Membrane structures of the hemifusion-inducing fusion peptide mutant G1S and the fusion-blocking mutant G1V of influenza virus hemagglutinin suggest a mechanism for pore opening in membrane fusion.
about
Membrane Mediated Antimicrobial and Antitumor Activity of Cathelicidin 6: Structural Insights from Molecular Dynamics Simulation on Multi-Microsecond ScaleStructures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeThe complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interfaceShallow boomerang-shaped influenza hemagglutinin G13A mutant structure promotes leaky membrane fusion.Structure and function of the complete internal fusion loop from Ebolavirus glycoprotein 2.Fusion of Enveloped Viruses in Endosomes.Viral membrane fusion.Membrane Fusion and Infection of the Influenza Hemagglutinin.Role of sequence and structure of the Hendra fusion protein fusion peptide in membrane fusion.Molecular basis of the structure and function of H1 hemagglutinin of influenza virus.Fusion activity of HIV gp41 fusion domain is related to its secondary structure and depth of membrane insertion in a cholesterol-dependent fashion.Lipid tail protrusion in simulations predicts fusogenic activity of influenza fusion peptide mutants and conformational modelsFusion peptide of influenza hemagglutinin requires a fixed angle boomerang structure for activity.Combined NMR and EPR spectroscopy to determine structures of viral fusion domains in membranes.Transmembrane orientation and possible role of the fusogenic peptide from parainfluenza virus 5 (PIV5) in promoting fusionConformation and lipid interaction of the fusion peptide of the paramyxovirus PIV5 in anionic and negative-curvature membranes from solid-state NMR.The three lives of viral fusion peptidesHow could SNARE proteins open a fusion pore?Line-tension controlled mechanism for influenza fusion.Ensemble molecular dynamics yields submillisecond kinetics and intermediates of membrane fusionThiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus fusion protein.The influenza fusion peptide adopts a flexible flat V conformation in membranes.The Interaction between Influenza HA Fusion Peptide and Transmembrane Domain Affects Membrane StructureMutagenesis and nuclear magnetic resonance analyses of the fusion peptide of Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus F protein.Identification of the Fusion Peptide-Containing Region in Betacoronavirus Spike GlycoproteinsFusing simulation and experiment: The effect of mutations on the structure and activity of the influenza fusion peptideThe influenza hemagglutinin fusion domain is an amphipathic helical hairpin that functions by inducing membrane curvature.NMR structures of fusion peptide from influenza hemagglutinin H3 subtype and its mutants.The influenza fusion peptide promotes lipid polar head intrusion through hydrogen bonding with phosphates and N-terminal membrane insertion depth.Wild-type and mutant hemagglutinin fusion peptides alter bilayer structure as well as kinetics and activation thermodynamics of stalk and pore formation differently: mechanistic implications.The helical hairpin structure of the influenza fusion peptide can be seen on a hydrophobic moment map.Analysis of a membrane interacting region of herpes simplex virus type 1 glycoprotein H.Switching between Successful and Dead-End Intermediates in Membrane Fusion.Influenza Hemifusion Phenotype Depends on Membrane Context: Differences in Cell-Cell and Virus-Cell Fusion.
P2860
Q27335132-86E3A035-105A-490A-9321-E06B6052870BQ27487974-1F28015D-2EC5-412B-B8BC-F4F5C6D751F6Q27662151-0C2F363C-9761-43AB-8DDA-913924ED9FFAQ27664386-4EE3F12B-185F-4299-AEDE-5224E4E721A2Q27670489-D9C92287-912D-4162-A617-27D172C3CFD6Q28073406-A3C132E9-5D1F-4A08-BEAF-E8DFE155CA33Q28080422-7D9A95C5-29A5-4E5D-8180-04424002BF18Q30396401-7B253447-A2E7-4F8E-90AA-298422207ADFQ30417577-6F86F8E6-7509-4818-A638-0F509EFE8371Q30418463-894D3576-41A4-495E-80EF-85BD19ACBBA7Q30419302-610A0B21-7A6D-452F-BFF7-EF90D4808CF4Q30421918-A5323DF3-ED7B-4AAC-98C6-1A9464C8F507Q30439209-DD359D3D-6884-463B-B80D-C458A39540FBQ30443827-FCB942D6-0DBB-4686-A673-E4F40D386581Q30498517-A9B5F747-97D0-44D0-945E-24ED4E0EEA1DQ30734301-B5A9F788-2581-40AC-B6B0-631320658FDCQ33770459-1F023AF2-B838-471B-930B-F9B0E5091DE3Q33918609-DB556D26-5B10-406F-ABAB-49C7138DEC9FQ34325691-407055A6-CA85-4618-B830-4BB34229D34DQ35033090-CECB5D74-5C19-4AE9-AACC-D8D0A8B1426FQ35784690-59F56945-BE27-44AD-839F-C45CBAE38F3AQ35962567-9A2A25E2-925C-47AA-A6AD-D6190909B329Q36426451-F0BAF101-E9C6-4616-991E-5011B81A8046Q36845665-D406A716-CB5A-4662-91F8-AB278ED98950Q36950903-A06D20DB-CEF1-4C1B-8CE1-1AD9E3885010Q37006176-2BC6F927-8FCB-43FF-98A5-4D57C0885385Q41660440-4BCF259B-7B87-4EED-A871-5DAA1FE11CCCQ42228463-F87C1EB0-0AD8-4170-A101-E80E6C2973A4Q42229093-394DF3B9-32F3-405F-8A74-3B9A6EC8AC91Q42250651-0D5AD48F-DCDE-40C8-99AA-D1FF46B4E650Q42284023-6BB879BC-7C68-4889-BB5D-8456992F5556Q42736704-04C84964-031C-4363-A4B5-129EAB361CF9Q47281813-0EA3173C-37D1-4BF5-8994-D358DDFA6498Q47550631-A7E48ADF-07E9-4542-8080-857C72063672
P2860
Membrane structures of the hemifusion-inducing fusion peptide mutant G1S and the fusion-blocking mutant G1V of influenza virus hemagglutinin suggest a mechanism for pore opening in membrane fusion.
description
2005 nî lūn-bûn
@nan
2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Membrane structures of the hem ...... re opening in membrane fusion.
@ast
Membrane structures of the hem ...... re opening in membrane fusion.
@en
type
label
Membrane structures of the hem ...... re opening in membrane fusion.
@ast
Membrane structures of the hem ...... re opening in membrane fusion.
@en
prefLabel
Membrane structures of the hem ...... re opening in membrane fusion.
@ast
Membrane structures of the hem ...... re opening in membrane fusion.
@en
P2093
P2860
P1433
P1476
Membrane structures of the hem ...... re opening in membrane fusion.
@en
P2093
Alex L Lai
David S Cafiso
Lukas K Tamm
Yinling Li
P2860
P304
12065-12076
P356
10.1128/JVI.79.18.12065-12076.2005
P577
2005-09-01T00:00:00Z