Weapons of STAT destruction. Interferon evasion by paramyxovirus V protein.
about
RNA- and virus-independent inhibition of antiviral signaling by RNA helicase LGP2Pathogenesis of acute respiratory illness caused by human parainfluenza virusesThe C proteins of human parainfluenza virus type 1 block IFN signaling by binding and retaining Stat1 in perinuclear aggregates at the late endosomeUbiquitin-mediated response to microsporidia and virus infection in C. elegansInhibition of interferon-stimulated JAK-STAT signaling by a tick-borne flavivirus and identification of NS5 as an interferon antagonistClassical Swine Fever Virus Npro Interacts with Interferon Regulatory Factor 3 and Induces Its Proteasomal DegradationTLR3-dependent upregulation of RIG-I leads to enhanced cytokine production from cells infected with the parainfluenza virus SV5Morbillivirus Experimental Animal Models: Measles Virus Pathogenesis Insights from Canine Distemper VirusInteraction of mumps virus V protein variants with STAT1-STAT2 heterodimer: experimental and theoretical studies.Small-molecule activators of RNase L with broad-spectrum antiviral activityHuman parainfluenza virus type 2 V protein inhibits interferon production and signaling and is required for replication in non-human primates.Paramyxovirus assembly and budding: building particles that transmit infections.Human metapneumovirus inhibits IFN-β signaling by downregulating Jak1 and Tyk2 cellular levels.Recombinant human parainfluenza virus type 2 with mutations in V that permit cellular interferon signaling are not attenuated in non-human primates.Detecting remote sequence homology in disordered proteins: discovery of conserved motifs in the N-termini of Mononegavirales phosphoproteinsDissociation of paramyxovirus interferon evasion activities: universal and virus-specific requirements for conserved V protein amino acids in MDA5 interference.The interferon signaling antagonist function of yellow fever virus NS5 protein is activated by type I interferonVaccinia virus blocks Stat1-dependent and Stat1-independent gene expression induced by type I and type II interferons.A recombinant measles virus unable to antagonize STAT1 function cannot control inflammation and is attenuated in rhesus monkeys.Hepatitis B virus HBx protein interactions with the ubiquitin proteasome system.Morbillivirus v proteins exhibit multiple mechanisms to block type 1 and type 2 interferon signalling pathwaysParainfluenza virus 5 m protein interaction with host protein 14-3-3 negatively affects virus particle formation.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 primatesInhibition of hendra virus fusion.West Nile virus infection induces depletion of IFNAR1 protein levelsHenipaviruses employ a multifaceted approach to evade the antiviral interferon response.Cullin4 Is Pro-Viral during West Nile Virus Infection of Culex Mosquitoes.The immunomodulating V and W proteins of Nipah virus determine disease course.Role of ubiquitin in parainfluenza virus 5 particle formation.Mouse STAT2 restricts early dengue virus replicationNewcastle Disease Virus V Protein Targets Phosphorylated STAT1 to Block IFN-I Signaling.Recombinant human parainfluenza virus type 2 vaccine candidates containing a 3' genomic promoter mutation and L polymerase mutations are attenuated and protective in non-human primates.HSV-2 inhibits type-I interferon signaling via multiple complementary and compensatory STAT2-associated mechanismsRole for the phosphoprotein P subunit of the paramyxovirus polymerase in limiting induction of host cell antiviral responsesViral modulators of cullin RING ubiquitin ligases: culling the host defense.HIV-1 accessory proteins VPR and Vif modulate antiviral response by targeting IRF-3 for degradationEctromelia virus BTB/kelch proteins, EVM150 and EVM167, interact with cullin-3-based ubiquitin ligases.Human parvovirus B19 NS1 protein modulates inflammatory signaling by activation of STAT3/PIAS3 in human endothelial cells.Human immunodeficiency virus type 1 Vpr links proteasomal degradation and checkpoint activation.Region between the canine distemper virus M and F genes modulates virulence by controlling fusion protein expression.
