some of the most important partners of RelAp43 (Fig 1A left panel, 1B).
	0.98	p105/p50 and p100/p52, ABIN2 was one of the most significant proteins interacting with RelAp43 in the absence of MTha.
	0.97	NF-kappaB pathway is divided in a canonical pathway, which mostly relies on RelA-p105/p50 dimers, and a non-canonical pathway involving RelB-p100/p52 dimers.
	0.97	p105, acting both as precursors and inhibitors, are phosphorylated and cleaved into maturated p52 and p50 upon IKK activation.
	0.97	p105/p50 and p100/p52 are the most significant NF-kappaB proteins interacting with RelAp43.
	0.96	NF-kappaB dimers are mainly composed of RelA-p50 dimers, RelA is also involved in the regulation of p100/p52.
	0.95	NF-kappaB signaling, involving a modulation of IkappaBalpha-, IkappaBbeta-, and IkappaBepsilon-RelAp43 interaction and a favored interaction of RelAp43 with the non-canonical pathway (RelB and p100/p52).
20711193	0.98	NF-kappaB signaling pathway, p100 is processed to active p52 only when the pathway is activated.
	0.97	p52 expression represses the basal level of both canonical and noncanonical NF-kappaB target genes.
	0.97	p52 in monocytes, (data not shown and Fig. 5b), we inferred that the higher basal level of ELC mRNA expression in monocytes is provided through canonical NF-kappaB molecules.
	0.97	NF-kappaB targets, including ICAM, CCL4, and IL-10, but not A20, suggesting that p52 also repressed basal transcription from some, but not all, of these promoters (Supplementary Fig. 9).
	0.96	NF-kappaB complexes in both monocytes and macrophages in the absence of treatment, p52 was bound only to kappaB sites in macrophages, and not monocytes, as shown by supershifting (Fig. 5b).
	0.92	p52 and p50 homodimers, which lack transactivation domains, can activate gene expression in association with proteins such as Bcl-3 and IkappaBzeta, normally p50 and p52 homodimers repress gene transcription.
	0.91	NF-kappaB target, lipopolysaccharide (LPS)-induced RelB protein expression in macrophages over 24 h of treatment (Fig. 7b) and led to a large increase in ELC mRNA over this same time course (Fig. 7c), which is consistent with a conversion of repressive p52 homodimers to transcriptionally active p52-RelB heterodimers upon stimulation.
25170898	0.98	NF-kappaB p50, p52 and p65, were aberrantly expressed in CCA patient tissues.
	0.98	NF-kappaB. DHMEQ inhibited the nuclear translocation of all NF-kappaB subunits p50, p65 and p52 and suppressed the action of NF-kappaB. This action of DHMEQ is confirmed by many previous studies.
	0.97	NF-kappaB complexes are dimers of various combinations of the Rel family of polypeptides consisting of p50 (NF-kappaB1), p52 (NF-kappaB2), c-Rel, v-Rel, Rel A (p65) and Rel B. NF-kappaB is activated by a wide variety of stimuli and cytokines, including UV radiation, chemical carcinogens, tumor necrosis factor-alpha, chemotherapeutic agents and radiation therapy, which cause dissociation of the binding of inhibitory IkappaB proteins and consequently leads to the relocation of the NF-kappaB complex into the nucleus.
	0.97	p50, p65 and p52 and their precursors, p105 and p100, of KKU-M213 cells treated with DHMEQ were not different from those of the controls.
	0.97	NF-kappaB family of transcription factors is comprised of RelA (p65), RelB, c-Rel, NF-kappaB1/p50 and NF-kappaB2/p52.
	0.96	p50, p52 and p65 NF-kappaB subunits (Fig. 1C).
	0.75	NF-kappaB, p50, p52 and p65 in total cell lysate and the nuclear fraction of human CCA cell lines were further analyzed by western blotting using beta-actin and histone H1 as the internal controls for total cell lysate and nuclear fraction, respectively.
25622756	0.98	NF-kappaB signaling, loss of RelB attenuates invasion without affecting RelA expression or phosphorylation and RelB is sufficient to promote invasion in the absence of RelA. The cytokine TWEAK preferentially activates the noncanonical NF-kappaB pathway through induction of p100 processing to p52 and nuclear accumulation of both RelB and p52 without activating the canonical NF-kappaB pathway.
	0.98	NF-kappaB signaling is mediated by RelB-p52 heterodimers whose activation is dependent on NF-kappaB-inducing kinase (NIK).
	0.98	NF-kappaB signaling cascade, as evidenced by induction of p100 processing to p52, and nuclear accumulation of p52 and RelB (Figure 3).
	0.97	NF-kappaB proteins, RelB is inherently unstable and its protein levels are stabilized by interaction with p100/p52 in the cytoplasm and DNA binding in the nucleus.
	0.93	NFKB1 (p105/p50), and NFKB2 (p100/p52) share an evolutionarily conserved Rel homology domain that mediates DNA binding and dimerization with other NF-kappaB subunits.
	0.92	NF-kappaB activity, as evidenced by increased p100 processing to p52, as well as nuclear accumulation of both RelB and p52 (Figure 3B).
	0.73	NF-kappaB activity is required for TWEAK-induced MMP9 expression, we transduced BT25, BT116, and U87 cells with shRNAs targeting NFKB2 (p100) or a scrambled shRNA.
26999213	0.98	NF-kappaB is of course a family of related transcription factors; RelA/p65, c-Rel, RelB, p50 and p52 that may hetero- and homo-dimerise to form at least 12 different identified dimers.
	0.98	p50 and p52 subunits do not contain a TAD and in the homodimeric form mostly act as transcriptional repressors.
