Structural organization of a filamentous influenza A virus. - Wikidata - wikimedia - TriplyDB

Structural organization of a filamentous influenza A virus.

Structural organization of a filamentous influenza A virus.

http://www.wikidata.org/entity/Q30495070

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Virion architecture unifies globally distributed pleolipoviruses infecting halophilic archaea Dynamic Viral Glycoprotein Machines: Approaches for Probing Transient States That Drive Membrane Fusion The organisation of Ebola virus reveals a capacity for extensive, modular polyploidy Cryotomography of budding influenza A virus reveals filaments with diverse morphologies that mostly do not bear a genome at their distal end A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins Receptor binding by a ferret-transmissible H5 avian influenza virus Viral membrane fusion.Compounds with anti-influenza activity: present and future of strategies for the optimal treatment and management of influenza. Part I: Influenza life-cycle and currently available drugs Residue 41 of the Eurasian avian-like swine influenza a virus matrix protein modulates virion filament length and efficiency of contact transmission Specific residues in the 2009 H1N1 swine-origin influenza matrix protein influence virion morphology and efficiency of viral spread in vitro Structure and accessibility of HA trimers on intact 2009 H1N1 pandemic influenza virus to stem region-specific neutralizing antibodies Influenza viral membrane fusion is sensitive to sterol concentration but surprisingly robust to sterol chemical identity.Distinct functional determinants of influenza hemagglutinin-mediated membrane fusion Critical assessment of influenza VLP production in Sf9 and HEK293 expression systems.The M segment of the 2009 new pandemic H1N1 influenza virus is critical for its high transmission efficiency in the guinea pig model Cross-reactive humoral responses to influenza and their implications for a universal vaccine.Architecture of respiratory syncytial virus revealed by electron cryotomography.Visualization and Sequencing of Membrane Remodeling Leading to Influenza Virus Fusion.How cells tune viral mechanics--insights from biophysical measurements of influenza virus.Assembly, maturation and three-dimensional helical structure of the teratogenic rubella virus.Biological activities of 'noninfectious' influenza A virus particles A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein.Structural changes in Influenza virus at low pH characterized by cryo-electron tomography Dissection of influenza A virus M1 protein: pH-dependent oligomerization of N-terminal domain and dimerization of C-terminal domain Effect of envelope proteins on the mechanical properties of influenza virus Distribution of surface glycoproteins on influenza A virus determined by electron cryotomography.The compensatory G88R change is essential in restoring the normal functions of influenza A/WSN/33 virus matrix protein 1 with a disrupted nuclear localization signal.Filament-producing mutants of influenza A/Puerto Rico/8/1934 (H1N1) virus have higher neuraminidase activities than the spherical wild-type.An in vitro network of intermolecular interactions between viral RNA segments of an avian H5N2 influenza A virus: comparison with a human H3N2 virus.Bending and puncturing the influenza lipid envelope.Stepwise priming by acidic pH and a high K+ concentration is required for efficient uncoating of influenza A virus cores after penetration.At low pH, influenza virus matrix protein M1 undergoes a conformational change prior to dissociating from the membrane.Influenza virus assembly and budding.Interaction of NS2 with AIMP2 facilitates the switch from ubiquitination to SUMOylation of M1 in influenza A virus-infected cells.Structural analysis of influenza A virus matrix protein M1 and its self-assemblies at low pH.Morphology of influenza B/Lee/40 determined by cryo-electron microscopy Nothing to sneeze at: a dynamic and integrative computational model of an influenza A virion.From high symmetry to high resolution in biological electron microscopy: a commentary on Crowther (1971) 'Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs'Crystal structures of influenza A virus matrix protein M1: variations on a theme Electron cryotomography of measles virus reveals how matrix protein coats the ribonucleocapsid within intact virions.

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P2860

Structural organization of a filamentous influenza A virus.

http://www.wikidata.org/entity/Q30495070

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2010 nî lūn-bûn

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2010 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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Structural organization of a filamentous influenza A virus.

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Structural organization of a filamentous influenza A virus.

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Structural organization of a filamentous influenza A virus.

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Structural organization of a filamentous influenza A virus.

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John A Berriman

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Lesley J Calder

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Peter B Rosenthal

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Sebastian Wasilewski

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P2860

Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding

The structure of a biologically active influenza virus ribonucleoprotein complex

N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coil

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

Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2)

Crystal structures of oseltamivir-resistant influenza virus neuraminidase mutants

Structure of influenza haemagglutinin at the pH of membrane fusion

Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin

Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion.

3D structure of the influenza virus polymerase complex: localization of subunit domains.

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