A strong correlation between fusogenicity and membrane insertion depth of the HIV fusion peptide.
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Magic angle spinning NMR of virusesDihydroceramides: From Bit Players to Lead ActorsStructure of the Disulfide Bond Generating Membrane Protein DsbB in the Lipid BilayerFusion of Enveloped Viruses in Endosomes.Internal dynamics of the homotrimeric HIV-1 viral coat protein gp41 on multiple time scalesProbing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy.Membrane protein structure and dynamics from NMR spectroscopy.Fusion activity of HIV gp41 fusion domain is related to its secondary structure and depth of membrane insertion in a cholesterol-dependent fashion.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 peptidesHIV fusion peptide penetrates, disorders, and softens T-cell membrane mimics.HIV-1 envelope protein gp41: an NMR study of dodecyl phosphocholine embedded gp41 reveals a dynamic prefusion intermediate conformation.Multiple locations of peptides in the hydrocarbon core of gel-phase membranes revealed by peptide (13)C to lipid (2)H rotational-echo double-resonance solid-state nuclear magnetic resonance.REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins.Structural basis for the geometry-driven localization of a small protein.Spherical nanoparticle supported lipid bilayers for the structural study of membrane geometry-sensitive molecules.Protein-driven membrane stresses in fusion and fission.Solid-state NMR spectroscopy on complex biomolecules.Comparative analysis of membrane-associated fusion peptide secondary structure and lipid mixing function of HIV gp41 constructs that model the early pre-hairpin intermediate and final hairpin conformations.Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach.Structural Study of a New HIV-1 Entry Inhibitor and Interaction with the HIV-1 Fusion Peptide in Dodecylphosphocholine Micelles.Antimicrobial and cell-penetrating peptides induce lipid vesicle fusion by folding and aggregation.Major antiparallel and minor parallel β sheet populations detected in the membrane-associated human immunodeficiency virus fusion peptide.The influenza hemagglutinin fusion domain is an amphipathic helical hairpin that functions by inducing membrane curvature.HIV gp41 six-helix bundle constructs induce rapid vesicle fusion at pH 3.5 and little fusion at pH 7.0: understanding pH dependence of protein aggregation, membrane binding, and electrostatics, and implications for HIV-host cell fusion.Solid-state nuclear magnetic resonance measurements of HIV fusion peptide 13CO to lipid 31P proximities support similar partially inserted membrane locations of the α helical and β sheet peptide structures.Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel β sheet fusion peptide structure in the final six-helix bundle stateSolid-state NMR paramagnetic relaxation enhancement immersion depth studies in phospholipid bilayers.Residue-specific membrane location of peptides and proteins using specifically and extensively deuterated lipids and ¹³C-²H rotational-echo double-resonance solid-state NMR.Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.Switching between Successful and Dead-End Intermediates in Membrane Fusion.Conformation and Trimer Association of the Transmembrane Domain of the Parainfluenza Virus Fusion Protein in Lipid Bilayers from Solid-State NMR: Insights into the Sequence Determinants of Trimer Structure and Fusion Activity.Charged N-terminus of Influenza Fusion Peptide Facilitates Membrane Fusion.Evaluation of the effect of fluorination on the property of monofluorinated dimyristoylphosphatidylcholines.Conformation of a Seven-Helical Transmembrane Photosensor in the Lipid Environment
P2860
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P2860
A strong correlation between fusogenicity and membrane insertion depth of the HIV fusion peptide.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on 24 August 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
A strong correlation between f ...... pth of the HIV fusion peptide.
@en
A strong correlation between f ...... pth of the HIV fusion peptide.
@nl
type
label
A strong correlation between f ...... pth of the HIV fusion peptide.
@en
A strong correlation between f ...... pth of the HIV fusion peptide.
@nl
prefLabel
A strong correlation between f ...... pth of the HIV fusion peptide.
@en
A strong correlation between f ...... pth of the HIV fusion peptide.
@nl
P2093
P2860
P356
P1476
A strong correlation between f ...... pth of the HIV fusion peptide.
@en
P2093
David P Weliky
P2860
P304
15314-15319
P356
10.1073/PNAS.0907360106
P407
P577
2009-08-24T00:00:00Z