Mapping the phosphoproteome of influenza A and B viruses by mass spectrometry. - Test2 - elhamkhani - TriplyDB

Mapping the phosphoproteome of influenza A and B viruses by mass spectrometry.

Mapping the phosphoproteome of influenza A and B viruses by mass spectrometry.

http://www.wikidata.org/entity/Q36384462

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Emerging roles for the influenza A virus nuclear export protein (NEP)Structure-based discovery of the novel antiviral properties of naproxen against the nucleoprotein of influenza A virus.Phosphorylation of Single Stranded RNA Virus Proteins and Potential for Novel Therapeutic Strategies Nucleocytoplasmic shuttling of influenza A virus proteins MAIT cells are activated during human viral infections Monomeric Nucleoprotein of Influenza A Virus Principles of Virus Uncoating: Cues and the Snooker Ball A Novel Antiviral Target Structure Involved in the RNA Binding, Dimerization, and Nuclear Export Functions of the Influenza A Virus Nucleoprotein Interactome analysis of the influenza A virus transcription/replication machinery identifies protein phosphatase 6 as a cellular factor required for efficient virus replication.Adaptation of avian influenza A virus polymerase in mammals to overcome the host species barrier Characterization of the nucleocytoplasmic shuttle of the matrix protein of influenza B virus Sumoylation of influenza A virus nucleoprotein is essential for intracellular trafficking and virus growth.Conserved and host-specific features of influenza virion architecture.Phosphorylation at the homotypic interface regulates nucleoprotein oligomerization and assembly of the influenza virus replication machinery Phosphorylation controls the nuclear-cytoplasmic shuttling of influenza A virus nucleoprotein Functional Constraint Profiling of a Viral Protein Reveals Discordance of Evolutionary Conservation and Functionality Tyrosine 132 phosphorylation of influenza A virus M1 protein is crucial for virus replication by controlling the nuclear import of M1.Transport of the influenza virus genome from nucleus to nucleus Ubiquitination up-regulates influenza virus polymerase function.Functional genomics approaches to understand cytomegalovirus replication, latency and pathogenesis.Influenza virus nucleoprotein: structure, RNA binding, oligomerization and antiviral drug target.At the centre: influenza A virus ribonucleoproteins.Phosphoproteomic analysis reveals the importance of kinase regulation during orbivirus infection.Phosphorylation of influenza A virus NS1 protein at threonine 49 suppresses its interferon antagonistic activity.Proteomics Tracing the Footsteps of Infectious Disease.An experimental evaluation of drug-induced mutational meltdown as an antiviral treatment strategy.Effect of Phosphorylation of CM2 Protein on Influenza C Virus Replication.Influenza virus recruits host protein kinase C to control assembly and activity of its replication machinery.Influenza A virus nucleoprotein targets subnuclear structures.Polycomb repressive complex 2 facilitates the nuclear export of the influenza viral genome through the interaction with M1.Phosphorylation of highly conserved serine residues in the influenza A virus nuclear export protein NEP plays a minor role in viral growth in human cells and mice.Threonine 80 phosphorylation of non-structural protein 1 regulates the replication of influenza A virus by reducing the binding affinity with RIG-I.Regulation of influenza A virus nucleoprotein oligomerization by phosphorylation In Silico Functional and Structural Characterization of H1N1 Influenza A Viruses Hemagglutinin, 2010-2013, Shiraz, Iran.Three-dimensional context rather than NLS amino acid sequence determines importin α subtype specificity for RCC1 Structural analysis of the complex between influenza B nucleoprotein and human importin-α.Histone Deacetylase 1 Plays an Acetylation-Independent Role in Influenza A Virus Replication.Phospholipid scramblase 1 interacts with influenza A virus NP, impairing its nuclear import and thereby suppressing virus replication.Amino acid substitutions affecting aspartic acid 605 and valine 606 decrease the interaction strength between the influenza virus RNA polymerase PB2 '627' domain and the viral nucleoprotein.Proteome-wide analysis of human motif-domain interactions mapped on influenza a virus.

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P2860

Mapping the phosphoproteome of influenza A and B viruses by mass spectrometry.

http://www.wikidata.org/entity/Q36384462

description

2012 nî lūn-bûn

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name

Mapping the phosphoproteome of influenza A and B viruses by mass spectrometry.

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Mapping the phosphoproteome of influenza A and B viruses by mass spectrometry.

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Mapping the phosphoproteome of influenza A and B viruses by mass spectrometry.

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Mapping the phosphoproteome of influenza A and B viruses by mass spectrometry.

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prefLabel

Mapping the phosphoproteome of influenza A and B viruses by mass spectrometry.

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Mapping the phosphoproteome of influenza A and B viruses by mass spectrometry.

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Mapping the phosphoproteome of influenza A and B viruses by mass spectrometry.

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Benjamin Thomas

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David C Trudgian

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Eleanor M Denham

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Gabriela Ridlova

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Lauren Turrell

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Svenja S Hester

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P2860

A probability-based approach for high-throughput protein phosphorylation analysis and site localization

Influenza B and C virus NEP (NS2) proteins possess nuclear export activities.

Leptomycin B-sensitive nuclear export of MAPKAP kinase 2 is regulated by phosphorylation

MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform

Evolution and ecology of influenza A viruses

Hemagglutinin receptor binding avidity drives influenza A virus antigenic drift

Jalview Version 2--a multiple sequence alignment editor and analysis workbench

Role of ran binding protein 5 in nuclear import and assembly of the influenza virus RNA polymerase complex

Combined results from solution studies on intact influenza virus M1 protein and from a new crystal form of its N-terminal domain show that M1 is an elongated monomer

The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA

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Edward C Hutchinson

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