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acetyl-lysine-4-nitroanilide + H2O
acetyl-lysine + 4-nitroaniline
-
-
-
-
?
acid-soluble human placental type I collagen + H2O
fragments of acid-soluble human placental type I collagen
-
-
-
-
?
adrenocorticotropic hormone fragment 11-24 + H2O
fragments of adrenocorticotropic hormone fragment 11-24
-
-
-
?
benzyloxycarbonyl-L-Lys-p-nitroanilide + H2O
benzyloxycarbonyl-L-Lys + p-nitroaniline + H2O
beta-endorphin + H2O
fragments of beta-endorphin
-
-
-
?
bovine hemoglobin + H2O
fragments of bovine hemoglobin
-
-
-
-
?
bovine serum albumin + H2O
fragments of bovine serum albumin
-
-
-
-
?
bradykinin + H2O
fragments of bradykinin
-
together with gingipain R, gingipain K induces vascular permeability enhancement in human plasma by cleaving bradykinin from high molecular weight kininogen
-
?
casein + H2O
fragments of casein
-
-
-
-
?
CBZ-Phe-Arg-4-methyl-coumaryl-7-amide + H2O
?
-
-
-
-
?
CD46 + H2O
?
-
recombinant CD46 is degraded by Lys-gingipain in a dose-dependent manner
-
-
?
D-Val-Leu-Lys-p-nitroanilide + H2O
D-Val-Leu-Lys + p-nitroaniline
D-Val-Phe-Lys-p-nitroanilide + H2O
D-Val-Phe-Lys + p-nitroaniline
elafin + H2O
?
all three gingipains have the ability to degrade elafin (endogenous inhibitor secreted by epithelial cells)
-
-
?
Fibrinogen + H2O
Fragments of fibrinogen
focal adhesion kinase + H2O
?
-
Kgp is responsible for degradation of integrin-related molecules
-
-
?
haptoglobin + H2O
fragments of haptoglobin
-
human serum haptoglobin
-
?
hemoglobin + H2O
fragments of hemoglobin
-
human serum hemoglobin
-
?
hemopexin + H2O
fragments of hemopexin
-
human serum hemopexin
-
?
human beta-defensin 3 + H2O
?
-
-
-
-
?
human IgA + H2O
cleaved human IgA
-
-
-
-
?
human IgG + H2O
fragments of human IgG
-
-
-
-
?
IgG1 + H2O
?
-
The heavy chain of IgG1 is cleaved at a single site within the hinge region, generating Fab and Fc fragments
-
-
?
IgG3 + H2O
?
-
IgG3 is cleaved within the heavy chain and at several sites around the CH2 region
-
-
?
IL-6 + H2O
fragments of IL-6
-
-
-
?
interleukin 8 + H2O
fragments of interleukin 8
interleukin-1beta + H2O
?
melittin + H2O
fragments of melittin
-
-
-
?
MeoSuc-Ala-Ala-Pro-Val-4-nitroanilide + H2O
?
-
-
-
?
Met-Lys-bradykinin + H2O
fragments of Met-Lys-bradykinin
-
-
-
?
monocyte chemotactic protein 1 + H2O
fragments of monocyte chemotactic protein 1
-
degradation of human monocyte chemotactic protein 1 in Porphyromonas gingivalis-infected human umbilical vein endothelial cells
-
?
N-(p-tosyl)-Gly-Pro-Lys 4-nitroanilide + H2O
?
-
-
-
-
?
N-(p-tosyl)-Gly-Pro-Lys-4-nitroanilide + H2O
N-(p-tosyl)-Gly-Pro-Lys + 4-nitroaniline
-
-
-
-
?
N-4-tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
N-4-tosyl-Gly-Pro-Lys + 4-nitroaniline
-
-
-
-
?
N-alpha-acetyl-L-lysine-4-nitroanilide + H2O
N-alpha-acetyl-L-lysine + 4-nitroaniline
-
-
-
-
?
N-alpha-acetyl-L-lysine-p-nitroanilide + H2O
N-alpha-acetyl-L-lysine + 4-nitroaniline
-
-
-
-
r
N-alpha-benzoyl-DL-lysine 4-nitroanilide + H2O
N-alpha-benzoyl-DL-lysine + 4-nitroaniline
-
-
-
-
?
