Structural basis for dsRNA recognition and interferon antagonism by Ebola VP35 - Test2 - elhamkhani - TriplyDB

Structural basis for dsRNA recognition and interferon antagonism by Ebola VP35

Structural basis for dsRNA recognition and interferon antagonism by Ebola VP35

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Characterization of uncultivable bat influenza virus using a replicative synthetic virus Unexpected inheritance: multiple integrations of ancient bornavirus and ebolavirus/marburgvirus sequences in vertebrate genomes Filoviral immune evasion mechanisms DRBP76 associates with Ebola virus VP35 and suppresses viral polymerase function Mutual antagonism between the Ebola virus VP35 protein and the RIG-I activator PACT determines infection outcome Evolutionary maintenance of filovirus-like genes in bat genomes Addressing Therapeutic Options for Ebola Virus Infection in Current and Future Outbreaks Mutations Abrogating VP35 Interaction with Double-Stranded RNA Render Ebola Virus Avirulent in Guinea Pigs Structural and Functional Characterization of Reston Ebola Virus VP35 Interferon Inhibitory Domain Structural and functional insights into 5′-ppp RNA pattern recognition by the innate immune receptor RIG-I Structure of the Lassa virus nucleoprotein reveals a dsRNA-specific 3' to 5' exonuclease activity essential for immune suppression Structural implications into dsRNA binding and RNA silencing suppression by NS3 protein of Rice Hoja Blanca Tenuivirus Marburg Virus VP35 Can Both Fully Coat the Backbone and Cap the Ends of dsRNA for Interferon Antagonism Structural basis for Marburg virus VP35-mediated immune evasion mechanisms The Ebola Virus Interferon Antagonist VP24 Directly Binds STAT1 and Has a Novel, Pyramidal Fold Structure of the C-Terminal Domain of Lettuce Necrotic Yellows Virus Phosphoprotein Ebolavirus VP35 Coats the Backbone of Double-Stranded RNA for Interferon Antagonism Development of RNA Aptamers Targeting Ebola Virus VP35 Rescue of non-human primates from advanced Sudan ebolavirus infection with lipid encapsulated siRNA The structure of the C-terminal domain of the Zaire ebolavirus nucleoprotein Ebolavirus is evolving but not changing: No evidence for functional change in EBOV from 1976 to the 2014 outbreak.Investigating Engineered Ribonucleoprotein Particles to Improve Oral RNAi Delivery in Crop Insect Pests.Crystallization and preliminary X-ray analysis of Ebola VP35 interferon inhibitory domain mutant proteins Recognition of virus infection and innate host responses to viral gene therapy vectors.HepG2 cells mount an effective antiviral interferon-lambda based innate immune response to hepatitis C virus infection.Molecular mechanisms of viral inhibitors of RIG-I-like receptors.Hiding the evidence: two strategies for innate immune evasion by hemorrhagic fever viruses.How Ebola virus counters the interferon system.Camouflage and misdirection: the full-on assault of ebola virus disease An upstream open reading frame modulates ebola virus polymerase translation and virus replication.Ebolavirus VP35 is a multifunctional virulence factor.Ebolavirus proteins suppress the effects of small interfering RNA by direct interaction with the mammalian RNA interference pathway.Marburg virus VP40 antagonizes interferon signaling in a species-specific manner.Ebola virus failure to stimulate plasmacytoid dendritic cell interferon responses correlates with impaired cellular entry.Innate immune evasion by filoviruses The role of antigen-presenting cells in filoviral hemorrhagic fever: gaps in current knowledge.Assembly of the Ebola Virus Nucleoprotein from a Chaperoned VP35 Complex Different Temporal Effects of Ebola Virus VP35 and VP24 Proteins on Global Gene Expression in Human Dendritic Cells.Assessing the contribution of interferon antagonism to the virulence of West African Ebola viruses Amino Acid Residue at Position 79 of Marburg Virus VP40 Confers Interferon Antagonism in Mouse Cells.

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Structural basis for dsRNA recognition and interferon antagonism by Ebola VP35

http://www.wikidata.org/entity/Q27659023

description

2010 nî lūn-bûn

@nan

2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

@zh-mo

2010年論文

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2010年论文

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name

Structural basis for dsRNA recognition and interferon antagonism by Ebola VP35

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Structural basis for dsRNA recognition and interferon antagonism by Ebola VP35

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Structural basis for dsRNA recognition and interferon antagonism by Ebola VP35

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type

label

Structural basis for dsRNA recognition and interferon antagonism by Ebola VP35

@ast

Structural basis for dsRNA recognition and interferon antagonism by Ebola VP35

@en

Structural basis for dsRNA recognition and interferon antagonism by Ebola VP35

@nl

prefLabel

Structural basis for dsRNA recognition and interferon antagonism by Ebola VP35

@ast

Structural basis for dsRNA recognition and interferon antagonism by Ebola VP35

@en

Structural basis for dsRNA recognition and interferon antagonism by Ebola VP35

@nl

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Nature Structural & Molecular Biology

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Structural basis for dsRNA recognition and interferon antagonism by Ebola VP35

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Daisy W Leung

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

Jay C Nix

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

JoAnn M Tufariello

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Kathleen C Prins

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Luke A Helgeson

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Mina Farahbakhsh

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Parameshwaran Ramanan

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

Richard B Honzatko

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

P2860

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

Solution structures of cytosolic RNA sensor MDA5 and LGP2 C-terminal domains: identification of the RNA recognition loop in RIG-I-like receptors

Ebola virus protein VP35 impairs the function of interferon regulatory factor-activating kinases IKKepsilon and TBK-1

The RIG-I-like receptor LGP2 recognizes the termini of double-stranded RNA

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

Structural basis of double-stranded RNA recognition by the RIG-I like receptor MDA5

5'-triphosphate RNA requires base-paired structures to activate antiviral signaling via RIG-I

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

Processing of Genome 5′ Termini as a Strategy of Negative-Strand RNA Viruses to Avoid RIG-I-Dependent Interferon Induction

Structure of the Ebola VP35 interferon inhibitory domain

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165-72

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10.1038/NSMB.1765

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2

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17

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Gaya K. Amarasinghe

Christopher F Basler

Zbyszek Otwinowski

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2010-02-01T00:00:00Z

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41041521

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1008066588

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20081868

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structural biology

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2872155

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