The 2'-5'-oligoadenylate synthetase 3 enzyme potently synthesizes the 2'-5'-oligoadenylates required for RNase L activation.
about
Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseasesStructural mechanism of sensing long dsRNA via a noncatalytic domain in human oligoadenylate synthetase 3Overlapping Patterns of Rapid Evolution in the Nucleic Acid Sensors cGAS and OAS1 Suggest a Common Mechanism of Pathogen Antagonism and Escape.Structural and functional analysis reveals that human OASL binds dsRNA to enhance RIG-I signalingEnzyme assays for synthesis and degradation of 2-5As and other 2'-5' oligonucleotides.Activation of RNase L is dependent on OAS3 expression during infection with diverse human virusesTwo interferon-independent double-stranded RNA-induced host defense strategies suppress the common cold virus at warm temperature.A Simple Screening Approach To Prioritize Genes for Functional Analysis Identifies a Role for Interferon Regulatory Factor 7 in the Control of Respiratory Syncytial Virus DiseasecGAS is activated by DNA in a length-dependent manner.Mitochondrial C11orf83 is a potent Antiviral Protein Independent of interferon production.Functional evolution of the OAS1 viral sensor: Insights from old world primates.OAS3 produces oligoadenylates
P2860
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P2860
The 2'-5'-oligoadenylate synthetase 3 enzyme potently synthesizes the 2'-5'-oligoadenylates required for RNase L activation.
description
2014 nî lūn-bûn
@nan
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
2014年论文
@zh
2014年论文
@zh-cn
name
The 2'-5'-oligoadenylate synth ...... quired for RNase L activation.
@en
type
label
The 2'-5'-oligoadenylate synth ...... quired for RNase L activation.
@en
prefLabel
The 2'-5'-oligoadenylate synth ...... quired for RNase L activation.
@en
P2093
P2860
P50
P356
P1433
P1476
The 2'-5'-oligoadenylate synth ...... equired for RNase L activation
@en
P2093
Karthiga Thavachelvam
Philippe Desprès
Thomas Boesen
P2860
P304
14222-14231
P356
10.1128/JVI.01763-14
P407
P577
2014-10-01T00:00:00Z