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Abz-AIKFFSA-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-AIKFF + SA-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-ALFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-ALF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-FLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-FLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-GFSPFRSSRI-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-GFSPF + RSSRI-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-GFSPFRSSRIGEIKEETT-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-GFSPF + RSSRIGEIKEETT-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-GLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-GLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-HLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-HLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-ILFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-ILF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KAFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KAF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KFFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KFF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KLFSSE-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KLF + SSE-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KLTWLPL-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KLTW + LPL-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KLYSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KLY + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KPFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KPF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KVFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KVF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KYFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KYF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-LLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-LLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-LMEKWTW-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-LMEKW + TW-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-MISLMKRP-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-MISLM + KRP-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-NLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-NLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-PHVMRFP-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-PHVM + RFP-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-QLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-QLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-RLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-RLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-VARPYYL-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-VARPYY + L-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-VLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-VLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-VQFYQGP-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-VQFY + QGP-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-VQMRGFA-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-VQM + RGF + A-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-YNPFVFT-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-YNPF + VF + T-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-YWSIQPF-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-Y + WSIQPF + Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Ac-ED(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)KPILFRLGK(4-(4-dimethylaminophenylazo)benzoic acid)E-NH2 + H2O
?
-
-
-
?
Ac-EFKPILWRLGC-(6-(9-oxo-9H-acridin-10-yl)-hexanoate)E-NH2 + H2O
?
-
-
-
?
acetyl-Phe-Val-Arg-4-nitroanilide + H2O
acetyl-Phe-Val-Arg + 4-nitroaniline
-
chromogenic substrate
-
-
?
acidic sphingomyelinase + H2O
?
-
-
-
-
?
acidic-sphingomyelinase + H2O
?
-
-
-
-
?
AGCKNFFWKTFTSC + H2O
AGCKNFF + WKTFTSC
-
-
-
?
Arg-Pro-Tyr-4-nitroanilide + H2O
?
-
-
-
-
?
ATHPFIIQ + H2O
ATHPF + IIQ
-
-
-
?
benzoyl-Phe-Val-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-Phe-Val-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-FR-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-FR + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-LR-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-LR + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
beta-amyloid peptide + H2O
?
beta-glucocerebrosidase + H2O
?
-
-
-
-
?
cathelicidin + H2O
?
-
-
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
desmocollin 1 + H2O
?
-
-
-
?
desmoglein 1 + H2O
?
-
kallikrein 7 cleaves both recombinant desmoglein 1 and desmoglein 2 in vitro
-
-
?
desmoglein 2 + H2O
?
-
kallikrein 7 cleaves both recombinant desmoglein 1 and desmoglein 2 in vitro. Ectopic expression of kallikrein 7 in BxPC-3 pancreatic cancer cells which express desoglein 2 but not desmoglein 1 or kallikrein 7 confirms the cleavage of desmoglein 2 in vivo
-
-
?
DYEAGGY + H2O
L-Asp-L-Tyr + EAGGY
-
-
-
?
GNYDGPD + H2O
GNY + DGPD
-
-
-
?
GVRPHGF + H2O
GV + RPHGF
-
-
-
?
human pro-interleukin 1beta + H2O
human interleukin beta1 + ?
insulin beta chain + H2O
?
-
the most preferred P1 residue of KLK7 is Tyr, followed by Ala and Met, whereas Phe, Arg, and Lys are ranked quite low. Tyr is favored at S2 over the medium-sized hydrophobic residues Leu, Thr, Met, and Phe. In agreement with these findings, KLK7 cleaves the insulin B-chain after Asn-Gln-His-Leu, Glu-Ala-Leu-Tyr, Gly-Phe-Phe-Tyr, and Arg-Gly-Phe-Phe
-
-
?
kallistatin + H2O
?
-
-
-
?
KHLF-4-nitroanilide + H2O
KLHLF + 4-nitroaniline
-
-
-
?
KHLY-4-nitroanilide + H2O
KLHLY + 4-nitroaniline
-
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
-
-
-
?
L-Tyr-7-amido-4-methylcoumarin + H2O
L-Tyr + 7-amino-4-methylcoumarin
-
-
-
?
LLVY-7-amido-4-methylcoumarin + H2O
LLVY + 7-amino-4-methylcoumarin
-
-
-
?
LMQHPQD + H2O
LM + QHPQD
-
-
-
?
Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 + H2O
?
MeO-succinly-Arg-Pro-Tyr-4-nitroanilide + H2O
?
