Mechanism of mda-5 Inhibition by paramyxovirus V proteins. - Wikidata - awgldk - TriplyDB

Mechanism of mda-5 Inhibition by paramyxovirus V proteins.

Mechanism of mda-5 Inhibition by paramyxovirus V proteins.

http://www.wikidata.org/entity/Q39914626

about

Herpes simplex virus 1 tegument protein US11 downmodulates the RLR signaling pathway via direct interaction with RIG-I and MDA-5 A shared interface mediates paramyxovirus interference with antiviral RNA helicases MDA5 and LGP2 The measles virus V protein binds to p65 (RelA) to suppress NF-kappaB activity Paramyxovirus V proteins interact with the RNA Helicase LGP2 to inhibit RIG-I-dependent interferon induction TLR3-dependent upregulation of RIG-I leads to enhanced cytokine production from cells infected with the parainfluenza virus SV5 MDA5 cooperatively forms dimers and ATP-sensitive filaments upon binding double-stranded RNA Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling The Immune Response in Measles: Virus Control, Clearance and Protective Immunity RIG-I in RNA virus recognition Interferons and viruses: an evolutionary arms race of molecular interactions Viral evasion of intracellular DNA and RNA sensing Negative regulation of interferon-β gene expression during acute and persistent virus infections Induction of type I interferon by RNA viruses: cellular receptors and their substrates Human parainfluenza virus type 2 V protein inhibits interferon production and signaling and is required for replication in non-human primates.Identification of DNA-damage DNA-binding protein 1 as a conditional essential factor for cytomegalovirus replication in interferon-γ-stimulated cells.Measles virus-induced suppression of immune responses.Dissociation of paramyxovirus interferon evasion activities: universal and virus-specific requirements for conserved V protein amino acids in MDA5 interference.Interplay between innate immunity and negative-strand RNA viruses: towards a rational model Distinct and overlapping roles of Nipah virus P gene products in modulating the human endothelial cell antiviral response.The V protein of Tioman virus is incapable of blocking type I interferon signaling in human cells.LGP2 plays a critical role in sensitizing mda-5 to activation by double-stranded RNA Targeting viral dsRNA for antiviral prophylaxis.Identification of human parainfluenza virus type 2 (HPIV-2) V protein amino acid residues that reduce binding of V to MDA5 and attenuate HPIV-2 replication in nonhuman primates Functions of the cytoplasmic RNA sensors RIG-I and MDA-5: key regulators of innate immunity.Antagonism of innate immunity by paramyxovirus accessory proteins.Henipaviruses employ a multifaceted approach to evade the antiviral interferon response.Proteomic analysis of virus-host interactions in an infectious context using recombinant viruses.Measles virus, immune control, and persistence.A correlation of measles specific antibodies and the number of plasmacytoid dendritic cells is observed after measles vaccination in 9 month old infants.Inhibition of interferon regulatory factor 3 activation by paramyxovirus V protein.Middle East respiratory syndrome coronavirus ORF4b protein inhibits type I interferon production through both cytoplasmic and nuclear targets.Control of the induction of type I interferon by Peste des petits ruminants virus.Type I interferons: diversity of sources, production pathways and effects on immune responses.Parainfluenza Virus 3 Blocks Antiviral Mediators Downstream of the Interferon Lambda Receptor by Modulating Stat1 Phosphorylation Deep sequencing analysis of defective genomes of parainfluenza virus 5 and their role in interferon induction Decreased SARI expression predicts poor prognosis of Chinese patients with non-small cell lung cancer.Similarities and differences in antagonism of neuron alpha/beta interferon responses by Venezuelan equine encephalitis and Sindbis alphaviruses.Differential cellular immune responses to wild-type and attenuated edmonston tag measles virus strains are primarily defined by the viral phosphoprotein gene.The regulation of type I interferon production by paramyxoviruses.Paramyxovirus activation and inhibition of innate immune responses.

