Kinetic mechanism for viral dsRNA length discrimination by MDA5 filaments - Wikidata - awgldk - TriplyDB

Kinetic mechanism for viral dsRNA length discrimination by MDA5 filaments

Kinetic mechanism for viral dsRNA length discrimination by MDA5 filaments

http://www.wikidata.org/entity/Q36471292

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Regulation of antiviral innate immune signaling by stress-induced RNA granules Ubiquitin in the activation and attenuation of innate antiviral immunity ADAR1, inosine and the immune sensing system: distinguishing self from non-self MDA5 and LGP2: accomplices and antagonists of antiviral signal transduction RNAs Containing Modified Nucleotides Fail To Trigger RIG-I Conformational Changes for Innate Immune Signaling mRNA capping: biological functions and applications Structural basis for Z-DNA binding and stabilization by the zebrafish Z-DNA dependent protein kinase PKZ 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 Assembly-driven activation of the AIM2 foreign-dsDNA sensor provides a polymerization template for downstream ASC Evaluation of fluorophores to label SNAP-tag fused proteins for multicolor single-molecule tracking microscopy in live cells.The innate immune sensor LGP2 activates antiviral signaling by regulating MDA5-RNA interaction and filament assembly.Kinetic discrimination of self/non-self RNA by the ATPase activity of RIG-I and MDA5 MDA5-filament, dynamics and disease.De Novo Transcriptome Analysis Shows That SAV-3 Infection Upregulates Pattern Recognition Receptors of the Endosomal Toll-Like and RIG-I-Like Receptor Signaling Pathways in Macrophage/Dendritic Like TO-Cells.Cooperative assembly of IFI16 filaments on dsDNA provides insights into host defense strategy.When your cap matters: structural insights into self vs non-self recognition of 5' RNA by immunomodulatory host proteins.Identification of an LGP2-associated MDA5 agonist in picornavirus-infected cells.USP3 inhibits type I interferon signaling by deubiquitinating RIG-I-like receptors.Gain-of-function mutations in IFIH1 cause a spectrum of human disease phenotypes associated with upregulated type I interferon signaling.Toward a crystal-clear view of the viral RNA sensing and response by RIG-I-like receptors.Antiviral RNA recognition and assembly by RLR family innate immune sensors.Pattern Recognition and Signaling Mechanisms of RIG-I and MDA5 Effects of type 1 diabetes-associated IFIH1 polymorphisms on MDA5 function and expression.Helicases in Antiviral Immunity: Dual Properties as Sensors and Effectors.Dicer-related helicase 3 forms an obligate dimer for recognizing 22G-RNA.Filament assemblies in foreign nucleic acid sensors.The role of RNA editing by ADAR1 in prevention of innate immune sensing of self-RNA.ATP-dependent effector-like functions of RIG-I-like receptors.Adenosine-to-inosine RNA editing by ADAR1 is essential for normal murine erythropoiesis.MDA5-Associated Neuroinflammation and the Singleton-Merten Syndrome: Two Faces of the Same Type I Interferonopathy Spectrum.Protein recoding by ADAR1-mediated RNA editing is not essential for normal development and homeostasis.High-resolution HDX-MS reveals distinct mechanisms of RNA recognition and activation by RIG-I and MDA5.Viral counterattack against the host innate immune system Breaching Self-Tolerance to Alu Duplex RNA Underlies MDA5-Mediated Inflammation.DHX29 functions as an RNA co-sensor for MDA5-mediated EMCV-specific antiviral immunity.Understanding Viral dsRNA-Mediated Innate Immune Responses at the Cellular Level Using a Rainbow Trout Model.RIG-I-Like Receptors as Novel Targets for Pan-Antivirals and Vaccine Adjuvants Against Emerging and Re-Emerging Viral Infections.

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P2860

Kinetic mechanism for viral dsRNA length discrimination by MDA5 filaments

http://www.wikidata.org/entity/Q36471292

description

2012 nî lūn-bûn

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2012年の論文

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年學術文章

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2012年學術文章

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2012年學術文章

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name

Kinetic mechanism for viral dsRNA length discrimination by MDA5 filaments

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Kinetic mechanism for viral dsRNA length discrimination by MDA5 filaments

@en

type

label

Kinetic mechanism for viral dsRNA length discrimination by MDA5 filaments

@ast

Kinetic mechanism for viral dsRNA length discrimination by MDA5 filaments

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prefLabel

Kinetic mechanism for viral dsRNA length discrimination by MDA5 filaments

@ast

Kinetic mechanism for viral dsRNA length discrimination by MDA5 filaments

@en

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PNAS.1208618109

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Kinetic mechanism for viral dsRNA length discrimination by MDA5 filaments

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P2093

Alys Peisley

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

Bin Wu

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

Cecilie Lin

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McGhee Orme-Johnson

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

Myung Hyun Jo

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

Sun Hur

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

Sungchul Hohng

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

Thomas Walz

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P2860

The C-terminal regulatory domain is the RNA 5'-triphosphate sensor of RIG-I

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

Kinetic proofreading: a new mechanism for reducing errors in biosynthetic processes requiring high specificity

Length-dependent recognition of double-stranded ribonucleic acids by retinoic acid-inducible gene-I and melanoma differentiation-associated gene 5

Negative staining and image classification — powerful tools in modern electron microscopy

Widespread A-to-I RNA editing of Alu-containing mRNAs in the human transcriptome

Nonself RNA-sensing mechanism of RIG-I helicase and activation of antiviral immune responses

Structural and functional insights into 5′-ppp RNA pattern recognition by the innate immune receptor RIG-I

The Structural Basis of 5′ Triphosphate Double-Stranded RNA Recognition by RIG-I C-Terminal Domain

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10.1073/PNAS.1208618109

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49

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109

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2012-11-05T00:00:00Z

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232920410

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23129641

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3523859

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