The glycosylation of the influenza A virus hemagglutinin by mammalian cells. A site-specific study.
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Diversifying Selection Analysis Predicts Antigenic Evolution of 2009 Pandemic H1N1 Influenza A Virus in Humans.Dengue virus type 1 nonstructural glycoprotein NS1 is secreted from mammalian cells as a soluble hexamer in a glycosylation-dependent fashionThiazolides, a new class of anti-influenza molecules targeting viral hemagglutinin at the post-translational levelEvolution of H3N2 influenza virus in a guinea pig modelThe Galalpha1,3Galbeta1,4GlcNAc-R (alpha-Gal) epitope: a carbohydrate of unique evolution and clinical relevanceAirborne transmission of influenza A/H5N1 virus between ferretsRecent avian H5N1 viruses exhibit increased propensity for acquiring human receptor specificity.Entry Inhibition of Influenza Viruses with High Mannose Binding Lectin ESA-2 from the Red Alga Eucheuma serra through the Recognition of Viral HemagglutininInfluenza antivirals currently in late-phase clinical trial.High mannose-binding lectin with preference for the cluster of alpha1-2-mannose from the green alga Boodlea coacta is a potent entry inhibitor of HIV-1 and influenza viruses.Molecular basis of the structure and function of H1 hemagglutinin of influenza virus.All-atom ensemble modeling to analyze small-angle x-ray scattering of glycosylated proteins.Vaccination against influenza with recombinant hemagglutinin expressed by Schizochytrium sp. confers protective immunity.Effect of hemagglutinin glycosylation on influenza virus susceptibility to neuraminidase inhibitors.Glycosylation focuses sequence variation in the influenza A virus H1 hemagglutinin globular domain.Dynamics of glycoprotein charge in the evolutionary history of human influenzaPrediction of biological functions on glycosylation site migrations in human influenza H1N1 virusesHigh mannose-binding antiviral lectin PFL from Pseudomonas fluorescens Pf0-1 promotes cell death of gastric cancer cell MKN28 via interaction with α2-integrinStructural basis for influence of viral glycans on ligand binding by influenza hemagglutinin.N-linked glycosylation attenuates H3N2 influenza viruses.Comparative characterization of the glycosylation profiles of an influenza hemagglutinin produced in plant and insect hostsEndoplasmic reticulum chaperones are involved in the morphogenesis of rotavirus infectious particles.Protein-lipid interactions critical to replication of the influenza A virus.Structural insights into key sites of vulnerability on HIV-1 Env and influenza HA.A Novel High-Mannose Specific Lectin from the Green Alga Halimeda renschii Exhibits a Potent Anti-Influenza Virus Activity through High-Affinity Binding to the Viral Hemagglutinin.Human follicular lymphoma cells contain oligomannose glycans in the antigen-binding site of the B-cell receptor.Topological N-glycosylation and site-specific N-glycan sulfation of influenza proteins in the highly expressed H1N1 candidate vaccinesNew insights into influenza A specificity: an evolution of paradigms.Dengue Virus Glycosylation: What Do We Know?Sulphation of N-linked oligosaccharides of vesicular stomatitis and influenza virus envelope glycoproteins: host cell specificity, subcellular localization and identification of substituted saccharidesIn Silico Functional and Structural Characterization of H1N1 Influenza A Viruses Hemagglutinin, 2010-2013, Shiraz, Iran.Guiding the immune response against influenza virus hemagglutinin toward the conserved stalk domain by hyperglycosylation of the globular head domainEvidence for N-glycan shielding of antigenic sites during evolution of human influenza A virus hemagglutininSynthesis and Membrane-Binding Properties of a Characteristic Lipopeptide from the Membrane-Anchoring Domain of Influenza Virus A Hemagglutinin This research was supported by the Deutsche Forschungsgemeinschaft and the Fonds der Chemischen IndustrieAnimal Cell Expression Systems.Site-specific glycosylation profile of influenza A (H1N1) hemagglutinin through tandem mass spectrometry.Detailed functional characterization of glycosylated and nonglycosylated variants of malaria vaccine candidate PfAMA1 produced in Nicotiana benthamiana and analysis of growth inhibitory responses in rabbits.
P2860
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P2860
The glycosylation of the influenza A virus hemagglutinin by mammalian cells. A site-specific study.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
The glycosylation of the influ ...... cells. A site-specific study.
@en
type
label
The glycosylation of the influ ...... cells. A site-specific study.
@en
prefLabel
The glycosylation of the influ ...... cells. A site-specific study.
@en
P2093
P2860
P356
P1476
The glycosylation of the influ ...... cells. A site-specific study.
@en
P2093
Ashford DA
Mir-Shekari SY
Schulze IT
P2860
P304
P356
10.1074/JBC.272.7.4027
P407
P577
1997-02-01T00:00:00Z