Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases
about
NleG Type 3 effectors from enterohaemorrhagic Escherichia coli are U-Box E3 ubiquitin ligasesAtomic interaction networks in the core of protein domains and their native foldsA bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory responseThe Salmonella type III secretion effector, salmonella leucine-rich repeat protein (SlrP), targets the human chaperone ERdj3Salmonella type III secretion effector SlrP is an E3 ubiquitin ligase for mammalian thioredoxinA family of Salmonella virulence factors functions as a distinct class of autoregulated E3 ubiquitin ligasesHijacking the host ubiquitin pathway: structural strategies of bacterial E3 ubiquitin ligasesImplications of Spatiotemporal Regulation of Shigella flexneri Type Three Secretion Activity on Effector Functions: Think Globally, Act LocallyBacteria-host relationship: ubiquitin ligases as weapons of invasionShigella IpaH Family Effectors as a Versatile Model for Studying Pathogenic BacteriaBacterial effectors and their functions in the ubiquitin-proteasome system: insight from the modes of substrate recognitionEpigenetics and bacterial infectionsGogB is an anti-inflammatory effector that limits tissue damage during Salmonella infection through interaction with human FBXO22 and Skp1A Structural Element within the HUWE1 HECT Domain Modulates Self-ubiquitination and Substrate Ubiquitination ActivitiesA disulfide driven domain swap switches off the activity of Shigella IpaH9.8 E3 ligaseBiochemical and Structural Studies of a HECT-like Ubiquitin Ligase from Escherichia coli O157:H7Structure of HHARI, a RING-IBR-RING Ubiquitin Ligase: Autoinhibition of an Ariadne-Family E3 and Insights into Ligation MechanismStructure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligasesStructure of an SspH1-PKN1 Complex Reveals the Basis for Host Substrate Recognition and Mechanism of Activation for a Bacterial E3 Ubiquitin LigaseThe Legionella effector SidC defines a unique family of ubiquitin ligases important for bacterial phagosomal remodeling.Shigella: a model of virulence regulation in vivo.The structure of the Slrp-Trx1 complex sheds light on the autoinhibition mechanism of the type III secretion system effectors of the NEL familyIdentification of an unconventional E3 binding surface on the UbcH5 ~ Ub conjugate recognized by a pathogenic bacterial E3 ligaseComplex structure of OspI and Ubc13: the molecular basis of Ubc13 deamidation and convergence of bacterial and host E2 recognitionStructure of the Legionella Virulence Factor, SidC Reveals a Unique PI(4)P-Specific Binding Domain Essential for Its Targeting to the Bacterial PhagosomeThe Yersinia Type III secretion effector YopM Is an E3 ubiquitin ligase that induced necrotic cell death by targeting NLRP3A pathogen type III effector with a novel E3 ubiquitin ligase architecture.Legionella metaeffector exploits host proteasome to temporally regulate cognate effector.The C-terminal tail of Yersinia pseudotuberculosis YopM is critical for interacting with RSK1 and for virulenceFunctional analysis of NopM, a novel E3 ubiquitin ligase (NEL) domain effector of Rhizobium sp. strain NGR234.Repertoire, unified nomenclature and evolution of the Type III effector gene set in the Ralstonia solanacearum species complex.Five mechanisms of manipulation by bacterial effectors: a ubiquitous theme.Shigella IpaH7.8 E3 ubiquitin ligase targets glomulin and activates inflammasomes to demolish macrophages.Large-scale identification and translocation of type IV secretion substrates by Coxiella burnetii.Patterns of expression and translocation of the ubiquitin ligase SlrP in Salmonella enterica serovar Typhimurium.The Shigella type three secretion system effector OspG directly and specifically binds to host ubiquitin for activation.Convergent evolution in the assembly of polyubiquitin degradation signals by the Shigella flexneri IpaH9.8 ligaseShigella IpaH0722 E3 ubiquitin ligase effector targets TRAF2 to inhibit PKC-NF-κB activity in invaded epithelial cells.IS3 profiling identifies the enterohaemorrhagic Escherichia coli O-island 62 in a distinct enteroaggregative E. coli lineage.Middle-down mass spectrometry enables characterization of branched ubiquitin chains.
