Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin.
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IFITM proteins restrict viral membrane hemifusion.Fusion of Rous sarcoma virus with host cells does not require exposure to low pHRole of the integrin-associated protein CD9 in binding between sperm ADAM 2 and the egg integrin alpha6beta1: implications for murine fertilization.Dynamic Viral Glycoprotein Machines: Approaches for Probing Transient States That Drive Membrane FusionAn epitope of the Semliki Forest virus fusion protein exposed during virus-membrane fusion.Conformational changes and fusion activity of influenza virus hemagglutinin of the H2 and H3 subtypes: effects of acid pretreatmentStructures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeStructural Characterization of an Early Fusion Intermediate of Influenza Virus HemagglutininMembrane fusion mechanisms: the influenza hemagglutinin paradigm and its implications for intracellular fusion.Fusion of Enveloped Viruses in Endosomes.Comprehensive kinetic analysis of influenza hemagglutinin-mediated membrane fusion: role of sialate binding.Characterization of potent fusion inhibitors of influenza virusStructural features of membrane fusion between influenza virus and liposome as revealed by quick-freezing electron microscopyThe transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transitionEvidence of human-to-swine transmission of the pandemic (H1N1) 2009 influenza virus in South Korea.The transmembrane domain and acidic lipid flip-flop regulates voltage-dependent fusion mediated by class II and III viral proteins.Synchronized 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.The pathway of membrane fusion catalyzed by influenza hemagglutinin: restriction of lipids, hemifusion, and lipidic fusion pore formation.Activation of a retroviral membrane fusion protein: soluble receptor-induced liposome binding of the ALSV envelope glycoprotein.GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes.pH-induced conformational changes of membrane-bound influenza hemagglutinin and its effect on target lipid bilayers.The receptor for the subgroup A avian leukosis-sarcoma viruses binds to subgroup A but not to subgroup C envelope glycoprotein.Structure-based identification of an inducer of the low-pH conformational change in the influenza virus hemagglutinin: irreversible inhibition of infectivity.New insights into the spring-loaded conformational change of influenza virus hemagglutinin.Reversible stages of the low-pH-triggered conformational change in influenza virus hemagglutinin.Substitutions in the receptor-binding domain of the avian sarcoma and leukosis virus envelope uncouple receptor-triggered structural rearrangements in the surface and transmembrane subunitsArchitecture of a nascent viral fusion pore.Visualization and Sequencing of Membrane Remodeling Leading to Influenza Virus Fusion.Inhibition of influenza A virus replication by compounds interfering with the fusogenic function of the viral hemagglutininpH-dependent insertion of proteins into membranes: B-chain mutation of diphtheria toxin that inhibits membrane translocation, Glu-349----LysStructural intermediates in influenza haemagglutinin-mediated fusion.Biochemical and structural characterization of cathepsin L-processed Ebola virus glycoprotein: implications for viral entry and immunogenicityConformational intermediates and fusion activity of influenza virus hemagglutinin.The structure of a membrane fusion mutant of the influenza virus haemagglutinin.Intermediates in influenza induced membrane fusion.Single event recording shows that docking onto receptor alters the kinetics of membrane fusion mediated by influenza hemagglutinin.Membrane fusion of Semliki Forest virus in a model system: correlation between fusion kinetics and structural changes in the envelope glycoprotein.Structural changes in Influenza virus at low pH characterized by cryo-electron tomographyMorphological changes and fusogenic activity of influenza virus hemagglutinin.
P2860
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P2860
Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin.
description
1987 nî lūn-bûn
@nan
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
1987年论文
@zh
1987年论文
@zh-cn
name
Anti-peptide antibodies detect ...... influenza virus hemagglutinin.
@ast
Anti-peptide antibodies detect ...... influenza virus hemagglutinin.
@en
type
label
Anti-peptide antibodies detect ...... influenza virus hemagglutinin.
@ast
Anti-peptide antibodies detect ...... influenza virus hemagglutinin.
@en
prefLabel
Anti-peptide antibodies detect ...... influenza virus hemagglutinin.
@ast
Anti-peptide antibodies detect ...... influenza virus hemagglutinin.
@en
P2860
P356
P1476
Anti-peptide antibodies detect ...... influenza virus hemagglutinin.
@en
P2093
P2860
P304
P356
10.1083/JCB.105.6.2887
P407
P433
P577
1987-12-01T00:00:00Z