P2860
Q24673649-B68978A3-BF7E-40CC-BD64-6D752F361F4DQ27000151-36342649-AF9C-4CCA-9CDC-7E15632DDD30Q27311445-146302E9-1634-42C3-B692-02D3D90C0001Q27324783-CDA2EFCA-7C8C-4529-B6FE-B8D1150C4C1FQ27472136-3506E492-5DB8-4435-8DF8-7CBCB6E6F1ECQ27478373-C6032FDC-ED17-4B8F-9A82-A62063AC07EDQ27490869-2B75B6C2-714A-46A3-A14B-87B3AAB9CDB9Q28069402-D343EF25-BCBD-4093-97FE-0D3DF3E5AF22Q30394753-4C2D2614-A87D-4FA9-99DA-AA24838C53B3Q33286117-9946750E-3E86-4979-A2E2-B467C419DF25Q33653692-5D0CE249-450B-4419-80FC-811636EBCDA6Q34020498-E4C1564D-9653-4E94-B8A1-900BB36DB6B0Q34031372-FE86F106-0377-4847-B085-A48CDFB2E8A6Q34101229-9B8013A3-9D70-4779-991F-3672A1AA0D68Q34189305-93F08A60-DE7D-4FA8-B4A1-DD2F5654B3D3Q34190615-DC529654-C853-4074-B798-11491E6DDCBEQ34251294-55F2880E-6507-4596-A646-F732A55F24DEQ34328870-38CD0A29-0112-47EE-AEA9-7C0C850424A2Q34457823-D7FBD6D9-D230-4B08-9C4E-41A2E0E99A7BQ34580906-E0E65227-94EA-4313-81BE-C8A17088DDEDQ34595223-49A1B461-15A1-4DA9-858F-B423D96E76A3Q34741972-7E01D3E5-F6AB-4036-9BEC-CFB527AD6137Q35076577-4E6F7D3D-6B27-4AA9-A919-6903F6EB3A35Q35101317-D7377A67-6660-4575-B6F3-4F5B4CB697E0Q35159163-7DFFF97C-03D6-4A05-A0C8-C7634292803DQ35260006-824EA000-968D-42A4-BC83-017EF76B2F3DQ35760782-6E32580E-13E1-4B1D-97EB-AAEB89B64D33Q35785921-5FF97C73-5852-46F1-9153-1DFFBD96EE47Q35826872-5940B461-F653-4699-B36E-80D94B08CD0FQ35846922-2A8082A7-96AE-4669-9452-DB9024ADAAE9Q35918371-B0CEDCB4-FF9F-46F6-BFC8-5EDF0FDFEC50Q36088161-E4370E00-64A7-4599-9E66-8FAF1F0A5708Q36098919-863443E0-E64A-4986-AC2E-9520949CDD3AQ36099330-DEE7CB69-5E5C-40E5-B45A-608308B75911Q36480678-E37EDD37-2901-4414-B93C-61A6A744DBA0Q36559594-69F633BD-229E-411A-ACE9-1B0BD19D0160Q36740202-9D907617-B5DA-4C65-A162-26DB31C74EB1Q36845694-26F08F7D-B44C-4C3B-A2F2-A999C91C346FQ36940407-F14AD66C-81ED-47FD-992A-90A1F404511EQ36949674-AA41BE94-C529-46F8-9358-86366E4D4DFF
P2860
Weapons of STAT destruction. Interferon evasion by paramyxovirus V protein.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Weapons of STAT destruction. Interferon evasion by paramyxovirus V protein.
@ast
Weapons of STAT destruction. Interferon evasion by paramyxovirus V protein.
@en
type
label
Weapons of STAT destruction. Interferon evasion by paramyxovirus V protein.
@ast
Weapons of STAT destruction. Interferon evasion by paramyxovirus V protein.
@en
prefLabel
Weapons of STAT destruction. Interferon evasion by paramyxovirus V protein.
@ast
Weapons of STAT destruction. Interferon evasion by paramyxovirus V protein.
@en
P2860
P1433
P1476
Weapons of STAT destruction. Interferon evasion by paramyxovirus V protein.
@en
P2093
Curt M Horvath
P2860
P304
P356
10.1111/J.1432-1033.2004.04425.X
P407
P577
2004-12-01T00:00:00Z