Agonist and Antagonist Recognition by RIG-I, a Cytoplasmic Innate Immunity Receptor - Test2 - elhamkhani - TriplyDB

Agonist and Antagonist Recognition by RIG-I, a Cytoplasmic Innate Immunity Receptor

Agonist and Antagonist Recognition by RIG-I, a Cytoplasmic Innate Immunity Receptor

http://www.wikidata.org/entity/Q27487543

about

Immune signaling by RIG-I-like receptors The RIG-I-like receptor LGP2 recognizes the termini of double-stranded RNA 5'-triphosphate RNA requires base-paired structures to activate antiviral signaling via RIG-I Nucleotide Sequences and Modifications That Determine RIG-I/RNA Binding and Signaling Activities The Structural Basis of 5′ Triphosphate Double-Stranded RNA Recognition by RIG-I C-Terminal Domain MDA5 cooperatively forms dimers and ATP-sensitive filaments upon binding double-stranded RNA Lateral Clustering of TLR3:dsRNA Signaling Units Revealed by TLR3ecd:3Fabs Quaternary Structure Structural basis for the prion-like MAVS filaments in antiviral innate immunity Green tea catechin, epigallocatechin gallate, suppresses signaling by the dsRNA innate immune receptor RIG-I A cell-based assay for RNA synthesis by the HCV polymerase reveals new insights on mechanism of polymerase inhibitors and modulation by NS5A LL37 and cationic peptides enhance TLR3 signaling by viral double-stranded RNAs Induction of type I interferon by RNA viruses: cellular receptors and their substrates RETRACTED: Norovirus RNA synthesis is modulated by an interaction between the viral RNA-dependent RNA polymerase and the major capsid protein, VP1.Effects of chemical modification on the potency, serum stability, and immunostimulatory properties of short shRNAs.Hepatitis C virus nonstructural protein 5A: biochemical characterization of a novel structural class of RNA-binding proteins Poly-thymidine oligonucleotides mediate activation of murine glial cells primarily through TLR7, not TLR8.Preference of RIG-I for short viral RNA molecules in infected cells revealed by next-generation sequencing.Interplay between innate immunity and negative-strand RNA viruses: towards a rational model Conformational rearrangements of RIG-I receptor on formation of a multiprotein:dsRNA assembly.Functional characterizations of RIG-I to GCRV and viral/bacterial PAMPs in grass carp Ctenopharyngodon idella.Sensing of viral nucleic acids by RIG-I: from translocation to translation RIG-I self-oligomerization is either dispensable or very transient for signal transduction.Induction and evasion of type I interferon responses by influenza viruses.Duplex RNA activated ATPases (DRAs): platforms for RNA sensing, signaling and processing.RNA synthesis by the brome mosaic virus RNA-dependent RNA polymerase in human cells reveals requirements for de novo initiation and protein-protein interaction.Dependence of RIG-I Nucleic Acid-Binding and ATP Hydrolysis on Activation of Type I Interferon Response.Early innate recognition of herpes simplex virus in human primary macrophages is mediated via the MDA5/MAVS-dependent and MDA5/MAVS/RNA polymerase III-independent pathways The RIG-I ATPase core has evolved a functional requirement for allosteric stabilization by the Pincer domain.RIGorous detection: exposing virus through RNA sensing.

P2860

Q24304438-B378E5E2-06F7-4FF9-BCB1-8B7AB848392D Q24320147-EFBB52AE-ADB7-4EDF-83FE-8C21C0141C06 Q24653786-3DC4C7AE-66B4-477D-8C9B-769B2065109F Q27488308-A51E05C3-280F-4141-91F0-42F32C1BE015 Q27663557-AB2C8E3E-4880-4A37-8075-33EFD66E825F Q27677137-A3ACDEBA-CD3C-4005-8F2C-57DDE3036815 Q27679054-02340626-872A-4F9B-BE1C-1AA78D15E658 Q27681906-4C72FF0C-1739-4F17-BAED-108FE6ED6FC5 Q28475559-71F88B7E-7AEA-4AC7-8A82-71AE1240B254 Q28479254-6E6EAB7E-BC16-4CEA-A8E8-436FBF32E3F7 Q28743558-FC373813-7FC7-4298-8E95-B424E22DD2B0 Q29042349-2D38E497-5723-451C-940F-92CE6E90ADC7 Q30155275-20095DAC-2E84-4D25-9376-F3DED973CD7E Q33572902-46B79422-31EB-4FAE-8536-935BFE8B1A0D Q33711743-63B2C452-3746-48A5-8B40-D8B2E0303ACD Q33979985-963B10ED-BD2B-426C-8477-72400CAEFF80 Q34136483-ADA9188A-73FF-4B41-9906-F6B36D489C4B Q34212787-D99C3EE5-F51A-4E2B-B61E-979AD29F003A Q34323065-B45E12A7-7CA6-49CC-8AEB-8A61C161C9FE Q34364612-8AA53872-8320-4297-8EAE-FDD4684CC31A Q35163321-DD371D82-6E43-4BDD-A4EC-0B1F2AAA9499 Q35279959-E6DC924F-1C88-4037-8C21-D5ADC2AD1CCF Q37949459-54482ACF-1931-4BF0-9E4F-AF52BD79DFA6 Q38066334-44E2509A-1A04-415F-8AB4-27E00D17772D Q39399577-C6E29033-2C07-4432-8856-EED4BD2D38D1 Q40962303-5D0AC226-4CC6-4391-A00B-1D1F695B5CCF Q41867125-3BC42934-BF72-402C-B7C7-0E6FB7592DF6 Q42047850-68EEF529-0F59-40F4-8EB3-D2F180039AC2 Q54698410-DE060F0E-989C-4A1F-9C2F-29D2990AFDCC

