The trimerization domain of NEMO is composed of the interacting C-terminal CC2 and LZ coiled-coil subdomains.
about
Oligomerization of optineurin and its oxidative stress- or E50K mutation-driven covalent cross-linking: possible relationship with glaucoma pathologyPositive regulation of IkappaB kinase signaling by protein serine/threonine phosphatase 2AIntermolecular disulfide bond formation in the NEMO dimer requires Cys54 and Cys347Molecular basis of hypohidrotic ectodermal dysplasia: an updateNF-κB, the first quarter-century: remarkable progress and outstanding questionsNF-kappaB-related genetic diseasesQuantification of cellular NEMO content and its impact on NF-κB activation by genotoxic stressNEMO oligomerization in the dynamic assembly of the IkappaB kinase core complexInhibition of NF-kappaB activation with designed ankyrin-repeat proteins targeting the ubiquitin-binding/oligomerization domain of NEMO.Differential signaling circuits in regulation of ultraviolet C light-induced early- and late-phase activation of NF-κB.TNF receptor-1 (TNF-R1) ubiquitous scaffolding and signaling protein interacts with TNF-R1 and TRAF2 via an N-terminal docking interface.The IκB kinase complex in NF-κB regulation and beyond.Evidence that the kinase-truncated c-Src regulates NF-κB signaling by targeting NEMO.Impediment of NEMO oligomerization inhibits osteoclastogenesis and osteolysisHuman disease resulting from gene mutations that interfere with appropriate nuclear factor-kappaB activation.X-linked susceptibility to mycobacteria is caused by mutations in NEMO impairing CD40-dependent IL-12 production.Signal processing by its coil zipper domain activates IKK gamma.The CARMA1 signalosome links the signalling machinery of adaptive and innate immunity in lymphocytes.NEMO oligomerization and its ubiquitin-binding properties.Hypomorphic nuclear factor-kappaB essential modulator mutation database and reconstitution system identifies phenotypic and immunologic diversity.IκB kinase γ/nuclear factor-κB-essential modulator (IKKγ/NEMO) facilitates RhoA GTPase activation, which, in turn, activates Rho-associated KINASE (ROCK) to phosphorylate IKKβ in response to transforming growth factor (TGF)-β1Therapeutic peptides for cancer therapy. Part I - peptide inhibitors of signal transduction cascades.Regulation of NF-κB by TNF family cytokines.Disulfide-mediated stabilization of the IκB kinase binding domain of NF-κB essential modulator (NEMO).The zinc finger of NEMO is a functional ubiquitin-binding domain.Heptad repeats regulate protein phosphatase 2a recruitment to I-kappaB kinase gamma/NF-kappaB essential modulator and are targeted by human T-lymphotropic virus type 1 tax.Mutation of nonessential cysteines shows that the NF-κB essential modulator forms a constitutive noncovalent dimer that binds IκB kinase-β with high affinity.Inhibition of NEMO, the regulatory subunit of the IKK complex, induces apoptosis in high-risk myelodysplastic syndrome and acute myeloid leukemia.The TFG protein, involved in oncogenic rearrangements, interacts with TANK and NEMO, two proteins involved in the NF-kappaB pathway.A point mutation in NEMO associated with anhidrotic ectodermal dysplasia with immunodeficiency pathology results in destabilization of the oligomer and reduces lipopolysaccharide- and tumor necrosis factor-mediated NF-kappa B activation.Inhibition of NF-kappa B activation by peptides targeting NF-kappa B essential modulator (nemo) oligomerization.Dimerization of the I kappa B kinase-binding domain of NEMO is required for tumor necrosis factor alpha-induced NF-kappa B activity.Alterations of the IKBKG locus and diseases: an update and a report of 13 novel mutations.
P2860
Q24300251-8181C8F1-DE27-4FA4-B4CB-B083A4767CD6Q24318289-3B10BCEC-93E9-4C15-9F2B-3BCC7B4E5B29Q24647995-94A1EF70-5F5B-4DD4-BEC7-B44D30F0D133Q26796229-9BD30A38-8650-4DBB-8106-EAC3EAAC7498Q26822516-BDD00364-7222-400E-91BA-71BE171085DDQ28290224-E7378F02-52D9-412B-A799-6B552DB49E05Q28543866-FB626A7B-BD63-4149-8371-D212E290A0CAQ28584007-4C0BD520-F5A1-48E9-9D46-16DA13011CB1Q33296431-41B9AC1D-8668-4AD5-AAA8-7493EC5F1A08Q34145906-8057EE36-1C9E-486F-A00D-9BDFCCBE26B9Q34187687-9CB833A4-7274-4CA2-9BFF-F62C2C8B4046Q35001723-2FB20168-237A-47E6-9913-13A492541EB1Q35860261-2E0C814C-5333-42E3-AD16-D68EC7AE1F1FQ35860271-6981B4EC-6ACE-411E-ADDC-D22AFC782822Q36015009-227475D4-2510-4AC7-9E04-B43577436C40Q36228741-1B0F7054-FED2-4A3A-89C7-59396D8C75FCQ36446179-A69CEB2C-80E9-4C69-B875-1E4A3E5780C6Q36634002-06115054-0E26-4D76-A49A-7031D9FA2499Q37257501-630B3D47-8A7F-4313-8C03-C210F6D2DEBDQ37262549-5F42DE64-C192-4E14-A938-A335E8584111Q37488455-36F4F2B1-0573-42EB-B29C-9393CFC30B89Q37564522-A6E57BB7-CF07-469A-88F9-202AEC4BC3D3Q38222709-DCD40B92-4A40-4474-A273-E7A2A9B6AD6DQ38940206-041D62ED-CB29-4602-9BA3-7F1D1B43EC81Q39912363-59187F49-4BEB-4D56-BD6A-F3FE4968E40FQ40168522-FDFD3E19-8A80-4CF5-8525-72B2C75BC4B4Q40192267-40FEB474-AC1C-48FD-B43D-866FFEB43254Q40219923-6BA2208D-10E9-4D65-9920-420DA4F758E4Q40302096-897A2F05-93E4-40E0-9F26-83720227B056Q40335919-57E1F65C-0D9D-4CD3-84D2-E9C666494144Q40507772-DE613D09-3B44-4D1A-8B00-598E8979211AQ41077731-7EFB6256-B158-4406-9FEF-0EC037ECAD97Q43785411-16C3D84D-B259-449A-9465-415A269A2D24
P2860
The trimerization domain of NEMO is composed of the interacting C-terminal CC2 and LZ coiled-coil subdomains.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
The trimerization domain of NE ...... and LZ coiled-coil subdomains.
@en
type
label
The trimerization domain of NE ...... and LZ coiled-coil subdomains.
@en
prefLabel
The trimerization domain of NE ...... and LZ coiled-coil subdomains.
@en
P2093
P2860
P356
P1476
The trimerization domain of NE ...... and LZ coiled-coil subdomains.
@en
P2093
Alain Israël
Emilie Vinolo
Fabrice Agou
François Traincard
Gilles Courtois
Michel Véron
Shoji Yamaoka
P2860
P304
27861-27869
P356
10.1074/JBC.M314278200
P407
P577
2004-04-23T00:00:00Z