-
-
-
-
?
methoxy-succinyl-Ala-Ala-Pro-Met-4-nitroanilide + H2O
methoxy-succinyl-Ala-Ala-Pro-Met + 4-nitroaniline
methoxy-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
methoxy-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
methoxy-succinyl-Arg-Pro-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Pro-Tyr + 4-nitroaniline
methoxy-succinyl-Arg-Pro-Tyr-7-amido-4-methylcoumarin + H2O
methoxy-succinyl-Arg-Pro-Tyr + 7-amino-4-methylcoumarin
-
-
-
?
methoxy-succinyl-Arg-Pro-Tyr-p-nitroanilide + H2O
methoxy-succinyl-Arg-Pro-Tyr + p-nitroaniline
-
-
-
?
N-carbobenzoxy-Gly-Pro-Arg-4-nitroanilide + H2O
N-carbobenzoxy-Gly-Pro-Arg + 4-nitroaniline
N-carbobenzoxy-Val-Gly-Arg-4-nitroanilide + H2O
N-carbobenzoxy-Val-Gly-Arg + 4-nitroaniline
o-aminobenzoyl-FRAPR-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
low activity
-
-
?
o-aminobenzoyl-FRLVR-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-FR + LVR-(2,4-dinitrophenyl)ethylenediamine
-
low activity
-
?
o-aminobenzoyl-SVIRRVQ-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-TSVIRRPQ-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
low activity
-
-
?
oxidized bovine insulin B chain + H2O
peptides + (Tyr)26
-
recombinant enzyme
product identification, cleavage sites are: Leu6-cysteic acid7, Tyr16-Leu17, Phe25-Tyr26, Tyr26-Tr27
?
PDETYFF + H2O
PDETY + L-Phe-L-Phe
-
-
-
?
PFR-7-amido-4-methylcoumarin + H2O
?
-
best substrate
-
-
?
Phe-7-amido-4-methylcoumarin + H2O
Phe + 7-amino-4-methylcoumarin
-
-
-
?
polypeptide + H2O
peptides
pro-matrix metalloproteinase-2 + H2O
?
-
KLK7 degrades, but does not activate, pro-matrix metalloproteinase-2
-
-
?
pro-matrix metalloproteinase-9 + H2O
matrix metalloproteinase-9
-
KLK7 degrades and activates pro-matrix metalloproteinase-9, cleavage occurs between Tyr443 and Gly444
the product is a truncated, active matrix metalloproteinase-9 lacking the C-terminal hemopexin domains which is not generated by other proteases
-
?
QHLY-4-nitroanilide + H2O
QLHLY + 4-nitroaniline
-
-
-
?
QMELPVH + H2O
Gln-Met + ELPVH
-
-
-
?
RPKPQQFFGLM + H2O
RPKPQQ + L-Phe + FGLM
-
-
-
?
SANSNPAMAPRERKAGCKNFFWKTFTSC + H2O
SANSNPAMAPRERKAGCKNFF + WKTFTSC
-
-
-
?
SFPQVHS + H2O
SFPQV + L-His-L-Ser
-
-
-
?
somatostatin + H2O
?
-
-
-
?
STLDWQD + H2O
STLDW + QD
-
-
-
?
STLDWQH + H2O
STLDW + QH
-
-
-
?
Substance P + H2O
?
-
-
-
?
Suc-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
Suc-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-AAPF-7-amido-4-methylcoumarin + H2O
succinyl-AAPF + 7-amino-4-methylcoumarin
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
chromogenic substrate
-
-
?
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Pro-Phe + 7-amino-4-methylcoumarin
-
-
-
?
succinyl-Ala-Val-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Val-Pro-Phe + 4-nitroaniline
-
-
-
?
succinyl-Leu-Leu-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Tyr + 7-amino-4-methylcoumarin
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Phe-Leu-Phe-4-nitroanilide + H2O
succinyl-Phe-Leu-Phe + 4-nitroaniline
succinyl-Val-Pro-Phe-4-nitroanilide + H2O
succinyl-Val-Pro-Phe + 4-nitroaniline
tenascin-C + H2O
?
-
-
-
?
tert-butyloxycarbonyl-Leu-Gly-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Leu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
TGQPIGI + H2O
TGQPI + Gly-L-Ile
-
-
-
?
Tyr-7-amido-4-methylcoumarin + H2O
Tyr + 7-amino-4-methylcoumarin
-
-
-
?
VQPFHDP + H2O
VQPF + HDP
-
-
-
?
VREHMVD + H2O
VREHM + L-Val-L-Asp
-
-
-
?
additional information
?
-
beta-amyloid peptide + H2O
?