	0.98	p105 and p100 are synthesized as large precursor proteins, which are partially processed by the proteasome to produce NF-kappaB subunits p50 and p52, respectively.
	0.97	p50 and p52 subunits also share the distinction that they are both generated by the proteolytic processing of a larger precursor protein, p105 and p100, respectively.
	0.97	p52, the importance of RelB in the non-canonical rather than the classical NF-kappaB pathway has likely reduced the focus on its regulation by phosphorylation.
	0.96	NF-kappaB dimers composed of the RelB and p52 subunits and requires the IKKalpha- and NIK- dependent proteasomal processing of p100 to p52.
	0.96	p105, the processing of p100 to p52 is regulated by phosphorylation of p100.
23259744	0.98	p50/RelA or p50/RelB nuclear translocation and can enhance the transactivation potential of RelA. Moreover, it has been shown that AKT can directly phosphorylate IKK-alpha leading to the processing of p100 and nuclear accumulation of p52/RelB dimers.
	0.97	NF-kappaB transcriptional activity, IkappaB-alpha degradation, NF-kappaB2/p52 generation, and RelA and NF-kappaB2/p52 nuclear translocation were investigated in TMZ-treated MMR-deficient (HCT116, 293TLalpha-) and/or MMR-proficient (HCT116/3-6, 293TLalpha+, M10) cells.
	0.97	NF-kappaB-dependent luciferase activity and to induce nuclear translocation of RelA and NF-kappaB2/p52 in the MMR-proficient cell line pUSE2 but not in the isogenic KD12 cells, which express a dominant-negative kinase-dead form of AKT1.
	0.95	NF-kappaB/p52 subunit.
	0.88	NF-kappaB family is composed of RelA (p65), c-Rel, RelB, NF-kappaB1 (p50) and NF-kappaB2 (p52), which can form homo- and heterodimers.
	0.87	NF-kappaB activation promoted by TMZ, drug-induced changes in pNF-kappaB-Luc reporter activity and nuclear levels of RelA and NF-kB2/p52 were evaluated in pUSE2 and KD12 cells.
25063873	0.98	NF-kappaB subunits p52 and RelB, 4 biotinylated detective probes containing putative binding sequences were generated (Figure.
	0.98	NF-kappaB subunits RelB and p52 regulate IDO expression via direct binding to the IDO promoter region in MDSCs.
	0.97	NF-kappaB pathway triggers IKKalpha-mediated phosphorylation of p100 and generation of transcriptionally active p52-RelB complexes.
	0.97	p50, p52, RelA and RelB subunits in nuclear extracts of CD33+ controls, MDSCs and J-MDSCs.
	0.91	NF-kappaB pathway, including increased NIK protein level, phosphorylation of IKKalpha and p100 in cytoplasm, and RelB-p52 nuclear translocation.
	0.66	NF-kappaB subunits p52 and RelB translocation to nuclear and directly interact with the IDO promoter sequence to promote IDO transcription in MDSCs.
27043634	0.98	p52 in mammalian cells, as opposed to the constitutive production of p50 from p105.
	0.97	NF-kappaB family is composed of five members, including RelA (p65), RelB, c-Rel, NF-kappaB1 p50, and NF-kappaB2 p52, which form various dimeric complexes that transactivate numerous target genes via binding to the kappaB enhancer.
	0.96	NF-kappaB pathway involves different signaling molecules and leads to the activation of the p52/RelB dimer.
	0.94	NF-kappaB pathway activates the RelB/p52 NF-kappaB complex using a mechanism that relies on the inducible processing of p100 instead of degradation of IkappaBalpha (Figure 1).
	0.93	p105 and p100 produces the mature NF-kappaB1 and NF-kappaB2 proteins (p50 and p52) and results in disruption of the IkappaB-like function of these precursor proteins.
	0.90	NF-kappaB transcription complexes have a variety of homo- and heterodimers consisting of the subunits p50, p52, c-Rel, RelA (p65) and RelB. NF-kappaB signaling pathways can be divided into canonical and noncanonical pathways.
27576892	0.98	NFKB1 (NF-kappa B p50) and NFKB2 (NF-kappa B p52) as interacting partners of the M4 motif in the context of a human lymphocyte nuclear extract (Figs. 2 and 3).
	0.98	NF-kappa B-factors (NFKB1/NF-kappa B p50 or NFKB2/NF-kappa p52) are strongly believed to be tethered to the M4 element in an Ikaros-dependent manner (Fig. 6).
	0.97	NFKB1 (NF-kappa B p50) or NFKB2 (NF-kappa B p52) is essential for tethering these Rel TF family proteins to the M4 motif
	0.97	NFKB1 (p50) and NFKB2 (p52).
	0.96	NFKB1 and NFKB2, while THAP11 and HCF-1 are absent.
	0.83	NF-kappa B proteins NFKB1 and NFKB2 (NF-kappa B p50 and NF-kappa B p52), the pluripotency factor Ronin/THAP11 and host cell factor-1 (HCF-1) are able to bind specifically, either directly or indirectly, to the M4 motif in vitro.
23547054	0.98	NF-kappaB pathway by promoting/stabilizing nuclear p52, thus leading to constitutive non-canonical NF-kappaB activation.
	0.95	p52 different from that derived via inhibition of TAK1-regulated canonical NF-kappaB. GSK-3 has been earlier shown to be accumulated in the nucleus in pancreatic cancers which raises the potential that the GSK-3 effect on non-canonical NF-kappaB is via processing of nuclear p100.
	0.80	p52 levels upon TAK1 inhibition, which is consistent with p100 being a known transcriptional target of canonical NF-kappaB (data not shown).
	0.68	NF-kappaB pathway leading to processing of NF-kappaB2/p100 to p52, has been shown to be constitutively active in pancreatic cancer cells.
