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Disease on EC 3.4.22.47 - gingipain K

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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Chronic Periodontitis
Design and synthesis of sensitive fluorogenic substrates specific for Lys-gingipain.
Porphyromonas gingivalis Gingipains Trigger a Proinflammatory Response in Human Monocyte-derived Macrophages Through the p38? Mitogen-activated Protein Kinase Signal Transduction Pathway.
Selective proteolysis of apolipoprotein B-100 by Arg-gingipain mediates atherosclerosis progression accelerated by bacterial exposure.
Gingivitis
Suppression of gingival inflammation induced by Porphyromonas gingivalis in rats by leupeptin.
[Clinical association of gingipain K-caspase like subdomain expression of Porphyromonas gingivalis with puberty gingivitis]
[Detection of gingipain K in the gingival crevicular fluid of orthodontic patients].
Infections
Specific antibodies to Porphyromonas gingivalis Lys-gingipain by DNA vaccination inhibit bacterial binding to hemoglobin and protect mice from infection.
Structure and mechanism of cysteine peptidase gingipain K (Kgp), a major virulence factor of Porphyromonas gingivalis in periodontitis.
Neoplasms
Porphyromonas gingivalis-derived lysine gingipain enhances osteoclast differentiation induced by tumor necrosis factor-? and interleukin-1? but suppresses that by interleukin-17A: importance of proteolytic degradation of osteoprotegerin by lysine gingipain.
Periodontal Diseases
A novel, potent dual inhibitor of Arg-gingipains and Lys-gingipain as a promising agent for periodontal disease therapy.
Arg-gingipain is responsible for the degradation of cell adhesion molecules of human gingival fibroblasts and their death induced by Porphyromonas gingivalis.
Biochemical and functional properties of lysine-specific cysteine proteinase (Lys-gingipain) as a virulence factor of Porphyromonas gingivalis in periodontal disease.
Cleavage of host cytokeratin-6 by lysine-specific gingipain induces gingival inflammation in periodontitis patients.
Exploring the Sn binding pockets in gingipains by newly developed inhibitors: structure-based design, chemistry, and activity.
Porphyromonas gingivalis proteinases as virulence determinants in progression of periodontal diseases.
Suppression of pathogenicity of Porphyromonas gingivalis by newly developed gingipain inhibitors.
Periodontal Pocket
Degradation of host heme proteins by lysine- and arginine-specific cysteine proteinases (gingipains) of Porphyromonas gingivalis.
Periodontitis
A functional virulence complex composed of gingipains, adhesins, and lipopolysaccharide shows high affinity to host cells and matrix proteins and escapes recognition by host immune systems.
Cleavage of host cytokeratin-6 by lysine-specific gingipain induces gingival inflammation in periodontitis patients.
Cleavage of IgG1 and IgG3 by gingipain K from Porphyromonas gingivalis may compromise host defense in progressive periodontitis.
Novel synthetic peptide derived from Porphyromonas gingivalis Lys-gingipain detects IgG-mediated host response in periodontitis.
Porphyromonas gingivalis proteinases in periodontitis, a review.
Structure and mechanism of cysteine peptidase gingipain K (Kgp), a major virulence factor of Porphyromonas gingivalis in periodontitis.