Lipid-dependent pore formation by antimicrobial peptides arenicin-2 and melittin demonstrated by their proton transfer activity.

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Melittin-Induced Lipid Extraction Modulated by the Methylation Level of Phosphatidylcholine Headgroups.Marine antimicrobial peptide arenicin adopts a monomeric twisted β-hairpin structure and forms low conductivity pores in zwitterionic lipid bilayers.

P2860

Q41911319-30392B04-39CF-4703-A5A3-22092028A7CE Q47745887-FA95EEA6-A23E-4DF8-9184-BE457672E668

P2860

Lipid-dependent pore formation by antimicrobial peptides arenicin-2 and melittin demonstrated by their proton transfer activity.

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http://www.wikidata.org/entity/Q41672370

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2014 nî lūn-bûn

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2014年の論文

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2014年論文

@yue

2014年論文

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2014年論文

@zh-hk

2014年論文

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2014年論文

@zh-tw

2014年论文

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2014年论文

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2014年论文

@zh-cn

name

Lipid-dependent pore formation ...... heir proton transfer activity.

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type

Item

label

Lipid-dependent pore formation ...... heir proton transfer activity.

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prefLabel

Lipid-dependent pore formation ...... heir proton transfer activity.

@en

P1476

Lipid-dependent pore formation ...... heir proton transfer activity.

@en

P2093

Leonid I Barsukov

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

Pavel V Panteleev

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

Sergei V Sychev

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

Sergey V Balandin

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

Tatiana V Ovchinnikova

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

P2860

Recombinant expression, synthesis, purification, and solution structure of arenicin

Structure and mode of action of the antimicrobial peptide arenicin

Molecular mechanism of action of β-hairpin antimicrobial peptide arenicin: oligomeric structure in dodecylphosphocholine micelles and pore formation in planar lipid bilayers

Barrel-stave model or toroidal model? A case study on melittin pores.

Membrane-dependent oligomeric structure and pore formation of a beta-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR.

Aggregation and porin-like channel activity of a beta sheet peptide.

Effect of membrane environment on proton permeation through gramicidin A channels.

Phosphate-mediated arginine insertion into lipid membranes and pore formation by a cationic membrane peptide from solid-state NMR.

Molecular insight into mechanism of antimicrobial action of the beta-hairpin peptide arenicin: specific oligomerization in detergent micelles.

Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action.

P304

71-76

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P31

scholarly article

P356

10.1002/PSC.2724

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P433

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

P478

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

P577

2014-12-17T00:00:00Z

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P698

25522354

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

Lipid-dependent pore formation by antimicrobial peptides arenicin-2 and melittin demonstrated by their proton transfer activity.

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P2860

P2860

Lipid-dependent pore formation by antimicrobial peptides arenicin-2 and melittin demonstrated by their proton transfer activity.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698