N-alpha-benzyloxycarbonyl-L-lysine-4-nitroanilide + H2O
N-alpha-benzyloxycarbonyl-L-lysine + 4-nitroaniline
N-p-tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Lys + 4-nitroaniline
-
-
-
-
?
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Lys + p-nitroaniline
Nalpha-acetyl-L-lysine 4-nitroanilide + H2O
Nalpha-acetyl-L-lysine + 4-nitroaniline
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-lysine 4-nitroanilide + H2O
Nalpha-benzyloxycarbonyl-L-lysine + 4-nitroaniline
-
-
-
-
?
neurotensin + H2O
pGlu-Leu-Tyr-Glu-Asn-Lys + Pro-Arg-Arg-Pro-Tyr-Ile-Leu
oxyhaemoglobin + H2O
?
-
-
-
-
?
paxillin + H2O
?
-
Kgp is responsible for degradation of integrin-related molecules
-
-
?
protease-activated receptor-2 + H2O
?
-
specific substrate for Lys-gingipain
-
-
?
t-butyl-oxycarbonyl-L-Glu-L-Lys-L-Lys-4-methyl-7-coumarylamide + H2O
t-butyl-oxycarbonyl-L-Glu-L-Lys-L-Lys + 7-amino-4-methylcoumarin
-
41% of activity with t-butyl-oxycarbonyl-L-Val-L-Leu-L-Lys-4-methyl-7-coumarylamide
-
?
t-butyl-oxycarbonyl-L-Val-L-Leu-L-Lys-4-methyl-7-coumarylamide + H2O
t-butyl-oxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
-
gingipain K has a stron preference for substrates containing Lys in the p1 site
-
?
t-butyloxycarbonyl-Val-Leu-Lys-Phe-Arg-4-methyl-7-coumarylamide
t-butyl-oxycarbonyl-Val-Leu-Lys + Phe-Arg-4-methyl-7-coumarylaminde
-
-
-
-
?
thrombomodulin + H2O
?
-
Lys-gingipain and Arg-gingipain cleave thrombomodulin in vitro
-
-
?
transferrin + H2O
fragments of transferrin
-
human serum transferrin
-
?
Val-Leu-Lys-4-nitroanilide + h2O
Val-Leu-Lys + 4-nitroaniline
-
-
-
-
?
additional information
?
-
benzyloxycarbonyl-L-Lys-p-nitroanilide + H2O
benzyloxycarbonyl-L-Lys + p-nitroaniline + H2O
-
-
-
?
benzyloxycarbonyl-L-Lys-p-nitroanilide + H2O
benzyloxycarbonyl-L-Lys + p-nitroaniline + H2O
-
7% of activity with N-p-tosyl-Gly-Pro-Lys-p-nitroanilide
-
-
?
benzyloxycarbonyl-L-Lys-p-nitroanilide + H2O
benzyloxycarbonyl-L-Lys + p-nitroaniline + H2O
-
-
-
?
D-Val-Leu-Lys-p-nitroanilide + H2O
D-Val-Leu-Lys + p-nitroaniline
-
-
-
?
D-Val-Leu-Lys-p-nitroanilide + H2O
D-Val-Leu-Lys + p-nitroaniline
-
-
-
?
D-Val-Leu-Lys-p-nitroanilide + H2O
D-Val-Leu-Lys + p-nitroaniline
-
-
-
?
D-Val-Phe-Lys-p-nitroanilide + H2O
D-Val-Phe-Lys + p-nitroaniline
-
-
-
?
D-Val-Phe-Lys-p-nitroanilide + H2O
D-Val-Phe-Lys + p-nitroaniline
-
70% of activity with N-p-tosyl-Gly-Pro-Lys-p-nitroanilide
-
?
D-Val-Phe-Lys-p-nitroanilide + H2O
D-Val-Phe-Lys + p-nitroaniline
-
-
-
?
Fibrinogen + H2O
Fragments of fibrinogen
-
prominent target among plasma proteins
-
?
Fibrinogen + H2O
Fragments of fibrinogen
-
most prominent target among plasma proteins
-
-
?
Hemoglobin + H2O
?
-
degradation
-
-
?
Hemoglobin + H2O
?
