Identification of paramyxovirus V protein residues essential for STAT protein degradation and promotion of virus replication. - Wikidata - awgldk - TriplyDB

Identification of paramyxovirus V protein residues essential for STAT protein degradation and promotion of virus replication.

Identification of paramyxovirus V protein residues essential for STAT protein degradation and promotion of virus replication.

http://www.wikidata.org/entity/Q33843478

about

Hepatitis C virus core protein blocks interferon signaling by interaction with the STAT1 SH2 domain Synthesis of human parainfluenza virus 2 nucleocapsid protein in yeast as nucleocapsid-like particles and investigation of its antigenic structure.Interaction of mumps virus V protein variants with STAT1-STAT2 heterodimer: experimental and theoretical studies.Human parainfluenza virus type 2 V protein inhibits interferon production and signaling and is required for replication in non-human primates.Recombinant human parainfluenza virus type 2 with mutations in V that permit cellular interferon signaling are not attenuated in non-human primates.Human parainfluenza virus type 4 is incapable of evading the interferon-induced antiviral effect Human parainfluenza virus type 2 L protein regions required for interaction with other viral proteins and mRNA capping.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 Antagonism of innate immunity by paramyxovirus accessory proteins.Independent structural domains in paramyxovirus polymerase protein.VIGOR extended to annotate genomes for additional 12 different viruses.Human parainfluenza virus type 2 V protein inhibits genome replication by binding to the L protein: possible role in promoting viral fitness.Human parainfluenza virus type 2 vector induces dendritic cell maturation without viral RNA replication/transcription.A point mutation, E95D, in the mumps virus V protein disengages STAT3 targeting from STAT1 targeting.Paramyxovirus disruption of interferon signal transduction: STATus report A Point Mutation in the RNA-Binding Domain of Human Parainfluenza Virus Type 2 Nucleoprotein Elicits Abnormally Enhanced Polymerase Activity.Graf1 Controls the Growth of Human Parainfluenza Virus Type 2 through Inactivation of RhoA Signaling.Human parainfluenza virus type 2 V protein inhibits induction of tetherin.La Piedad Michoacán Mexico Virus V protein antagonizes type I interferon response by binding STAT2 protein and preventing STATs nuclear translocation Human parainfluenza virus type 2 polymerase complex recognizes leader promoters of other species belonging to the genus Rubulavirus.Tetherin antagonism by V proteins is a common trait among the genus Rubulavirus.Enhanced growth of influenza A virus by coinfection with human parainfluenza virus type 2.Identification of two essential aspartates for polymerase activity in parainfluenza virus L protein by a minireplicon system expressing secretory luciferase.Human parainfluenza virus type 2 V protein inhibits TRAF6-mediated ubiquitination of IRF7 to prevent TLR7- and TLR9-dependent interferon induction.Effects of hemagglutinin-neuraminidase protein mutations on cell-cell fusion mediated by human parainfluenza type 2 virus Modulation of apoptosis by V protein mumps virus.A tryptophan-rich motif in the human parainfluenza virus type 2 V protein is critical for the blockade of toll-like receptor 7 (TLR7)- and TLR9-dependent signaling.

P2860

Q24301056-5D1EF863-C473-4D6A-B091-9CC44C04C4DF Q30383975-998E2202-BBC4-4075-A814-5A8C9D6B4E11 Q30394753-DCF3851D-F545-434F-A0C1-FB5804F79D8F Q33653692-559C44AD-B191-459F-B822-98948B4C7DCB Q34101229-BB933A63-F637-4482-9811-43EABC96663C Q34142854-78C065A1-D952-49C4-82B3-5A8F9EEA8B48 Q34485273-2C710E73-259F-47AF-BF3A-B635E94910F4 Q35076577-05F0A832-1CA5-44AD-8D5C-7705C066D6E0 Q35259962-5F4E5859-F4E4-4417-B686-B5E00C5B5B4F Q35838944-E19AF10A-A4D8-4D99-B9D0-2CAA65BF965F Q36088457-98B753B4-BA86-47ED-906B-95785419412D Q36747923-5464E41E-F469-4741-AC65-C7C0CC126DF7 Q37035660-D8E2CA87-2612-4561-B32F-68D66F470E4F Q37232874-5B6A2363-9DA3-4E8D-B2B3-A704E4AEC66F Q37582936-DCE98BFE-BE8F-44BC-A57F-4371361A67D6 Q38717196-941430C3-931A-40D9-B883-C4B75A022AFA Q38752538-D79C58AE-65BF-4A0F-8015-AAF99781B734 Q38813353-5EE39B99-358B-4D41-8408-EB418FD63D6D Q38821414-8C2209B6-CB9A-47C1-B1BA-DA5FDFE37785 Q40051698-15A2CE3C-2764-42CE-8EB6-9FAF8507E4A5 Q40217772-0BE1D8E0-A189-40F2-9D06-EDC768E9EEAF Q40904705-BC2F423D-E8A7-423F-9E83-A5FD706E0595 Q41249509-0BA77DC8-6948-4C96-ADB0-5E972BCF3E9E Q41945976-27BD1311-76F7-4D18-AAC4-2C8CB25E0A0A Q42081316-418D77ED-2987-406A-B2B4-E98BFAD66091 Q42273321-C47BDDA8-4CF8-4996-B576-ECF137E6C7BB Q42779789-E6DF670C-92DC-441B-BD6E-60CF3685E88E

P2860

Identification of paramyxovirus V protein residues essential for STAT protein degradation and promotion of virus replication.

http://www.wikidata.org/entity/Q33843478

description

2005 nî lūn-bûn

@nan

2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2005年の論文

@ja

2005年論文

@yue

2005年論文

@zh-hant

2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

@wuu

name

Identification of paramyxoviru ...... romotion of virus replication.

