MDA5 cooperatively forms dimers and ATP-sensitive filaments upon binding double-stranded RNA
about
MDA5-positive dermatomyositis: an uncommon entity in Europe with variable clinical presentationsPrion-like polymerization as a signaling mechanismMDA5 and LGP2: accomplices and antagonists of antiviral signal transductionVisualizing the Determinants of Viral RNA Recognition by Innate Immune Sensor RIG-IStructural basis for Marburg virus VP35-mediated immune evasion mechanismsDefining the functional determinants for RNA surveillance by RIG-IStructural basis for the prion-like MAVS filaments in antiviral innate immunityParamyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signalingLGP2 synergy with MDA5 in RLR-mediated RNA recognition and antiviral signalingInsights into the antiviral immunity against grass carp (Ctenopharyngodon idella) reovirus (GCRV) in grass carpMDA5 assembles into a polar helical filament on dsRNA.The innate immune sensor LGP2 activates antiviral signaling by regulating MDA5-RNA interaction and filament assembly.Conformational rearrangements of RIG-I receptor on formation of a multiprotein:dsRNA assembly.Molecular Mechanisms of Innate Immune Inhibition by Non-Segmented Negative-Sense RNA Viruses.LGP2 plays a critical role in sensitizing mda-5 to activation by double-stranded RNAMulti-signal sedimentation velocity analysis with mass conservation for determining the stoichiometry of protein complexes.In vivo ligands of MDA5 and RIG-I in measles virus-infected cells.Emerging principles governing signal transduction by pattern-recognition receptorsStructural biology of innate immunity.Kinetic discrimination of self/non-self RNA by the ATPase activity of RIG-I and MDA5Monitoring activation of the antiviral pattern recognition receptors RIG-I and PKR by limited protease digestion and native PAGE.MDA5-filament, dynamics and disease.Resurrecting ancestral structural dynamics of an antiviral immune receptor: adaptive binding pocket reorganization repeatedly shifts RNA preference.Cell-intrinsic innate immune control of West Nile virus infection.Enterovirus RNA in peripheral blood may be associated with the variants of rs1990760, a common type 1 diabetes associated polymorphism in IFIH1.MDA5 complements TLR3 in suppression of neuroblastomaKinetic mechanism for viral dsRNA length discrimination by MDA5 filamentsATP hydrolysis by the viral RNA sensor RIG-I prevents unintentional recognition of self-RNA.Overview of current methods in sedimentation velocity and sedimentation equilibrium analytical ultracentrifugation.ATPase-driven oligomerization of RIG-I on RNA allows optimal activation of type-I interferonThe essential, nonredundant roles of RIG-I and MDA5 in detecting and controlling West Nile virus infection.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.Enter at your own risk: how enteroviruses navigate the dangerous world of pattern recognition receptor signaling.Structural insights into RNA recognition and activation of RIG-I-like receptors.Multi-level regulation of cellular recognition of viral dsRNA.Structural basis of innate immune recognition of viral RNA.Duplex RNA activated ATPases (DRAs): platforms for RNA sensing, signaling and processing.West Nile virus infection and immunity.
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P2860
MDA5 cooperatively forms dimers and ATP-sensitive filaments upon binding double-stranded RNA
description
2012 nî lūn-bûn
@nan
2012 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
MDA5 cooperatively forms dimer ...... on binding double-stranded RNA
@ast
MDA5 cooperatively forms dimer ...... on binding double-stranded RNA
@en
MDA5 cooperatively forms dimer ...... on binding double-stranded RNA
@nl
type
label
MDA5 cooperatively forms dimer ...... on binding double-stranded RNA
@ast
MDA5 cooperatively forms dimer ...... on binding double-stranded RNA
@en
MDA5 cooperatively forms dimer ...... on binding double-stranded RNA
@nl
prefLabel
MDA5 cooperatively forms dimer ...... on binding double-stranded RNA
@ast
MDA5 cooperatively forms dimer ...... on binding double-stranded RNA
@en
MDA5 cooperatively forms dimer ...... on binding double-stranded RNA
@nl
P2860
P3181
P356
P1433
P1476
MDA5 cooperatively forms dimer ...... on binding double-stranded RNA
@en
P2093
Ian C Berke
P2860
P304
P3181
P356
10.1038/EMBOJ.2012.19
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P50
P577
2012-04-04T00:00:00Z