Fusion of influenza hemagglutinin-expressing fibroblasts with glycophorin-bearing liposomes: role of hemagglutinin surface density.
about
Inhibition of human immunodeficiency virus type 1 infectivity by the gp41 core: role of a conserved hydrophobic cavity in membrane fusionComprehensive kinetic analysis of influenza hemagglutinin-mediated membrane fusion: role of sialate binding.The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transitionInduction of Cell-Cell Fusion by Ebola Virus Glycoprotein: Low pH Is Not a TriggerSynchronized activation and refolding of influenza hemagglutinin in multimeric fusion machinesDilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41Inner but not outer membrane leaflets control the transition from glycosylphosphatidylinositol-anchored influenza hemagglutinin-induced hemifusion to full fusionMembrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers.Tension of membranes expressing the hemagglutinin of influenza virus inhibits fusion.Stoichiometry of envelope glycoprotein trimers in the entry of human immunodeficiency virus type 1Receptor-triggered membrane association of a model retroviral glycoprotein.Architecture of a nascent viral fusion pore.Biophysical characterization of the structure of the amino-terminal region of gp41 of HIV-1. Implications on viral fusion mechanism.Visualization and Sequencing of Membrane Remodeling Leading to Influenza Virus Fusion.Mode of action of an antiviral peptide from HIV-1. Inhibition at a post-lipid mixing stage.Inhibition of influenza A virus replication by compounds interfering with the fusogenic function of the viral hemagglutininMembrane fusion promoted by increasing surface densities of the paramyxovirus F and HN proteins: comparison of fusion reactions mediated by simian virus 5 F, human parainfluenza virus type 3 F, and influenza virus HA.Role of the cytoplasmic tail of ecotropic moloney murine leukemia virus Env protein in fusion pore formation.Role of hemagglutinin surface density in the initial stages of influenza virus fusion: lack of evidence for cooperativityMutations within the putative membrane-spanning domain of the simian immunodeficiency virus transmembrane glycoprotein define the minimal requirements for fusion, incorporation, and infectivity.Poly(ethylene glycol) (PEG)-mediated fusion between pure lipid bilayers: a mechanism in common with viral fusion and secretory vesicle release?Intermediates in influenza induced membrane fusion.Intermediates and kinetics of membrane fusion.Morphological changes and fusogenic activity of influenza virus hemagglutinin.Polymorphism and interactions of a viral fusion peptide in a compressed lipid monolayer.Delay of influenza hemagglutinin refolding into a fusion-competent conformation by receptor binding: a hypothesisKinetically differentiating influenza hemagglutinin fusion and hemifusion machines.Oligomerization of fusogenic peptides promotes membrane fusion by enhancing membrane destabilizationDynamic clustered distribution of hemagglutinin resolved at 40 nm in living cell membranes discriminates between raft theories.DC-SIGN and influenza hemagglutinin dynamics in plasma membrane microdomains are markedly different.Heterogeneity of early intermediates in cell-liposome fusion mediated by influenza hemagglutinin.Stochastic fusion simulations and experiments suggest passive and active roles of hemagglutinin during membrane fusion.Superresolution imaging of multiple fluorescent proteins with highly overlapping emission spectra in living cells.Cell entry by measles virus: long hybrid receptors uncouple binding from membrane fusionMolecular mechanism underlying the action of a novel fusion inhibitor of influenza A virusRestricted movement of lipid and aqueous dyes through pores formed by influenza hemagglutinin during cell fusion.Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events.Membrane fusion mediated by baculovirus gp64 involves assembly of stable gp64 trimers into multiprotein aggregates.Quantitative electron microscopy and fluorescence spectroscopy of the membrane distribution of influenza hemagglutinin.Intrinsic temperature sensitivity of influenza C virus hemagglutinin-esterase-fusion protein.
