Structural analysis of influenza A virus matrix protein M1 and its self-assemblies at low pH. - Wikidata - wikimedia - TriplyDB

Structural analysis of influenza A virus matrix protein M1 and its self-assemblies at low pH.

Structural analysis of influenza A virus matrix protein M1 and its self-assemblies at low pH.

http://www.wikidata.org/entity/Q35072754

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Drug resistance in influenza A virus: the epidemiology and management.Broad Spectrum Anti-Influenza Agents by Inhibiting Self-Association of Matrix Protein 1.Involvement of an Arginine Triplet in M1 Matrix Protein Interaction with Membranes and in M1 Recruitment into Virus-Like Particles of the Influenza A(H1N1)pdm09 Virus.Crystal structures of influenza A virus matrix protein M1: variations on a theme Mutations Designed by Ensemble Defect to Misfold Conserved RNA Structures of Influenza A Segments 7 and 8 Affect Splicing and Attenuate Viral Replication in Cell Culture Two polar residues within C-terminal domain of M1 are critical for the formation of influenza A Virions.pH-Dependent Formation and Disintegration of the Influenza A Virus Protein Scaffold To Provide Tension for Membrane Fusion The Matrix protein M1 from influenza C virus induces tubular membrane invaginations in an in vitro cell membrane model.Crystal structure of an orthomyxovirus matrix protein reveals mechanisms for self-polymerization and membrane association.Isolated Potato Virus A coat protein possesses unusual properties and forms different short virus-like particles.Amphipathic secondary structure elements and putative cholesterol recognizing amino acid consensus (CRAC) motifs as governing factors of highly specific matrix protein interactions with raft-type membranes in enveloped viruses.Influenza A matrix protein M1 multimerizes upon binding to lipid membranes.Co-evolution analysis to predict protein-protein interactions within influenza virus envelope.Maintaining pH-dependent conformational flexibility of M1 is critical for efficient influenza A virus replication.Influenza virus Matrix Protein M1 preserves its conformation with pH, changing multimerization state at the priming stage due to electrostatics.Mutations in the Influenza A virus M1 protein enhance virus budding to complement lethal mutations in the M2 cytoplasmic tail.Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae.Small-Angle Scattering of Neutrons and X-Rays

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P2860

Structural analysis of influenza A virus matrix protein M1 and its self-assemblies at low pH.

http://www.wikidata.org/entity/Q35072754

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2013 nî lūn-bûn

@nan

2013 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

Structural analysis of influen ...... its self-assemblies at low pH.

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Structural analysis of influen ...... its self-assemblies at low pH.

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type

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Structural analysis of influen ...... its self-assemblies at low pH.

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Structural analysis of influen ...... its self-assemblies at low pH.

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Structural analysis of influen ...... its self-assemblies at low pH.

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Structural analysis of influen ...... its self-assemblies at low pH.

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JOURNAL.PONE.0082431

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Structural analysis of influen ...... its self-assemblies at low pH.

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Alexander V Shishkov

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Alexey A Dolgov

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Liudmila A Shilova

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Lyudmila A Baratova

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Natalia V Fedorova

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Victor A Radyukhin

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Vladimir V Volkov

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P2860

Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing

Determination of domain structure of proteins from X-ray solution scattering

Global rigid body modeling of macromolecular complexes against small-angle scattering data

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

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

Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1

Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling

Nuclear traffic of influenza virus proteins and ribonucleoprotein complexes.

New developments in the ATSAS program package for small-angle scattering data analysis

Structural characterization of flexible proteins using small-angle X-ray scattering

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e82431

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scholarly article

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10.1371/JOURNAL.PONE.0082431

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12

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8

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Oleg V. Batishchev

Eleonora Shtykova

Alexander Ksenofontov

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2013-12-16T00:00:00Z

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259395987

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24358182

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3865061

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