Feline herpesvirus 1 (FHV-1) US3 blocks type I IFN signal pathway by targeting IRF3 dimerization in a kinase-independent manner.

about

Feline herpesvirus 1 (FHV-1) US3 blocks type I IFN signal pathway by targeting IRF3 dimerization in a kinase-independent manner.

Item

http://www.wikidata.org/entity/Q52606469

description

2018 nî lūn-bûn

@nan

2018年の論文

@ja

2018年学术文章

@wuu

2018年学术文章

@zh

2018年学术文章

@zh-cn

2018年学术文章

@zh-hans

2018年学术文章

@zh-my

2018年学术文章

@zh-sg

2018年學術文章

@yue

2018年學術文章

@zh-hant

name

Feline herpesvirus 1 (FHV-1) U ...... n a kinase-independent manner.

@en

Feline herpesvirus 1

@nl

type

Item

label

Feline herpesvirus 1 (FHV-1) U ...... n a kinase-independent manner.

@en

Feline herpesvirus 1

@nl

prefLabel

Feline herpesvirus 1 (FHV-1) U ...... n a kinase-independent manner.

@en

Feline herpesvirus 1

@nl

P1476

Feline herpesvirus 1 (FHV-1) U ...... n a kinase-independent manner.

@en

P2093

Jikai Zhang

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

Jin Tian

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

Liandong Qu

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

Xiaoxiao Liu

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

Xue Sun

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

Yongxiang Liu

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

P2860

IFI16 is an innate immune sensor for intracellular DNA

Herpes simplex virus 1 tegument protein US11 downmodulates the RLR signaling pathway via direct interaction with RIG-I and MDA-5

Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the type I interferon pathway

RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway

DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response

Herpes simplex virus 1 DNA polymerase processivity factor UL42 inhibits TNF-α-induced NF-κB activation by interacting with p65/RelA and p50/NF-κB1

The herpes simplex virus ICP0 RING finger domain inhibits IRF3- and IRF7-mediated activation of interferon-stimulated genes

The order Herpesvirales

Structural Analysis of the STING Adaptor Protein Reveals a Hydrophobic Dimer Interface and Mode of Cyclic di-GMP Binding

The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses

P31

scholarly article

P356

10.1128/JVI.00047-18

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

P407

English

P577

2018-04-04T00:00:00Z

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

P698

29618645

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

P932

5974484

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