The lipid-anchored ectodomain of influenza virus hemagglutinin (GPI-HA) is capable of inducing nonenlarging fusion pores
about
Transmembrane peptides stabilize inverted cubic phases in a biphasic length-dependent manner: implications for protein-induced membrane fusion.Herpesvirus gB: A Finely Tuned Fusion MachineCell entry of enveloped virusesImaging single retrovirus entry through alternative receptor isoforms and intermediates of virus-endosome fusionIFITM3 restricts influenza A virus entry by blocking the formation of fusion pores following virus-endosome hemifusionStructures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeStudies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics.Comprehensive kinetic analysis of influenza hemagglutinin-mediated membrane fusion: role of sialate binding.Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusionThe transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transitionReevaluating herpes simplex virus hemifusion.Sequential roles of receptor binding and low pH in forming prehairpin and hairpin conformations of a retroviral envelope glycoproteinCholesterol promotes hemifusion and pore widening in membrane fusion induced by influenza hemagglutinin.Imaging individual retroviral fusion events: from hemifusion to pore formation and growth.Transmembrane orientation and possible role of the fusogenic peptide from parainfluenza virus 5 (PIV5) in promoting fusionDeletion of the cytoplasmic tail of the fusion protein of the paramyxovirus simian virus 5 affects fusion pore enlargement.The fusion pores of Ca2+ -triggered exocytosisTime-resolved imaging of HIV-1 Env-mediated lipid and content mixing between a single virion and cell membrane.Evolution of intermediates of influenza virus hemagglutinin-mediated fusion revealed by kinetic measurements of pore formation.Structural and functional roles of HIV-1 gp41 pretransmembrane sequence segmentation.Class I and class II viral fusion protein structures reveal similar principles in membrane fusion.A point mutation in the binding subunit of a retroviral envelope protein arrests virus entry at hemifusion.A point mutation in the transmembrane domain of the hemagglutinin of influenza virus stabilizes a hemifusion intermediate that can transit to fusion.The final conformation of the complete ectodomain of the HA2 subunit of influenza hemagglutinin can by itself drive low pH-dependent fusionHIV-1 envelope proteins complete their folding into six-helix bundles immediately after fusion pore formationReovirus FAST protein transmembrane domains function in a modular, primary sequence-independent manner to mediate cell-cell membrane fusion.Progressive truncations C terminal to the membrane-spanning domain of simian immunodeficiency virus Env reduce fusogenicity and increase concentration dependence of Env for fusion.Beyond anchoring: the expanding role of the hendra virus fusion protein transmembrane domain in protein folding, stability, and function.The energetics of membrane fusion from binding, through hemifusion, pore formation, and pore enlargement.Paramyxovirus fusion and entry: multiple paths to a common endTransition from hemifusion to pore opening is rate limiting for vacuole membrane fusionClose is not enough: SNARE-dependent membrane fusion requires an active mechanism that transduces force to membrane anchorsAnionic lipids are required for vesicular stomatitis virus G protein-mediated single particle fusion with supported lipid bilayersMechanics of membrane fusion.Nanodisc-cell fusion: control of fusion pore nucleation and lifetimes by SNARE protein transmembrane domains.Common principles and intermediates of viral protein-mediated fusion: the HIV-1 paradigm.Modification of the cytoplasmic domain of influenza virus hemagglutinin affects enlargement of the fusion pore.Functional analysis of the transmembrane (TM) domain of the Autographa californica multicapsid nucleopolyhedrovirus GP64 protein: substitution of heterologous TM domains.The gaussian curvature elastic modulus of N-monomethylated dioleoylphosphatidylethanolamine: relevance to membrane fusion and lipid phase behavior.Membrane fusion by single influenza hemagglutinin trimers. Kinetic evidence from image analysis of hemagglutinin-reconstituted vesicles.
P2860
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P2860
The lipid-anchored ectodomain of influenza virus hemagglutinin (GPI-HA) is capable of inducing nonenlarging fusion pores
description
2000 nî lūn-bûn
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2000 թուականի Ապրիլին հրատարակուած գիտական յօդուած
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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name
The lipid-anchored ectodomain ...... cing nonenlarging fusion pores
@ast
The lipid-anchored ectodomain ...... cing nonenlarging fusion pores
@en
type
label
The lipid-anchored ectodomain ...... cing nonenlarging fusion pores
@ast
The lipid-anchored ectodomain ...... cing nonenlarging fusion pores
@en
prefLabel
The lipid-anchored ectodomain ...... cing nonenlarging fusion pores
@ast
The lipid-anchored ectodomain ...... cing nonenlarging fusion pores
@en
P2093
P2860
P356
P1476
The lipid-anchored ectodomain ...... cing nonenlarging fusion pores
@en
P2093
G B Melikyan
R M Markosyan
P2860
P304
P356
10.1091/MBC.11.4.1143
P577
2000-04-01T00:00:00Z