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

Mutagenesis of conserved amino acids of Helicobacter pylori fur reveals residues important for function.

Journal of bacteriology - 1 Oct 2010

Carpenter Beth M, Gancz Hanan, Benoit Stéphane L, Evans Sarah, Olsen Cara H, Michel Sarah L J, Maier Robert J, Merrell D Scott

Abstract excerpt

The ferric uptake regulator (Fur) of the medically important pathogen Helicobacter pylori is unique in that it has been shown to function as a repressor both in the presence of an Fe2+ cofactor and in its apo (non-Fe2+-bound) form. However, virtually nothing is known concerning the amino acid residues that are important for Fur functioning. Therefore, mutations in six conserved amino acid residues of H. pylori...

Read the complete abstract on PubMed

Topics

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

Share to Circular Dichroism
Share to Electrophoretic Mobility Shift Assay

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

Share to Helicobacter pylori

Share to Protein Multimerization

Share to Protein Structure, Secondary

Share to Repressor Proteins

Share to Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 20644138
DOI: 10.1128/JB.00198-10
PMCID: PMC2944535

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

Mutagenesis of conserved amino acids of Helicobacter pylori fur reveals residues important for function.PMID 20644138Read ↗

Random and site-specific mutagenesis of the Helicobacter pylori ferric uptake regulator provides insight into Fur structure-function relationships.Semantic proximity Read ↗

A single nucleotide change affects fur-dependent regulation of sodB in H. pylori.Semantic proximity Read ↗

Autoregulation of Helicobacter pylori Fur revealed by functional analysis of the iron-binding site.Semantic proximity Read ↗

The Ferric Uptake Regulator of Helicobacter Pylori : a Critical Player in the Battle for Iron and Colonization of the StomachSemantic proximity Read ↗

Point mutations in Helicobacter pylori's fur regulatory gene that alter resistance to metronidazole, a prodrug activated by chemical reduction.Semantic proximity Read ↗

Proteomic analysis of a ferric uptake regulator mutant of Helicobacter pylori: regulation of Helicobacter pylori gene expression by ferric uptake regulator and iron.Semantic proximity Read ↗

Two amino acids mutation of ferric uptake regulator determines Helicobacter pylori resistance to metronidazole.Semantic proximity Read ↗

The ferric uptake regulator (Fur) homologue of Helicobacter pylori: functional analysis of the coding gene and controlled production of the recombinant protein in Escherichia coli.Semantic proximity Read ↗

The role of the Ferric Uptake Regulator (Fur) in regulation of Helicobacter pylori iron uptake.Semantic proximity Read ↗

In Vivo Dissection of theHelicobacter pyloriFur Regulatory Circuit by Genome-Wide Location AnalysisSemantic proximity Read ↗

The Helicobacter pylori Homologue of the Ferric Uptake Regulator Is Involved in Acid ResistanceSemantic proximity Read ↗

Resistance to hydrogen peroxide in Helicobacter pylori: role of catalase (KatA) and Fur, and functional analysis of a novel gene product designated 'KatA-associated protein', KapA (HP0874).Semantic proximity Read ↗

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