Membrane perturbation induced by interfacially adsorbed peptides. - sprookjes - yvandenbroek - TriplyDB

Membrane perturbation induced by interfacially adsorbed peptides.

Membrane perturbation induced by interfacially adsorbed peptides.

http://www.wikidata.org/entity/Q40284484

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Active fragments from pro- and antiapoptotic BCL-2 proteins have distinct membrane behavior reflecting their functional divergence Antimicrobial peptides temporins B and L induce formation of tubular lipid protrusions from supported phospholipid bilayers Benchmark experimental data set and assessment of adsorption free energy for peptide-surface interactions Understanding detergent effects on lipid membranes: a model study of lysolipids Probing the Huntingtin 1-17 membrane anchor on a phospholipid bilayer by using all-atom simulations The lantibiotic nisin induces lipid II aggregation, causing membrane instability and vesicle budding.Förster resonance energy transfer evidence for lysozyme oligomerization in lipid environment Binding of lysozyme to phospholipid bilayers: evidence for protein aggregation upon membrane association Mechanism for calcium ion sensing by the C2A domain of synaptotagmin I Ischemic preconditioning prevents protein aggregation after transient cerebral ischemia.Inclusion of lateral pressure/curvature stress effects in implicit membrane models Factors influencing local membrane curvature induction by N-BAR domains as revealed by molecular dynamics simulations H-ras protein in a bilayer: interaction and structure perturbation Molecular understanding of a potential functional link between antimicrobial and amyloid peptides.Diffusion as a probe of the heterogeneity of antimicrobial peptide-membrane interactions.Coarse-grained simulation studies of peptide-induced pore formation.Modulation of physiological and pathological activities of lysozyme by biological membranes.Nematic membranes: Shape instabilities of closed achiral vesicles

P2860

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P2860

Membrane perturbation induced by interfacially adsorbed peptides.

http://www.wikidata.org/entity/Q40284484

description

2004 nî lūn-bûn

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

2004年论文

@zh

2004年论文

@zh-cn

name

Membrane perturbation induced by interfacially adsorbed peptides.

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type

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Membrane perturbation induced by interfacially adsorbed peptides.

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Membrane perturbation induced by interfacially adsorbed peptides.

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BIOPHYSJ.103.033605

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Biophysical Journal

P1476

Membrane perturbation induced by interfacially adsorbed peptides.

@en

P2093

Assaf Zemel

http://www.w3.org/2001/XMLSchema#string

Avinoam Ben-Shaul

http://www.w3.org/2001/XMLSchema#string

Sylvio May

http://www.w3.org/2001/XMLSchema#string

P2860

Structure, location, and lipid perturbations of melittin at the membrane interface

Insertion and pore formation driven by adsorption of proteins onto lipid bilayer membrane-water interfaces.

Site-specific deuterium order parameters and membrane-bound behavior of a peptide fragment from the intracellular domain of HIV-1 gp41.

Orientation and dynamics of an antimicrobial peptide in the lipid bilayer by solid-state NMR spectroscopy.

The structure of the antimicrobial peptide Ac-RRWWRF-NH2 bound to micelles and its interactions with phospholipid bilayers.

Mode of action of linear amphipathic alpha-helical antimicrobial peptides.

Theoretical analysis of hydrophobic matching and membrane-mediated interactions in lipid bilayers containing gramicidin.

Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes.

Diversity of antimicrobial peptides and their mechanisms of action.

Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells.

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3607-3619

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10.1529/BIOPHYSJ.103.033605

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