Antimicrobial peptides at work: interaction of myxinidin and its mutant WMR with lipid bilayers mimicking the P. aeruginosa and E. coli membranes.

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Cyclic Peptides as Novel Therapeutic Microbicides: Engineering of Human Defensin Mimetics.Exploring the role of unnatural amino acids in antimicrobial peptides.

P2860

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P2860

Antimicrobial peptides at work: interaction of myxinidin and its mutant WMR with lipid bilayers mimicking the P. aeruginosa and E. coli membranes.

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http://www.wikidata.org/entity/Q38745454

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2017 nî lūn-bûn

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2017年の論文

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2017年論文

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2017年論文

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2017年論文

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2017年論文

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2017年論文

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2017年论文

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2017年论文

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2017年论文

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name

Antimicrobial peptides at work ...... uginosa and E. coli membranes.

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type

Item

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Antimicrobial peptides at work ...... uginosa and E. coli membranes.

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Antimicrobial peptides at work ...... uginosa and E. coli membranes.

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P1476

Antimicrobial peptides at work ...... ruginosa and E. coli membranes

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P2093

Annarita Falanga

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

Augusta De Santis

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

Geradino D'Errico

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

Luigi Petraccone

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

Marco Ignazio Stellato

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

Massimiliano Galdiero

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

Rosario Oliva

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

Stefania Galdiero

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

P2860

Antimicrobial peptides of multicellular organisms

Cardiolipins and biomembrane function

The efficacy of trivalent cyclic hexapeptides to induce lipid clustering in PG/PE membranes correlates with their antimicrobial activity.

Peptide induced demixing in PG/PE lipid mixtures: a mechanism for the specificity of antimicrobial peptides towards bacterial membranes?

Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent.

Quasielastic light scattering for protein assembly studies.

Interaction of antimicrobial peptides with biological and model membranes: structural and charge requirements for activity.

Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides.

Differential scanning calorimetry and X-ray diffraction studies of the specificity of the interaction of antimicrobial peptides with membrane-mimetic systems.

Leakage of membrane vesicle contents: determination of mechanism using fluorescence requenching.

P2888

srep44425

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44425

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scholarly article

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10.1038/SREP44425

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English

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

P50

Pompea Del Vecchio

Lucia Lombardi

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2017-03-15T00:00:00Z

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1084132315

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28294185

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P921

Escherichia coli

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5353584

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Antimicrobial peptides at work: interaction of myxinidin and its mutant WMR with lipid bilayers mimicking the P. aeruginosa and E. coli membranes.

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P2860

P2860

Antimicrobial peptides at work: interaction of myxinidin and its mutant WMR with lipid bilayers mimicking the P. aeruginosa and E. coli membranes.

description

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type

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P1433

P1476

P2093

P2860

P2888

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P31

P356

P407

P478

P50

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P6179

P698

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P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P478

P50

P577

P6179

P698

P921

P932