Structure and topology of the influenza virus fusion peptide in lipid bilayers.
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Mutational analysis of the subgroup A avian sarcoma and leukosis virus putative fusion peptide domain.The impact of influenza hemagglutinin fusion peptide length and viral subtype on its structure and dynamicsImplicit solvent model studies of the interactions of the influenza hemagglutinin fusion peptide with lipid bilayers.Interaction of synthetic HA2 influenza fusion peptide analog with model membranesA host-guest system to study structure-function relationships of membrane fusion peptides.Membrane Fusion and Infection of the Influenza Hemagglutinin.A bundling of viral fusion mechanisms.Effect of the N-terminal glycine on the secondary structure, orientation, and interaction of the influenza hemagglutinin fusion peptide with lipid bilayers.Transmembrane orientation and possible role of the fusogenic peptide from parainfluenza virus 5 (PIV5) in promoting fusionStructure of an analog of fusion peptide from hemagglutinin.Structure and membrane interaction of the internal fusion peptide of avian sarcoma leukosis virus.Properties and structures of the influenza and HIV fusion peptides on lipid membranes: implications for a role in fusionThe amino-terminal region of the fusion peptide of influenza virus hemagglutinin HA2 inserts into sodium dodecyl sulfate micelle with residues 16-18 at the aqueous boundary at acidic pH. Oligomerization and the conformational flexibility.Atypical fusion peptide of Nelson Bay virus fusion-associated small transmembrane proteinThe three lives of viral fusion peptidesA mechanism of protein-mediated fusion: coupling between refolding of the influenza hemagglutinin and lipid rearrangements.Orientation of the pore-forming peptide GALA in POPC vesicles determined by a BODIPY-avidin/biotin binding assay.15N NMR study of the ionization properties of the influenza virus fusion peptide in zwitterionic phospholipid dispersions.Modulation of membrane curvature by peptides.Bilayer conformation of fusion peptide of influenza virus hemagglutinin: a molecular dynamics simulation study.Conformation of the synaptobrevin transmembrane domainWhole-body rocking motion of a fusion peptide in lipid bilayers from size-dispersed 15N NMR relaxationModeling a spin-labeled fusion peptide in a membrane: implications for the interpretation of EPR experimentsThe influenza fusion peptide adopts a flexible flat V conformation in membranes.Structural and functional properties of an unusual internal fusion peptide in a nonenveloped virus membrane fusion protein.Functional peptides for siRNA delivery.Functional implications of the human T-lymphotropic virus type 1 transmembrane glycoprotein helical hairpin structure.Modification of the cytoplasmic domain of influenza virus hemagglutinin affects enlargement of the fusion pore.Quantitation of secondary structure in ATR infrared spectroscopy.Membrane structure of the human immunodeficiency virus gp41 fusion domain by molecular dynamics simulation.The presence of a single N-terminal histidine residue enhances the fusogenic properties of a Membranotropic peptide derived from herpes simplex virus type 1 glycoprotein H.Relationship of membrane sidedness to the effects of the lipophosphoglycan of Leishmania donovani on the fusion of influenza virus.Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy.What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion (review).The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment.Determination of molecular order in supported lipid membranes by internal reflection Fourier transform infrared spectroscopy.Permeabilization and fusion of uncharged lipid vesicles induced by the HIV-1 fusion peptide adopting an extended conformation: dose and sequence effects.Multiple membrane interactions and versatile vesicle deformations elicited by melittin.Structural characterizations of fusion peptide analogs of influenza virus hemagglutinin. Implication of the necessity of a helix-hinge-helix motif in fusion activity.Domain V of m-calpain shows the potential to form an oblique-orientated alpha-helix, which may modulate the enzyme's activity via interactions with anionic lipid.
P2860
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P2860
Structure and topology of the influenza virus fusion peptide in lipid bilayers.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
Structure and topology of the influenza virus fusion peptide in lipid bilayers.
@en
Structure and topology of the influenza virus fusion peptide in lipid bilayers.
@nl
type
label
Structure and topology of the influenza virus fusion peptide in lipid bilayers.
@en
Structure and topology of the influenza virus fusion peptide in lipid bilayers.
@nl
prefLabel
Structure and topology of the influenza virus fusion peptide in lipid bilayers.
@en
Structure and topology of the influenza virus fusion peptide in lipid bilayers.
@nl
P2093
P2860
P356
P1476
Structure and topology of the influenza virus fusion peptide in lipid bilayers.
@en
P2093
Herrmann A
Lüneberg J
Ruysschaert JM
P2860
P304
27606-27614
P356
10.1074/JBC.270.46.27606
P407
P577
1995-11-01T00:00:00Z