A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation.
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Anti-HIV-1 activity of cellulose acetate phthalate: synergy with soluble CD4 and induction of "dead-end" gp41 six-helix bundles.Herpesvirus gB: A Finely Tuned Fusion MachineFormation and characterization of the trimeric form of the fusion protein of Semliki Forest VirusThe Coronavirus Spike Protein Is a Class I Virus Fusion Protein: Structural and Functional Characterization of the Fusion Core ComplexStructural basis of viral invasion: lessons from paramyxovirus FCrystal structure of human T cell leukemia virus type 1 gp21 ectodomain crystallized as a maltose-binding protein chimera reveals structural evolution of retroviral transmembrane proteinsN- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coilInteractions between HIV-1 gp41 core and detergents and their implications for membrane fusionMutations that destabilize the gp41 core are determinants for stabilizing the simian immunodeficiency virus-CPmac envelope glycoprotein complexThe reovirus sigma1 aspartic acid sandwich: a trimerization motif poised for conformational changeThe Receptor-Binding Domain of Influenza Virus Hemagglutinin Produced in Escherichia coli Folds into Its Native, Immunogenic StructureComprehensive kinetic analysis of influenza hemagglutinin-mediated membrane fusion: role of sialate binding.The ectodomain of HIV-1 env subunit gp41 forms a soluble, alpha-helical, rod-like oligomer in the absence of gp120 and the N-terminal fusion peptideMolecular tectonic model of virus structural transitions: the putative cell entry states of poliovirusInfluenza hemagglutinin stem-fragment immunogen elicits broadly neutralizing antibodies and confers heterologous protectionDesign of an HA2-based Escherichia coli expressed influenza immunogen that protects mice from pathogenic challenge.The breadth of cross sub-type neutralisation activity of a single domain antibody to influenza hemagglutinin can be increased by antibody valency.Multi-epitope Models Explain How Pre-existing Antibodies Affect the Generation of Broadly Protective Responses to InfluenzaHuman Monoclonal Antibody 81.39a Effectively Neutralizes Emerging Influenza A Viruses of Group 1 and 2 HemagglutininsCross-Neutralising Nanobodies Bind to a Conserved Pocket in the Hemagglutinin Stem Region Identified Using Yeast Display and Deep Mutational Scanning.Design of Escherichia coli-expressed stalk domain immunogens of H1N1 hemagglutinin that protect mice from lethal challenge.Considering protonation as a posttranslational modification regulating protein structure and function.Specific single or double proline substitutions in the "spring-loaded" coiled-coil region of the influenza hemagglutinin impair or abolish membrane fusion activity.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 fragmentsVisualization and Sequencing of Membrane Remodeling Leading to Influenza Virus Fusion.Production and characterization of a soluble, active form of Tva, the subgroup A avian sarcoma and leukosis virus receptorSubdomain folding and biological activity of the core structure from human immunodeficiency virus type 1 gp41: implications for viral membrane fusion.The fusion-controlling disulfide bond isomerase in retrovirus Env is triggered by protein destabilization.Role of the specific amino acid sequence of the membrane-spanning domain of human immunodeficiency virus type 1 in membrane fusion.Control of biological activities of influenza virus hemagglutinin by its carbohydrate moiety.Proteolysis of monomeric recombinant rotavirus VP4 yields an oligomeric VP5* coreStructure of the uncleaved ectodomain of the paramyxovirus (hPIV3) fusion protein.Stalking influenza.Mutation-directed chemical cross-linking of human immunodeficiency virus type 1 gp41 oligomers.Order and disorder control the functional rearrangement of influenza hemagglutinin.The prefusogenic intermediate of HIV-1 gp41 contains exposed C-peptide regions.Morphological changes and fusogenic activity of influenza virus hemagglutinin.Delay 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.
P2860
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P2860
A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation.
description
1995 nî lūn-bûn
@nan
1995 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
A soluble domain of the membra ...... e low-pH-induced conformation.
@ast
A soluble domain of the membra ...... e low-pH-induced conformation.
@en
type
label
A soluble domain of the membra ...... e low-pH-induced conformation.
@ast
A soluble domain of the membra ...... e low-pH-induced conformation.
@en
prefLabel
A soluble domain of the membra ...... e low-pH-induced conformation.
@ast
A soluble domain of the membra ...... e low-pH-induced conformation.
@en
P2093
P2860
P356
P1476
A soluble domain of the membra ...... e low-pH-induced conformation.
@en
P2093
Hughson FM
Weissenhorn W
Wharton SA
P2860
P304
12205-12209
P356
10.1073/PNAS.92.26.12205
P407
P577
1995-12-01T00:00:00Z