Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: analysis by proton nuclear magnetic resonance spectroscopy and X-ray crystallography
about
Interspecies and intraspecies transmission of triple reassortant H3N2 influenza A virusesCombining mutual information with structural analysis to screen for functionally important residues in influenza hemagglutininPeramivir: A Novel Intravenous Neuraminidase Inhibitor for Treatment of Acute Influenza InfectionsDynamic Viral Glycoprotein Machines: Approaches for Probing Transient States That Drive Membrane FusionViruses and sialic acids: rules of engagementConformational reorganization of the SARS coronavirus spike following receptor binding: implications for membrane fusionImage Restoration and Analysis of Influenza Virions Binding to Membrane Receptors Reveal Adhesion-Strengthening KineticsAn unusual carbohydrate binding site revealed by the structures of two Maackia amurensis lectins complexed with sialic acid-containing oligosaccharidesX-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogsStructure, Receptor Binding, and Antigenicity of Influenza Virus Hemagglutinins from the 1957 H2N2 PandemicStructural basis for receptor specificity of influenza B virus hemagglutininBluetongue virus coat protein VP2 contains sialic acid-binding domains, and VP5 resembles enveloped virus fusion proteins.Structure and Receptor binding properties of a pandemic H1N1 virus hemagglutininMolecular Mechanisms of Inhibition of Influenza by Surfactant Protein D Revealed by Large-Scale Molecular Dynamics SimulationCarbohydrate recognition mechanism of HA70 from Clostridium botulinum deduced from X-ray structures in complexes with sialylated oligosaccharidesCrystal structure of the ligand-binding domain of the receptor tyrosine kinase EphB2Co- and Post-Translational Protein Folding in the ERRecognition of microbial glycans by human intelectin-1The anti-influenza virus agent 4-GU-DANA (zanamivir) inhibits cell fusion mediated by human parainfluenza virus and influenza virus HA.A sialic acid binding site in a human picornavirusAureonitol, a Fungi-Derived Tetrahydrofuran, Inhibits Influenza Replication by Targeting Its Surface Glycoprotein HemagglutininDesign of an HA2-based Escherichia coli expressed influenza immunogen that protects mice from pathogenic challenge.Infection of human airway epithelium by human and avian strains of influenza a virus.Shotgun glycomics of pig lung identifies natural endogenous receptors for influenza viruses.Role of viral hemagglutinin glycosylation in anti-influenza activities of recombinant surfactant protein DCo-evolution positions and rules for antigenic variants of human influenza A/H3N2 viruses.Analysis of hemagglutinin-mediated entry tropism of H5N1 avian influenza.Distinct glycan topology for avian and human sialopentasaccharide receptor analogues upon binding different hemagglutinins: a molecular dynamics perspective.Hemagglutinin Sequence Conservation Guided Stem Immunogen Design from Influenza A H3 SubtypeMutagenesis of surfactant protein D informed by evolution and x-ray crystallography enhances defenses against influenza A virus in vivoMolecular-level simulation of pandemic influenza glycoproteins.Clusters of charged residues in protein three-dimensional structuresH5N1 receptor specificity as a factor in pandemic riskSynchronized activation and refolding of influenza hemagglutinin in multimeric fusion machinesInfluenza virus binds its host cell using multiple dynamic interactions.Influenza A virus hemagglutinin and neuraminidase act as novel motile machinerySabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans.The surface glycoproteins of H5 influenza viruses isolated from humans, chickens, and wild aquatic birds have distinguishable properties.Molecular mechanisms of serum resistance of human influenza H3N2 virus and their involvement in virus adaptation in a new host.Influenza A viruses lacking sialidase activity can undergo multiple cycles of replication in cell culture, eggs, or mice.