	0.67	NF-kappaB represents a family of evolutionary conserved transcription factors consisting of RelA (p65), c-Rel, RelB, p50 (precursor p105) or p52 (precursor p100) subunits.
24141032	0.98	NFkappaB subunits (A) NFKB1, (B) NFKB2, (C) REL, (D) RELB, (E) RELA was analyzed by qPCR.
	0.97	p50/NFkappaB1, p52/NFkappaB2, and c-Rel was detected in breast tumors compared to adjacent normal tissue.
	0.97	NFkappaB subunit genes NFKB2, REL, RELA, and RELB and NFkappaB target genes ICAM1, IL6, and TNFAIP3 (Table 1).
	0.91	NFkappaB subunits NFKB2, REL, and RELB was higher in LCC9 compared to MCF-7 cells (Fig. 1B), accounting for the higher NFkappaB activity in LCC9 cells.
	0.73	NFkappaB subunit genes NFKB2, REL, RELA, and RELB and NFkappaB target genes ICAM1, IL6, and TNFAIP3 in microarray data from 298 ERalpha+ breast tumors from patients treated with TAM for 5 years (Table 1).
27187478	0.98	NF-kappaB is in fact a family of dimeric transcription factors consisting of five proteins; p65 also known as RelA, RelB, c-Rel, p50 and p52.
	0.98	p52, and RelB NF-kappaB subunits although its deubiquitinase activity has only been demonstrated for p65.
	0.98	NF-kappaB pathway relies on the inducible processing of p100 and is characterised by nuclear translocation of the RelB/p52 heterodimer.
	0.97	p52 are distinctive family members in that they are generated from proteasomal processing of larger precursor proteins p105 and p100, respectively and do not contain a transactivation domain required to initiate transcription and as such are generally considered to be repressors of NF-kappaB dependent transcription.
	0.96	NF-kappaB subunits p50 and p52 from p105 and p100, respectively.
29673141	0.98	NF-kappaB family members can form homo- or heterodimers, like p50/RELAp65, RELB/p50, p52/c-REL, or RELA/RELA.
	0.96	p50- and p52-containing complexes, also including p50/p52 heterodimers.
	0.95	NF-kappaB family is composed of five subunits, namely, RELA (p65), RELB, c-REL, p50, and p52 (Figure 1A), all comprising a conserved REL homology domain (RHD) near the N-terminus.
	0.95	p50 and p52 are likewise known to be autoregulated.
	0.87	p52 pathway was associated with abnormalities like bi-allelic deletion events, mutations, and gene rearrangements in the genes NFKB1 (p50/p105) and NFKB2 (p52/p100).
18723484	0.98	p50 or p52 antibody.
	0.96	p50 or 335-344 residues of p52.
	0.71	p50, and p52 were used as loading controls.
	0.68	nuclear factor-kappaB inhibitor, blocks nuclear import of RelB:p52 dimer and sensitizes prostate cancer cells to ionizing radiation
21196225	0.98	NF-kappaB heterodimer containing p52 and RelB is formed and translocated to the nucleus to turn on gene expression.
	0.97	NF-kappaB family members are found: p65 (RelA), RelB, c-Rel, p50/p105 (NF-kappaB1) and p52/p100 (NF-kappaB2).
	0.97	p50 or p52, while p50 and p52 lack TADs, and their homodimers serve as transcription repressors that provide a threshold for NF-kappaB activation.
	0.97	NF-kappaB complex (p52/RelB) moves to the nucleus to activate gene transcription.
23508954	0.98	kappaB gene, NvNF-kappaB p50, with p50 and p52 being the closest human homologs.
	0.93	kappaB p50 binding profile was compared with those of HsNF-kappaB p50, HsNF-kappaB p52, and another mammalian homodimer, NF-kappaB RelA. As expected, HsNF-kappaB p50 and HsNF-kappaB p52 had the most similar profiles to NvNF-kappaB p50 (z-score correlation coefficients of 0.88 and 0.95, respectively), whereas the RelA binding profile was the most distant (z-score coefficient of 0.65) (Fig. 1C).
	0.93	p50 and p52 subunits are most closely related to Nematostella p50 and have similar DNA binding specificities, a subunit more distantly related to them, NF-kappaB RelA, shows divergent DNA sequence preferences.
	0.73	p50 and NF-kappaB2 p52.
20388792	0.98	NF-kappaB/p52 can activate the AR, resulting in increased transactivation of AR-responsive genes, such as PSA and NKX3.1, in a ligand-independent manner.
	0.96	NF-kappaB family comprises five proteins:RelA/p65, NF-kappaB1/p50, c-Rel, RelB, and NF-kappaB2/p52:which have been identified as important mediators in the oncogenesis of many cancers.
	0.89	NF-kappaB/p52 activates the AR and enhances nuclear translocation and activation of AR by interacting with its NTD.
21203422	0.98	p105, which can be processed to form the NF-kappaB family members p52 and p50, respectively; and (c) atypical/nuclear IkappaB proteins, namely IkappaBzeta, Bcl-3 and IkappaBNS, which are not generally expressed in unstimulated cells but are induced upon activation to mediate their effects in the nucleus.
	0.71	NF-kappaB transcription factor family are p65 (RelA), RelB, c-Rel, p105/p50 (NF-kappaB1) and p100/p52 (NF-kappaB2), which associate with each other to form various transcriptionally active homo- and hetero-dimeric complexes.
	0.50	p50 and p52; hence, NF-kappaB is capable of functioning in three different possible ways: by altering kappaB-site specificity as part of a heterodimer with TAD-containing family members; by repressing transcription as part of a homodimer when bound to kappaB sites; or by promoting transcription through recruitment of other TAD-containing proteins to kappaB sites.