-
degradation, the enzyme forms a complex with the outer membrane receptor HmuR required for binding and utilization of hemoglobin and hemin, overview
-
-
?
interleukin 8 + H2O
fragments of interleukin 8
-
-
-
-
?
interleukin 8 + H2O
fragments of interleukin 8
-
degradation of human interleukin 8 in Porphyromonas gingivalis-infected human umbilical vein endothelial cells
-
?
interleukin-1beta + H2O
?
-
low activity
-
-
?
interleukin-1beta + H2O
?
-
biological inactivation and degradation, low activity, cytokine degradation is mainly the result of Lys-gingipain
-
-
?
interleukin-6 + H2O
?
-
-
-
-
?
interleukin-6 + H2O
?
-
biological inactivation and degradation
-
-
?
interleukin-8 + H2O
?
-
-
-
-
?
interleukin-8 + H2O
?
-
biological inactivation and degradation
-
-
?
methemoglobin + H2O
?
-
methemoglobin, formed by treatment of oxyHb with either NaNO2 or by pre-incubation with HRgpA, is rapidly degraded by Kgp compared to oxyhemoglobin
-
-
?
methemoglobin + H2O
?
-
degradation, ligation of methemoglobin with N3-, which effectively blocks heme dissociation from the protein, prevents hemoglobin breakdown
-
-
?
methemoglobin + H2O
?
-
from horse, degradation, no activity with oxyhemoglobin
-
-
?
methemoglobin + H2O
?
-
methemoglobin, formed by treatment of oxyHb with either NaNO2 or by pre-incubation with HRgpA, is rapidly degraded by Kgp compared to oxyhemoglobin
-
-
?
N-alpha-benzyloxycarbonyl-L-lysine-4-nitroanilide + H2O
N-alpha-benzyloxycarbonyl-L-lysine + 4-nitroaniline
-
-
-
-
?
N-alpha-benzyloxycarbonyl-L-lysine-4-nitroanilide + H2O
N-alpha-benzyloxycarbonyl-L-lysine + 4-nitroaniline
-
-
-
-
?
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Lys + p-nitroaniline
-
-
-
?
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Lys + p-nitroaniline
-
-
-
?
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Lys + p-nitroaniline
-
gingipain K cleaves specifically on the C-terminal side of peptide substrates
-
?
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Lys + p-nitroaniline
-
gingipain K cleaves specifically on the C-terminal side of peptide substrates
-
?
neurotensin + H2O
pGlu-Leu-Tyr-Glu-Asn-Lys + Pro-Arg-Arg-Pro-Tyr-Ile-Leu
-
-
-
?
neurotensin + H2O
pGlu-Leu-Tyr-Glu-Asn-Lys + Pro-Arg-Arg-Pro-Tyr-Ile-Leu
-
-
-
?
osteoprotegerin + H2O
?
-
degradation
-
-
?
osteoprotegerin + H2O
?
-
digestion, enhanced osteoclastogenesis by Kgp, in co-cultures of mouse bone-marrow cells and osteoblasts, formation of multinucleated osteoclasts induced by 1alpha,25-dihydroxyvitamin D3 is augmented by Kgp. The specific enzymatic activity of Kgp is necessary for osteoclast formation, overview
-
-
?
osteoprotegerin + H2O
?
-
degradation
-
-
?
osteoprotegerin + H2O
?
-
digestion, enhanced osteoclastogenesis by Kgp, in co-cultures of mouse bone-marrow cells and osteoblasts, formation of multinucleated osteoclasts induced by 1alpha,25-dihydroxyvitamin D3 is augmented by Kgp. The specific enzymatic activity of Kgp is necessary for osteoclast formation, overview
-
-
?
TNFalpha + H2O
?
-
degradation
-
-
?
TNFalpha + H2O
?
-
degradation, leading to inhibition of biological functions of TNFalpha, overview
-
-
?
additional information
?
-
-
a combination of both arginine- and lysine-specific gingipain activity is necessary for the generation of the micro-oxo bishaem-containing pigment from haemoglobin, interaction with oxyhemoglobin, overview
-
-
?
additional information
?
-
-
gingipain K adds to gingipain R-mediated coaggregation of Porphyromonas gingivalis with other oral bacteria, it is a virulence factor, overview
-
-
?
additional information
?
-
-
gingipains are essential for bacterial virulence and survival
-
-
?
additional information
?
