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acetyl-Pro-Phe-Arg-4-nitroanilide + H2O
acetyl-Pro-Phe-Arg + 4-nitroaniline
D-Val-Leu-Arg-4-nitroanilide + H2O
D-Val-Leu-Arg + 4-nitroaniline
native and recombinant enzyme
-
?
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
native and recombinant enzyme
-
?
polypeptide + H2O
peptides
Pro-Phe-Arg-4-methylcoumaryl-7-amide
Pro-Phe-Arg + 7-amino-4-methylcoumarin
recombinant wild-type and mutants
-
?
tert-butyloxycarbonyl-Ala-Gly-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Ala-Gly-Pro-Arg + 7-amino-4-methylcoumarin
recombinant, not native, enzyme
-
?
tert-butyloxycarbonyl-Asp(benzyloxy)-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Asp(benzyloxy)-Pro-Arg + 7-amino-4-methylcoumarin
wild-type and mutants
-
?
tert-butyloxycarbonyl-Asp-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Asp-Pro-Arg + 7-amino-4-methylcoumarin
recombinant, not native, enzyme
-
?
tert-butyloxycarbonyl-Glu-Gly-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Glu-Gly-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-Glu-Lys-Lys-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Glu-Lys-Lys + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-Leu-Arg-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Leu-Arg-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-Leu-Thr-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Leu-Thr-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-pyroglutamyl-Gly-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-pyroglutamyl-Gly-Arg + 7-amino-4-methylcoumarin
recombinant and native enzyme
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
Boc-Phe-Ser-Arg-4-methylcoumarin-7-amide + H2O
?
-
-
-
-
?
Boc-Val-Pro-Arg-4-methylcoumarin-7-amide + H2O
?
-
-
-
-
?
additional information
?
-
acetyl-Pro-Phe-Arg-4-nitroanilide + H2O
acetyl-Pro-Phe-Arg + 4-nitroaniline
low activity
-
?
acetyl-Pro-Phe-Arg-4-nitroanilide + H2O
acetyl-Pro-Phe-Arg + 4-nitroaniline
recombinant, not native enzyme
-
?
Fibronectin + H2O
?
recombinant enzyme
-
-
?
Fibronectin + H2O
?
-
recombinant enzyme
-
-
?
Fibronectin + H2O
?
affects cell adhesion or cell migration by modulating the content and/or chemical characteristics of fibronectin in the extracellular matrix
-
-
?
polypeptide + H2O
peptides
-
-
?
polypeptide + H2O
peptides
-
-
?
polypeptide + H2O
peptides
-
-
?
polypeptide + H2O
peptides
-
-
?
polypeptide + H2O
peptides
-
-
?
polypeptide + H2O
peptides
-
-
?
polypeptide + H2O
peptides
-
-
?
polypeptide + H2O
peptides
-
-
?
polypeptide + H2O
peptides
enzyme has significant limbic effects by changing the extracellular matrix environment
-
?
polypeptide + H2O
peptides
involvement in neural plasticity
-
?
polypeptide + H2O
peptides
involvement in neural plasticity
-
?
polypeptide + H2O
peptides
enzyme is implicated in various neurological processes including formation of memory
-
?
tert-butyloxycarbonyl-Glu-Gly-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Glu-Gly-Arg + 7-amino-4-methylcoumarin
native and recombinant enzyme
-
?
tert-butyloxycarbonyl-Glu-Gly-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Glu-Gly-Arg + 7-amino-4-methylcoumarin
recombinant, not native, enzyme
-
?
tert-butyloxycarbonyl-Glu-Lys-Lys-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Glu-Lys-Lys + 7-amino-4-methylcoumarin
low activity
-
?
tert-butyloxycarbonyl-Glu-Lys-Lys-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Glu-Lys-Lys + 7-amino-4-methylcoumarin
recombinant and native enzyme
-
?
tert-butyloxycarbonyl-Leu-Arg-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Leu-Arg-Arg + 7-amino-4-methylcoumarin
low activity
-
?
tert-butyloxycarbonyl-Leu-Arg-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Leu-Arg-Arg + 7-amino-4-methylcoumarin
recombinant, not native, enzyme
-
?
tert-butyloxycarbonyl-Leu-Thr-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Leu-Thr-Arg + 7-amino-4-methylcoumarin
low activity
-
?
tert-butyloxycarbonyl-Leu-Thr-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Leu-Thr-Arg + 7-amino-4-methylcoumarin
recombinant, not native, enzyme
-
?
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
native and recombinant enzyme
-
?