@ast

Identification of paramyxoviru ...... romotion of virus replication.

@en

type

label

Identification of paramyxoviru ...... romotion of virus replication.

@ast

Identification of paramyxoviru ...... romotion of virus replication.

@en

prefLabel

Identification of paramyxoviru ...... romotion of virus replication.

@ast

Identification of paramyxoviru ...... romotion of virus replication.

@en

P1433

Q33843478-B0464839-9ABB-4081-B00E-E8449436A3F0

P1476

Q33843478-BC25B664-F43B-4C7C-BF99-DBD9E8671833

P2093

Q33843478-203DCAA3-1BC6-425C-8874-2CF1E1610297

Q33843478-84B562C1-8603-4CCC-BD09-424C023117F7

Q33843478-9E7A1D0F-10ED-487F-9AF9-6C632A38E827

Q33843478-BFDFDAC2-6D35-47E8-BBFD-29B07082AA0C

Q33843478-E035E3B3-0E20-49C4-9653-13F38B119F50

Q33843478-E3028898-8DE3-4D56-974C-D4AD9A92AEDE

P2860

Q33843478-05A0310D-5275-4056-A31C-7CF6AE885F06

Q33843478-061D225F-C596-487F-88A9-D4D940B18878

Q33843478-136723B8-CC55-415D-89B9-FB690E8250E0

Q33843478-1849409A-D52B-489B-BAE9-84D9C9B90E91

Q33843478-1CB768F2-08F8-4505-A048-0A521655BBF9

Q33843478-1FACACF9-8B35-45B0-859A-DA87197F7BEE

Q33843478-2748403D-AFA6-4C7E-A61F-A949F0213A30

Q33843478-2AB0974A-9C31-4C4E-87CA-3F204D043358

Q33843478-2F726166-FC42-44F9-8D1B-2FE724C7D124

Q33843478-376E52F8-0D94-42A4-A565-91F5461A08A4

P304

Q33843478-2C14D7BA-349A-47C8-8B19-0525D0EB9ACE

P31

Q33843478-C3525237-2525-463A-841F-9D9E6D78351B

P356

Q33843478-B10FEBC7-0668-4C06-92EE-5971283E1CF5

P433

Q33843478-87E4B99B-C68F-4A63-83F1-95648A8AE008

P478

Q33843478-6704237F-27A7-4FCA-8B71-27D6AABCE43C

P577

Q33843478-48614E85-3ABC-40C1-8E94-88DB3B238F25

P698

Q33843478-B8315240-95DA-4963-B94D-B13D0765BBA1

P932

Q33843478-6851BC52-DDC2-409C-8269-C34D9E171F86

P356

JVI.79.13.8591-8601.2005

P1433

Journal of Virology

P1476

Identification of paramyxoviru ...... romotion of virus replication.

@en

P2093

Daniel Kolakofsky

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

Dominique Garcin

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

Machiko Nishio

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

Masato Tsurudome

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

Morihiro Ito

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

Yasuhiko Ito

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

P2860

The paramyxovirus, Sendai virus, V protein encodes a luxury function required for viral pathogenesis.

The p127 subunit (DDB1) of the UV-DNA damage repair binding protein is essential for the targeted degradation of STAT1 by the V protein of the paramyxovirus simian virus 5

Stat protein transactivation domains recruit p300/CBP through widely divergent sequences

Sendai virus C proteins must interact directly with cellular components to interfere with interferon action

The paramyxovirus simian virus 5 V protein slows progression of the cell cycle.

Sendai virus and simian virus 5 block activation of interferon-responsive genes: importance for virus pathogenesis

Sendai virus C proteins counteract the interferon-mediated induction of an antiviral state

Single amino acid substitution in the V protein of simian virus 5 differentiates its ability to block interferon signaling in human and murine cells

High resistance of human parainfluenza type 2 virus protein-expressing cells to the antiviral and anti-cell proliferative activities of alpha/beta interferons: cysteine-rich V-specific domain is required for high resistance to the interferons.

Y2, the smallest of the Sendai virus C proteins, is fully capable of both counteracting the antiviral action of interferons and inhibiting viral RNA synthesis.

P304

8591-8601

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

P31

scholarly article

P356

10.1128/JVI.79.13.8591-8601.2005

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

P433

13

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

P478

79

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

P577

2005-07-01T00:00:00Z

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

P698

15956600

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

P932

1143765

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