P2860
Q21245134-1CAA6F19-1B00-43CF-975F-168BD6468457Q24657504-3FBF117D-D5EA-49F2-8E51-55EB219C3F15Q26749578-022285A8-0DB7-4937-AD47-D99B768D0E96Q26772129-B50BAD8A-0CA9-4C76-B9FF-1E099EFD356EQ26852325-9FBC6C67-20A6-438E-A1A1-67FCB4219378Q27302420-8E73E139-D328-4A77-8ED1-9B72A5C69508Q27321503-CFEFEF21-B9C0-48CB-90FA-B856F10BB239Q27622064-F7B3E9A6-DB1C-41CD-A893-CB0F7BDB7DBDQ27634875-AAE63C05-687D-4C08-863B-DC0E336F3A21Q27646580-D9016B08-FE10-41E7-8C99-5AAAE8FB6407Q27648813-0D03BAB0-DB30-44D4-B148-7DD2C44ACF4AQ27660311-5F8D6F5F-BFC8-474F-A8C3-ACB0A2B40445Q27660366-4747A78E-57CF-498B-95D2-6C334FCF9DA8Q27680598-C9A3246A-B075-4246-B46F-71EAAF209BC0Q27681065-F9C548A8-966C-447F-9CCF-502B672E0495Q27766349-B4C76C65-8F00-4A88-B262-0F2C372A4EBBQ28078736-37DB59F4-F1FE-43E6-9F54-B2F2B655AB9BQ28118757-A0F388F3-313D-4050-83D4-0BF982A37879Q28344907-5A5F8B31-F76C-46D0-8046-9D50EA45F3D8Q28543886-32CEAC2F-7E64-40FC-86E1-DDA95AD3AC68Q28550191-9EA21314-4360-491D-89CC-671042C03179Q30227081-366261A6-5725-437F-9D53-8050300E7F34Q30355972-04DA5FB0-D736-4D46-874E-7DF03B09C6EDQ30362721-711E4DE9-93FB-4975-A90D-95A5E4B4B537Q30372223-39282807-9B5A-4E49-8CA8-A6F5A8A14541Q30374869-CF927F4C-2C6F-420C-8C79-254E2C8925D1Q30375938-E9B43662-E4CC-4FB0-8A71-18429C3EF304Q30376058-00A93A15-A3CC-4B22-8FE7-F4EAED4745C2Q30376605-21880D79-A7C5-44C5-AC5E-288E9D3F3A03Q30407670-DEC24CB0-9742-497F-9BA9-07C355B4B4E3Q30410858-04595F30-23F3-4A5C-B9C5-25F86AFDBBA9Q30424416-428010D1-29C8-4DC5-B0C7-452B7B0A4E1EQ30429803-B1BFC32C-587C-43B9-9C3C-7D709FD121CBQ30441948-AA675837-2478-4431-B5C6-E3419C8A340CQ30524354-13714743-618B-4D1A-8345-DEA7A77D9B1FQ30842920-2DCB6CAC-E20B-48F1-84EC-DA0A1CC61B52Q33264403-47404152-56FB-4647-971B-CA4AEEF6BBF9Q33640697-D3BC38C4-F69B-460F-96B6-8C4138D730F6Q33783336-79B6D582-C93E-4AAE-A641-1C6228E1792FQ33787108-9E33A4DF-A2BF-429D-9FF8-A0781C1B09B3
P2860
Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: analysis by proton nuclear magnetic resonance spectroscopy and X-ray crystallography
description
1992 nî lūn-bûn
@nan
1992 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年学术文章
@wuu
1992年学术文章
@zh-cn
1992年学术文章
@zh-hans
1992年学术文章
@zh-my
1992年学术文章
@zh-sg
1992年學術文章
@yue
name
Binding of influenza virus hem ...... copy and X-ray crystallography
@ast
Binding of influenza virus hem ...... copy and X-ray crystallography
@en
Binding of influenza virus hem ...... copy and X-ray crystallography
@nl
type
label
Binding of influenza virus hem ...... copy and X-ray crystallography
@ast
Binding of influenza virus hem ...... copy and X-ray crystallography
@en
Binding of influenza virus hem ...... copy and X-ray crystallography
@nl
prefLabel
Binding of influenza virus hem ...... copy and X-ray crystallography
@ast
Binding of influenza virus hem ...... copy and X-ray crystallography
@en
Binding of influenza virus hem ...... copy and X-ray crystallography
@nl
P2093
P3181
P356
P1433
P1476
Binding of influenza virus hem ...... copy and X-ray crystallography
@en
P2093
J E Hanson
J J Skehel
N K Sauter
R L Crowther
P304
P3181
P356
10.1021/BI00155A013
P407
P577
1992-10-13T00:00:00Z