Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity
about
Modulation of tumor necrosis factor by microbial pathogens.The HTLV-1 Tax interactomeRegulation of the transcription factor NF-kappaB1 by microRNA-9 in human gastric adenocarcinomaOpposite effect of NF-kB and c-Jun N-terminal kinase on p53-independent GADD45 induction by arseniteSignaling from toxic metals to NF-kappaB and beyond: not just a matter of reactive oxygen speciesCIKS, a connection to Ikappa B kinase and stress-activated protein kinaseCARD9 is a novel caspase recruitment domain-containing protein that interacts with BCL10/CLAP and activates NF-kappa BA diverse family of proteins containing tumor necrosis factor receptor-associated factor domainsCSN3 interacts with IKKgamma and inhibits TNF- but not IL-1-induced NF-kappaB activationA DAP12-mediated pathway regulates expression of CC chemokine receptor 7 and maturation of human dendritic cellsPIAS3 suppresses NF-kappaB-mediated transcription by interacting with the p65/RelA subunitNF-{kappa}B is transported into the nucleus by importin {alpha}3 and importin {alpha}4ABIN-2 forms a ternary complex with TPL-2 and NF-kappa B1 p105 and is essential for TPL-2 protein stabilityOTULIN antagonizes LUBAC signaling by specifically hydrolyzing Met1-linked polyubiquitinAn integrated approach to elucidate the intra-viral and viral-cellular protein interaction networks of a gamma-herpesvirusThe IκB kinase complex regulates the stability of cytokine-encoding mRNA induced by TLR-IL-1R by controlling degradation of regnase-1A splice variant of stress response gene ATF3 counteracts NF-kappaB-dependent anti-apoptosis through inhibiting recruitment of CREB-binding protein/p300 coactivatorNuclear factor κB subunits RelB and cRel negatively regulate Toll-like receptor 3-mediated β-interferon production via induction of transcriptional repressor protein YY1IKKβ phosphorylation regulates RPS3 nuclear translocation and NF-κB function during infection with Escherichia coli strain O157:H7Transcriptional activation of the NF-kappaB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1)CSN controls NF-kappaB by deubiquitinylation of IkappaBalphaPhosphorylation and ubiquitination of the IkappaB kinase complex by two distinct signaling pathwaysRetroviral oncoprotein Tax deregulates NF-kappaB by activating Tak1 and mediating the physical association of Tak1-IKKOncoprotein p28 GANK binds to RelA and retains NF-kappaB in the cytoplasm through nuclear exportHydrogen sulfide-linked sulfhydration of NF-κB mediates its antiapoptotic actionsRING finger protein AO7 supports NF-kappaB-mediated transcription by interacting with the transactivation domain of the p65 subunitA20 inhibits tumor necrosis factor (TNF) alpha-induced apoptosis by disrupting recruitment of TRADD and RIP to the TNF receptor 1 complex in Jurkat T cells.A novel eIF5A complex functions as a regulator of p53 and p53-dependent apoptosisPriming and extending: a UbcH5/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrateNOD2 controls the nature of the inflammatory response and subsequent fate of Mycobacterium tuberculosis and M. bovis BCG in human macrophagesComparative analysis of apoptosis and inflammation genes of mice and humansNF-kappaB1 p105 negatively regulates TPL-2 MEK kinase activityTumor necrosis factor-alpha-induced IKK phosphorylation of NF-kappaB p65 on serine 536 is mediated through the TRAF2, TRAF5, and TAK1 signaling pathwayCopine-I represses