Tilted peptides: a motif for membrane destabilization (hypothesis).
about
Role of the lid hydrophobicity pattern in pancreatic lipase activity.Membrane translocation of penetratin and its derivatives in different cell lines.Structure and membrane interaction of the internal fusion peptide of avian sarcoma leukosis virus.Statistical thermodynamics of membrane bending-mediated protein-protein attractions."De novo" design of peptides with specific lipid-binding properties.Prolactin/growth hormone-derived antiangiogenic peptides highlight a potential role of tilted peptides in angiogenesis.Targeting HIV-1 gp41-induced fusion and pathogenesis for anti-viral therapyDistribution of hydrophobic residues is crucial for the fusogenic properties of the Ebola virus GP2 fusion peptide.Atomic force microscopy of model lipid membranes.Simulation studies of protein-induced bilayer deformations, and lipid-induced protein tilting, on a mesoscopic model for lipid bilayers with embedded proteins.Determination of the functionality of common APOA5 polymorphisms.Common molecular mechanism of amyloid pore formation by Alzheimer's β-amyloid peptide and α-synuclein.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.Lipid-induced conformational transition of the amyloid core fragment Abeta(28-35) and its A30G and A30I mutants.The membrane bound N-terminal domain of human adenosine diphosphate ribosylation factor-1 (ARF1).Lipid-destabilizing properties of the hydrophobic helices H8 and H9 from colicin E1.Use of hydrophobic moment plot methodology to aid the identification of oblique orientated alpha-helices.The interaction of a histidine-rich protein hpn with the membrane mimics: implications for pathologic roles of Hpn in Helicobacter pylori.Investigations into the ability of an oblique alpha-helical template to provide the basis for design of an antimicrobial anionic amphiphilic peptide.Investigations into the mechanisms used by the C-terminal anchors of Escherichia coli penicillin-binding proteins 4, 5, 6 and 6b for membrane interaction.
P2860
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P2860
Tilted peptides: a motif for membrane destabilization (hypothesis).
description
2000 nî lūn-bûn
@nan
2000 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունվարին հրատարակված գիտական հոդված
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2000年の論文
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2000年学术文章
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2000年学术文章
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2000年学术文章
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2000年学术文章
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2000年学术文章
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2000年學術文章
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name
Tilted peptides: a motif for membrane destabilization (hypothesis).
@ast
Tilted peptides: a motif for membrane destabilization (hypothesis).
@en
type
label
Tilted peptides: a motif for membrane destabilization (hypothesis).
@ast
Tilted peptides: a motif for membrane destabilization (hypothesis).
@en
prefLabel
Tilted peptides: a motif for membrane destabilization (hypothesis).
@ast
Tilted peptides: a motif for membrane destabilization (hypothesis).
@en
P2860
P356
P1476
Tilted peptides: a motif for membrane destabilization (hypothesis).
@en
P2093
Brasseur R
P2860
P356
10.1080/096876800294461
P577
2000-01-01T00:00:00Z