(Q27666903)

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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

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scholarly article

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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 (English)

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Norbert Sträter

5

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author name string

Daniel Knappe

1

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Michael Zahn

2

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Ute Sauer

3

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Guido Schiffer

4

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Ralf Hoffmann

6

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publication date

11 April 2011

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12

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6

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874-6

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Resistance patterns among nosocomial pathogens: trends over the past few years

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Extended-spectrum beta-lactamase-producing Enterobacteriaceae: an emerging public-health concern

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Emergence of carbapenem-resistant Klebsiella species possessing the class A carbapenem-hydrolyzing KPC-2 and inhibitor-resistant TEM-30 beta-lactamases in New York City

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The epidemiology and control of Acinetobacter baumannii in health care facilities

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Multicity outbreak of carbapenem-resistant Acinetobacter baumannii isolates producing the carbapenemase OXA-40.

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Bad bugs, no drugs: no ESKAPE! An update from the Infectious Diseases Society of America

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The short proline-rich antibacterial peptide family

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Oncocin (VDKPPYLPRPRPPRRIYNR-NH2): a novel antibacterial peptide optimized against gram-negative human pathogens.

1 reference

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21 January 2018

Role of the Escherichia coli SbmA in the antimicrobial activity of proline-rich peptides.

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https://api.crossref.org/works/10.1002%2FCBIC.201000792

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The antibacterial peptide pyrrhocoricin inhibits the ATPase actions of DnaK and prevents chaperone-assisted protein folding

1 reference

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21 January 2018

Rational design of novel peptidic DnaK ligands

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Structural analysis of substrate binding by the molecular chaperone DnaK

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Sequence-dependent peptide binding orientation by the molecular chaperone DnaK.

1 reference

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Identifiers

10.1002/CBIC.201000792

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