NF-kappaB transcription by endoproteolysis of p65Termination of NF-kappaB activity through a gammaherpesvirus protein that assembles an EC5S ubiquitin-ligaseInflammatory cardiac valvulitis in TAX1BP1-deficient mice through selective NF-kappaB activationThe ubiquitin-editing enzyme A20 requires RNF11 to downregulate NF-kappaB signallingA20-binding inhibitor of nuclear factor-kappaB (NF-kappaB)-2 (ABIN-2) is an activator of inhibitor of NF-kappaB (IkappaB) kinase alpha (IKKalpha)-mediated NF-kappaB transcriptional activityCompetitive control of independent programs of tumor necrosis factor receptor-induced cell death by TRADD and RIP1Negative regulation of NF-kappaB action by Set9-mediated lysine methylation of the RelA subunit
P2860
Q21089629-07DEFA72-066C-42E1-87ED-49ED54D3EA2DQ21093224-6142921A-4D5A-4B6C-ABA7-3F52C8F8C014Q21093275-B454E53A-2D8C-4D07-AB30-B62DFECF9DC3Q23912784-4BE1BF76-FD8D-4851-A706-7BA0E4CFB6D0Q23923272-CE2248EC-7B3D-4DA7-B014-95181E2894AFQ24290148-B967C798-CBA4-41E7-BB1A-0E0F1677FA59Q24290440-6A29BC9D-4104-44A2-849D-C14B2C5B1359Q24291050-62F0B1F8-9484-490F-AAA8-C35D6CCF2D89Q24291350-C4E8B088-03EE-4954-8994-8BC481B9AB60Q24291798-F75C833E-051D-4899-8BC2-045E11CBF5F5Q24292903-105A3174-EC8A-41C4-9217-123825F50E33Q24293000-40531B85-AE42-46B3-97F3-C441C0E34BDAQ24294653-7C2671B0-A705-4F9E-BA79-7F4905241808Q24294696-1B49A829-4539-40F5-8FE3-07076010B0D5Q24294710-FD84FBEE-6781-477F-AC12-2F6C31AD2C21Q24294979-F23636DF-3856-43BF-9851-444D73417509Q24295232-3DFCDB3B-6A36-48CE-A382-123A9F11C839Q24296410-188A3826-51D8-4C47-BD27-A7C7F3915AC4Q24297066-432535E2-1C73-4535-B5D6-9658EF3762A8Q24297420-87F25583-CFA0-444F-AFD8-B5CF21759CD5Q24298155-2FE6981F-CE69-4DC4-A0F6-60DA50B242EAQ24300430-BBBD0C34-ED11-4980-AD5E-1452714FD0B2Q24300455-0B4461FF-F3F9-49D1-B6DF-02BBBE072A64Q24301532-E223EB9E-605A-46F7-A75B-2DBD7BE17EC5Q24301813-0D35AF95-71CE-46C2-BA0B-2D613580E47CQ24301876-9D4EE536-BE83-4E95-B8EA-9E7F1021A382Q24304048-6EC1F7EA-CF26-4155-82AA-116CBF6AED6EQ24304245-03532CBF-CD16-491B-A41D-8DFAA2B97C4FQ24304915-7A89856E-F274-4503-9B97-687BC32B2EEEQ24305119-8DCFA2FA-FB72-42CE-A777-078DB8199646Q24306056-B2F144EC-616E-4E2E-8ECB-F6C1F420F5E6Q24306480-2E10E544-53C4-4AE5-8945-F0B9F490FFE3Q24306909-2D8175B9-AF52-42BF-9048-E5612D4B09EAQ24307551-AD65A666-D706-4C25-96E6-AE6B669B0370Q24309461-D8008812-A18F-4575-AB8F-58BBBDB93D3FQ24309469-8169ECDC-9672-4F38-8AC1-C2D25F10F181Q24314649-8221F065-6E61-4B77-AA7B-9FB8A2A4AAD0Q24316467-E8722CBF-84DF-4A68-8B80-65FB35CECE7BQ24317322-3555F2E1-7D6E-4139-82F5-3DE55AD85416Q24317508-4B48CFE7-C0D9-4937-AF76-03D292365569
P2860
Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity
description
2000 nî lūn-bûn
@nan
2000 թուականին հրատարակուած գիտական յօդուած
@hyw
2000 թվականին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity
@ast
Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity
@en
Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity
@nl
type
label
Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity
@ast
Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity
@en
Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity
@nl
prefLabel
Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity
@ast
Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity
@en
Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity
@nl
P921
P3181
P1476
Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity
@en
P2093
P304
P3181
P356
10.1146/ANNUREV.IMMUNOL.18.1.621
P407
P577
2000-01-01T00:00:00Z