29377600	0.97	p50, p52, and CUL4B were measured in hFOB1.19, U2OS, MG63, Saos-2, and HOS cells.
	0.97	p50 or p52 overexpression.
	0.97	p50 and p52 proteins have no intrinsic ability to activate gene transcription, and they may act as transcriptional repressors when binding to kappaB elements as homodimers.
	0.96	p50, p52, and CUL4B were examined in hFOB1.19, HOB, Ho-f, U2OS, MG63, Saos-2, and HOS cells.
	0.96	p50 or p52 (Fig. 4B).
	0.95	NF-kappaB subunits, including RelA, RelB, and c-Rel, but not to p50 or p52.
	0.95	NF-kappaB subunits, RelA, RelB, and c-Rel, were able to bind to the promoter region of CUL4B, but p50 and p52 did not bind.
	0.95	p50, p52, and CUL4B were examined in U2OS, MG63, Saos-2, and HOS cells by normalizing them against the expression levels in hFOB1.19 cells.
	0.95	p50 and p52.
	0.92	p50 and p52, were able to modulate the expression of CUL4B.
	0.92	p50, p52, and CUL4B levels in these three portions.
	0.89	p50 and p52 under similar conditions.
	0.84	NF-kappaB subunits including RelA, RelB, and c-Rel, but not p50 and p52, were able to bind to the CUL4B promoter, thereby regulating CUL4B expression.
	0.75	p50, or p52 were subjected to the ChIP assay using specific antibodies, and the binding to Cullin genes was measured by qRT-PCR.
	0.73	p50-Flag, pCDNA3-p52-Flag, and pCDNA3-CUL4B-Flag and transfected them into hFOB1.19 cells.
29973405	0.97	kappaB sites showed that, in the presence of high BCL-3, p50 DNA binding was lost, whereas p52 binding was induced at both kappaB sites (Fig. 5J and fig. S5D).
	0.97	p50 and p52.
	0.96	p50, p52, and p65 are recruited to kappaB1 and kappaB2, but not kappaB3, and gel shift analysis showed that NF-kappaB binds the kappaB2 probe (fig. S6G).
	0.96	p50 and p52 for induction of CAII by TMZ.
	0.95	p50 recruitment decreased at CD44, LIF, and CCL2 promoters, the recruitment of p52 increased (Fig. 5I and fig. S5C).
	0.94	NF-kappaB subunits p50, p52, and p65.
	0.94	p50 at kappaB1 and kappaB2, increased enrichment of p52 (Fig. 6H), and had no effect on either BCL-3 or p65 (fig. S6H).
	0.94	NF-kappaB dimer at MES gene promoters involving replacement of p50 by p52.
	0.93	p50 or p52, we examined whether it promoted MES differentiation by altering the chromatin recruitment of these subunits.
	0.87	p52/NFKB2 not only attenuated basal NF-kappaB-regulated MES gene expression but also blocked the increase induced by BCL-3 overexpression (fig. S5G).
	0.70	NF-kappaB subunits, p50 (NF-kappaB1, p105), p52 (NF-kappaB2, p100), p65 (RelA), RelB, and c-Rel, multiple co-regulators also contribute to the overall downstream response.
	0.54	NF-kappaB signaling in conjunction with p50- and p52-containing dimers.
23974100	0.97	nfkb2 -/- MEFs were fixed with formaldehyde and processed for ChIP analysis, using antibodies against the indicated NFkappaB subunits, using RNApolII as a positive and IgG as a negative control.
	0.96	p52 and other NFkappaB subunits to regulate genes required for mitosis and have identified Polo-like kinase 4 (PLK4) as a bona fide NFkappaB target gene.
	0.96	nfkb2-/- MEFS, the absence of p52 binding appears to be compensated for by increased levels of binding of other NFkappaB subunits, correlating with higher levels of PLK4 mRNA in these cells (Fig. 6C).
	0.95	p52 NFkappaB subunit, to proliferate in vitro, our understanding of the gene targets involved in this process is limited.
	0.94	nfkb2 -/- MEFs were analyzed by qPCR to determine the basal levels for PLK4 expression.(D)Schematic representation of the full-length human PLK4 promoter luciferase reporter and its core promoter mutant.(E)The PLK4 core promoter is sufficient to confer NFkappaB responsiveness.
	0.92	NFkappaB regulates PLK4 expression.(A) p52/p100 depletion regulates the expression of various genes involved in centrosome duplication.
	0.87	nuclear factor kappaB (NFkappaB) family of transcription factors contains 5 members: RelA (p65), RelB, c-Rel, NFkappaB1 (p105/p50), and NFkappaB2 (p100/p52), which can induce or repress the expression of target genes by binding DNA as homo- or hetero-dimers.
	0.79	p52 containing NFkappaB complexes.
24409185	0.97	p50, p65) and non-classical (p52, RelB) NFkappaB pathways.
	0.96	NFkappaB subunits (p50, p65, RelB, p52) by siRNA reduced enavatuzumab activity in sensitive cell lines (MDA-MB-468 and BT549).
	0.91	NFkappaB subunits (p50, p65, p52, RelB, and c-Rel) was observed in sensitive cell lines following treatment.
	0.89	p50, p65) as well as non-classical (p52, RelB) NFkappaB pathways could be activated by enavatuzumab treatment.
	0.89	p52 expression reduced enavatuzumab growth inhibition in MDA-MB-468 cells, while BT549 cells primarily showed a dependency on p50 and p65 for enavatuzumab activity (Figure 5C).
	0.87	p50, p52, or RelB and treated with enavatuzumab/crosslinker (blue and brown lines) are also displayed.
	0.85	p52, suggesting that p21 induction was NFkappaB-dependent.