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
recombinant wild-type and mutants
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
best substrate
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
best substrate
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
native and recombinant enzyme
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
recombinant wild-type and mutants
-
?
additional information
?
-
recombinant enzyme is produced as inactive proform and needs to be processed by an endoprotease, e.g. protease-1, EC 3.4.21.50, or trypsin, EC 3.4.21.4, for activation by specific cleavage of the Lys32-Ile33 bond near the N-terminus
-
-
?
additional information
?
-
-
recombinant enzyme is produced as inactive proform and needs to be processed by an endoprotease, e.g. protease-1, EC 3.4.21.50, or trypsin, EC 3.4.21.4, for activation by specific cleavage of the Lys32-Ile33 bond near the N-terminus
-
-
?
additional information
?
-
recombinant enzyme is produced as inactive proform and needs to be processed by an endoprotease, e.g. protease-1, EC 3.4.21.50, or trypsin, EC 3.4.21.4, for activation by specific cleavage of the Lys32-Ile33 bond near the N-terminus
-
-
?
additional information
?
-
-
recombinant enzyme is produced as inactive proform and needs to be processed by an endoprotease, e.g. protease-1, EC 3.4.21.50, or trypsin, EC 3.4.21.4, for activation by specific cleavage of the Lys32-Ile33 bond near the N-terminus
-
-
?
additional information
?
-
loop C and the N-linked oligosaccharide chain on the kallikrein loop affect the catalytic efficiency and P2 specificity, respectively
-
-
?
additional information
?
-
-
loop C and the N-linked oligosaccharide chain on the kallikrein loop affect the catalytic efficiency and P2 specificity, respectively
-
-
?
additional information
?
-
substrate specificty of native and recombinant enzyme
-
-
?
additional information
?
-
-
substrate specificty of native and recombinant enzyme
-
-
?
additional information
?
-
disulfide bonds SS1 in loop E, Gly142-Leu155, and SS6 in loop G, Ser185-Gly197, are essential for catalytic activity
-
-
?
additional information
?
-
-
disulfide bonds SS1 in loop E, Gly142-Leu155, and SS6 in loop G, Ser185-Gly197, are essential for catalytic activity
-
-
?
additional information
?
-
-
enzyme is involved in the synaptogenesis/maturation of orphan and small synaptic boutons in the Schaffer-collateral pathway
-
-
?
additional information
?
-
-
enzyme is necessary for establishment of long-term potentiation and has a significant role in memory acquisition
-
-
?
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0.23 - 0.28
D-Val-Leu-Arg-4-nitroanilide
8.36
Pro-Phe-Arg-4-methylcoumaryl-7-amide
recombinant wild-type enzyme, pH 8.0, 25°C
0.32
tert-butyloxycarbonyl-Asp(benzyloxy)-Pro-Arg-4-methylcoumaryl-7-amide
recombinant wild-type enzyme, pH 8.0, 25°C
0.34
tert-butyloxycarbonyl-Asp-Pro-Arg-4-methylcoumaryl-7-amide
recombinant enzyme, pH 8.0, 37°C
0.22 - 0.54
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide
0.27 - 0.3
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
0.23
D-Val-Leu-Arg-4-nitroanilide
recombinant enzyme, pH 8.0, 37°C
0.28
D-Val-Leu-Arg-4-nitroanilide
native enzyme, pH 8.0, 37°C
0.22
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide
recombinant wild-type enzyme, pH 8.0, 25°C
0.5
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide
recombinant enzyme, pH 8.0, 37°C
0.54
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide
native enzyme, pH 8.0, 37°C
0.27
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
recombinant enzyme, pH 8.0, 37°C
0.28
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
recombinant wild-type enzyme, pH 8.0, 25°C
0.3
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
native enzyme, pH 8.0, 37°C
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C108S
oligonucleotide-directed mutagenesis, reduced Km, increased kcat, increased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
C145S
oligonucleotide-directed mutagenesis of disulfide bond SS3, reduced Km and kcat, increased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
C208S
oligonucleotide-directed mutagenesis of disulfide bond SS6, highly reduced Km and reduced kcat, increased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
C233S
oligonucleotide-directed mutagenesis, highly reduced Km and slightly reduced kcat, reduced activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
