Phosphorylation of Human Metapneumovirus M2-1 Protein Upregulates Viral Replication and Pathogenesis. - Wikidata - wikimedia - TriplyDB

Phosphorylation of Human Metapneumovirus M2-1 Protein Upregulates Viral Replication and Pathogenesis.

Phosphorylation of Human Metapneumovirus M2-1 Protein Upregulates Viral Replication and Pathogenesis.

http://www.wikidata.org/entity/Q37174437

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Current developments and prospects on human metapneumovirus vaccines.RSV hijacks cellular protein phosphatase 1 to regulate M2-1 phosphorylation and viral transcription.Human Metapneumovirus: Mechanisms and Molecular Targets Used by the Virus to Avoid the Immune System Interferon-Mediated Response to Human Metapneumovirus Infection

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Phosphorylation of Human Metapneumovirus M2-1 Protein Upregulates Viral Replication and Pathogenesis.

http://www.wikidata.org/entity/Q37174437

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on June 2016

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Phosphorylation of Human Metap ...... Replication and Pathogenesis.

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Phosphorylation of Human Metap ...... Replication and Pathogenesis.

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type

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Phosphorylation of Human Metap ...... Replication and Pathogenesis.

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Phosphorylation of Human Metap ...... Replication and Pathogenesis.

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prefLabel

Phosphorylation of Human Metap ...... Replication and Pathogenesis.

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Phosphorylation of Human Metap ...... Replication and Pathogenesis.

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Journal of Virology

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Phosphorylation of Human Metap ...... Replication and Pathogenesis.

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Hui Cai

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Jianrong Li

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Mijia Lu

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Ryan Jennings

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Stefan Niewiesk

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Xueya Liang

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Yu Zhang

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P2860

Cloning and expression of the vesicular stomatitis virus phosphoprotein gene in Escherichia coli: analysis of phosphorylation status versus transcriptional activity

Human Metapneumovirus: lessons learned over the first decade

Structure and Functional Analysis of the RNA- and Viral Phosphoprotein-Binding Domain of Respiratory Syncytial Virus M2-1 Protein

Crystal structure of the essential transcription antiterminator M2-1 protein of human respiratory syncytial virus and implications of its phosphorylation

Drastic changes in conformational dynamics of the antiterminator M2-1 regulate transcription efficiency in Pneumovirinae

Newly identified phosphorylation site in the vesicular stomatitis virus P protein is required for viral RNA synthesis

Respiratory syncytial virus M2-1 protein requires phosphorylation for efficient function and binds viral RNA during infection

Transcription elongation factor of respiratory syncytial virus, a nonsegmented negative-strand RNA virus.

Phosphorylation of rabies virus nucleoprotein regulates viral RNA transcription and replication by modulating leader RNA encapsidation.

Production of infectious human respiratory syncytial virus from cloned cDNA confirms an essential role for the transcription elongation factor from the 5' proximal open reading frame of the M2 mRNA in gene expression and provides a capability for va

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7323-7338

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scholarly article

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10.1128/JVI.00755-16

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16

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90

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2016-06-01T00:00:00Z

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27252537

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phosphorylation

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