	0.70	p50/p65 NFkappaB subunits and a more sustained activation of the non-classical p52/RelB subunits in response to TWEAK.
19502791	0.97	p52 forms a heterodimer with RelB, and these RelB-p52 NFkappaB complexes translocate to the nucleus to regulate transcription of specific NC NFkappaB target genes.
	0.97	NFkappaB activation including enhanced levels of p52 and specific phosphorylation of p100.
	0.97	NFkappaB complex consisting of p52 and RelB was present in human tumors, we stained paraffin-embedded tissues representing malignant pancreas for the presence of p52 and RelB. We immunohistochemically (IHC) stained 15 specimens using anti-p100/p52 and anti-RelB and found positive staining for p100/p52 and RelB in the malignant tissues.
	0.96	NFkappaB family member p100/NFkappaB2 to generate p52.
	0.91	p52 is a hallmark of the NC NFkappaB pathway.
	0.87	NFkappaB family proteins, elevated levels of nuclear p52 and RelB have been reported in primary tumor tissues including prostate cancer and oral cancers, as well as in tumor cell lines including prostate and pancreatic.
	0.85	p52-RelB NFkappaB complexes
20151024	0.97	p52 becomes apparent, effecting a change in the predominant dimer composition from RelA:p50 (and RelB:p50) to RelB : p52 (and RelA:p52) (Figure 4).
	0.97	p50 or p52 only containing dimers) bind DNA but do not activate transcription (medium grey), and 3 do not bind DNA (dark grey).
	0.93	NF-kappaB activation by these developmental signals focused on the generation of the RelB:p52 dimer by cotranslational proteolytic processing of de novo synthesized p100 to p52.
	0.86	NF-kappaB dimers, but do not inhibit DNA binding:instead these proteins may function as coactivators, for example, for the TAD-deficient NF-kappaB dimers p50:p50 or p52:p52.
	0.84	p105 and p100 (which are proteolytically processed to p50 and p52 NF-kappaB monomers, respectively) can act to self-inhibit p50 and p52.
	0.69	p50 and p52 do not.
23915189	0.97	p50 and p52, which bind to NF-kappaB elements of gene promoters, act as transcriptional repressors.
	0.97	p105 and p100 are processed to their shorter forms p50 and p52, respectively.
	0.96	p50 or p52 are bound to a member containing a transactivation domain, such as p65 or RelB, they constitute a transcriptional activator.
	0.93	NF-kappaB proteins, RelA, Rel (c-Rel), RelB, NFKB1 and NFKB2 obtained from: http://string-db.org/. The five NF-kappaB proteins are highlighted in red.
	0.90	p52 NF-kappaB by inducing acetylation of histones via recruitment of CBP and Stat2 on its promoter via CBP-mediated acetylation.
	0.65	p105 and p100) and are proteolytically processed to p50 and p52 (Figure 1A, black arrows), respectively.
28166267	0.97	p52 and (B) p50 levels were measured by immunoblot and compared to nuclear Lamin B1 levels.
	0.90	NF-kappaB subunit p52.
	0.90	NF-kappaB subunits p52 and p50.
	0.88	NF-kappaB, the non-canonical pathway is generally not associated with innate immune responses and results in nuclear translocation of heterodimerized RelB and p52.
	0.86	p52 nuclear entry and NIK-dependent NF-kappaB activation than Yersinia expressing these effectors.
	0.67	NF-kappaB response to Yersinia lacking actin-targeting effectors is NIK-dependent, both p50 and p52 subunits enter the nucleus following HEK293T infection with Deltayop6.
29315242	0.97	NFKB1 and NFKB2 are expressed as the precursors p105 and p100, which are cleaved to the functional transcription factors p50 and p52, respectively.
	0.96	NF-kappaB transcription factors: NFKB1, NFKB2, RELA, RELB, and REL, the protein products of which are p50, p52, p65 (RelA), RelB, and c-Rel, respectively.
	0.86	NF-kappaB by inducing p100 processing to p52, similar to CD40, BAFFR, and Lymphotoxin receptor (LTR).
	0.78	p50 and RelB/p52 are the more stable dimers.
	0.60	NF-kappaB members because p50 and p52 are products of partial proteolysis, and thus have a glycine-rich region instead of TAD.
27931134	0.97	NFkappaB activation pathways; the classical (canonical) pathway, which is mediated by p50, p65, and c-Rel, and the alternative (non-canonical) pathway, which is mediated by p52 and RelB. The classical pathway is activated by a variety of stimuli, such as tumor necrosis factor alpha (TNFalpha), interleukin-1 beta (IL-1beta), IL-6, bacterial lipopolysaccharide (LPS), and it regulates a multitude of cellular pathways, such as inflammation, the immune response, proliferation, and apoptosis.
	0.97	NFkappaB pathway utilizes p50, p65, and c-Rel, and the alternative NFkappaB pathway utilizes p52 and RelB for signaling.
	0.92	p52 staining in 17 of 17 naive canine DLBCL samples analyzed using immunohistochemistry (IHC), suggesting activation of the alternative NFkappaB pathway.
	0.91	NFkappaB complexes on super-shift assays (Figure 3(C)), but also resulted in decreased p52 binding.
31277415	0.97	NF-kappaB signaling transcription factor genes are Nfkb1 (p105-p50), Nfkb2 (p100-p52), Rela (RelA, p65), Rel (c-Rel), and Relb (RelB).
	0.96	NF-kappaB activation requires inducible proteolytic truncation of p100 protein to p52.
	0.78	p52 heterodimer is the general, transcriptionally active downstream component of the non-canonical NF-kappaB signaling pathway.
	0.70	p105 to p50 and p100 to p52).
20818435	0.97	NF-kappaB signaling involves phosphorylation and processing of p100 to p52.