P2860

Agonist and Antagonist Recognition by RIG-I, a Cytoplasmic Innate Immunity Receptor

http://www.wikidata.org/entity/Q27487543

description

2009 nî lūn-bûn

@nan

2009 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Agonist and Antagonist Recognition by RIG-I, a Cytoplasmic Innate Immunity Receptor

@ast

Agonist and Antagonist Recognition by RIG-I, a Cytoplasmic Innate Immunity Receptor

@en

Agonist and Antagonist Recognition by RIG-I, a Cytoplasmic Innate Immunity Receptor

@nl

type

label

Agonist and Antagonist Recognition by RIG-I, a Cytoplasmic Innate Immunity Receptor

@ast

Agonist and Antagonist Recognition by RIG-I, a Cytoplasmic Innate Immunity Receptor

@en

Agonist and Antagonist Recognition by RIG-I, a Cytoplasmic Innate Immunity Receptor

@nl

prefLabel

Agonist and Antagonist Recognition by RIG-I, a Cytoplasmic Innate Immunity Receptor

@ast

Agonist and Antagonist Recognition by RIG-I, a Cytoplasmic Innate Immunity Receptor

@en

Agonist and Antagonist Recognition by RIG-I, a Cytoplasmic Innate Immunity Receptor

@nl

P1433

Q27487543-45EF3924-5DEB-464B-863F-94C4B07C61C8

P1476

Q27487543-CEC967B2-1991-4DC4-9B6B-DB626039E951

P2093

Q27487543-03D040F3-9346-427C-9E4C-36CEF605FEDD

Q27487543-0970A6CC-C77E-4408-8641-2DC626DE2B49

Q27487543-1298C7BC-3A77-4B3B-9B98-D69F2F49A601

Q27487543-3258D1E8-E96C-4440-BD4D-B8EB998A252F

Q27487543-3CBD3F62-B7B2-4E56-AAFE-F61A37D1EE85

Q27487543-41E757E2-A058-41D0-BAF5-AEB7774056C2

Q27487543-AF090F7B-B050-4947-8481-0F9B26EAAA79

Q27487543-DECD8DB3-C5C4-427B-B990-A4C6DD0FFC1A

Q27487543-EAC832AD-D882-4DF0-8E45-47E6211F1313

P2860

Q27487543-01DBA024-38C1-42A6-8424-F76EC64C5354

Q27487543-0F5B9D60-2884-4721-AD72-62C91F0C4D79

Q27487543-12376FF6-B926-4654-BE2E-00C570D3E51D

Q27487543-12A46190-E9DD-49E9-9577-990F738607F5

Q27487543-19E6855C-D3C2-4830-B30C-EAC51B27D167

Q27487543-2106B5DB-BD95-4766-AF85-D9C52BF214FA

Q27487543-232A8ADC-6C02-4793-B73E-3C1A3DCE4D47

Q27487543-242FBF60-239B-4D85-8481-2D9AF5BA4518

Q27487543-30C1E9DC-D4B3-435F-8940-8B975486AFB8

Q27487543-39BB389D-0BB9-4D90-AA7E-FC3A7F13374F

P304

Q27487543-A618A604-FE26-48E8-8EAC-3A37BC86F0DD

P31

Q27487543-672CA950-29CD-4AEE-B9A9-9E5B76A677B9

P3181

Q27487543-A8184525-6095-4BDB-BCC7-1EFECF57ACDD

P356

Q27487543-491B4206-6E98-45A7-843C-E4573523BE4F

P407

Q27487543-F6877BA1-7BDB-438A-9FE4-4F2509C2481E

P433

Q27487543-54193082-4495-4C3E-8F04-3DBFF1A77C0E

P478

Q27487543-01445AD6-9CD5-455C-9A1F-B66C1EBFE217

P50

Q27487543-EE1DE604-AC68-418F-AD0E-908246DE2C5A

P577

Q27487543-E545D36D-202A-4C08-8C85-4CEA5DEF73B5

P698

Q27487543-5609C174-3202-4412-ABD5-C55BEFDD5505

P921

Q27487543-B00A1E3A-0053-417F-8F3E-7D9C144483A0

P932

Q27487543-6DBBF3F7-A172-4F44-9D3F-58E08FC8DABE

P3181

P356

P1433

Journal of Biological Chemistry

P1476

Agonist and Antagonist Recognition by RIG-I, a Cytoplasmic Innate Immunity Receptor

@en

P2093

C T Ranjith-Kumar

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

Cheng C Kao

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

Dharmaiah Srisathiyanarayanan

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

Joanna Ortiz-Alacantara

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

Kanchan Bhardwaj

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

Pingwei Li

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

Robert Vaughan

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

Wen Dong

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

Xiaojun Li

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

P2860

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

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

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

Viral and therapeutic control of IFN-beta promoter stimulator 1 during hepatitis C virus infection

Inhibition of dsRNA-induced signaling in hepatitis C virus-infected cells by NS3 protease-dependent and -independent mechanisms

Regulating intracellular antiviral defense and permissiveness to hepatitis C virus RNA replication through a cellular RNA helicase, RIG-I

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

Structural and functional analyses of the severe acute respiratory syndrome coronavirus endoribonuclease Nsp15

P304

1155-65

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

P31

scholarly article

P3181

3934096

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

P356

10.1074/JBC.M806219200

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

P407

P433

2

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

P478

284

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

P50

P577

2009-01-09T00:00:00Z

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

P698

19019822

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

P921

P932

2613625

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