-
-
the C-terminal domains of the gingipain K polyprotein are necessary for assembly of the active enzyme and expression of associated activities
-
-
?
additional information
?
-
-
the enzyme degrades host iron- and heme-containing proteins, regulation of enzyme expression, overview, inhibition of gingipain increases the hmuR gene expression encoding the heme/hemoglobin receptor HmuR, and decreases the cell growth in the early and middle stages, but not in the late stages, hmuR expression inhibition decreases enzyme expression
-
-
?
additional information
?
-
-
the enzyme inactivates a cell surface ligand on Porphyromonas gingivalis that induces TLR2-and TLR4-independent signaling involving CD25, but has no effect on TLR2-and TLR4-dependent signaling, overview
-
-
?
additional information
?
-
-
role of the Sn binding pocket, molecular basis for substrate specificity, overview
-
-
?
additional information
?
-
-
extracellular gingipain protease activities cause a lack of secondary cytokine response in human cells after challenge with live Porphyromonas gingivalis
-
-
?
additional information
?
-
-
gingipains are considered to be key virulence factors of the bacterium in relation to periodontal diseases. Kgp suppresses interleukin-8 production in human HSC-2 epithelial cells requiring both the hemagglutinin and the enzymic domains. Suppression of IL-8 resultes in attenuation of the cellular recognition of bacteria, and as a consequence, sustain chronic inflammation
-
-
?
additional information
?
-
-
gingipains are cysteine proteinases and virulence factors of Porphyromonas gingivalis, the major causative bacterium of periodontal disease. Gingipains stimulate interleukin-8 secretion from human THP-1 cells, which is completely inhibited by proteinase inhibitors of gingipain and is increased in the presence of pathogen-associated molecular patterns, PAMPs. The synergism of gingipain HRgpA and PAMPs stimulates interleukin IL-6, and monocyte chemoattractant protein MCP-1 secretion, overview
-
-
?
additional information
?
-
-
gingipains are key virulence determinants of Porphyromonas gingivalis and play a crucial role in pathogenicity
-
-
?
additional information
?
-
-
gingipains reduce cyclin expression and cause early G1 arrest, leading to the inhibition of cellular proliferation in murine ST2 osteoblastic/stromal cells, overview
-
-
?
additional information
?
-
-
the membrane protein PG27, encoded by gene PG0027, is essential for the secretion of gingipains, overview
-
-
?
additional information
?
-
-
gingipains reduce cyclin expression and cause early G1 arrest, leading to the inhibition of cellular proliferation in murine ST2 osteoblastic/stromal cells, overview
-
-
?
additional information
?
-
-
gingipains are essential for bacterial virulence and survival
-
-
?
additional information
?
-
-
role of the Sn binding pocket, molecular basis for substrate specificity, overview
-
-
?
additional information
?
-
-
gingipains are considered to be key virulence factors of the bacterium in relation to periodontal diseases. Kgp suppresses interleukin-8 production in human HSC-2 epithelial cells requiring both the hemagglutinin and the enzymic domains. Suppression of IL-8 resultes in attenuation of the cellular recognition of bacteria, and as a consequence, sustain chronic inflammation
-
-
?
additional information
?
-
-
the membrane protein PG27, encoded by gene PG0027, is essential for the secretion of gingipains, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
bradykinin + H2O
fragments of bradykinin
-
together with gingipain R, gingipain K induces vascular permeability enhancement in human plasma by cleaving bradykinin from high molecular weight kininogen
-
-
?
elafin + H2O
?
all three gingipains have the ability to degrade elafin (endogenous inhibitor secreted by epithelial cells)
-
-
?
Fibrinogen + H2O
Fragments of fibrinogen
-
most prominent target among plasma proteins
-
-
?
focal adhesion kinase + H2O
?
-
Kgp is responsible for degradation of integrin-related molecules
-
-
?
Hemoglobin + H2O
?
-
degradation, the enzyme forms a complex with the outer membrane receptor HmuR required for binding and utilization of hemoglobin and hemin, overview
-
-
?
interleukin 8 + H2O
fragments of interleukin 8
interleukin-1beta + H2O
?
-
biological inactivation and degradation, low activity, cytokine degradation is mainly the result of Lys-gingipain
-
-
?
interleukin-6 + H2O
?
-
biological inactivation and degradation
-
-
?
interleukin-8 + H2O
?
