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

Purification and Characterization of a Novel Cysteine Proteinase (Periodontain) from Porphyromonas gingivalis

1 Apr 1999

Abstract excerpt

Periodontal disease is characterized by inflammation of the periodontium manifested by recruitment of neutrophils, which can degranulate, releasing powerful proteinases responsible for destruction of connective tissues, and eventual loss of tooth attachment. Although the presence of host proteinase inhibitors (serpins) should minimize tissue damage by endogenous proteinases, this is not seen clinically, and it...

Read the complete abstract on PubMed

Topics

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

Share to Bone and Dental Protein Studies
Share to Enzyme Production and Characterization
Share to Oral microbiology and periodontitis research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 10212191
DOI: 10.1074/jbc.274.18.12245

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

Purification and Characterization of a Novel Cysteine Proteinase (Periodontain) from Porphyromonas gingivalisPMID 10212191Read ↗

Porphyromonas gingivalis proteinases as virulence factors in the development of periodontitisSemantic proximity Read ↗

Lysine- and arginine-specific proteinases from Porphyromonas gingivalis. Isolation, characterization, and evidence for the existence of complexes with hemagglutinins.Semantic proximity Read ↗

Cysteine Proteases of Porphyromonas GingivalisSemantic proximity Read ↗

Protease activities of vaginal <i>Porphyromonas</i> species disrupt coagulation and extracellular matrix in the cervicovaginal nicheSemantic proximity Read ↗

Structure and Mechanism of Cysteine Peptidase Gingipain K (Kgp), a Major Virulence Factor of Porphyromonas gingivalis in PeriodontitisSemantic proximity Read ↗

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

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

Activation of complement components C3 and C5 by a cysteine proteinase (gingipain-1) from Porphyromonas (Bacteroides) gingivalis.Semantic proximity Read ↗

Role of bacterial proteinases in matrix destruction and modulation of host responsesSemantic proximity Read ↗

Proteases of <i>Porphyromonas gingivalis</i>: what don't they do?Semantic proximity Read ↗

Molecular genetics and nomenclature of proteases of Porphyromonas gingivalisSemantic proximity Read ↗

Cloning and sequencing of the gene encoding a novel lysine-specific cysteine proteinase (Lys-gingipain) in Porphyromonas gingivalis: structural relationship with the arginine-specific cysteine proteinase (Arg-gingipain).Semantic proximity Read ↗

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