Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases - Wikidata - awgldk - TriplyDB

Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases

Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases

http://www.wikidata.org/entity/Q27652850

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NleG Type 3 effectors from enterohaemorrhagic Escherichia coli are U-Box E3 ubiquitin ligases Atomic interaction networks in the core of protein domains and their native folds A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response The Salmonella type III secretion effector, salmonella leucine-rich repeat protein (SlrP), targets the human chaperone ERdj3 Salmonella type III secretion effector SlrP is an E3 ubiquitin ligase for mammalian thioredoxin A family of Salmonella virulence factors functions as a distinct class of autoregulated E3 ubiquitin ligases Hijacking the host ubiquitin pathway: structural strategies of bacterial E3 ubiquitin ligases Implications of Spatiotemporal Regulation of Shigella flexneri Type Three Secretion Activity on Effector Functions: Think Globally, Act Locally Bacteria-host relationship: ubiquitin ligases as weapons of invasion Shigella IpaH Family Effectors as a Versatile Model for Studying Pathogenic Bacteria Bacterial effectors and their functions in the ubiquitin-proteasome system: insight from the modes of substrate recognition Epigenetics and bacterial infections GogB is an anti-inflammatory effector that limits tissue damage during Salmonella infection through interaction with human FBXO22 and Skp1 A Structural Element within the HUWE1 HECT Domain Modulates Self-ubiquitination and Substrate Ubiquitination Activities A disulfide driven domain swap switches off the activity of Shigella IpaH9.8 E3 ligase Biochemical and Structural Studies of a HECT-like Ubiquitin Ligase from Escherichia coli O157:H7 Structure of HHARI, a RING-IBR-RING Ubiquitin Ligase: Autoinhibition of an Ariadne-Family E3 and Insights into Ligation Mechanism Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases Structure of an SspH1-PKN1 Complex Reveals the Basis for Host Substrate Recognition and Mechanism of Activation for a Bacterial E3 Ubiquitin Ligase The 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 family Identification of an unconventional E3 binding surface on the UbcH5 ~ Ub conjugate recognized by a pathogenic bacterial E3 ligase Complex structure of OspI and Ubc13: the molecular basis of Ubc13 deamidation and convergence of bacterial and host E2 recognition Structure of the Legionella Virulence Factor, SidC Reveals a Unique PI(4)P-Specific Binding Domain Essential for Its Targeting to the Bacterial Phagosome The Yersinia Type III secretion effector YopM Is an E3 ubiquitin ligase that induced necrotic cell death by targeting NLRP3 A 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 virulence Functional 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 ligase Shigella 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.

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P2860

Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases

http://www.wikidata.org/entity/Q27652850

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

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2008年論文

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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

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Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases

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type

label

Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases

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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

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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

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Nature Structural & Molecular Biology

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Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases

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P2093

Alexander U Singer

http://www.w3.org/2001/XMLSchema#string

Claude Parsot

http://www.w3.org/2001/XMLSchema#string

John R Rohde

http://www.w3.org/2001/XMLSchema#string

Marianne E Cuff

http://www.w3.org/2001/XMLSchema#string

Mike Tyers

http://www.w3.org/2001/XMLSchema#string

Nickolay Y Chirgadze

http://www.w3.org/2001/XMLSchema#string

Olga Kagan

http://www.w3.org/2001/XMLSchema#string

Philippe J Sansonetti

http://www.w3.org/2001/XMLSchema#string

Robert Lam

http://www.w3.org/2001/XMLSchema#string

Rosa Dileo

http://www.w3.org/2001/XMLSchema#string

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Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase

An altered-specificity ubiquitin-conjugating enzyme/ubiquitin-protein ligase pair

Structure of Thermotoga maritima stationary phase survival protein SurE: a novel acid phosphatase

PROCHECK: a program to check the stereochemical quality of protein structures

Crystal structure of SopA, a Salmonella effector protein mimicking a eukaryotic ubiquitin ligase

Use of TLS parameters to model anisotropic displacements in macromolecular refinement

HKL-3000: the integration of data reduction and structure solution--from diffraction images to an initial model in minutes

Coot: model-building tools for molecular graphics

Automated protein model building combined with iterative structure refinement

Macromolecular TLS refinement in REFMAC at moderate resolutions

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1293-301

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10.1038/NSMB.1511

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12

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15

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Andrzej Joachimiak

Tatiana Skarina

Alexei Savchenko

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2008-12-01T00:00:00Z

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23462293

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1018948760

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18997778

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structural biology

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2764551

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