	0.83	p50 but not by anti-p65, p52, or RelB (Figure 2g) demonstrating that C2 is a p50 homodimer.
	0.76	NF-kappaB transcription factor family contains five members named NF-kappaB1 (p105/p50), NF-kappaB2 (p100/p52), RelA (p65), RelB, and c-Rel that form homo- or heterodimers which are normally held inactive in the cytosol by a group of proteins named the inhibitors of kappaB or IkappaBs.
31040851	0.97	NFkappaB proteins such as RelB, p52, or p50 have rarely been described.
	0.93	NFkappaB is a protein family consisting of 5 dimers, RelA (p65), RelB, c-Rel, p50 (generated from p105), and p52 (generated from p100), which can form a variety of homodimers or heterodimers.
	0.86	p50 or p52 without transactivation domains repress active dimer binding.
30093619	0.96	NF-kappaB family are subjects of intense investigation over two decades, it is surprising that the interaction between p52 and ETS1 has not been characterized before.
	0.95	p52 or ETS1 siRNA during non-canonical NF-kappaB signaling in regulation of the -146C>T mutant TERT promoter.
	0.92	p52/ETS1 heterotetramer is capable of binding to two ETS motifs to activate -146C>T TERT promoter which could be activated downstream of non-canonical NF-kappaB signaling.
	0.82	p52 binding, are not conserved among the large ETS transcription factor family in humans (Supplementary Fig. 6), providing a plausible explanation of why only ETS1/2 are selected from ETS transcription factor family to function through the non-canonical NF-kappaB signaling to activate -146C>T TERT promoter.
	0.81	NF-kappaB pathway, stabilization of NF-kappaB-inducing kinase (NIK) triggers the processing of NF-kappaB p100 to p52, leading to the nuclear accumulation of p52.
	0.73	p52 is a member of the NF-kappaB family of transcription factors which regulate gene expression in response to a wide array of signaling by binding to consensus kappaB sites of 5'-GGGRNYYYCC-3' (R is a purine, Y is a pyrimidine, and N is any nucleotide).
	0.70	p52 needs to associate with consensus kappaB sites on the DNA to function during non-canonical NF-kappaB signaling, we show that p52 can activate the -146C>T TERT promoter without binding DNA.
26389665	0.96	NF-kappaB factors have been previously demonstrated to interact with ETS proteins, we performed immunoprecipitation with anti-Flag beads in T98G cells expressing Flag-tagged p52.
	0.96	p52 cooperation occurs only in context of the mutant C250T sequence (Fig. 7a,b) and these data explain why TERT is not activated by NF-kappaB signalling in somatic cells with the WT TERT promoter sequence.
	0.93	NF-kappaB signalling is insufficient to activate TERT transcription and efficient reactivation requires cooperation with the p52 subunit of NF-kappaB, downstream of non-canonical NF-kappaB signalling.
	0.89	NF-kappaB pathway, resulting in the generation of mature p52 (ref.).
	0.77	NF-kappaB pathway induces NF-kappaB-inducing kinase (NIK) to stimulate the processing of NF-kappaB2 p100 to p52 (ref.), which forms a heterodimer with RelB, leading to transcriptional activation of selective NF-kappaB target genes.
	0.72	NF-kappaB signalling through exogenous ligands (for example, TWEAK) or constitutive NIK expression, p52 is recruited to the C250T promoter and cooperates with ETS factors to drive efficient TERT transcription (Fig. 7g).
21113390	0.96	p50 and p52 lack this TAD, they may repress transcription when they are not associated with p65, c-Rel or RelB. In unstimulated cells, NF-kappaB dimers are retained in the cytoplasm by a family of inhibitory proteins known as inhibitors of NF-kappaB (IkappaBs).
	0.92	p105 and p100 proteins:the precursors of p50 and p52, respectively:also harbor multiple ankyrin repeats.
	0.91	p50/p50 and p52/p52, converting them from transcriptional repressors to transcriptional activators, and thereby elevating the expression of proliferation-promoting target genes such as cyclin D1.
	0.80	NF-kappaB family of TFs consists of five members: p105/p50 (NF-kappaB1), p100/p52 (NF-kappaB2), p65 (RelA), c-Rel and RelB. All NF-kappaB family members contain an N-terminal Rel homology domain (RHD), which mediates DNA binding and homo- and heterodimerization.
	0.80	NF-kappaB pathways, as siRNA-mediated knockdown of NIK in these cell lines affects signaling by both, decreasing phosphorylation of IkappaBalpha and the abundance of nuclear p52.
26269411	0.96	NF-kappaB pathway, NIK directly regulates the non-canonical NF-kappaB pathway through the phosphorylation of IKK and the processing of p52 from p100.
	0.80	p52 from p100 and the transcriptional activity of NF-kappaB. Whereas NIK-WT transfection induced the phosphorylation of NIK-Thr559 and the processing of p52 from p100 and enhanced the transcription of NF-kappaB, transfection of the NIK-T559A or NIK-KK429/430AA mutant could not induce the activation of each step of the non-canonical NF-kappaB pathway (Fig. 5f).
	0.78	p52 from p100 and enhanced the NF-kappaB transcription activity by four fold, co-transfection of NDRG2 and NIK suppressed the NIK-derived activation of each step in the non-canonical NF-kappaB pathway (Fig. 4c,d).
	0.61	NF-kappaB pathway was up-regulated in OSCC and ATL cells along with the phosphorylation of IKK and the degradation of IkappaBalpha, the non-canonical NF-kappaB pathway was activated in ATL cells along with the processing of p52 from p100 due to low or no p100 expression in OSCC cells.
