Control of baculovirus gp64-induced syncytium formation by membrane lipid composition
about
Membrane fusion and the lamellar-to-inverted-hexagonal phase transition in cardiolipin vesicle systems induced by divalent cationsInteraction of the Most Membranotropic Region of the HCV E2 Envelope Glycoprotein with Membranes. Biophysical CharacterizationInner but not outer membrane leaflets control the transition from glycosylphosphatidylinositol-anchored influenza hemagglutinin-induced hemifusion to full fusionFusion-pore expansion during syncytium formation is restricted by an actin networkPersistent gene expression in mouse nasal epithelia following feline immunodeficiency virus-based vector gene transfer.The hemifusion intermediate and its conversion to complete fusion: regulation by membrane composition.Membrane fusion promoters and inhibitors have contrasting effects on lipid bilayer structure and undulationsEvolution of intermediates of influenza virus hemagglutinin-mediated fusion revealed by kinetic measurements of pore formation.The baculovirus GP64 protein mediates highly stable infectivity of a human respiratory syncytial virus lacking its homologous transmembrane glycoproteinsThe final conformation of the complete ectodomain of the HA2 subunit of influenza hemagglutinin can by itself drive low pH-dependent fusionProgressive 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.Baculovirus GP64-mediated entry into mammalian cellsAn early stage of membrane fusion mediated by the low pH conformation of influenza hemagglutinin depends upon membrane lipids.Membrane fusion mediated by baculovirus gp64 involves assembly of stable gp64 trimers into multiprotein aggregates.The initial fusion pore induced by baculovirus GP64 is large and forms quicklyFusion peptide from influenza hemagglutinin increases membrane surface order: an electron-spin resonance studyMaturation of the Gag core decreases the stability of retroviral lipid membranes.SARS-CoV fusion peptides induce membrane surface ordering and curvature.Palmitoylation of the Autographa californica multicapsid nucleopolyhedrovirus envelope glycoprotein GP64: mapping, functional studies, and lipid rafts.The GP64 envelope fusion protein is an essential baculovirus protein required for cell-to-cell transmission of infectionThe influence of lysolipids on the spontaneous curvature and bending elasticity of phospholipid membranes.Mapping the conformational epitope of a neutralizing antibody (AcV1) directed against the AcMNPV GP64 protein.Evidence that rabies virus forms different kinds of fusion machines with different pH thresholds for fusion.Positive reinforcement for viruses.Effect of membrane curvature-modifying lipids on membrane fusion by tick-borne encephalitis virus.Measurement of membrane fusion activity from viral membrane fusion proteins based on a fusion-dependent promoter induction system in insect cells.Lysophosphatidylcholine reversibly arrests pore expansion during syncytium formation mediated by diverse viral fusogens.Ligand-directed gene targeting to mammalian cells by pseudotype baculoviruses.
P2860
Q24537308-3164B41C-F4BA-423F-8CCE-D71AC1E4F9C8Q27486157-7FD8BED8-075C-42D6-999F-70C712CAA618Q30442161-5898FF02-A122-4638-B7B2-31D0F3FFE0B9Q30532780-649ADD67-8CBE-489D-9B72-4C20A1F191DAQ34045671-DF41812C-9522-4CA6-A297-C4C0D8DC0C88Q34047180-22A0131D-20EB-4CAD-A73B-998163A1E1DBQ34170247-5DFD399E-EBBB-4CD5-9026-327BA11F471CQ34174969-16A408FA-FAF4-44CC-81BF-F530950BBC87Q34553841-68253930-5052-4907-8A41-E5FDF374D28CQ34787116-8BBF51E4-652F-4DB6-9D6D-0B2A616887C9Q35020532-02BCAD0F-B8C4-4905-B13B-32B3D4498831Q35549868-5B0AD4F4-A93B-4D6A-9B3C-542DC38697FAQ35826077-6D327A03-A340-4FFE-B28D-FDC9D13D9E83Q36254482-D3ED38AA-FCB3-4A2C-AB42-1A20D6F9BEFDQ36256359-C82AC296-6B42-45B4-BC51-254A43898119Q36257699-819387DB-8619-414C-9360-34A0932277CCQ37265364-28EBBF0F-65D4-4699-AD13-662779522A39Q37359745-E72AC02C-AF3A-45C7-BAFA-180F8E78DC66Q37444357-982C7438-E7F6-461E-9557-6D3A493D3217Q39752634-066014C6-590D-4B69-ADF0-3A8C24C623EBQ39875210-5E6B8163-B2FB-4D89-A38F-3B6D7C263595Q40185940-4A7C852D-2F5A-47AC-91EF-D7ACBCFBE383Q40267475-E409566D-CD35-4258-BF96-F7C78AE0EC07Q40530753-A969A89A-8C12-4236-9ADD-0287AE80E4CEQ41139167-4D4A6D83-45C7-4C9C-A000-49BB37FD19F3Q41275686-8FEC7A52-A956-49E7-B860-3AF0D1E1514AQ41867210-9127AEF9-3A3F-41D3-BEF3-8032D6E5F999Q42228826-E3962486-BE2C-4770-8806-797E5954B55FQ42716737-ADE243C6-489B-4C04-A550-FA00E50028BA
P2860
Control of baculovirus gp64-induced syncytium formation by membrane lipid composition
description
1995 nî lūn-bûn
@nan
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
1995年论文
@zh
1995年论文
@zh-cn
name
Control of baculovirus gp64-induced syncytium formation by membrane lipid composition
@ast
Control of baculovirus gp64-induced syncytium formation by membrane lipid composition
@en
type
label
Control of baculovirus gp64-induced syncytium formation by membrane lipid composition
@ast
Control of baculovirus gp64-induced syncytium formation by membrane lipid composition
@en
prefLabel
Control of baculovirus gp64-induced syncytium formation by membrane lipid composition
@ast
Control of baculovirus gp64-induced syncytium formation by membrane lipid composition
@en
P2093
P2860
P1433
P1476
Control of baculovirus gp64-induced syncytium formation by membrane lipid composition
@en
P2093
J Zimmerberg
L Chernomordik
P2860
P304
P407
P577
1995-05-01T00:00:00Z