In vivo Efficacy and Pharmacokinetics of Optimized Apidaecin Analogs. - Wikidata - awgldk - TriplyDB

In vivo Efficacy and Pharmacokinetics of Optimized Apidaecin Analogs.

In vivo Efficacy and Pharmacokinetics of Optimized Apidaecin Analogs.

http://www.wikidata.org/entity/Q37710376

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Differential stability of therapeutic peptides with different proteolytic cleavage sites in blood, plasma and serum Correlating uptake and activity of proline-rich antimicrobial peptides in Escherichia coli.

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In vivo Efficacy and Pharmacokinetics of Optimized Apidaecin Analogs.

http://www.wikidata.org/entity/Q37710376

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 20 March 2017

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

In vivo Efficacy and Pharmacokinetics of Optimized Apidaecin Analogs.

@en

In vivo Efficacy and Pharmacokinetics of Optimized Apidaecin Analogs.

@nl

type

label

In vivo Efficacy and Pharmacokinetics of Optimized Apidaecin Analogs.

@en

In vivo Efficacy and Pharmacokinetics of Optimized Apidaecin Analogs.

@nl

prefLabel

In vivo Efficacy and Pharmacokinetics of Optimized Apidaecin Analogs.

@en

In vivo Efficacy and Pharmacokinetics of Optimized Apidaecin Analogs.

@nl

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FCHEM.2017.00015

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Frontiers in Chemistry

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In vivo Efficacy and Pharmacokinetics of Optimized Apidaecin Analogs.

@en

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Daniel Knappe

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

Elisabeth Wende

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

Eszter Ostorházi

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

Ralf Hoffmann

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

Rico Schmidt

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

P2860

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Rational design of oncocin derivatives with superior protease stabilities and antibacterial activities based on the high-resolution structure of the oncocin-DnaK complex

Api88 is a novel antibacterial designer peptide to treat systemic infections with multidrug-resistant Gram-negative pathogens

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Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?

The proline-rich peptide Bac7(1-35) reduces mortality from Salmonella typhimurium in a mouse model of infection.

Preclinical advantages of intramuscularly administered peptide A3-APO over existing therapies in Acinetobacter baumannii wound infections.

Functional characterization of SbmA, a bacterial inner membrane transporter required for importing the antimicrobial peptide Bac7(1-35).

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15

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scholarly article

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10.3389/FCHEM.2017.00015

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5

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2017-03-20T00:00:00Z

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28373972

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5357639

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