Maculatin 1.1 disrupts Staphylococcus aureus lipid membranes via a pore mechanism. - Wikidata - awgldk - TriplyDB

Maculatin 1.1 disrupts Staphylococcus aureus lipid membranes via a pore mechanism.

Maculatin 1.1 disrupts Staphylococcus aureus lipid membranes via a pore mechanism.

http://www.wikidata.org/entity/Q41790323

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A Rapid and Quantitative Flow Cytometry Method for the Analysis of Membrane Disruptive Antimicrobial Activity Membrane Active Antimicrobial Peptides: Translating Mechanistic Insights to Design.Combating multidrug-resistant Gram-negative bacteria with structurally nanoengineered antimicrobial peptide polymers.Bacteria May Cope Differently from Similar Membrane Damage Caused by the Australian Tree Frog Antimicrobial Peptide Maculatin 1.1.Melittin peptides exhibit different activity on different cells and model membranes.Antimicrobial activity of the indolicidin-derived novel synthetic peptide In-58.The effect of a beta-lactamase inhibitor peptide on bacterial membrane structure and integrity: a comparative study.Antimicrobial Peptide Structures: From Model Membranes to Live Cells.One pathogen two stones: are Australian tree frog antimicrobial peptides synergistic against human pathogens?Dye-release assay for investigation of antimicrobial peptide activity in a competitive lipid environment.

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P2860

Maculatin 1.1 disrupts Staphylococcus aureus lipid membranes via a pore mechanism.

http://www.wikidata.org/entity/Q41790323

description

2013 nî lūn-bûn

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

Maculatin 1.1 disrupts Staphylococcus aureus lipid membranes via a pore mechanism.

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Maculatin 1.1 disrupts Staphylococcus aureus lipid membranes via a pore mechanism.

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Maculatin 1.1 disrupts Staphylococcus aureus lipid membranes via a pore mechanism.

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Antimicrobial Agents and Chemotherapy

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Maculatin 1.1 disrupts Staphylococcus aureus lipid membranes via a pore mechanism

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N Pantarat

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

T C Whitwell

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T J Attard

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P2860

Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?

Lipid composition regulates the conformation and insertion of the antimicrobial peptide maculatin 1.1.

Maculatin 1.1, an anti-microbial peptide from the Australian tree frog, Litoria genimaculata solution structure and biological activity.

Pro-apoptotic bax-alpha1 synthesis and evidence for beta-sheet to alpha-helix conformational change as triggered by negatively charged lipid membranes.

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

Amphipathic, alpha-helical antimicrobial peptides.

Control of cell selectivity of antimicrobial peptides.

Protegrin-1: a broad-spectrum, rapidly microbicidal peptide with in vivo activity.

New mechanism for methicillin resistance in Staphylococcus aureus: clinical isolates that lack the PBP 2a gene and contain normal penicillin-binding proteins with modified penicillin-binding capacity.

Database screening and in vivo efficacy of antimicrobial peptides against methicillin-resistant Staphylococcus aureus USA300.

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3593-3600

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scholarly article

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10.1128/AAC.00195-13

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8

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57

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Frances Šeparović

Eric C. Reynolds

Neil M O'Brien-Simpson

Roy M Robins-Browne

Marc-Antoine Sani

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2013-05-20T00:00:00Z

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236923945

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23689707

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3719708

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