-
biological inactivation and degradation
-
-
?
methemoglobin + H2O
?
-
degradation, ligation of methemoglobin with N3-, which effectively blocks heme dissociation from the protein, prevents hemoglobin breakdown
-
-
?
monocyte chemotactic protein 1 + H2O
fragments of monocyte chemotactic protein 1
-
degradation of human monocyte chemotactic protein 1 in Porphyromonas gingivalis-infected human umbilical vein endothelial cells
-
-
?
paxillin + H2O
?
-
Kgp is responsible for degradation of integrin-related molecules
-
-
?
protease-activated receptor-2 + H2O
?
-
specific substrate for Lys-gingipain
-
-
?
TNFalpha + H2O
?
-
degradation, leading to inhibition of biological functions of TNFalpha, overview
-
-
?
additional information
?
-
interleukin 8 + H2O
fragments of interleukin 8
-
-
-
-
?
interleukin 8 + H2O
fragments of interleukin 8
-
degradation of human interleukin 8 in Porphyromonas gingivalis-infected human umbilical vein endothelial cells
-
-
?
osteoprotegerin + H2O
?
-
digestion, enhanced osteoclastogenesis by Kgp, in co-cultures of mouse bone-marrow cells and osteoblasts, formation of multinucleated osteoclasts induced by 1alpha,25-dihydroxyvitamin D3 is augmented by Kgp. The specific enzymatic activity of Kgp is necessary for osteoclast formation, overview
-
-
?
osteoprotegerin + H2O
?
-
digestion, enhanced osteoclastogenesis by Kgp, in co-cultures of mouse bone-marrow cells and osteoblasts, formation of multinucleated osteoclasts induced by 1alpha,25-dihydroxyvitamin D3 is augmented by Kgp. The specific enzymatic activity of Kgp is necessary for osteoclast formation, overview
-
-
?
additional information
?
-
-
a combination of both arginine- and lysine-specific gingipain activity is necessary for the generation of the micro-oxo bishaem-containing pigment from haemoglobin, interaction with oxyhemoglobin, overview
-
-
?
additional information
?
-
-
gingipain K adds to gingipain R-mediated coaggregation of Porphyromonas gingivalis with other oral bacteria, it is a virulence factor, overview
-
-
?
additional information
?
-
-
gingipains are essential for bacterial virulence and survival
-
-
?
additional information
?
-
-
the C-terminal domains of the gingipain K polyprotein are necessary for assembly of the active enzyme and expression of associated activities
-
-
?
additional information
?
-
-
the enzyme degrades host iron- and heme-containing proteins, regulation of enzyme expression, overview, inhibition of gingipain increases the hmuR gene expression encoding the heme/hemoglobin receptor HmuR, and decreases the cell growth in the early and middle stages, but not in the late stages, hmuR expression inhibition decreases enzyme expression
-
-
?
additional information
?
-
-
the enzyme inactivates a cell surface ligand on Porphyromonas gingivalis that induces TLR2-and TLR4-independent signaling involving CD25, but has no effect on TLR2-and TLR4-dependent signaling, overview
-
-
?
additional information
?
-
-
extracellular gingipain protease activities cause a lack of secondary cytokine response in human cells after challenge with live Porphyromonas gingivalis
-
-
?
additional information
?
-
-
gingipains are considered to be key virulence factors of the bacterium in relation to periodontal diseases. Kgp suppresses interleukin-8 production in human HSC-2 epithelial cells requiring both the hemagglutinin and the enzymic domains. Suppression of IL-8 resultes in attenuation of the cellular recognition of bacteria, and as a consequence, sustain chronic inflammation
-
-
?
additional information
?
-
-
gingipains are cysteine proteinases and virulence factors of Porphyromonas gingivalis, the major causative bacterium of periodontal disease. Gingipains stimulate interleukin-8 secretion from human THP-1 cells, which is completely inhibited by proteinase inhibitors of gingipain and is increased in the presence of pathogen-associated molecular patterns, PAMPs. The synergism of gingipain HRgpA and PAMPs stimulates interleukin IL-6, and monocyte chemoattractant protein MCP-1 secretion, overview
-
-
?
additional information
?
-
-
gingipains are key virulence determinants of Porphyromonas gingivalis and play a crucial role in pathogenicity
-
-
?
additional information
?
