Oligomeric beta-structure of the membrane-bound HIV-1 fusion peptide formed from soluble monomers.
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Structure and plasticity of the human immunodeficiency virus gp41 fusion domain in lipid micelles and bilayersMembrane-dependent conformation, dynamics, and lipid interactions of the fusion peptide of the paramyxovirus PIV5 from solid-state NMRHexapeptides that interfere with HIV-1 fusion peptide activity in liposomes block GP41-mediated membrane fusion.The three lives of viral fusion peptidesFolded monomers and hexamers of the ectodomain of the HIV gp41 membrane fusion protein: potential roles in fusion and synergy between the fusion peptide, hairpin, and membrane-proximal external regionStructure, topology, and tilt of cell-signaling peptides containing nuclear localization sequences in membrane bilayers determined by solid-state NMR and molecular dynamics simulation studiesIdentification of the Fusion Peptide-Containing Region in Betacoronavirus Spike GlycoproteinsComputer-Aided Approaches for Targeting HIVgp41.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.Structural Study of a New HIV-1 Entry Inhibitor and Interaction with the HIV-1 Fusion Peptide in Dodecylphosphocholine Micelles.Major antiparallel and minor parallel β sheet populations detected in the membrane-associated human immunodeficiency virus fusion peptide.Solid-state NMR spectroscopy of human immunodeficiency virus fusion peptides associated with host-cell-like membranes: 2D correlation spectra and distance measurements support a fully extended conformation and models for specific antiparallel strandChemical shift assignment and structural plasticity of a HIV fusion peptide derivative in dodecylphosphocholine micellesHIV 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.Conformational flexibility and strand arrangements of the membrane-associated HIV fusion peptide trimer probed by solid-state NMR spectroscopySolid-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 nuclear magnetic resonance measurements of HIV fusion peptide to lipid distances reveal the intimate contact of beta strand peptide with membranes and the proximity of the Ala-14-Gly-16 region with lipid headgroups.HIV fusion peptide and its cross-linked oligomers: efficient syntheses, significance of the trimer in fusion activity, correlation of beta strand conformation with membrane cholesterol, and proximity to lipid headgroupspH-dependent vesicle fusion induced by the ectodomain of the human immunodeficiency virus membrane fusion protein gp41: Two kinetically distinct processes and fully-membrane-associated gp41 with predominant β sheet fusion peptide conformation.Immobilization of the influenza A M2 transmembrane peptide in virus envelope-mimetic lipid membranes: a solid-state NMR investigation.Hairpin folding of HIV gp41 abrogates lipid mixing function at physiologic pH and inhibits lipid mixing by exposed gp41 constructs.Nuclear magnetic resonance evidence for retention of a lamellar membrane phase with curvature in the presence of large quantities of the HIV fusion peptide.Charged residues are involved in membrane fusion mediated by a hydrophilic peptide located in vesicular stomatitis virus G protein.Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers containing the Fusion Peptide and Transmembrane Domain.
P2860
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P2860
Oligomeric beta-structure of the membrane-bound HIV-1 fusion peptide formed from soluble monomers.
description
2004 nî lūn-bûn
@nan
2004 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
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2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Oligomeric beta-structure of t ...... formed from soluble monomers.
@ast
Oligomeric beta-structure of t ...... formed from soluble monomers.
@en
Oligomeric beta-structure of t ...... formed from soluble monomers.
@nl
type
label
Oligomeric beta-structure of t ...... formed from soluble monomers.
@ast
Oligomeric beta-structure of t ...... formed from soluble monomers.
@en
Oligomeric beta-structure of t ...... formed from soluble monomers.
@nl
prefLabel
Oligomeric beta-structure of t ...... formed from soluble monomers.
@ast
Oligomeric beta-structure of t ...... formed from soluble monomers.
@en
Oligomeric beta-structure of t ...... formed from soluble monomers.
@nl
P2093
P2860
P1433
P1476
Oligomeric beta-structure of t ...... formed from soluble monomers.
@en
P2093
David P Weliky
Francis J Castellino
Mary Prorok
P2860
P304
P356
10.1529/BIOPHYSJ.103.028530
P407
P577
2004-09-01T00:00:00Z