The initial fusion pore induced by baculovirus GP64 is large and forms quickly
about
Visualizing fusion of pseudotyped HIV-1 particles in real time by live cell microscopy.The broad anti-viral agent glycyrrhizin directly modulates the fluidity of plasma membrane and HIV-1 envelopeEffects of membrane potential and sphingolipid structures on fusion of Semliki Forest virus.Viral membrane fusionThe postfusion structure of baculovirus gp64 supports a unified view of viral fusion machinesInvasive podosomes and myoblast fusion.The anti-influenza virus agent 4-GU-DANA (zanamivir) inhibits cell fusion mediated by human parainfluenza virus and influenza virus HA.Induction of Cell-Cell Fusion by Ebola Virus Glycoprotein: Low pH Is Not a TriggerCholesterol promotes hemifusion and pore widening in membrane fusion induced by influenza hemagglutinin.Synchronized activation and refolding of influenza hemagglutinin in multimeric fusion machinesThe pathway of membrane fusion catalyzed by influenza hemagglutinin: restriction of lipids, hemifusion, and lipidic fusion pore formation.Genetic control of fusion pore expansion in the epidermis of Caenorhabditis elegans.Fusion-pore expansion during syncytium formation is restricted by an actin networkElectron tomography of the contact between T cells and SIV/HIV-1: implications for viral entry.Rabies virus-induced membrane fusion.Role of the cytoplasmic tail of ecotropic moloney murine leukemia virus Env protein in fusion pore formation.A GP64-null baculovirus pseudotyped with vesicular stomatitis virus G proteinNegative potentials across biological membranes promote fusion by class II and class III viral proteinsPersistent gene expression in mouse nasal epithelia following feline immunodeficiency virus-based vector gene transfer.Fusion pore conductance: experimental approaches and theoretical algorithms.Hemifusion between cells expressing hemagglutinin of influenza virus and planar membranes can precede the formation of fusion pores that subsequently fully enlargeMembrane permeability changes at early stages of influenza hemagglutinin-mediated fusion.A study of low pH-induced refolding of Env of avian sarcoma and leukosis virus into a six-helix bundle.Furin is involved in baculovirus envelope fusion protein activation.An invasive podosome-like structure promotes fusion pore formation during myoblast fusion.The baculovirus GP64 protein mediates highly stable infectivity of a human respiratory syncytial virus lacking its homologous transmembrane glycoproteinsProgressive truncations C terminal to the membrane-spanning domain of simian immunodeficiency virus Env reduce fusogenicity and increase concentration dependence of Env for fusion.Intracellular curvature-generating proteins in cell-to-cell fusion.Membrane fusion mediated by baculovirus gp64 involves assembly of stable gp64 trimers into multiprotein aggregates.Class II fusion protein of alphaviruses drives membrane fusion through the same pathway as class I proteins.Rabies virus-induced membrane fusion pathway.Flickering fusion pores comparable with initial exocytotic pores occur in protein-free phospholipid bilayers.Initial size and dynamics of viral fusion pores are a function of the fusion protein mediating membrane fusionA discrete stage of baculovirus GP64-mediated membrane fusion.Nanodisc-cell fusion: control of fusion pore nucleation and lifetimes by SNARE protein transmembrane domains.Autographa californica multiple nucleopolyhedrovirus GP64 protein: roles of histidine residues in triggering membrane fusion and fusion pore expansion.Functional analysis of the Autographa californica multiple nucleopolyhedrovirus GP64 terminal fusion loops and interactions with membranesBaculovirus infection of nondividing mammalian cells: mechanisms of entry and nuclear transport of capsids.The pre-transmembrane domain of the Autographa californica multicapsid nucleopolyhedrovirus GP64 protein is critical for membrane fusion and virus infectivity.The Autographa californica multicapsid nucleopolyhedrovirus GP64 protein: analysis of transmembrane domain length and sequence requirements
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P2860
The initial fusion pore induced by baculovirus GP64 is large and forms quickly
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
The initial fusion pore induced by baculovirus GP64 is large and forms quickly
@ast
The initial fusion pore induced by baculovirus GP64 is large and forms quickly
@en
type
label
The initial fusion pore induced by baculovirus GP64 is large and forms quickly
@ast
The initial fusion pore induced by baculovirus GP64 is large and forms quickly
@en
prefLabel
The initial fusion pore induced by baculovirus GP64 is large and forms quickly
@ast
The initial fusion pore induced by baculovirus GP64 is large and forms quickly
@en
P2860
P356
P1476
The initial fusion pore induced by baculovirus GP64 is large and forms quickly
@en
P2093
Zimmerberg J
P2860
P304
P356
10.1083/JCB.135.6.1831
P407
P433
P577
1996-12-01T00:00:00Z