Structural Basis for Recognition of Diubiquitins by NEMO
about
NEMO specifically recognizes K63-linked poly-ubiquitin chains through a new bipartite ubiquitin-binding domainLUBAC regulates NF-κB activation upon genotoxic stress by promoting linear ubiquitination of NEMOTwo-sided ubiquitin binding explains specificity of the TAB2 NZF domainUbc13: the Lys63 ubiquitin chain building machineOptimising methods for the preservation, capture and identification of ubiquitin chains and ubiquitylated proteins by immunoblottingWhen ubiquitin meets NF-κB: a trove for anti-cancer drug developmentNF-κB regulation: lessons from structuresRegulation of nuclear factor-κB in autoimmunityDeath receptor-ligand systems in cancer, cell death, and inflammationUbiquitin in the immune systemThe TLR and IL-1 signalling network at a glanceLinear ubiquitination signals in adaptive immune responsesSuper-resolution microscopy reveals a preformed NEMO lattice structure that is collapsed in incontinentia pigmentiCrystal structure of the NEMO ubiquitin-binding domain in complex with Lys 63-linked di-ubiquitinThe Yeast E4 Ubiquitin Ligase Ufd2 Interacts with the Ubiquitin-like Domains of Rad23 and Dsk2 via a Novel and Distinct Ubiquitin-like Binding DomainCrystal structure of inhibitor of κB kinase βSpecific recognition of linear polyubiquitin by A20 zinc finger 7 is involved in NF-κB regulationMechanism Underlying I B Kinase Activation Mediated by the Linear Ubiquitin Chain Assembly ComplexThe role of pattern-recognition receptors in innate immunity: update on Toll-like receptorsMolecular basis for specificity of the Met1-linked polyubiquitin signalLinear ubiquitination in immunityRegulation of tumour necrosis factor signalling: live or let dieProbing the Solution Structure of IκB Kinase (IKK) Subunit γ and Its Interaction with Kaposi Sarcoma-associated Herpes Virus Flice-interacting Protein and IKK Subunit β by EPR SpectroscopyTNF and IL-1 exhibit distinct ubiquitin requirements for inducing NEMO-IKK supramolecular structuresCan I solve my structure by SAD phasing? Planning an experiment, scaling data and evaluating the useful anomalous correlation and anomalous signal.The IKK complex, a central regulator of NF-kappaB activationSignaling to NF-kappaB: regulation by ubiquitination.Recent advances in polyubiquitin chain recognition.NF-κB essential modulator (NEMO) interaction with linear and lys-63 ubiquitin chains contributes to NF-κB activationGeneration and physiological roles of linear ubiquitin chains.Epstein-Barr latent membrane protein 1 transformation site 2 activates NF-kappaB in the absence of NF-kappaB essential modifier residues 133-224 or 373-419.Emerging complexity of protein ubiquitination in the NF-κB pathway.Covalent modification of the NF-κB essential modulator (NEMO) by a chemical compound can regulate its ubiquitin binding properties in vitro.ATM- and NEMO-dependent ELKS ubiquitination coordinates TAK1-mediated IKK activation in response to genotoxic stress.A structural basis for IκB kinase 2 activation via oligomerization-dependent trans auto-phosphorylationA distinct role of Riplet-mediated K63-Linked polyubiquitination of the RIG-I repressor domain in human antiviral innate immune responsesThe IκB kinase complex in NF-κB regulation and beyond.Kaposi's sarcoma-associated herpesvirus vFLIP and human T cell lymphotropic virus type 1 Tax oncogenic proteins activate IkappaB kinase subunit gamma by different mechanisms independent of the physiological cytokine-induced pathwaysCrystal structure of a complex of NOD1 CARD and ubiquitin.Nuclear initiated NF-κB signaling: NEMO and ATM take center stage.
