Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin.
about
MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domainsDynamic Viral Glycoprotein Machines: Approaches for Probing Transient States That Drive Membrane FusionConformational reorganization of the SARS coronavirus spike following receptor binding: implications for membrane fusionEntry and uncoating of enveloped virusesStructures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeStructural Characterization of an Early Fusion Intermediate of Influenza Virus HemagglutininInfluenza Human Monoclonal Antibody 1F1 Interacts with Three Major Antigenic Sites and Residues Mediating Human Receptor Specificity in H1N1 VirusesA Potent Anti-influenza Compound Blocks Fusion through Stabilization of the Prefusion Conformation of the Hemagglutinin ProteinIntermonomer Interactions in Hemagglutinin Subunits HA1 and HA2 Affecting Hemagglutinin Stability and Influenza Virus InfectivitySynchronized activation and refolding of influenza hemagglutinin in multimeric fusion machinesSpecific single or double proline substitutions in the "spring-loaded" coiled-coil region of the influenza hemagglutinin impair or abolish membrane fusion activity.Activation of a retroviral membrane fusion protein: soluble receptor-induced liposome binding of the ALSV envelope glycoprotein.Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers.pH-induced conformational changes of membrane-bound influenza hemagglutinin and its effect on target lipid bilayers.Structural studies on membrane-embedded influenza hemagglutinin and its fragmentsReceptor-induced conformational changes in the SU subunit of the avian sarcoma/leukosis virus A envelope protein: implications for fusion activation.Structure-based identification of an inducer of the low-pH conformational change in the influenza virus hemagglutinin: irreversible inhibition of infectivity.Single event recording shows that docking onto receptor alters the kinetics of membrane fusion mediated by influenza hemagglutinin.Structural changes in Influenza virus at low pH characterized by cryo-electron tomographyDelay of influenza hemagglutinin refolding into a fusion-competent conformation by receptor binding: a hypothesisInvestigation of pathways for the low-pH conformational transition in influenza hemagglutinin.A point mutation in the binding subunit of a retroviral envelope protein arrests virus entry at hemifusion.Redox-triggered infection by disulfide-shackled human immunodeficiency virus type 1 pseudovirionsHuman immunodeficiency virus type 1 Env with an intersubunit disulfide bond engages coreceptors but requires bond reduction after engagement to induce fusionPhorbol ester-induced down modulation of tailless CD4 receptors requires prior binding of gp120 and suggests a role for accessory molecules.GPI- and transmembrane-anchored influenza hemagglutinin differ in structure and receptor binding activity.Reversible inhibition of fusion activity of a paramyxovirus fusion protein by an engineered disulfide bond in the membrane-proximal external region.Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion.Stabilization of TM trimer interactions during activation of moloney murine leukemia virus Env.Structure and stabilization of the Hendra virus F glycoprotein in its prefusion formMutations in or near the fusion peptide of the influenza virus hemagglutinin affect an antigenic site in the globular regionCharacterization of stable Chinese hamster ovary cells expressing wild-type, secreted, and glycosylphosphatidylinositol-anchored human immunodeficiency virus type 1 envelope glycoprotein.Modulation of the pH Stability of Influenza Virus Hemagglutinin: A Host Cell Adaptation Strategy.Generation of a water-soluble oligomeric ectodomain of the Rous sarcoma virus envelope glycoprotein.Protonation and stability of the globular domain of influenza virus hemagglutinin.A New Strategy to Reduce Influenza Escape: Detecting Therapeutic Targets Constituted of Invariance Groups.Dynamic changes during acid-induced activation of influenza hemagglutinin.A histidine residue of the influenza virus hemagglutinin controls the pH dependence of the conformational change mediating membrane fusion.Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.Influenza Hemagglutinin Protein Stability, Activation, and Pandemic Risk.
P2860
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P2860
Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin.
@ast
Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin.
@en
type
label
Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin.
@ast
Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin.
@en
prefLabel
Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin.
@ast
Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin.
@en
P2093
P2860
P1433
P1476
Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin
@en
P2093
P2860
P304
P407
P577
1992-08-01T00:00:00Z