P2860

Q24304261-3CF07669-0F5F-4238-98F8-CFCB83768892 Q24320094-5B5BB424-3481-4A3E-ABAF-4D277143D2F5 Q24338483-E9A4E323-2718-4280-9ACF-646A25C20C77 Q24617419-38A25794-72F2-4E4E-B61E-955D6B07735A Q27490869-77A2D707-83E8-47FE-9814-63761225E27C Q27677137-6CA72CFC-D860-4531-A874-D161BAB5BA9C Q27683783-4AD66050-0FA6-45A3-BE1B-6B9121D66847 Q28074714-1F278C5A-0DA2-457B-B440-34C46DCC3A8D Q28081618-1C7F82A8-8DD6-4D08-9035-3A76D1B0C4B5 Q28083788-383D9FF3-4E83-494E-8402-5229083BB0DF Q28392078-0155A769-505E-41C6-A708-6D94B15FAF37 Q28478468-01299B62-8C30-4C35-80C8-7ADCF86359B8 Q29042349-62E7DCAA-18C8-42F5-8C80-27FC8DCF005E Q33653692-437DA3A5-9C04-45B3-AF63-14C731651D70 Q33941023-9B881120-6C41-488C-B2DE-5BD2456E930D Q34015320-4289B912-A7DE-48DC-B4EE-B6C865DC5F02 Q34190615-6600732B-96C0-403F-806B-83252271F230 Q34212787-C2EA4D05-A2AF-4C2A-867C-54CFF1F988FF Q34456557-5DA5ED04-9D65-4682-8A18-67C7545623F0 Q34558886-B9EEF3D9-12E8-408F-A74A-4730724CEB1A Q34721341-BFF9F31D-B0DD-4491-96A8-43733F15A8CF Q34813401-7AB5DF75-5E2C-4579-860E-33923CA7C13D Q35076577-3F76B502-EDD1-4314-9140-4BA0BD3A0C07 Q35190533-E30B4339-25BF-42CE-A1A9-BD77DAD3E15A Q35259962-A29395A6-5F36-4695-B946-B19F5CC41B24 Q35260006-798BCC08-6167-4E6D-BF45-ECD1A3CCF8B5 Q35610639-FC65FC0A-33CB-43C1-BBD3-6CA305196E78 Q35870777-78CA3F56-CA50-471D-B8A0-8978CC25C6B3 Q35886800-2EB1710A-95A4-4097-ACA7-F73878135A70 Q36155618-9663A81F-DDBA-4E07-842D-B062BBF7C015 Q36343316-CAE43664-24CE-4A2B-9531-AE69664A59B5 Q36364287-1E4D1F0B-BE37-47AF-BADC-AFDAC77190A7 Q36611339-1A283DC2-A5AD-4E27-8704-5770A2678315 Q36736583-25A1D1C9-97DA-4D16-8A4D-CBBF6D50FBDE Q36759987-CE18DD5F-7289-4309-96AA-BD219BD00548 Q37228817-732B03A7-5268-426B-B0D7-BE117AC9B7C8 Q37356071-7BCAE645-EF69-42D2-A2BB-00F5D6C9DD62 Q37583896-6E1DBAA0-91B2-4BF7-AEC9-90DCA4DF41B3 Q37585325-02E683D7-A6CF-477D-A0C2-C58445AD32C5 Q37613401-B582405A-8426-4CE5-B37F-A0D01B5666EA

P2860

Mechanism of mda-5 Inhibition by paramyxovirus V proteins.

http://www.wikidata.org/entity/Q39914626

description

2008 nî lūn-bûn

@nan

2008年の論文

@ja

2008年学术文章

@wuu

2008年学术文章

@zh-cn

2008年学术文章

@zh-hans

2008年学术文章

@zh-my

2008年学术文章

@zh-sg

2008年學術文章

@yue

2008年學術文章

@zh

2008年學術文章

@zh-hant

name

Mechanism of mda-5 Inhibition by paramyxovirus V proteins.