P2860
Q24317367-D8000CA5-7685-4370-B2DA-F59CCB77FDACQ24318791-701E86DB-F7F4-4DF5-8D4B-8463B7EFCEA1Q24320937-4C3574E9-BD1E-4DE9-A55E-C80A67AD75B7Q26739716-27B00719-CAC1-4B6E-B5BE-640682DB5B95Q26795621-B9C38C39-25B5-4128-84CB-75BF9EB52AEDQ26827754-39853327-9528-4E3C-A15F-A444C15B840FQ26859097-E3C6CE6C-720F-471A-9828-026CA10AE83AQ26860148-ED23EE73-8DF7-47A2-9A16-799068D4893AQ26865568-62DA7714-225E-45B8-BFAE-D33504E42A1DQ26998711-6D7AC6EC-8AF2-4C5D-9B14-E6E07D4E4963Q27013358-38E438F0-E3F1-48DF-9267-E550396A6698Q27027872-36410E1B-7CF8-4F88-AF9A-86258654F94DQ27330416-751DD62A-D2D3-4231-9EDF-585579EBFDE1Q27657476-0D676CC4-8EBA-4488-8C3E-B9A5DA6AA78DQ27660967-9D5838DB-7CE2-4FAB-833B-415BF94DEEDEQ27667308-DDD7103E-73DC-4606-AB78-48451023ACC5Q27674024-505356CD-1BED-4B5A-9FA1-566CBA24141BQ27681474-983BDAFA-A076-4839-8F8E-B12EDF634F08Q27860900-37241428-38E3-40DD-BD37-FDCB2E30B830Q28072740-FD4CAB16-0704-4B9A-BC0D-295C0D59B2B7Q28082899-0198D980-3471-4E80-8A57-CAE3BC49A54EQ28262381-0B37B3F5-239F-493D-B103-E32EDF22A944Q30374718-3855EE08-EE20-41BE-B485-488BD308B37EQ30566060-4467EC3F-98BB-497F-B8E6-CEF11913B913Q31056061-F6D8F7BC-A72A-40EA-9560-5ACB7BB070B4Q33693802-75942B16-A8D6-4C9D-9DFE-84D0735EF468Q33693806-9B5B7544-7625-4709-BC0D-679279AFEBD2Q33760446-460F53AA-DA2F-4EDF-BC7F-FCF9F8EC1DB7Q33915312-F94D4C0E-E598-42C2-99A7-228BD5E3E423Q34197025-CEFB015E-62A0-48FE-BE16-C47ED740DF0FQ34241279-B574440C-BA81-4DD6-A4B9-8FDB9E2FD414Q34346080-5F44FEB2-636E-4C62-8D65-8483788C3861Q34580265-E2A7DFC5-12B9-45C4-B547-BCE132EB8A0DQ34620780-09C75C25-4E3D-4880-8EFC-3D65EA87BF64Q34775516-1851810F-E250-4F37-857F-5E0492731A74Q34945431-5D7608B7-1FE6-4B91-B78B-6A8BFB20C2A7Q35001723-46DC4A52-5D36-4F6E-BB2E-3E6AD5137112Q35077741-8918CB56-9A60-47D7-9650-78352EF1554BQ35225740-B46B3B04-680B-45DC-A15C-B27038E0194DQ35347865-3FC65264-4B12-408C-8B12-8BF7E93E5B5F
P2860
Structural Basis for Recognition of Diubiquitins by NEMO
description
2009 nî lūn-bûn
@nan
2009 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի մարտին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Structural Basis for Recognition of Diubiquitins by NEMO
@ast
Structural Basis for Recognition of Diubiquitins by NEMO
@en
Structural Basis for Recognition of Diubiquitins by NEMO
@nl
type
label
Structural Basis for Recognition of Diubiquitins by NEMO
@ast
Structural Basis for Recognition of Diubiquitins by NEMO
@en
Structural Basis for Recognition of Diubiquitins by NEMO
@nl
prefLabel
Structural Basis for Recognition of Diubiquitins by NEMO
@ast
Structural Basis for Recognition of Diubiquitins by NEMO
@en
Structural Basis for Recognition of Diubiquitins by NEMO
@nl
P2093
P2860
P3181
P1433
P1476
Structural basis for recognition of diubiquitins by NEMO
@en
P2093
Carla C Rospigliosi
Chuan-Jin Wu
David Eliezer
Dietrich B Conze
Jonathan D Ashwell
Yu-Chih Lo
P2860
P304
P3181
P356
10.1016/J.MOLCEL.2009.01.012
P50
P577
2009-01-29T00:00:00Z