Structural basis for the sequence-specific recognition of human ISG15 by the NS1 protein of influenza B virus (Q27671342)

8

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author name string

Rongjin Guan

1

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Li-Chung Ma

2

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Paul G Leonard

3

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Brendan R Amer

4

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Haripriya Sridharan

5

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Chen Zhao

6

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Robert M Krug

Proceedings of the National Academy of Sciences of the United States of America

7

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language of work or name

English

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publication date

16 August 2011

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published in

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volume

108

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issue

33

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page(s)

13468-73

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cites work

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Interferon-inducible ubiquitin E2, Ubc8, is a conjugating enzyme for protein ISGylation

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The UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, an IFN-alpha/beta-induced ubiquitin-like protein

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Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein

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Herc5 attenuates influenza A virus by catalyzing ISGylation of viral NS1 protein

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HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets

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Structural basis for ubiquitin-like ISG 15 protein binding to the NS1 protein of influenza B virus: a protein-protein interaction function that is not shared by the corresponding N-terminal domain of the NS1 protein of influenza A virus

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Crystal structure of the interferon-induced ubiquitin-like protein ISG15

21 January 2018

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PubMed

https://pubmed.ncbi.nlm.nih.gov/21808041

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1073/PNAS.1107032108

1 reference

release_ak33fy56hve2notetf2f66zk54

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1 reference

Fatcat

https://api.fatcat.wiki/v0/release/ak33fy56hve2notetf2f66zk54

mapped directly with Wikidata item

24 November 2022

based on heuristic

1510194

1 reference

1 reference

1510194

PubMed publication ID

21808041

1 reference