C246S
oligonucleotide-directed mutagenesis, reduced Km and kcat, decreased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
C39S
oligonucleotide-directed mutagenesis of disulfide bond SS1, increased Km, reduced kcat, reduced activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
C7S
oligonucleotide-directed mutagenesis, reduced Km and kcat, slightly decreased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
D206V
oligonucleotide-directed mutagenesis, reduced Km and highly reduced kcat, decreased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-7-amino-4-methylcoumarin
N110A
oligonucleotide-directed mutagenesis, reduced Km and kcat, slightly increased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
additional information
additional deletion N113-E115 in mutant N110S: decreased kcat and Km, increased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
additional information
-
additional deletion N113-E115 in mutant N110S: decreased kcat and Km, increased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
additional information
-
enzyme knock-out mice are significantly impaired in the Morris water maze and Y-mazes and fail to exhibit early phase long-term potentiation by a single tetanus. A dose of recombinant enzyme alone, without tetanic stimulation, elicits either long-lasting potentiation or depression, depending on the dose, by increase of phosphorylation at different sites on the GluR1 subunit of the AMPA receptor
additional information
-
enzyme-deficient mouse, number of L1-immunoreactive boutons is markedly higher than in wild-type, their number reverts to wild-type level upon microinjection of enzyme. L1-immunoreactive boutons are hypertrophied in the mutant
additional information
-
Klk8-/- mice, show less proliferation and an increase in the number of cell layers in the stratum corneum. Inefficient cleavage of adhesion molecules DSG1 and CDSN in Klk8-/- skin, which contributes to a delay in corneocyte shedding, resulting in hyperkeratosis phenotype
additional information
-
neuropsin-deficient mice, are significantly impaired in hippocampus-dependent behavioral memory. Synaptic late associativity is impaired
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Boeckmann, B.; Bairoch, A.; Apweiler, R.; Blatter, M.C.; Estreicher, A.; Gasteiger, E.; Martin M.J.; Michoud, K.; O'Donovan, C.; Phan, I.; Pilbout, S.; Schneider, M.
The SWISS-PROT protein knowledgebase and its supplement TrEMBL
Nucleic Acids Res.
31
365-370
2003
Homo sapiens (O60259), Mus musculus (P07628), Mus musculus (Q61955), Rattus norvegicus (O88780), Rattus norvegicus (P36374)
brenda
Kishi, T.; Kato, M.; Shimizu, T.; Kato, K.; Matsumoto, K.; Yoshida, S.; Shiosaka, S.; Hakoshima, T.
Crystallization and preliminary X-ray analysis of neuropsin, a serine protease expressed in the limbic system of mouse brain
J. Struct. Biol.
118
248-251
1997
Mus musculus (Q61955), Mus musculus
brenda
Yoshida, S.; Taniguchi, M.; Hirata, A.; Shiosaka, S.
Sequence analysis and expression of human neuropsin cDNA and gene
Gene
213
9-16
1998
Homo sapiens (O60259), Homo sapiens, Mus musculus (Q61955), Mus musculus
brenda
Shimizu, C.; Yoshida, S.; Shibata, M.; Kato, K.; Momota, Y.; Matsumoto, K.; Shiosaka, T.; Midorikawa, R.; Kamachi, T.; Kawabe, A.; Shiosaka, S.
Characterization of recombinant and brain neuropsin, a plasticity-related serine protease
J. Biol. Chem.
273
11189-11196
1998
Mus musculus (Q61955), Mus musculus
brenda
Kishi, T.; Kato, M.; Shimizu, T.; Kato, K.; Matsumoto, K.; Yoshida, S.; Shiosaka, S.; Hakoshima, T.
Crystal structure of neuropsin, a hippocampal protease involved in kindling epileptogenesis
J. Biol. Chem.
274
4220-4224
1999
Mus musculus (Q61955), Mus musculus
brenda
Tani, N.; Matsumoto, K.; Ota, I.; Yoshida, S.; Takada, Y.; Shiosaka, S.; Matsuura, N.
Effects of fibronectin cleaved by neuropsin on cell adhesion and migration
Neurosci. Res.
39
247-251
2001
Mus musculus (Q61955), Mus musculus
brenda
Kato, K.; Kishi, T.; Kamachi, T.; Akisada, M.; Oka, T.; Midorikawa, R.; Takio, K.; Dohmae, N.; Bird, P.I.; Sun, J.; Scott, F.; Miyake, Y.; Yamamoto, K.; Machida, A.; Tanaka, T.; Matsumoto, K.; Shibata, M.; Shiosaka, S.
Serine proteinase inhibitor 3 and murinoglobulin I are potent inhibitors of neuropsin in adult mouse brain
J. Biol. Chem.
276
14562-14571
2001
Mus musculus (Q61955), Mus musculus
brenda
Oka, T.; Hakoshima, T.; Itakura, M.; Yamamori, S.; Takahashi, M.; Hashimoto, Y.; Shiosaka, S.; Kato, K.
