Inhibition of outer membrane proteases of the omptin family by aprotinin.

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The arsenal of pathogens and antivirulence therapeutic strategies for disarming them Antimicrobial Peptide Conformation as a Structural Determinant of Omptin Protease Specificity

P2860

Q26745604-846416DE-43A7-464B-B0E8-8DE26B0D47AE Q40562061-BE6B432A-3A53-4B6A-B748-103364709468

P2860

Inhibition of outer membrane proteases of the omptin family by aprotinin.

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http://www.wikidata.org/entity/Q40696229

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2015 nî lūn-bûn

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2015年の論文

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2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

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2015年论文

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2015年论文

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name

Inhibition of outer membrane proteases of the omptin family by aprotinin.

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type

Item

label

Inhibition of outer membrane proteases of the omptin family by aprotinin.

@en

prefLabel

Inhibition of outer membrane proteases of the omptin family by aprotinin.

@en

P1476

Inhibition of outer membrane proteases of the omptin family by aprotinin.

@en

P2093

Andrea Portt

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

David L Burk

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

Hervé Le Moual

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

Jean-Mathieu Leclerc

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

John R Brannon

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P2860

Identification of OmpT as the protease that hydrolyzes the antimicrobial peptide protamine before it enters growing cells of Escherichia coli

Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site

OmpT outer membrane proteases of enterohemorrhagic and enteropathogenic Escherichia coli contribute differently to the degradation of human LL-37

The omptins of Yersinia pestis and Salmonella enterica cleave the reactive center loop of plasminogen activator inhibitor 1

MEROPS: the database of proteolytic enzymes, their substrates and inhibitors

Purification, characterization, and primary structure of Escherichia coli protease VII with specificity for paired basic residues: identity of protease VII and OmpT

Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT Method

Enterohemorrhagic and enteropathogenic Escherichia coli evolved different strategies to resist antimicrobial peptides

An active site water network in the plasminogen activator pla from Yersinia pestis

Structural Basis for Activation of an Integral Membrane Protease by Lipopolysaccharide

P304

2300-2311

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P31

scholarly article

P356

10.1128/IAI.00136-15

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P407

English

P433

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

P478

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

P50

Samantha Gruenheid

Albert M Berghuis

Jenny-Lee Thomassin

P577

2015-03-30T00:00:00Z

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

P698

25824836

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P932

4432765

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Inhibition of outer membrane proteases of the omptin family by aprotinin.

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P2860

P2860

Inhibition of outer membrane proteases of the omptin family by aprotinin.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932