@en

Mechanism of mda-5 Inhibition by paramyxovirus V proteins.

@nl

type

label

Mechanism of mda-5 Inhibition by paramyxovirus V proteins.

@en

Mechanism of mda-5 Inhibition by paramyxovirus V proteins.

@nl

prefLabel

Mechanism of mda-5 Inhibition by paramyxovirus V proteins.

@en

Mechanism of mda-5 Inhibition by paramyxovirus V proteins.

@nl

P1433

Q39914626-8580221C-1D6A-4315-A854-8B43FF73FE55

P1476

Q39914626-3CF67FC3-B708-4079-8B48-F36CE9571A6B

P2093

Q39914626-7356DE0A-C7F0-42A1-853B-49AB566ED762

Q39914626-A542EBDF-E838-4BBE-A3E5-9F04585AAA01

P2860

Q39914626-080EBF8D-BB03-4E35-9B46-DAD7DED87987

Q39914626-0CBC482D-7A5A-4A62-BB42-32D2C16D7B42

Q39914626-0D590902-DF81-4776-837A-8CFA0A0713A5

Q39914626-11A1EE85-324C-47C8-9ADF-8FC7B17B8B6B

Q39914626-1494857F-D615-446A-9E36-FA9A83781674

Q39914626-1697B215-F1D8-4E73-BB1A-1F075F32E6DC

Q39914626-17AB9B5B-C9F8-4B7D-BFEB-61D4A6BA3FD1

Q39914626-19E48B9A-98B1-4843-ABC7-4FE8592C5303

Q39914626-1AFB7921-44B1-46F8-9F2B-27B53829A35B

Q39914626-39B93D13-1352-49B7-B12B-8AD0EDC739AA

P304

Q39914626-4983A262-682B-4C97-9653-BAF694344C31

P31

Q39914626-BB15E482-A61F-41DF-8E1B-DAE67E8675B1

P356

Q39914626-06ECE455-E8EA-406A-BD79-25F4E0C2CD23

P407

Q39914626-74FA2B65-0228-4590-86FA-99BB9EFAAE65

P433

Q39914626-CD2F9CB8-3C78-41B4-A9EF-3DBB2E343F9D

P478

Q39914626-78E9A97A-3F12-41AE-9349-87D7BEE42B5B

P50

Q39914626-286E5B11-A3C7-4B25-BDB6-FD0D8376B1F9

Q39914626-F48E2C2C-FD15-47ED-90E4-CE29CD564EA5

P577

Q39914626-236761AD-CD12-49B9-80A9-7590BE002A9E

P5875

Q39914626-DEAA9AE0-C4B0-44D4-8FC2-8D77EFFAA748

P698

Q39914626-F2EB49D9-A95E-4815-BC21-1667AC4A39AD

P921

Q39914626-CE15BBA1-DA0E-4655-8063-914FDD20717B

P932

Q39914626-AF89E85D-E8A4-44C2-8F4B-5810FF25485A

P356

P1433

Journal of Virology

P1476

Mechanism of mda-5 Inhibition by paramyxovirus V proteins

@en

P2093

J Andrejeva

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

K S Childs

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

P2860

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

Identification of double-stranded RNA-binding domains in the interferon-induced double-stranded RNA-activated p68 kinase

Regulation of innate antiviral defenses through a shared repressor domain in RIG-I and LGP2

The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the IFN-beta promoter

Innate immunity induced by composition-dependent RIG-I recognition of hepatitis C virus RNA

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

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

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

Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses

The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses

P304

1465-1473

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

P31

scholarly article

P356

10.1128/JVI.01768-08

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

P407

P433

3

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

P478

83

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

P50

Richard E Randall

Stephen Goodbourn

P577

2008-11-19T00:00:00Z

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

P5875

23484034

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

P698

19019954

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

P921

P932

2620892

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