	0.56	NF-kappaB inducible kinase (NIK) was found in ATL through low expression of miR31 and the accumulation of NIK protein led to the activation of IKK followed by the phosphorylation of p100 and processing to p52, resulting in the nuclear translocation of p52/RelB heterodimers.
30205516	0.96	p50 and p52, therefore they must either form a heterodimer with p65, c-Rel or RelB, or recruit co-activators to drive gene transcription, and when bound to DNA as homodimers they are generally thought to be transcriptional repressors (Figure 1).
	0.93	NFKB1 and NFKB2 have a glycine rich region (GRR), followed by an Ankyrin repeat domain (ANK) in the precursors p105 and p100.
	0.74	NFKB1 and NFKB2 are synthesized as precursors (p105 and p100) which are proteolytically cleaved to p50 and p52, respectively.
30778349	0.96	p50 and p52 operate as transcriptional repressors, as they can bind to promoter elements without activation of the transcriptional machinery.
	0.92	p105 (p52 and p50, respectively), do not contain a transactivation domain and need to dimerize with one of the other three family members, RelA (p65), RelB, or c-Rel to function as transcription factors.
	0.57	NFKB1 and NFKB2).
21918620	0.96	p52/p52 complex (equation 41) is impeded, which leads to the inactivation of the NF-kappaB complex p52/p52 and further induces apoptosis.
	0.63	NF-kappaB subunit p52 leading to repression of the antiapoptotic p52 target genes (equations 40, 41, 72).
30186235	0.96	p52 subunits of NF-kappaB in human primary thyroid cell cultures from Graves' patients, which indicates an involvement of both the canonical and noncanonical NF-kappaB pathways in CD40 signaling in Graves' disease.
22388891	0.95	NF-kappaB family, which consists of five evolutionarily conserved and structurally related activator proteins (RelA (p65), RelB, c-Rel (Rel), p50 and p52) and five inhibitory proteins (p100, p105 and the IkappaB proteins IkappaBalpha, IkappaBbeta and IkappaBepsilon).
	0.93	NF-kappaB elements at the NFKB2, MCP1 and MIP2 promoters (Fig. 4d).
	0.89	NFKB2, MCP-1, VCAM-1 and NFKBIA), but not LTbetaR-unresponsive genes (IL-6, CCND1) or non-NF-kappaB target genes (18S, SPARC), was impaired by expression of the nuclear p100 mutant (Fig. 4c and Supplementary Fig. S6a).
	0.86	NF-kappaB proteins (p52 and RelB) induced by NF-kappaB signalling may lead to p100 stabilization through competition with Fbxw7alpha.
	0.62	NF-kappaB stimuli, leading to p100 cleavage into p52 (refs).
30096845	0.95	NF-kappaB subunit, p52, specifically binds to multiple sites on the HIF-2alpha promoter.
	0.83	NF-kappaB is also able to induce the expression and activity of HIF transcription factors, but in this case, the effect is mediated by p52 on the HIF-2alpha gene in both cell lines that we tested.
	0.79	NF-kappaB subunit p52.
	0.70	NF-kappaB activation, via a mechanism that is dependent on the p52 subunit.
19746155	0.95	p50/p105, p52/p100, RelB and cRel), which share a common Rel homology domain, typically exists as homo- or hetero-dimers in the cytoplasm where they are bound by inhibitory kappaB proteins (IkappaB), such as IkappaBalpha.
	0.91	p52 is the result of true activation of the non-canonical pathway through IKKalpha-mediated phosphorylation of p100 and its subsequent cleavage to p52, or if there are other mechanisms downstream of IKKalpha and IKKbeta that are driving additional NF-kappaB subunits to the nucleus.
	0.75	p52, a critical component and effector of the alternative NF-kappaB pathway.
30941118	0.95	P50 in the current study were assigned according to the position of the genetic variant within the NFKB2 locus.
	0.61	NF-kappaB pathway has been shown to play an important role in TFH development by regulating the expression of inducible T cell costimulator (ICOS) ligand in B cells, and thus p52 haploinsufficiency is likely to cause the disturbances of the humoral immune axis.
	0.59	NFKB1 and NFKB2 now represent the largest CVID subgroups with known monogenetic mutations.
30250646	0.94	NF-kappaB complex in presence and absence of HPV infection, gel supershift assays were performed using specific antibodies (Santacruz, USA) raised against all five NF-kappaB family proteins; p50, p52, p65, c-Rel and RelB. The gel supershift assay revealed a differential DNA binding pattern and difference in composition of NF-kappaB complex.
	0.93	NF-kappaB family proteins between HPV+ve and HPV-ve tongue cancer cases, a slightly higher expression of p50, p52 and c-Rel proteins was observed mainly in HPV-ve cases as compared to HPV16+ve TSCCs that selectively overexpressed p65 protein (Figure 3A and Table 1C).
	0.68	p50, p52, p65 and c-Rel and the severity of tongue cancer lesions as they progressed from normal to precancer to malignant phenotype.
30984185	0.94	NF-kappaB family is made up of five proteins, p105/p50 (encoded by NFKB1), p100/p52 (encoded by NFKB2), RelA (also known as p65), RelB, and c-Rel, which can form a range of homo- and hetero-dimeric complexes [Figures 1A,B; ].
	0.93	p50 and p52 do not have a TD and homodimers or heterodimers made up of only p50 and p52 are not capable of inducing transcription without recruiting an additional TD-containing transcription factor.
	0.90	p52 abundance increases, not only could this induce an increase in repressive p52:p52 dimers, competition for NF-kappaB dimerization will reduce the abundance of lower dimerization affinity subunit pairs, which could lead to splitting of dimers containing two TD domains to generate p52-containing heterodimers, and effectively increase the abundance of transcription activating NF-kappaB dimers.