P2860
Q27619600-403BF444-E5E4-425E-935C-72D461E0AAB3Q28346181-CB7A9BE2-FDA7-4399-84F2-22FC80E1F67AQ30306248-ED35F655-894E-4E89-8E24-019F1D2E8C3CQ30361292-802DDDA2-2ADD-4F1B-9E89-01A69EB8D8BEQ30441948-81FCA599-24D9-4178-BDEA-5EE85AA0A858Q30442126-DE638293-CE03-49B8-AE18-B4E007A29029Q30442161-F9A58C3E-FEE1-4CE1-84C7-54801A3B2328Q30442203-372A62F9-CBD7-4D2E-B865-6C52477DBA22Q30447504-AFEAE343-0BC3-4B9A-9A97-8DF20ED8C717Q30447936-BAB492E2-EE77-469D-BECF-D2FD0D876FE2Q30454419-D1A676F9-27F8-432A-BC81-312AA12C62B2Q30494174-A093701A-C78C-460C-AFB6-8FE403344ADEQ30558462-2DD652DD-0EFF-4850-A172-736648EA3BCDQ30784849-66823D61-0508-4403-9219-6CC4D565F735Q31454800-E68F9698-261F-4045-999A-83392ECD179FQ31957799-16805C36-B55A-43CD-B464-F82F4342B6EAQ33784602-6B07193B-78F6-4F41-9529-9DA7C1A0B5C3Q33795219-8FE7AED9-95B0-49D4-9DCD-1CF3DD7FD05CQ33799995-DE7D18D1-E3F3-4FF4-9647-4A4EC5F03CADQ33846366-A2D688F3-C058-4848-8219-A7CF9E1BDDC6Q33892321-382CA720-7172-4D65-9819-C973B111A7BAQ33923518-EF2BC7D5-7B00-417D-BA93-5979E7116616Q34091600-0DB250C9-1DDF-41B3-9C0F-349EEF5436B8Q34166993-7E17FC42-519A-44E5-B5C9-71C9ED77A7B3Q34170662-61967437-1D04-45EE-866B-88F834EECB7BQ34173865-3F23FFA4-F059-4F5A-A368-5A693D027C45Q34182690-87FAA238-BFC0-4731-AAC3-510CA989C0E3Q34184290-5E2CC470-09ED-42FA-B153-7DF05E6018CBQ34706566-AF95E823-DCB6-4A07-AA36-AB11DC3FF7DBQ35051220-57101B90-655A-4CDC-B0A1-52E90E6EDADBQ35095839-08CDB18C-0A01-45E2-9CB4-1A1C1AE2170BQ35100328-130B0A35-004C-49AE-8945-A35BE0F469A5Q35224045-8457C4B1-B7FA-4826-AF2B-E10E4F58BCFAQ35861422-AE5179FA-F979-4C92-96D2-0ABAE9FAE08EQ35884171-5554C6B6-DAD0-4182-B5A5-A42D4789C420Q36234971-BD572031-71C8-42DD-B815-3F9E37E88161Q36237488-CA37840F-75A7-4B28-A156-39C3945F161BQ36256359-108B8773-8775-46FC-AEF5-34B438787C97Q36321226-4DF85751-F162-41F5-98A0-C4BEF3944FB9Q36397490-AF4DB590-4690-41FC-95DB-EF4A7E15F7DF
P2860
Fusion of influenza hemagglutinin-expressing fibroblasts with glycophorin-bearing liposomes: role of hemagglutinin surface density.
description
1990 nî lūn-bûn
@nan
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
1990年论文
@zh
1990年论文
@zh-cn
name
Fusion of influenza hemaggluti ...... hemagglutinin surface density.
@en
type
label
Fusion of influenza hemaggluti ...... hemagglutinin surface density.
@en
prefLabel
Fusion of influenza hemaggluti ...... hemagglutinin surface density.
@en
P2093
P356
P1433
P1476
Fusion of influenza hemaggluti ...... hemagglutinin surface density.
@en
P2093
P304
P356
10.1021/BI00493A027
P407
P577
1990-10-01T00:00:00Z