The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit (Q27653657)

7

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Darren J Hart

object named as

Darren J Hart

5

0 references

Thibaut Crépin

object named as

Thibaut Crépin

3

0 references

author name string

Alexandre Dias

1

0 references

Denis Bouvier

2

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Andrew A McCarthy

4

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Florence Baudin

6

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Rob W H Ruigrok

Inhibition of cap (m7GpppXm)-dependent endonuclease of influenza virus by 4-substituted 2,4-dioxobutanoic acid compounds

8

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language of work or name

English

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publication date

16 April 2009

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published in

Nature

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volume

458

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page(s)

914-8

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issue

7240

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cites work

1 reference

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https://api.crossref.org/works/10.1038%2FNATURE07745

Host Determinant Residue Lysine 627 Lies on the Surface of a Discrete, Folded Domain of Influenza Virus Polymerase PB2 Subunit

21 January 2018

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https://api.crossref.org/works/10.1038%2FNATURE07745

Crystal structure of the archaeal holliday junction resolvase Hjc and implications for DNA recognition

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Thermofluor-based high-throughput stability optimization of proteins for structural studies

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The role of metals in catalysis by the restriction endonuclease BamHI

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The polymerase complex genes contribute to the high virulence of the human H5N1 influenza virus isolate A/Vietnam/1203/04.

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Recombinant influenza virus polymerase: requirement of both 5' and 3' viral ends for endonuclease activity

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Metal ion catalysis of RNA cleavage by the influenza virus endonuclease

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The structural basis for cap binding by influenza virus polymerase subunit PB2

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A novel antiviral agent which inhibits the endonuclease of influenza viruses

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Realm of PD-(D/E)XK nuclease superfamily revisited: detection of novel families with modified transitive meta profile searches

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Crucial role of CA cleavage sites in the cap-snatching mechanism for initiating viral mRNA synthesis

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Crystal structure of the polymerase PA(C)-PB1(N) complex from an avian influenza H5N1 virus

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Use of a pharmacophore model to discover a new class of influenza endonuclease inhibitors

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A unique cap(m7GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription

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Two aromatic residues in the PB2 subunit of influenza A RNA polymerase are crucial for cap binding

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Influenza A virus RNA polymerase subunit PB2 is the endonuclease which cleaves host cell mRNA and functions only as the trimeric enzyme

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The viral polymerase mediates adaptation of an avian influenza virus to a mammalian host.

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Amino acid residues in the N-terminal region of the PA subunit of influenza A virus RNA polymerase play a critical role in protein stability, endonuclease activity, cap binding, and virion RNA promoter binding

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RNA and DNA hydrolysis are catalyzed by the influenza virus endonuclease

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DNA cleavage by EcoRV endonuclease: two metal ions in three metal ion binding sites.

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Anti-influenza virus activities of 4-substituted 2,4-dioxobutanoic acid inhibitors

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The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits

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Structure of influenza virus RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to the solvent

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12 December 2020

A single amino acid mutation in the PA subunit of the influenza virus RNA polymerase inhibits endonucleolytic cleavage of capped RNAs

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12 December 2020

Minimum molecular architectures for transcription and replication of the influenza virus

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12 December 2020

Innate immunity induced by composition-dependent RIG-I recognition of hepatitis C virus RNA

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12 December 2020

The structural basis for an essential subunit interaction in influenza virus RNA polymerase

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12 December 2020

Structural basis for the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism

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https://api.crossref.org/works/10.1038%2FNATURE07745

7 January 2021

inferred from DOI database lookup

Definition of the minimal viral components required for the initiation of unprimed RNA synthesis by influenza virus RNA polymerase

1 reference

12 December 2020

Identifiers

DOI

10.1038/NATURE07745

1 reference

Consolidated OpenCitations Corpus – April 2017

Dimensions Publication ID

690760

1035637811

0 references

Fatcat ID

release_7ul4vz4sozezdbj6nmj36c6ge4

0 references

690760

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference