(Q38295396)

English

Helicobacter pylori neutrophil-activating protein activates neutrophils by its C-terminal region even without dodecamer formation, which is a prerequisite for DNA protection--novel approaches against Helicobacter pylori inflammation

scientific article published on 12 December 2007

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scholarly article

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Europe PubMed Central

PubMed publication ID

1 September 2017

Helicobacter pylori neutrophil-activating protein activates neutrophils by its C-terminal region even without dodecamer formation, which is a prerequisite for DNA protection--novel approaches against Helicobacter pylori inflammation (English)

1 reference

Europe PubMed Central

PubMed publication ID

1 September 2017

Helicobacter pylori

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Helicobacter pylori infectious disease

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author name string

Filippos Kottakis

1

1 reference

Europe PubMed Central

PubMed publication ID

1 September 2017

Georgios Papadopoulos

2

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Europe PubMed Central

PubMed publication ID

1 September 2017

Eleni V Pappa

3

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Europe PubMed Central

PubMed publication ID

1 September 2017

Paul Cordopatis

4

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Europe PubMed Central

PubMed publication ID

1 September 2017

Stefanos Pentas

5

1 reference

Europe PubMed Central

PubMed publication ID

1 September 2017

Theodora Choli-Papadopoulou

6

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Europe PubMed Central

PubMed publication ID

1 September 2017

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publication date

12 December 2007

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Europe PubMed Central

PubMed publication ID

1 September 2017

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Europe PubMed Central

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1 September 2017

275

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Europe PubMed Central

PubMed publication ID

1 September 2017

2

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Europe PubMed Central

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1 September 2017

302-317

1 reference

Europe PubMed Central

PubMed publication ID

1 September 2017

Identification of four new prokaryotic bacterioferritins, from Helicobacter pylori, Anabaena variabilis, Bacillus subtilis and Treponema pallidum, by analysis of gene sequences.

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

The neutrophil-activating protein (HP-NAP) of Helicobacter pylori is a protective antigen and a major virulence factor

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

The neutrophil-activating protein (HP-NAP) of Helicobacter pylori is a potent stimulant of mast cells

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

Molecular and cellular mechanisms of action of the vacuolating cytotoxin (VacA) and neutrophil-activating protein (HP-NAP) virulence factors of Helicobacter pylori

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

The Helicobacter pylori neutrophil-activating protein is an iron-binding protein with dodecameric structure.

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

Neutrophil-activating protein (HP-NAP) versus ferritin (Pfr): comparison of synthesis in Helicobacter pylori.

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

Structure of the neutrophil-activating protein from Helicobacter pylori

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

The crystal structure of Dps, a ferritin homolog that binds and protects DNA

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

DNA protection by stress-induced biocrystallization

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

The Dps protein of Agrobacterium tumefaciens does not bind to DNA but protects it toward oxidative cleavage: x-ray crystal structure, iron binding, and hydroxyl-radical scavenging properties

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

An iron-binding protein, Dpr, from Streptococcus mutans prevents iron-dependent hydroxyl radical formation in vitro.

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritin-like DNA-binding protein of Escherichia coli.

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

The DpsA protein of Synechococcus sp. Strain PCC7942 is a DNA-binding hemoprotein. Linkage of the Dps and bacterioferritin protein families.

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

The iron-binding protein Dps confers hydrogen peroxide stress resistance to Campylobacter jejuni

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

Oxidative-stress resistance mutants of Helicobacter pylori

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

The neutrophil-activating Dps protein of Helicobacter pylori, HP-NAP, adopts a mechanism different from Escherichia coli Dps to bind and condense DNA.

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

Dual Roles of Helicobacter pylori NapA in inducing and combating oxidative stress

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps.

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

Structure of two iron-binding proteins from Bacillus anthracis

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

The multi-layered structure of Dps with a novel di-nuclear ferroxidase center

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

The O2- -forming NADPH oxidase of the phagocytes: nature, mechanisms of activation and function

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

A rapid and efficient one-tube PCR-based mutagenesis technique using Pfu DNA polymerase

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

The formation of ferritin from apoferritin. Kinetics and mechanism of iron uptake

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

Oxidation of phenolate siderophores by the multicopper oxidase encoded by the Escherichia coli yacK gene

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

9-Fluorenylmethoxycarbonyl amino-protecting group

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

VMD: visual molecular dynamics

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

Structure-based thermodynamic analysis of the dissociation of protein phosphatase-1 catalytic subunit and microcystin-LR docked complexes

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2007.06201.X

21 January 2018

Identifiers

10.1111/J.1742-4658.2007.06201.X

1 reference

Europe PubMed Central

PubMed publication ID

1 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 September 2017

ResearchGate publication ID

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