C-terminal region of STAT-1alpha is not necessary for its ubiquitination and degradation caused by mumps virus V protein - Wikidata - awgldk - TriplyDB

C-terminal region of STAT-1alpha is not necessary for its ubiquitination and degradation caused by mumps virus V protein

C-terminal region of STAT-1alpha is not necessary for its ubiquitination and degradation caused by mumps virus V protein

http://www.wikidata.org/entity/Q34351828

about

Hepatitis C virus core protein blocks interferon signaling by interaction with the STAT1 SH2 domain Simian virus 5 V protein acts as an adaptor, linking DDB1 to STAT2, to facilitate the ubiquitination of STAT1 Ubiquitination-mediated regulation of interferon responses The Ebola Virus Interferon Antagonist VP24 Directly Binds STAT1 and Has a Novel, Pyramidal Fold Interferons and viruses: an evolutionary arms race of molecular interactions Interferon-γ Inhibits Ebola Virus Infection Mumps Virus Induces Protein-Kinase-R-Dependent Stress Granules, Partly Suppressing Type III Interferon Production.Mumps virus V protein antagonizes interferon without the complete degradation of STAT1.Identification of paramyxovirus V protein residues essential for STAT protein degradation and promotion of virus replication.Mapuera virus, a rubulavirus that inhibits interferon signalling in a wide variety of mammalian cells without degrading STATs.Human parainfluenza virus type 4 is incapable of evading the interferon-induced antiviral effect Dissociation of paramyxovirus interferon evasion activities: universal and virus-specific requirements for conserved V protein amino acids in MDA5 interference.Association of mumps virus V protein with RACK1 results in dissociation of STAT-1 from the alpha interferon receptor complex.The V protein of Tioman virus is incapable of blocking type I interferon signaling in human cells.Antagonism of innate immunity by paramyxovirus accessory proteins.The V protein of mumps virus plays a critical role in pathogenesis.Newcastle Disease Virus V Protein Targets Phosphorylated STAT1 to Block IFN-I Signaling.Human parainfluenza virus type 2 V protein inhibits genome replication by binding to the L protein: possible role in promoting viral fitness.Herpes simplex virus 1 gene products occlude the interferon signaling pathway at multiple sites.Paramyxovirus disruption of interferon signal transduction: STATus report Immunogenicity of novel mumps vaccine candidates generated by genetic modification.Rescue of wild-type mumps virus from a strain associated with recent outbreaks helps to define the role of the SH ORF in the pathogenesis of mumps virus.Paramyxovirus evasion of innate immunity: Diverse strategies for common targets.Adherent-invasive Escherichia coli blocks interferon-γ-induced signal transducer and activator of transcription (STAT)-1 in human intestinal epithelial cells.STAT3 ubiquitylation and degradation by mumps virus suppress cytokine and oncogene signaling.STAT protein interference and suppression of cytokine signal transduction by measles virus V protein.Mumps virus Enders strain is sensitive to interferon (IFN) despite encoding a functional IFN antagonist.Hendra virus V protein inhibits interferon signaling by preventing STAT1 and STAT2 nuclear accumulation Targeting of the Sendai virus C protein to the plasma membrane via a peptide-only membrane anchor.Tetherin antagonism by V proteins is a common trait among the genus Rubulavirus.Function of small hydrophobic proteins of paramyxovirus.Nipah virus V and W proteins have a common STAT1-binding domain yet inhibit STAT1 activation from the cytoplasmic and nuclear compartments, respectively Suppression of thermotolerance in mumps virus-infected cells is caused by lack of HSP27 induction contributed by STAT-1.Inhibition of the gamma interferon response by a Sendai virus C protein mutant with no STAT1-binding ability.Stat3 cleavage by caspases: impact on full-length Stat3 expression, fragment formation, and transcriptional activity.

P2860

Q24301056-00B9F4EA-4A41-4C9D-864E-981ECF0117A1 Q24338310-24A71777-3819-4613-9D0C-625D565914C7 Q26853323-71E1C3EC-9613-4CC3-8C91-98E48C9D6FBE Q27677595-9764C4E7-CB51-40F1-BB9A-E1935A85F965 Q28083788-CA9D5C4B-2781-40AD-82D3-5BA89E22062F Q28550929-B781D5E4-5643-401C-BC04-C57707CD0CD6 Q30008870-11464C2B-D03B-4EC2-9C34-EF77E922C46B Q33707477-FE75C2B5-00AB-4FED-BFA6-E438D4FC2BD1 Q33843478-376E52F8-0D94-42A4-A565-91F5461A08A4 Q33910283-0896D4EA-3F09-4292-B15B-181A47EB3783 Q34142854-DF79CF76-56FD-4250-8999-7146E75E58C2 Q34190615-EB1BD161-E459-4FD9-9A1B-572C5A35B15A Q34351347-32723994-E64C-4178-8C88-9C22EC5924B5 Q34558886-C25164D8-4B9B-41A1-93C5-15E260EA0319 Q35259962-58EAE9A4-CCDD-4A13-8A9A-D223C8A0397D Q35689612-E70D28A6-A853-460A-A2CF-8C8721153508 Q35918371-608DA245-412D-438A-AEC3-0D4B7CE4520C Q36747923-5B48A063-D8BE-46BB-BABE-0648DD915025 Q37094247-B3D10C0C-27B5-42B9-8B9F-75D6085AA208 Q37582936-AEB8D9E1-AFC6-4781-9563-15BF9463D101 Q37644086-5FFEF231-F2FD-4FEF-B848-65FFF2E4CAA2 Q37649310-7CCA09DA-42F5-4AE1-B25C-60DC7BB32768 Q38156883-0A00E8B2-4804-4356-B82B-BE0F1F527BC6 Q39258188-51E2FB92-47CE-45D2-9131-65311AAB369A Q39752565-B790461A-838A-46A2-A0CF-994F64ED2702 Q39787663-0B913A33-7F27-4A61-AC6C-5ED6FBED39BE Q39822103-BDE50F07-53BD-43DC-B99F-5965517F1C71 Q40012127-58B17E85-A562-473E-A5DB-DFB4FD0B7FE3 Q40182215-1DEE355E-9ABB-43CE-B10F-EFC5B9951A23 Q40217772-DF592C83-C61A-4AEC-8093-CCF1FD712B8C Q40324541-15238110-FEC2-47C0-9768-605C53001DFD Q40883579-FE497D39-A737-4502-9DE2-66B7BE9F4D13 Q44067336-587F8864-D046-4378-B6E6-C892112A69E0 Q45631386-D7E83623-1900-4CFD-BB59-2A1906D29CC8 Q53625976-0C20A5AB-C4B3-4B9E-A6CE-6CF8CEE40530