P2860
Q21131552-1C099D35-77A2-4523-9DFA-F16E25CC8262Q21142643-27676927-8B76-4627-B599-913FFC6479A1Q22001534-AAD706F2-E2AF-4EDD-9F19-9618AD418DF0Q24304497-C6EA3C4E-BA3D-4E03-AD85-FB9B824AEAA3Q24336442-6DA047DF-29F5-4869-99F2-D83EFA2034D2Q24642649-B8F49E01-425F-4982-AC05-7BF74A4B3418Q24647624-AC334BD4-4226-4477-B5EC-41570742CAEAQ26750857-D0F155DA-D987-4FBF-9704-468869E0A57AQ26766507-229282B4-FC7B-4E5A-9440-4B9A3D78C4D2Q26771364-C72739AE-7FDE-44B3-A14A-AF9BAA2B2A4BQ26863733-92E1D051-FC5B-49A9-A42A-AF50C7773D4EQ27025593-C64341C3-2889-4ABE-9120-87DE0E48EC6EQ27345035-3587C9E3-DB2B-4CCF-ABC2-5715D6F3BF5EQ27658641-E9E90B19-F59D-4B52-BD7B-8852409A1100Q27664409-B7CD50DA-05EB-4B5E-9BB5-393CE95D33E5Q27665390-44F67284-C89F-47AA-855C-19FCD02E4BF7Q27678298-DAA8ACC7-7506-45AA-B22D-78DD5CC69AA0Q27678625-449D6826-07B5-40B5-AE5E-DD5300B19210Q27680640-07CB21B4-28FE-4C7F-82A1-EAC56F74578CQ27684624-2C5CDCD7-9E85-4293-8675-4AACF06FA9BEQ27687005-13097B14-E925-48F7-AACA-C643B78CC0A4Q27695047-66050361-AA16-4840-B0D5-B42E76AE78FFQ28118367-4AF8D57A-FBEB-46FE-A68D-0EC0867812D5Q28486903-977F1170-B28C-4B04-89F4-30203C1BB3BEQ28548314-78E78136-F335-45BF-A91D-8167D92D9CA5Q29248184-D277EDC1-4AA7-4BAB-ADAE-8802623B7A5DQ30422755-E60BA3F2-F0BF-4DB9-B822-8BAE7DB44A53Q33769572-A16E6D15-04E0-4915-AC48-419E0A0819E4Q33877120-FA252CFD-29C3-4039-8F8E-9CEF1AFD4CD4Q34277039-6AE69692-180A-4295-A40E-31C247DA0566Q34390259-ACAF59FE-EB13-4CDE-A9BF-D63971E650A7Q34395262-0A164572-9A9D-40F3-B126-5D064DC9838BQ34407723-A7C1D0B2-098C-48C4-8ECE-CE982D4E6CF3Q34411597-DA0069C5-033C-4BE9-8471-900B457715F9Q34593329-363CDDD8-7BE3-4A26-A13B-B82A8FCF4391Q34612233-CE5E6D99-43EE-4F02-9E4D-88BB2620C4FBQ34634239-C5F93C89-26B2-4A2A-9811-AE4531E9FEC7Q34765284-F3044FA9-DBAD-47FD-B55F-FCEDFF07E031Q34818305-9D6846BA-9D5D-4AED-B491-616CA29D1B3FQ35212971-8135572C-9F82-4FA7-ACB8-6FAF18F58838
P2860
Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases
description
2008 nî lūn-bûn
@nan
2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases
@ast
Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases
@en
Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases
@nl
type
label
Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases
@ast
Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases
@en
Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases
@nl
prefLabel
Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases
@ast
Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases
@en
Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases
@nl
P2093
P2860
P50
P356
P1476
Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases
@en
P2093
Alexander U Singer
Claude Parsot
John R Rohde
Marianne E Cuff
Mike Tyers
Nickolay Y Chirgadze
Olga Kagan
Philippe J Sansonetti
Robert Lam
Rosa Dileo
P2860
P2888
P304
P356
10.1038/NSMB.1511
P577
2008-12-01T00:00:00Z
P5875
P6179
1018948760