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

Arginine 66 residue of Fur is required for the regulatory function of this protein in the acid adaptation mechanism of Helicobacter pylori.

Helicobacter - 1 Feb 2012

Toledo Héctor, Villafaena Carlos, Valenzuela Manuel, López-Solís Remigio

Abstract excerpt

BACKGROUND: Helicobacter pylori colonizes the gastric mucosa and must survive the acid pH of that environment. Like other enteric bacterial pathogens, including Salmonella enterica, H. pylori develops an acid tolerance response that is dependent on the function of the transcriptional regulator protein Fur. OBJECTIVE: To explore by site-directed mutagenesis whether two particular amino acid residues in the amino...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Gastric Mucosa

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Expression Regulation, Bacterial

Share to Helicobacter Infections

Share to Helicobacter pylori

Share to Histidine

Share to Hydrogen-Ion Concentration

Share to Mutagenesis, Site-Directed

Source

Identifiers

PMID: 22221611
DOI: 10.1111/j.1523-5378.2011.00893.x

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Arginine 66 residue of Fur is required for the regulatory function of this protein in the acid adaptation mechanism of Helicobacter pylori.PMID 22221611Read ↗

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

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

The role of fur in the acid tolerance response of Salmonella typhimurium is physiologically and genetically separable from its role in iron acquisition.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 ↗

Characterization of the Arginine Decarboxylase Gene (<scp>ORF HP</scp>0422, <i>speA</i>) Involved in Acid Tolerance in <i><scp>H</scp>elicobacter pylori</i>Semantic proximity Read ↗

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

Chaperone-dependent mechanisms for acid resistance in enteric bacteriaSemantic proximity Read ↗

Characterization of the ArsRS Regulon ofHelicobacter pylori, Involved in Acid AdaptationSemantic proximity Read ↗

Histidine residue 94 is involved in pH sensing by histidine kinase ArsS of Helicobacter pylori.Semantic proximity Read ↗

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

Structural, functional and mutational analysis of the pfr gene encoding a ferritin from Helicobacter pylori.Semantic proximity Read ↗

Effects of a HP0859 (rfaD) knockout mutation on lipopolysaccharide structure of Helicobacter pylori 26695 and the bacterial adhesion on AGS cells.Semantic proximity Read ↗

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