Lipopolysaccharide interaction is decisive for the activity of the antimicrobial peptide NK-2 against Escherichia coli and Proteus mirabilis. (Q54389951)

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English	Lipopolysaccharide interaction is decisive for the activity of the antimicrobial peptide NK-2 against Escherichia coli and Proteus mirabilis.	scientific article

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/20187872

Lipopolysaccharide interaction is decisive for the activity of the antimicrobial peptide NK-2 against Escherichia coli and Proteus mirabilis. (English)

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/20187872

lipopolysaccharide

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Escherichia coli

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Proteus mirabilis

object named as

Proteus mirabilis

1 reference

based on heuristic

inferred from title

antimicrobial peptide

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based on heuristic

inferred from title

Gerald Brezesinski

4

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/20187872

Torsten Goldmann

5

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/20187872

author name string

Malte U Hammer

1

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Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/20187872

Annemarie Brauser

2

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/20187872

Claudia Olak

3

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/20187872

Thomas Gutsmann

6

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/20187872

Jörg Andrä

7

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/20187872

language of work or name

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publication date

14 April 2010

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Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/20187872

Biochemical Journal

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Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/20187872

427

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Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/20187872

3

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/20187872

477-488

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/20187872

Antibacterial resistance worldwide: causes, challenges and responses

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Antimicrobial peptides of multicellular organisms

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

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Human host defense peptide LL-37 prevents bacterial biofilm formation

1 reference

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Mode of action of membrane active antimicrobial peptides

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

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Role of membranes in the activities of antimicrobial cationic peptides

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

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Detergent-like actions of linear amphipathic cationic antimicrobial peptides

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

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Alternative mechanisms of action of cationic antimicrobial peptides on bacteria

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Candidacidal activity of shortened synthetic analogs of amoebapores and NK-lysin

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Amoebapores, a family of membranolytic peptides from cytoplasmic granules of Entamoeba histolytica: isolation, primary structure, and pore formation in bacterial cytoplasmic membranes

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Molecular cloning and characterization of equine NK-lysin

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Pore-forming polypeptides of the pathogenic protozoon Naegleria fowleri

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Saposin fold revealed by the NMR structure of NK-lysin

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Solution structure of the pore-forming protein of Entamoeba histolytica

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Cytolytic and antibacterial activity of synthetic peptides derived from amoebapore, the pore-forming peptide of Entamoeba histolytica

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Shortened amoebapore analogs with enhanced antibacterial and cytolytic activity

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Ancient weapons: NK-lysin, is a mammalian homolog to pore-forming peptides of a protozoan parasite

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Molecular basis for membrane selectivity of NK-2, a potent peptide antibiotic derived from NK-lysin.

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens.

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Interfacial properties and structural analysis of the antimicrobial peptide NK-2.

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

NK-lysin and its shortened analog NK-2 exhibit potent activities against Trypanosoma cruzi

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

The antimicrobial peptide NK-2, the core region of mammalian NK-lysin, kills intraerythrocytic Plasmodium falciparum

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

The NK-lysin derived peptide NK-2 preferentially kills cancer cells with increased surface levels of negatively charged phosphatidylserine

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Biophysical characterization of endotoxin inactivation by NK-2, an antimicrobial peptide derived from mammalian NK-lysin

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Molecular mechanisms of polymyxin B-membrane interactions: direct correlation between surface charge density and self-promoted transport.

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Enhancement of endotoxin neutralization by coupling of a C12-alkyl chain to a lactoferricin-derived peptide

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Lipid-specific membrane activity of human beta-defensin-3.

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

A New Method for the Extraction of R Lipopolysaccharides

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Structure and mode of action of the antimicrobial peptide arenicin

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Surface acoustic wave biosensor as a tool to study the interaction of antimicrobial peptides with phospholipid and lipopolysaccharide model membranes

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Lipopolysaccharide-binding protein mediates CD14-independent intercalation of lipopolysaccharide into phospholipid membranes

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Brucella abortus and its closest phylogenetic relative, Ochrobactrum spp., differ in outer membrane permeability and cationic peptide resistance

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Ultrastructural effects of antimicrobial peptides from bovine lactoferrin on the membranes of Candida albicans and Escherichia coli

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Antimicrobial psoriasin (S100A7) protects human skin from Escherichia coli infection

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Binding of protegrin-1 to Pseudomonas aeruginosa and Burkholderia cepacia

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

The antimicrobial peptide polyphemusin localizes to the cytoplasm of Escherichia coli following treatment

1 reference

https://api.crossref.org/works/10.1042%2FBJ20091607

21 January 2018

Single molecule resolution of the antimicrobial action of quantum dot-labeled sushi peptide on live bacteria

1 reference

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21 January 2018

Identifiers

10.1042/BJ20091607

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/20187872

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/20187872

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