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

Protein Hpn: cloning and characterization of a histidine-rich metal-binding polypeptide in Helicobacter pylori and Helicobacter mustelae

1 Jul 1995

Abstract excerpt

Helicobacter pylori is a human gastrointestinal pathogen involved in gastritis, duodenal ulcers, and gastric neoplasia. This microorganism produces large amounts of a urease which, like all known ureases, has nickel in the active site. We have identified a protein in clinical isolates of H. pylori and an identical protein in the ferret pathogen Helicobacter mustelae that strongly binds Ni2+ and Zn2+. This protein...

Read the complete abstract on PubMed

Topics

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

Share to Galectins and Cancer Biology
Share to Helicobacter pylori-related gastroenterology studies

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 7790085
DOI: 10.1128/iai.63.7.2682-2688.1995

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Protein Hpn: cloning and characterization of a histidine-rich metal-binding polypeptide in Helicobacter pylori and Helicobacter mustelaePMID 7790085Read ↗

Evolution of Helicobacter: Acquisition by Gastric Species of Two Histidine-Rich Proteins Essential for ColonizationSemantic proximity Read ↗

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

An ABC transporter and a TonB ortholog contribute to Helicobacter mustelae nickel and cobalt acquisition.Semantic proximity Read ↗

Helicobacter pylori stores nickel to aid its host colonization.Semantic proximity Read ↗

Characterization in Helicobacter pylori of a Nickel Transporter Essential for Colonization That Was Acquired during Evolution by Gastric Helicobacter SpeciesSemantic proximity Read ↗

Helicobacter pylori nickel‐transport gene nixA: synthesis of catalytically active urease in Escherichia coli independent of growth conditionsSemantic proximity Read ↗

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

The novel Helicobacter pylori CznABC metal efflux pump is required for cadmium, zinc, and nickel resistance, urease modulation, and gastric colonization.Semantic proximity Read ↗

The <i>Helicobacter pylori</i> GroES Cochaperonin HspA Functions as a Specialized Nickel Chaperone and Sequestration Protein through Its Unique C-Terminal ExtensionSemantic proximity Read ↗

The 2.2-Å structure of the HP0958 protein from Helicobacter pylori reveals a kinked anti-parallel coiled-coil hairpin domain and a highly conserved ZN-ribbon domain.Semantic proximity Read ↗

Comprehensive mapping of the Helicobacter pylori NikR regulon provides new insights in bacterial nickel responsesSemantic proximity Read ↗

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