Structural basis for the prion-like MAVS filaments in antiviral innate immunity - Wikidata - thesis-toulmin - TriplyDB

Structural basis for the prion-like MAVS filaments in antiviral innate immunity

Structural basis for the prion-like MAVS filaments in antiviral innate immunity

http://www.wikidata.org/entity/Q27681906

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Confocal Spectroscopy to Study Dimerization, Oligomerization and Aggregation of Proteins: A Practical Guide Regulation of antiviral innate immune signaling by stress-induced RNA granules DED or alive: assembly and regulation of the death effector domain complexes Prion-like polymerization as a signaling mechanism Structural plasticity of helical nanotubes based on coiled-coil assemblies Molecular imprinting as a signal-activation mechanism of the viral RNA sensor RIG-I.LGP2 synergy with MDA5 in RLR-mediated RNA recognition and antiviral signaling An Internally Translated MAVS Variant Exposes Its Amino-terminal TRAF-Binding Motifs to Deregulate Interferon Induction Engagement of nucleotide-binding oligomerization domain-containing protein 1 (NOD1) by receptor-interacting protein 2 (RIP2) is insufficient for signal transduction Structural basis for host membrane remodeling induced by protein 2B of hepatitis A virus Mechanism of TRIM25 Catalytic Activation in the Antiviral RIG-I Pathway.Three-dimensional reconstruction of helical polymers.Near-atomic resolution for one state of F-actin.Ambiguities in helical reconstruction.Structure determination of helical filaments by solid-state NMR spectroscopy Superresolution Imaging Identifies That Conventional Trafficking Pathways Are Not Essential for Endoplasmic Reticulum to Outer Mitochondrial Membrane Protein Transport PB1-F2 attenuates virulence of highly pathogenic avian H5N1 influenza virus in chickens.The innate immune sensor LGP2 activates antiviral signaling by regulating MDA5-RNA interaction and filament assembly.SMOCs: supramolecular organizing centres that control innate immunity.Superresolution imaging of viral protein trafficking.Structural and functional analysis reveals that human OASL binds dsRNA to enhance RIG-I signaling Structural Insights into mitochondrial antiviral signaling protein (MAVS)-tumor necrosis factor receptor-associated factor 6 (TRAF6) signaling.ATP hydrolysis by the viral RNA sensor RIG-I prevents unintentional recognition of self-RNA.Supramolecular organizing centers (SMOCs) as signaling machines in innate immune activation.Higher-order oligomerization promotes localization of SPOP to liquid nuclear speckles.ASC filament formation serves as a signal amplification mechanism for inflammasomes The mitochondrial ubiquitin ligase MARCH5 resolves MAVS aggregates during antiviral signalling.Intracellular detection of viral nucleic acids.Mitochondrial dynamics and the innate antiviral immune response.Antiviral RNA recognition and assembly by RLR family innate immune sensors.Pattern Recognition and Signaling Mechanisms of RIG-I and MDA5 Prions and Protein Assemblies that Convey Biological Information in Health and Disease.How RIG-I like receptors activate MAVS.CARMA3 Is a Host Factor Regulating the Balance of Inflammatory and Antiviral Responses against Viral Infection.Prion-Like Polymerization in Immunity and Inflammation.Dynasore enhances the formation of mitochondrial antiviral signalling aggregates and endocytosis-independent NF-κB activation A Novel Mechanism Underlying the Innate Immune Response Induction upon Viral-Dependent Replication of Host Cell mRNA: A Mistake of +sRNA Viruses' Replicases.Prion-like proteins and their computational identification in proteomes.ArfGAP Domain-Containing Protein 2 (ADAP2) Integrates Upstream and Downstream Modules of RIG-I Signaling and Facilitates Type I Interferon Production.Reactive oxygen species induce virus-independent MAVS oligomerization in systemic lupus erythematosus

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Structural basis for the prion-like MAVS filaments in antiviral innate immunity

http://www.wikidata.org/entity/Q27681906

description

2014 nî lūn-bûn

@nan

2014 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի հունվարին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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name

Structural basis for the prion-like MAVS filaments in antiviral innate immunity

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Structural basis for the prion-like MAVS filaments in antiviral innate immunity

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Structural basis for the prion-like MAVS filaments in antiviral innate immunity

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label

Structural basis for the prion-like MAVS filaments in antiviral innate immunity

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Structural basis for the prion-like MAVS filaments in antiviral innate immunity

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Structural basis for the prion-like MAVS filaments in antiviral innate immunity

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Correction: Structural basis f ...... s in antiviral innate immunity

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Structural basis for the prion-like MAVS filaments in antiviral innate immunity

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Structural basis for the prion-like MAVS filaments in antiviral innate immunity

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Structural basis for the prion-like MAVS filaments in antiviral innate immunity

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Structural basis for the prion-like MAVS filaments in antiviral innate immunity

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MAVS recruits multiple ubiquitin E3 ligases to activate antiviral signaling cascades

Mitochondrial dynamics regulate the RIG-I-like receptor antiviral pathway

Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity

Recognition of 5' triphosphate by RIG-I helicase requires short blunt double-stranded RNA as contained in panhandle of negative-strand virus.

MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response

IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction

Structure and function of LGP2, a DEX(D/H) helicase that regulates the innate immunity response

Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus

What the Myddosome structure tells us about the initiation of innate immunity

Structure of the cross-beta spine of amyloid-like fibrils

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10.7554/ELIFE.01489

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Michael Jason de la Cruz

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2014-01-01T00:00:00Z

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24569476

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Prion protein family

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3932521

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