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

Lysine-specific gingipain K and heme/hemoglobin receptor HmuR are involved in heme utilization in Porphyromonas gingivalis.

Acta biochimica Polonica - 1 Jan 2004

Simpson Waltena, Olczak Teresa, Genco Caroline A

Abstract excerpt

We have previously reported on the identification and characterization of the Porphyromonas gingivalis A7436 strain outer membrane receptor HmuR, which is involved in the acquisition of hemin and hemoglobin. We demonstrated that HmuR interacts with the lysine- (Kgp) and arginine- (HRgpA) specific proteases (gingipains) and that Kgp and HRgpA can bind and degrade hemoglobin. Here, we report on the physiological...

Read the complete abstract on PubMed

Topics

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

Share to Adhesins, Bacterial
Share to Cysteine Endopeptidases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hemagglutinins

Share to Hemoglobins

Share to Porphyromonas gingivalis

Share to Receptors, Cell Surface

Source

Identifiers

PMID: 15094847

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

Lysine-specific gingipain K and heme/hemoglobin receptor HmuR are involved in heme utilization in Porphyromonas gingivalis.PMID 15094847Read ↗

Identification of Amino Acid Residues Involved in Heme Binding and Hemoprotein Utilization in the Porphyromonas gingivalis Heme Receptor HmuRSemantic proximity Read ↗

Exploring heme and iron acquisition strategies of Porphyromonas gingivalis—current facts and hypothesesSemantic proximity Read ↗

Interplay between Porphyromonas gingivalis Hemophore-Like Protein HmuY and Kgp/RgpA Gingipains Plays a Superior Role in Heme SupplySemantic proximity Read ↗

Defining the role of Hmu and Hus systems in Porphyromonas gingivalis heme and iron homeostasis and virulenceSemantic proximity Read ↗

Involvement of a lysine-specific cysteine proteinase in hemoglobin adsorption and heme accumulation by Porphyromonas gingivalis.Semantic proximity Read ↗

Iron and heme utilization in<i>Porphyromonas gingivalis</i>Semantic proximity Read ↗

Hemophore-like proteins of the HmuY family in the oral and gut microbiome: unraveling the mystery of their evolutionSemantic proximity Read ↗

Bacteroides fragilis expresses three proteins similar to Porphyromonas gingivalis HmuY : Hemophore‐like proteins differentially evolved to participate in heme acquisition in oral and gut microbiomesSemantic proximity Read ↗

Hemoglobin hydrolysis and heme acquisition by Porphyromonas gingivalis.Semantic proximity Read ↗

Porphyromonas gingivalis Gingipains: The Molecular Teeth of a Microbial VampireSemantic proximity Read ↗

Porphyromonas gingivalis proteinases as virulence determinants in progression of periodontal diseases.Semantic proximity Read ↗

HmuY is an important virulence factor for Porphyromonas gingivalis growth in the heme-limited host environment and infection of macrophages.Semantic proximity Read ↗

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