-
-
gingipains reduce cyclin expression and cause early G1 arrest, leading to the inhibition of cellular proliferation in murine ST2 osteoblastic/stromal cells, overview
-
-
?
additional information
?
-
-
the membrane protein PG27, encoded by gene PG0027, is essential for the secretion of gingipains, overview
-
-
?
additional information
?
-
-
gingipains reduce cyclin expression and cause early G1 arrest, leading to the inhibition of cellular proliferation in murine ST2 osteoblastic/stromal cells, overview
-
-
?
additional information
?
-
-
gingipains are essential for bacterial virulence and survival
-
-
?
additional information
?
-
-
gingipains are considered to be key virulence factors of the bacterium in relation to periodontal diseases. Kgp suppresses interleukin-8 production in human HSC-2 epithelial cells requiring both the hemagglutinin and the enzymic domains. Suppression of IL-8 resultes in attenuation of the cellular recognition of bacteria, and as a consequence, sustain chronic inflammation
-
-
?
additional information
?
-
-
the membrane protein PG27, encoded by gene PG0027, is essential for the secretion of gingipains, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Potempa, J.; Pike, R.; Travis, J.
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Baba, A.; Kadowaki, T.; Asao, T.; Yamamoto, K.
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Porphyromonas gingivalis
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Smalley, J.W.; Thomas, M.F.; Birss, A.J.; Withnall, R.; Silver, J.
A combination of both arginine- and lysine-specific gingipain activity of Porphyromonas gingivalis is necessary for the generation of the micro-oxo bishaem-containing pigment from haemoglobin
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Liu, X.; Sroka, A.; Potempa, J.; Genco, C.A.
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Mezyk-Kopec, R.; Bzowska, M.; Potempa, J.; Bzowska, M.; Jura, N.; Sroka, A.; Black, R.A.; Bereta, J.
Inactivation of membrane tumor necrosis factor alpha by gingipains from Porphyromonas gingivalis
Infect. Immun.
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Porphyromonas gingivalis
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Bialas, A.; Grembecka, J.; Krowarsch, D.; Otlewski, J.; Potempa, J.; Mucha, A.
Exploring the Sn binding pockets in gingipains by newly developed inhibitors: structure-based design, chemistry, and activity
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Kishimoto, M.; Yoshimura, A.; Naito, M.; Okamoto, K.; Yamamoto, K.; Golenbock, D.T.; Hara, Y.; Nakayama, K.
Gingipains inactivate a cell surface ligand on Porphyromonas gingivalis that induces TLR2-and TLR4-independent signaling
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Sztukowska, M.; Sroka, A.; Bugno, M.; Banbula, A.; Takahashi, Y.; Pike, R.N.; Genco, C.A.; Travis, J.; Potempa, J.
The C-terminal domains of the gingipain K polyprotein are necessary for assembly of the active enzyme and expression of associated activities
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Cronan, C.A.; Potempa, J.; Travis, J.; Mayo, J.A.
Inhibition of Porphyromonas gingivalis proteinases (gingipains) by chlorhexidine: synergistic effect of Zn(II)
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Ishida, Y.; Hu, J.; Sakai, E.; Kadowaki, T.; Yamamoto, K.; Tsukuba, T.; Kato, Y.; Nakayama, K.; Okamoto, K.
Determination of active site of lysine-specific cysteine proteinase (Lys-gingipain) by use of a Porphyromonas gingivalis plasmid system
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Slaney, J.M.; Gallagher, A.; Aduse-Opoku, J.; Pell, K.; Curtis, M.A.
Mechanisms of resistance of Porphyromonas gingivalis to killing by serum complement
Infect. Immun.
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Porphyromonas gingivalis
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Hashimoto, M.; Kadowaki, T.; Tsukuba, T.; Yamamoto, K.
Selective proteolysis of apolipoprotein B-100 by Arg-gingipain mediates atherosclerosis progression accelerated by bacterial exposure
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Porphyromonas gingivalis
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Smalley, J.W.; Birss, A.J.; Szmigielski, B.; Potempa, J.
The HA2 haemagglutinin domain of the lysine-specific gingipain (Kgp) of Porphyromonas gingivalis promotes micro-oxo bishaem formation from monomeric iron(III) protoporphyrin IX
Microbiology
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Yasuhara, R.; Miyamoto, Y.; Takami, M.; Imamura, T.; Potempa, J.; Yoshimura, K.; Kamijo, R.
