N-linked glycosylation attenuates H3N2 influenza viruses. - Test2 - elhamkhani - TriplyDB

N-linked glycosylation attenuates H3N2 influenza viruses.

N-linked glycosylation attenuates H3N2 influenza viruses.

http://www.wikidata.org/entity/Q35947697

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Serum amyloid P is a sialylated glycoprotein inhibitor of influenza A viruses Connecting the study of wild influenza with the potential for pandemic disease Innate immunity to influenza virus: implications for future therapy Recognition of Mannosylated Ligands and Influenza A Virus by Human Surfactant Protein D: Contributions of an Extended Site and Residue 343 † , ‡Molecular Mechanisms of Inhibition of Influenza by Surfactant Protein D Revealed by Large-Scale Molecular Dynamics Simulation Structure and receptor binding preferences of recombinant human A(H3N2) virus hemagglutinins Elucidating the mechanisms of influenza virus recognition by Ncr1 Evolution of H3N2 influenza virus in a guinea pig model Playing hide and seek: how glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection.Molecular determinants of influenza virus pathogenesis in mice.Influenza A(H1N1)pdm09 resistance and cross-decreased susceptibility to oseltamivir and zanamivir antiviral drugs.Role of viral hemagglutinin glycosylation in anti-influenza activities of recombinant surfactant protein D Acute Lung Injury Results from Innate Sensing of Viruses by an ER Stress Pathway Glycans on influenza hemagglutinin affect receptor binding and immune response The effects of influenza A virus PB1-F2 protein on polymerase activity are strain specific and do not impact pathogenesis Does Glycosylation as a modifier of Original Antigenic Sin explain the case age distribution and unusual toxicity in pandemic novel H1N1 influenza?Neuraminidase Activity and Resistance of 2009 Pandemic H1N1 Influenza Virus to Antiviral Activity in Bronchoalveolar Fluid PB1-F2 proteins from H5N1 and 20 century pandemic influenza viruses cause immunopathology.Glycosylation changes in the globular head of H3N2 influenza hemagglutinin modulate receptor binding without affecting virus virulence Glycan shielding of the influenza virus hemagglutinin contributes to immunopathology in mice.Recent H3N2 Viruses Have Evolved Specificity for Extended, Branched Human-type Receptors, Conferring Potential for Increased Avidity.Pandemic influenza 1918 H1N1 and 1968 H3N2 DNA vaccines induce cross-reactive immunity in ferrets against infection with viruses drifted for decades.The ability of pandemic influenza virus hemagglutinins to induce lower respiratory pathology is associated with decreased surfactant protein D binding Preventing and treating secondary bacterial infections with antiviral agents Mutagenesis of surfactant protein D informed by evolution and x-ray crystallography enhances defenses against influenza A virus in vivo Impaired wound healing predisposes obese mice to severe influenza virus infection.Molecular and antigenic characterization of reassortant H3N2 viruses from turkeys with a unique constellation of pandemic H1N1 internal genes.A novel pathogenic mechanism of highly pathogenic avian influenza H5N1 viruses involves hemagglutinin mediated resistance to serum innate inhibitors.Immunodominance of antigenic site B over site A of hemagglutinin of recent H3N2 influenza viruses.N-linked glycosylation in the hemagglutinin of influenza A viruses.Glycosylations in the globular head of the hemagglutinin protein modulate the virulence and antigenic properties of the H1N1 influenza viruses Fatal cases of influenza A(H3N2) in children: insights from whole genome sequence analysis.Changing selective pressure during antigenic changes in human influenza H3.The Length of N-Glycans of Recombinant H5N1 Hemagglutinin Influences the Oligomerization and Immunogenicity of Vaccine Antigen Dynamics of glycoprotein charge in the evolutionary history of human influenza Strength and tempo of selection revealed in viral gene genealogies.Glycosylation site alteration in the evolution of influenza A (H1N1) viruses.Characterization of Variations in PB2, NS1, M, Neuraminidase and Hemagglutinin of Influenza A (H3N2) Viruses in Iran Monoclonal antibody-assisted structure-function analysis of the carbohydrate recognition domain of surfactant protein D Molecular characterization of influenza viruses collected from young children in Uberlandia, Brazil - from 2001 to 2010.

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P2860

N-linked glycosylation attenuates H3N2 influenza viruses.

http://www.wikidata.org/entity/Q35947697

description

2007 nî lūn-bûn

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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2007年论文

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2007年论文

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name

N-linked glycosylation attenuates H3N2 influenza viruses.

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N-linked glycosylation attenuates H3N2 influenza viruses.

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type

label

N-linked glycosylation attenuates H3N2 influenza viruses.

@ast

N-linked glycosylation attenuates H3N2 influenza viruses.

@en

prefLabel

N-linked glycosylation attenuates H3N2 influenza viruses.

@ast

N-linked glycosylation attenuates H3N2 influenza viruses.

@en

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Journal of Virology

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N-linked glycosylation attenuates H3N2 influenza viruses.

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David J Vigerust

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Jens Madsen

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Kelli L Boyd

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Kimberly B Ulett

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Samuel Hawgood

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P2860

Role of N-linked glycans in the functions of hepatitis C virus envelope glycoproteins.

N-Linked Glycosylation of West Nile Virus Envelope Proteins Influences Particle Assembly and Infectivity

West Nile Virus Discriminates between DC-SIGN and DC-SIGNR for Cellular Attachment and Infection

N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin.

Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution

Collectins and pulmonary innate immunity

Studies of the structure of lung surfactant protein SP-A

Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus

Porcine pulmonary collectins show distinct interactions with influenza A viruses: role of the N-linked oligosaccharides in the carbohydrate recognition domain.

Pathogenicity of influenza viruses with genes from the 1918 pandemic virus: functional roles of alveolar macrophages and neutrophils in limiting virus replication and mortality in mice

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8593-8600

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10.1128/JVI.00769-07

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16

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81

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Jonathan A McCullers

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