P2860

C-terminal region of STAT-1alpha is not necessary for its ubiquitination and degradation caused by mumps virus V protein

http://www.wikidata.org/entity/Q34351828

description

2002 nî lūn-bûn

@nan

2002 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

C-terminal region of STAT-1alp ...... aused by mumps virus V protein

@ast

C-terminal region of STAT-1alp ...... aused by mumps virus V protein

@en

C-terminal region of STAT-1alp ...... aused by mumps virus V protein

@nl

type

label

C-terminal region of STAT-1alp ...... aused by mumps virus V protein

@ast

C-terminal region of STAT-1alp ...... aused by mumps virus V protein

@en

C-terminal region of STAT-1alp ...... aused by mumps virus V protein

@nl

prefLabel

C-terminal region of STAT-1alp ...... aused by mumps virus V protein

@ast

C-terminal region of STAT-1alp ...... aused by mumps virus V protein

@en

C-terminal region of STAT-1alp ...... aused by mumps virus V protein

@nl

P1433

Q34351828-33D5D936-1D5C-421C-98AB-532D5AEDA7DD

P1476

Q34351828-F3B1FDF6-6118-4244-9858-A4D36FC03412

P2093

Q34351828-432007E7-7A9D-44A9-9875-928233E6743B

Q34351828-A1AC5B8F-063F-4303-AAAF-D2E7CC6B88AF

Q34351828-ABA87A36-6896-41BC-8A5A-586224A69C63

Q34351828-D7CE0DB8-DF41-452A-92CA-6A98F615C6BC

P2860

Q34351828-0921D957-2BB3-43CC-8F44-B0A823270CE7

Q34351828-0CA57819-0C68-4251-8B2D-E9FE794F7DAB

Q34351828-0EC91537-3522-4C7A-9348-96611DB88AF3

Q34351828-151B63EE-70B9-4A55-8D88-9E39DB47DB37

Q34351828-15DA51B5-2B73-40B4-80E2-632C4CF9A0B0

Q34351828-21ADEC93-B0CC-43BE-800A-992D9F6F11AB

Q34351828-22D2539B-C7E5-4EC0-B653-5EB096D1815F

Q34351828-44BB8190-2B84-4CE0-99B1-EF2A9C35F363

Q34351828-49016A0A-D166-4312-8343-E68C888299E7

Q34351828-548B8DA7-5E84-46A3-877D-7D2801F0DDEA

P304

Q34351828-AAEC7711-A8AF-4015-AE2F-C4A95BD211A8

P31

Q34351828-CD96AF3D-BA57-41A4-AD79-F14CAE782DAA

P356

Q34351828-2EB10C57-74BF-4C9A-9F57-3BA7CCC51617

P407

Q34351828-9A585070-F7CC-457E-A63C-DFAAEE915475

P433

Q34351828-F3D057C6-BCE2-470A-844C-0F9510DEFA90

P478

Q34351828-752EFB23-D245-4717-9D05-BAE6E90BDAD5

P577

Q34351828-666CD85A-0239-452F-9D73-9A152C92FB41

P698

Q34351828-E0F062EE-767D-43D8-BCD2-7F54D2AD92B1

P921

Q34351828-EE67537F-7F9C-4ACF-A8AC-F30C7537AE3C

P932

Q34351828-E04045D7-28A5-4F14-B526-0D88D98BA5A7

P356

JVI.76.24.12683-12690.2002

P1433

Journal of Virology

P1476

C-terminal region of STAT-1alp ...... aused by mumps virus V protein

@en

P2093

Nobuhiro Fujii

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

Noriko Yokosawa

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

Shin-Ichi Yokota

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

Toru Kubota

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

P2860

Interactions between STAT and non-STAT proteins in the interferon-stimulated gene factor 3 transcription complex

Themes and variations on ubiquitylation

Interferons: cell signalling, immune modulation, antiviral response and virus countermeasures

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

Nonstructural C protein is required for efficient measles virus replication in human peripheral blood cells.

Versatility of the accessory C proteins of Sendai virus: contribution to virus assembly as an additional role.

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.

Inhibition of interferon-mediated antiviral responses by influenza A viruses and other negative-strand RNA viruses.

Association of mumps virus V protein with RACK1 results in dissociation of STAT-1 from the alpha interferon receptor complex.

P304

12683-12690

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

P31

scholarly article

P356

10.1128/JVI.76.24.12683-12690.2002

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

P407

P433

24

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

P478

76

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

P577

2002-12-01T00:00:00Z

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

P698

12438594

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

P921

protein ubiquitination

P932

136684

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