Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Dependence of Helicobacter pylori urease activity on the nickel-sequestering ability of the UreE accessory protein.

Journal of bacteriology - 1 Aug 2003

Benoit Stéphane, Maier Robert J

Abstract excerpt

The Helicobacter pylori ureE gene product was previously shown to be required for urease expression, but its characteristics and role have not been determined. The UreE protein has now been overexpressed in Escherichia coli, purified, and characterized, and three altered versions were expressed to address a nickel-sequestering role of UreE. Purified UreE formed a dimer in solution and was capable of binding one...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Dimerization
Share to GTP-Binding Proteins
Share to Helicobacter pylori

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Histidine

Share to Hydrogenase

Share to Intracellular Signaling Peptides and Proteins

Share to Nickel

Share to Urease

Source

Open in PubMed Open full text

Identifiers

PMID: 12896998
DOI: 10.1128/JB.185.16.4787-4795.2003
PMCID: PMC166491

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dependence of Helicobacter pylori urease activity on the nickel-sequestering ability of the UreE accessory protein.PMID 12896998Read ↗

Purification, characterization, and functional analysis of a truncated Klebsiella aerogenes UreE urease accessory protein lacking the histidine-rich carboxyl terminus.Semantic proximity Read ↗

Nickel translocation between metallochaperones HypA and UreE in Helicobacter pyloriSemantic proximity Read ↗

UreE-UreG Complex Facilitates Nickel Transfer and Preactivates GTPase of UreG in Helicobacter pyloriSemantic proximity Read ↗

Requirement of nickel metabolism proteins HypA and HypB for full activity of both hydrogenase and urease in Helicobacter pylori.Semantic proximity Read ↗

Nickel trafficking system responsible for urease maturation inHelicobacter pyloriSemantic proximity Read ↗

Structural insights into how metallochaperones UreE and UreG interact to deliver a toxic metal to ureaseSemantic proximity Read ↗

Mutational and Computational Evidence That a Nickel-Transfer Tunnel in UreD Is Used for Activation of Klebsiella aerogenes Urease.Semantic proximity Read ↗

Nickel enzyme maturation in Helicobacter hepaticus: roles of accessory proteins in hydrogenase and urease activities.Semantic proximity Read ↗

Crystal structure of a truncated urease accessory protein UreF from Helicobacter pylori.Semantic proximity Read ↗

Common themes and unique proteins for the uptake and trafficking of nickel, a metal essential for the virulence of Helicobacter pyloriSemantic proximity Read ↗

In Vivo Interactome of Helicobacter pylori Urease Revealed by Tandem Affinity PurificationSemantic proximity Read ↗

Roles of His-rich hpn and hpn-like proteins in Helicobacter pylori nickel physiology.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.