A critical evaluation of the conformational requirements of fusogenic peptides in membranes

A critical evaluation of the conformational requirements of fusogenic peptides in membranes

Item
http://www.wikidata.org/entity/Q57528481
Structures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeFeatures of a spatially constrained cystine loop in the p10 FAST protein ectodomain define a new class of viral fusion peptides.HIV fusion peptide penetrates, disorders, and softens T-cell membrane mimics.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.A strong correlation between fusogenicity and membrane insertion depth of the HIV fusion peptide.Insights into the mechanism of HIV-1 envelope induced membrane fusion as revealed by its inhibitory peptides.Computer-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.The Relation Between Thermodynamic and Structural Properties and Cellular Uptake of Peptides Containing Tryptophan and Arginine.Antimicrobial and cell-penetrating peptides induce lipid vesicle fusion by folding and aggregation.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 strandHIV 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.Conformation and membrane orientation of amphiphilic helical peptides by oriented circular dichroism.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.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 headgroupsIrregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.Stereochemical effects on the aggregation and biological properties of the fibril-forming peptide [KIGAKI]3 in membranes.
P2860

A critical evaluation of the conformational requirements of fusogenic peptides in membranes

Item
http://www.wikidata.org/entity/Q57528481
description
im November 2006 veröffentlichter wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована в листопаді 2006
@uk
name
A critical evaluation of the c ...... usogenic peptides in membranes
@en
A critical evaluation of the c ...... usogenic peptides in membranes
@nl
type
label
A critical evaluation of the c ...... usogenic peptides in membranes
@en
A critical evaluation of the c ...... usogenic peptides in membranes
@nl
prefLabel
A critical evaluation of the c ...... usogenic peptides in membranes
@en
A critical evaluation of the c ...... usogenic peptides in membranes
@nl
P1433
P1476
P2093
P2860
P2888
P304
P31
P356
P433
P478
P50
P577
P698
P356
P1433
P1476
A critical evaluation of the c ...... usogenic peptides in membranes
@en
P2093
P2860
P2888
P304
P31
P356
P433
P478
P50
P577
P698