28561798	0.93	NF-kappaB canonical signaling by activating the IKKalpha/beta/gamma complex and the non-canonical pathway by inducing the expression of RelB and NFKB2 and activating IKKalpha homodimers.
	0.92	NF-kappaB activation, as evidenced by the detection of a higher p52/p100 ratio in BIRC3-mutated patients.
	0.79	NF-kappaB activation in HRS cells, as NOTCH1 induces the processing of the NFKB2 gene product p100 into its p52 active form and leads to an enhanced DNA binding activity of RelB/p52 heterodimers.
24533079	0.92	NFKB2/p100 largely depends on NF-kappaB activation through the canonical pathway may partly explain the abundant expression of NFKB2/p100 and its phosphorylated form as well as p52 in JHOC-5 cells.
	0.91	p50 or anti-c-Rel antibodies, pre-immune (PI), anti-p52, anti-RelA or anti-RelB sera, and then subjected to EMSA with the NF-kappaB-specific probe.
	0.89	NF-kappaB components, p52 and RelB in RMG-I cells (Figure 4E).
	0.82	NF-kappaB is composed of homo- and heterodimers of five members, NF-kappaB1 (p50 and its precursor p105), NF-kappaB2 (p52 and its precursor p100), RelA (p65), RelB and c-Rel.
	0.79	p52 DNA binding activity and NF-kappaB-dependent reporter gene expression as well as NF-kappaB target gene expression.
21383764	0.91	NF-kappaB subunits p105 and p100 to p50 and p52, respectively.
	0.91	NF-kappaB pathway is activated by the kinases NIK and IKKalpha, leading to the nuclear translocation of p52-RELB.
	0.85	NF-kappaB proteins are members of the Rel domain-containing protein family: RELA (also known as p65), RELB, c-REL, the NF-kappaB p105 subunit (also known as NF-kappaB1; which is cleaved into the p50 subunit) and the NF-kappaB p100 subunit (also known as NF-kappaB2; which is cleaved into the p52 subunit); these proteins can homodimerize or heterodimerize through their conserved Rel homology domain to mediate gene transcription.
22806876	0.90	NF-kappaB canonical activity included p65 , p50 , c-Rel ; NF-kappaB non-canonical activity included p52 and RelB .
	0.89	p50, and p52 nuclear translocation.
	0.83	p50, p52, and Nucleolin antibodies.
	0.72	p50 were inhibited by 62% and 56%, compared to 28% and 22% inhibition of p52 and RelB (Figure 1B).
	0.72	NF-kappaB binding to DNA even after a short exposure, with potent inhibition of p65, p50 (90-95%), p52 (63%), and RelB (79%) (Figure 1C).
	0.70	p50 and p52 was performed with the NIH image J Software and expressed as fold change relative to non-treated cells.
	0.68	NF-kappaB canonical activity included p65 , p50 , and c-Rel ; NF-kappaB non-canonical activity included p52 and RelB .
29772694	0.90	p50 NF-kappaB activation by canonical signals: interestingly, canonical TNF signaling induced an additional, long-lasting RelB:p50 activity in Nfkb2-/- MEFs, which lacked the expression of the non-canonical signal transducer p100.
	0.75	p50, c-Rel:p50 and RelB:p52 heterodimers not only bind to identical kappaB sites, but they also show similar affinities towards DNA.
	0.73	NF-kappaB family consists of five structurally related monomeric subunits: RelA (also called p65), RelB, c-Rel, p50 (encoded by NFKB1 and produced as a precursor protein p105) and p52 (encoded by NFKB2 and produced as a precursor p100).
	0.66	NF-kappaB pathways in the regulation of RelB NF-kappaB: canonical signaling also modulates the RelB:p52 activity induced by non-canonical inducers.
21170083	0.87	p50 and p52 and the full-length proteins p105 and p100 also function as IkappaB proteins.
	0.71	p50 and p52 homodimers, and induces its nuclear export (together with histone deacetylase 3) and degradation.
	0.56	NF-kappaB is a family of transcription factors that includes five members: RelA/p65, c-Rel, RelB, NF-kappaB1 (p50) and NF-kappaB2 (p52).
27732951	0.85	NF-kappaB pathway, driven by a RelB-p52 dimer, could be contributing to GSC maintenance as well.
	0.82	NF-kappaB is a family of transcription factors consisting of five members: p65 (RelA), RelB, c-Rel, p105/p50, and p100/p52 that homo- and heterodimerize to regulate transcription of target genes.
22864569	0.77	p50) and the non-canonical (RelB:p52) NF-kappaB pathways.
	0.67	p52 production, alterations in p52/NF-kappaB complex formation and activity on stimulation.
	0.55	NF-kappaB pathway stimuli, leads to increased p52 levels and activity.
31244811	0.77	p52, the final effector of the alternative NF-kappaB signaling.
	0.75	NF-kappaB pathway, only Tax-1 activates the non-canonical one by recruiting NEMO and IKKalpha to p100 and promoting the release of p52/RelB active heterodimers into the nucleus.
	0.66	NF-kappaB pathway, but we have not observed an accumulation of p52 in the presence of HBZ (data not shown).
24023754	0.74	p50/105 subunits but little or none of the p52/100 subunit, indicating the classical canonical pathway is activated in the lines tested (Figure 8A).
28629746	0.55	p52, which is dependent on activation of the non-canonical NF-kappaB pathway, was deficient in LPS+anti-LTbetaR mAb stimulated fibroblasts from these patients.
	0.52	NF-kappaB family of transcription factors includes RelA (p65), RelB, c-Rel, NF-kappaB1 (p50/p105) and NF-kappaB2 (p52/p100) and plays a critical role in innate and adaptive immunity.
20649549	0.53	p50-p50 and p52-p52 homodimers act as transcriptional repressors.