Lysine-specific gingipain promotes lipopolysaccharide- and active-vitamin D3-induced osteoclast differentiation by degrading osteoprotegerin
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Porphyromonas gingivalis, Porphyromonas gingivalis HG66
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Smalley, J.W.; Birss, A.J.; Szmigielski, B.; Potempa, J.
Mechanism of methaemoglobin breakdown by the lysine-specific gingipain of the periodontal pathogen Porphyromonas gingivalis
Biol. Chem.
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Uehara, A.; Imamura, T.; Potempa, J.; Travis, J.; Takada, H.
Gingipains from Porphyromonas gingivalis synergistically induce the production of proinflammatory cytokines through protease-activated receptors with Toll-like receptor and NOD1/2 ligands in human monocytic cells
Cell. Microbiol.
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Ishiguro, I.; Saiki, K.; Konishi, K.
PG27 is a novel membrane protein essential for a Porphyromonas gingivalis protease secretion system
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Porphyromonas gingivalis, Porphyromonas gingivalis W83
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Uehara, A.; Naito, M.; Imamura, T.; Potempa, J.; Travis, J.; Nakayama, K.; Takada, H.
Dual regulation of interleukin-8 production in human oral epithelial cells upon stimulation with gingipains from Porphyromonas gingivalis
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Porphyromonas gingivalis, Porphyromonas gingivalis HG66
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Bania, J.; Kubiak, A.; Wojtachnio, K.; Polanowski, A.
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Kato, T.; Tsuda, T.; Inaba, H.; Kawai, S.; Okahashi, N.; Shibata, Y.; Abiko, Y.; Amano, A.
Porphyromonas gingivalis gingipains cause G(1) arrest in osteoblastic/stromal cells
Oral Microbiol. Immunol.
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Porphyromonas gingivalis, Porphyromonas gingivalis ATCC 33277
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Stathopoulou, P.G.; Benakanakere, M.R.; Galicia, J.C.; Kinane, D.F.
The host cytokine response to Porphyromonas gingivalis is modified by gingipains
Oral Microbiol. Immunol.
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Porphyromonas gingivalis
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Taiyoji, M.; Shitomi, Y.; Taniguchi, M.; Saitoh, E.; Ohtsubo, S.
Identification of proteinaceous inhibitors of a cysteine proteinase (an Arg-specific gingipain) from Porphyromonas gingivalis in rice grain, using targeted-proteomics approaches
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Porphyromonas gingivalis
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Kantyka, T.; Latendorf, T.; Wiedow, O.; Bartels, J.; Glaeser, R.; Dubin, G.; Schroeder, J.M.; Potempa, J.; Meyer-Hoffert, U.
Elafin is specifically inactivated by RgpB from Porphyromonas gingivalis by distinct proteolytic cleavage
Biol. Chem.
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Porphyromonas gingivalis (B2RLK2)
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Stathopoulou, P.; Galicia, J.; Benakanakere, M.; Garcia, C.; Potempa, J.; Kinane, D.
Porphyromonas gingivalis induce apoptosis in human gingival epithelial cells through a gingipain-dependent mechanism
BMC Microbiol.
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Porphyromonas gingivalis
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Kuboniwa, M.; Amano, A.; Hashino, E.; Yamamoto, Y.; Inaba, H.; Hamada, N.; Nakayama, K.; Tribble, G.D.; Lamont, R.J.; Shizukuishi, S.
Distinct roles of long/short fimbriae and gingipains in homotypic biofilm development by Porphyromonas gingivalis
BMC Microbiol.
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Saiki, K.; Konishi, K.
The role of Sov protein in the secretion of gingipain protease virulence factors of Porphyromonas gingivalis
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Porphyromonas gingivalis
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Haruyama, K.; Yoshimura, A.; Naito, M.; Kishimoto, M.; Shoji, M.; Abiko, Y.; Hara, Y.; Nakayama, K.
Identification of a gingipain-sensitive surface ligand of Porphyromonas gingivalis that induces Toll-like receptor 2- and 4-independent NF-kappaB activation in CHO cells
Infect. Immun.
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Porphyromonas gingivalis
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Furuta, N.; Takeuchi, H.; Amano, A.
