The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface
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A highly conserved neutralizing epitope on group 2 influenza A virusesDisulfide-stabilized Helical Hairpin Structure and Activity of a Novel Antifungal Peptide EcAMP1 from Seeds of Barnyard Grass (Echinochloa crus-galli)Structure and function of the complete internal fusion loop from Ebolavirus glycoprotein 2.pH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMRSolution NMR Structure and Functional Analysis of the Integral Membrane Protein YgaP from Escherichia coliViral membrane fusion.The impact of influenza hemagglutinin fusion peptide length and viral subtype on its structure and dynamicsInhibition of influenza A virus infection in vitro by peptides designed in silicoReovirus FAST Proteins Drive Pore Formation and Syncytiogenesis Using a Novel Helix-Loop-Helix Fusion-Inducing Lipid Packing SensorOptimal Bicelle Size q for Solution NMR Studies of the Protein Transmembrane PartitionAn algorithm to enumerate all possible protein conformations verifying a set of distance constraintsCross-Neutralising Nanobodies Bind to a Conserved Pocket in the Hemagglutinin Stem Region Identified Using Yeast Display and Deep Mutational Scanning.Membrane Fusion and Infection of the Influenza Hemagglutinin.The use of residual dipolar coupling in studying proteins by NMR.Membrane protein structure and dynamics from NMR spectroscopy.Role of sequence and structure of the Hendra fusion protein fusion peptide in membrane fusion.Plasma membrane localization of Solanum tuberosum remorin from group 1, homolog 3 is mediated by conformational changes in a novel C-terminal anchor and required for the restriction of potato virus X movement].Lipid tail protrusion in simulations predicts fusogenic activity of influenza fusion peptide mutants and conformational modelsA bundling of viral fusion mechanisms.Transmembrane orientation and possible role of the fusogenic peptide from parainfluenza virus 5 (PIV5) in promoting fusionMembrane-dependent conformation, dynamics, and lipid interactions of the fusion peptide of the paramyxovirus PIV5 from solid-state NMRDetermining the depth of insertion of dynamically invisible membrane peptides by gel-phase ¹H spin diffusion heteronuclear correlation NMR.Conformation and lipid interaction of the fusion peptide of the paramyxovirus PIV5 in anionic and negative-curvature membranes from solid-state NMR.Viral fusion protein transmembrane domain adopts β-strand structure to facilitate membrane topological changes for virus-cell fusion.The three lives of viral fusion peptidesHelical hairpin structure of influenza hemagglutinin fusion peptide stabilized by charge-dipole interactions between the N-terminal amino group and the second helix.Transferring the PRIMO Coarse-Grained Force Field to the Membrane Environment: Simulations of Membrane Proteins and Helix-Helix Association.Modeling of the endosomolytic activity of HA2-TAT peptides with red blood cells and ghosts.Hemagglutinin fusion peptide mutants in model membranes: structural properties, membrane physical properties, and PEG-mediated fusionWhole-body rocking motion of a fusion peptide in lipid bilayers from size-dispersed 15N NMR relaxationREDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins.Cell-cell membrane fusion induced by p15 fusion-associated small transmembrane (FAST) protein requires a novel fusion peptide motif containing a myristoylated polyproline type II helix.Closed and Semiclosed Interhelical Structures in Membrane vs Closed and Open Structures in Detergent for the Influenza Virus Hemagglutinin Fusion Peptide and Correlation of Hydrophobic Surface Area with Fusion CatalysisThe influenza fusion peptide adopts a flexible flat V conformation in membranes.Assembly of Influenza Hemagglutinin Fusion Peptides in a Phospholipid Bilayer by Coarse-grained Computer Simulations.Mapping the phosphoproteome of influenza A and B viruses by mass spectrometry.Full-length trimeric influenza virus hemagglutinin II membrane fusion protein and shorter constructs lacking the fusion peptide or transmembrane domain: Hyperthermostability of the full-length protein and the soluble ectodomain and fusion peptide maThe Interaction between Influenza HA Fusion Peptide and Transmembrane Domain Affects Membrane StructureInfluenza-virus membrane fusion by cooperative fold-back of stochastically induced hemagglutinin intermediates.Modulating alignment of membrane proteins in liquid-crystalline and oriented gel media by changing the size and charge of phospholipid bicelles.
P2860
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P2860
The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
The complete influenza hemaggl ...... t at the lipid:water interface
@ast
The complete influenza hemaggl ...... t at the lipid:water interface
@en
The complete influenza hemaggl ...... t at the lipid:water interface
@nl
type
label
The complete influenza hemaggl ...... t at the lipid:water interface
@ast
The complete influenza hemaggl ...... t at the lipid:water interface
@en
The complete influenza hemaggl ...... t at the lipid:water interface
@nl
prefLabel
The complete influenza hemaggl ...... t at the lipid:water interface
@ast
The complete influenza hemaggl ...... t at the lipid:water interface
@en
The complete influenza hemaggl ...... t at the lipid:water interface
@nl
P2093
P2860
P3181
P356
P1476
The complete influenza hemaggl ...... t at the lipid:water interface
@en
P2093
John M Louis
Justin L Lorieau
P2860
P304
P3181
P356
10.1073/PNAS.1006142107
P407
P577
2010-06-22T00:00:00Z