Role of loop structures of neuropsin in the activity of serine protease and regulated secretion
J. Biol. Chem.
277
14724-14730
2002
Mus musculus (Q61955), Mus musculus
brenda
Matsumoto-Miyai, K.; Kitagawa, R.; Ninomiya, A.; Momota, Y.; Yoshida, S.; Shiosaka, S.
Decidualization induces the expression and activation of an extracellular protease neuropsin in mouse uterus
Biol. Reprod.
67
1414-1418
2002
Mus musculus (Q61955), Mus musculus
brenda
Chen, Z.L.; Yoshida, S.; Kato, K.; Momota, Y.; Suzuki, J.; Tanaka, T.; Ito, J.; Nishino, H.; Aimoto, S.; Kiyama, H.; Shiosaka, S.
Expression and activity-dependent changes of a novel limbic-serine protease gene in the hippocampus
J. Neurosci.
15
5088-5097
1995
Mus musculus (Q61955), Mus musculus
brenda
Nakamura, Y.; Tamura, H.; Horinouchi, K.; Shiosaka, S.
Role of neuropsin in formation and maturation of Schaffer-collateral L1cam-immunoreactive synaptic boutons
J. Cell Sci.
119
1341-1349
2006
Mus musculus
brenda
Tamura, H.; Ishikawa, Y.; Hino, N.; Maeda, M.; Yoshida, S.; Kaku, S.; Shiosaka, S.
Neuropsin is essential for early processes of memory acquisition and Schaffer collateral long-term potentiation in adult mouse hippocampus in vivo
J. Physiol.
570
541-551
2006
Mus musculus
brenda
Scott, F.L.; Sun, J.; Whisstock, J.C.; Kato, K.; Bird, P.I.
SerpinB6 is an inhibitor of kallikrein-8 in keratinocytes
J. Biochem.
142
435-442
2007
Homo sapiens, Mus musculus
brenda
Kishibe, M.; Bando, Y.; Terayama, R.; Namikawa, K.; Takahashi, H.; Hashimoto, Y.; Ishida-Yamamoto, A.; Jiang, Y.P.; Mitrovic, B.; Perez, D.; Iizuka, H.; Yoshida, S.
Kallikrein 8 is involved in skin desquamation in cooperation with other kallikreins
J. Biol. Chem.
282
5834-5841
2007
Mus musculus, Mus musculus C57BL/6
brenda
Ishikawa, Y.; Horii, Y.; Tamura, H.; Shiosaka, S.
Neuropsin (KLK8)-dependent and -independent synaptic tagging in the Schaffer-collateral pathway of mouse hippocampus
J. Neurosci.
28
843-849
2008
Mus musculus
brenda
Pettus, J.R.; Johnson, J.J.; Shi, Z.; Davis, J.W.; Koblinski, J.; Ghosh, S.; Liu, Y.; Ravosa, M.J.; Frazier, S.; Stack, M.S.
Multiple kallikrein (KLK 5, 7, 8, and 10) expression in squamous cell carcinoma of the oral cavity
Histol. Histopathol.
24
197-207
2009
Homo sapiens, Mus musculus
brenda
Yoshida, S.
Klk8, a multifunctional protease in the brain and skin: analysis of knockout mice
Biol. Chem.
391
375-380
2010
Mus musculus
brenda
Shingaki, K.; Matsuzaki, S.; Taniguchi, M.; Kubo, T.; Fujiwara, T.; Yamamoto, A.; Tamura, H.; Maeda, T.; Ooi, K.; Matsumoto, K.; Shiosaka, S.; Tohyama, M.
Molecular mechanism of kallikrein-related peptidase 8/neuropsin-induced hyperkeratosis in inflamed skin
Br. J. Dermatol.
163
466-475
2010
Homo sapiens, Mus musculus
brenda
Iinuma, S.; Kishibe, M.; Saito, N.; Igawa, S.; Honma, M.; Takahashi, H.; Bando, Y.; Yoshida, S.; Iizuka, H.; Ishida-Yamamoto, A.
Klk8 is required for microabscess formation in a mouse imiquimod model of psoriasis
Exp. Dermatol.
24
887-889
2015
Mus musculus (Q61955)
brenda
Konar, A.; Kumar, A.; Maloney, B.; Lahiri, D.; Thakur, M.
A serine protease KLK8 emerges as a regulator of regulators in memory Microtubule protein dependent neuronal morphology and PKA-CREB signaling
Sci. Rep.
8
9928
2018
Mus musculus (Q61955), Mus musculus
brenda