Entry of Porphyromonas gingivalis outer membrane vesicles into epithelial cells causes cellular functional impairment
Infect. Immun.
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Porphyromonas gingivalis
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Nhien, N.T.; Huy, N.T.; Naito, M.; Oida, T.; Uyen, D.T.; Huang, M.; Kikuchi, M.; Harada, S.; Nakayama, K.; Hirayama, K.; Kamei, K.
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Fitzpatrick, R.E.; Aprico, A.; Wijeyewickrema, L.C.; Pagel, C.N.; Wong, D.M.; Potempa, J.; Mackie, E.J.; Pike, R.N.
High molecular weight gingipains from Porphyromonas gingivalis induce cytokine responses from human macrophage-like cells via a nonproteolytic mechanism
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Porphyromonas gingivalis
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Inomata, M.; Ishihara, Y.; Matsuyama, T.; Imamura, T.; Maruyama, I.; Noguchi, T.; Matsushita, K.
Degradation of vascular endothelial thrombomodulin by arginine- and lysine-specific cysteine proteases from Porphyromonas gingivalis
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Porphyromonas gingivalis
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Giacaman, R.A.; Asrani, A.C.; Ross, K.F.; Herzberg, M.C.
Cleavage of protease-activated receptors on an immortalized oral epithelial cell line by Porphyromonas gingivalis gingipains
Microbiology
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Porphyromonas gingivalis
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Li, N.; Yun, P.; Nadkarni, M.; Ghadikolaee, N.; Nguyen, K.; Lee, M.; Hunter, N.; Collyer, C.
Structure determination and analysis of a haemolytic gingipain adhesin domain from Porphyromonas gingivalis
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Porphyromonas gingivalis
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Mahtout, H.; Chandad, F.; Rojo, J.M.; Grenier, D.
Porphyromonas gingivalis mediates the shedding and proteolysis of complement regulatory protein CD46 expressed by oral epithelial cells
Oral Microbiol. Immunol.
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Porphyromonas gingivalis
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Toh, E.C.; Dashper, S.G.; Huq, N.L.; Attard, T.J.; OBrien-Simpson, N.M.; Chen, Y.Y.; Cross, K.J.; Stanton, D.P.; Paolini, R.A.; Reynolds, E.C.
Porphyromonas gingivalis cysteine proteinase inhibition by kappa-casein peptides
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Porphyromonas gingivalis
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Dashper, S.G.; Pan, Y.; Veith, P.D.; Chen, Y.Y.; Toh, E.C.; Liu, S.W.; Cross, K.J.; Reynolds, E.C.
Lactoferrin inhibits Porphyromonas gingivalis proteinases and has sustained biofilm inhibitory activity
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Porphyromonas gingivalis
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Vincents, B.; Guentsch, A.; Kostolowska, D.; von Pawel-Rammingen, U.; Eick, S.; Potempa, J.; Abrahamson, M.
Cleavage of IgG1 and IgG3 by gingipain K from Porphyromonas gingivalis may compromise host defense in progressive periodontitis
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Porphyromonas gingivalis
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Maisetta, G.; Brancatisano, F.; Esin, S.; Campa, M.; Batoni, G.
Gingipains produced by Porphyromonas gingivalis ATCC49417 degrade human-beta-defensin 3 and affect peptides antibacterial activity in vitro
Peptides
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Porphyromonas gingivalis
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Smalley, J.; Byrne, D.; Birss, A.; Wojtowicz, H.; Sroka, A.; Potempa, J.; Olczak, T.
HmuY haemophore and gingipain proteases constitute a unique syntrophic system of haem acquisition by Porphyromonas gingivalis
PLoS ONE
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Porphyromonas gingivalis
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Pomowski, A.; Uson, I.; Nowakowska, Z.; Veillard, F.; Sztukowska, M.N.; Guevara, T.; Goulas, T.; Mizgalska, D.; Nowak, M.; Potempa, B.; Huntington, J.A.; Potempa, J.; Gomis-Rueth, F.X.
Structural insights unravel the zymogenic mechanism of the virulence factor gingipain K from Porphyromonas gingivalis, a causative agent of gum disease from the human oral microbiome
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Structural determinants of inhibition of Porphyromonas gingivalis gingipain K by KYT-36, a potent, selective, and bioavailable peptidase inhibitor
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