-
degradation
-
-
?
beta-amyloid peptide + H2O
?
-
degradation, the enzyme cleaves after both Phe residues within the core of Abeta42 in vitro, thereby inhibiting A? fibril formation and promoting the degradation of preformed fibrils
-
-
?
corneodesmosin + H2O
?
-
-
-
?
corneodesmosin + H2O
?
-
KLK7 degrades corneodesmosomes CDSN, DSC1, and DSG1
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
-
chromogenic substrate
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
-
low activity
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
-
i.e. S2288
-
-
?
E-cadherin + H2O
?
-
kallikrein 7 degrades extracellular matrix proteins, and enhances pancreatic cancer cell invasion by shedding E-cadherin, overview
-
-
?
E-cadherin + H2O
?
-
epithelial cell adhesion molecule
-
-
?
Fibronectin + H2O
?
-
kallikrein degrades components of the extracellular matrix
-
-
?
Fibronectin + H2O
?
-
kallikrein 7 is a chymostatin-like serine protease
-
-
?
human pro-interleukin 1beta + H2O
human interleukin beta1 + ?
-
several claevage sites
product can be further degraded by the enzyme leading to its inactivation, product is in the active form
?
human pro-interleukin 1beta + H2O
human interleukin beta1 + ?
-
recombinant enzyme and substrate
product can be further degraded by the enzyme leading to its inactivation, product is in the active form
?
human pro-interleukin 1beta + H2O
human interleukin beta1 + ?
-
substrate is in the inactive form
product can be further degraded by the enzyme leading to its inactivation, product is in the active form
?
Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 + H2O
?
-
-
-
?
Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 + H2O
?
-
a fluorogenic peptide substrate
-
-
?
methoxy-succinyl-Ala-Ala-Pro-Met-4-nitroanilide + H2O
methoxy-succinyl-Ala-Ala-Pro-Met + 4-nitroaniline
-
chromogenic substrate
-
-
?
methoxy-succinyl-Ala-Ala-Pro-Met-4-nitroanilide + H2O
methoxy-succinyl-Ala-Ala-Pro-Met + 4-nitroaniline
-
low activity
-
-
?
methoxy-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
methoxy-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
chromogenic substrate
-
-
?
methoxy-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
methoxy-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
low activity
-
-
?
methoxy-succinyl-Arg-Pro-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Pro-Tyr + 4-nitroaniline
-
-
-
?
methoxy-succinyl-Arg-Pro-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Pro-Tyr + 4-nitroaniline
-
best substrate
-
-
?
methoxy-succinyl-Arg-Pro-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Pro-Tyr + 4-nitroaniline
-
chromogenic substrate
-
-
?
methoxy-succinyl-Arg-Pro-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Pro-Tyr + 4-nitroaniline
-
i.e. S2586
-
-
?
N-carbobenzoxy-Gly-Pro-Arg-4-nitroanilide + H2O
N-carbobenzoxy-Gly-Pro-Arg + 4-nitroaniline
-
chromogenic substrate
-
-
?
N-carbobenzoxy-Gly-Pro-Arg-4-nitroanilide + H2O
N-carbobenzoxy-Gly-Pro-Arg + 4-nitroaniline
-
low activity
-
-
?
N-carbobenzoxy-Val-Gly-Arg-4-nitroanilide + H2O
N-carbobenzoxy-Val-Gly-Arg + 4-nitroaniline
-
chromogenic substrate
-
-
?
N-carbobenzoxy-Val-Gly-Arg-4-nitroanilide + H2O
N-carbobenzoxy-Val-Gly-Arg + 4-nitroaniline
-
low activity
-
-
?
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
-
-
?
polypeptide + H2O
peptides
-
mediates shedding and desquamation of skin cells
-
?
polypeptide + H2O
peptides
-
involved in desquamation in plantar stratum corneum
-
?
polypeptide + H2O
peptides
-
involved in desquamation in plantar stratum corneum
-
?
polypeptide + H2O
peptides
-
involved in desquamation in plantar stratum corneum
-
?
polypeptide + H2O
peptides
-
catalyzes the degradation of intercellular cohesive structures in the cornified layer of the skin in the continous sheeding of the cells from the skin surface
-
?
polypeptide + H2O
peptides
-
catalyzes the degradation of intercellular cohesive structures in the cornified layer of the skin in the continous sheeding of the cells from the skin surface
-
?
polypeptide + H2O
peptides
involved in pathological keratinization, psoriasis, and ovarian cancer
-
?
polypeptide + H2O
peptides
-
-
-
?
succinyl-Phe-Leu-Phe-4-nitroanilide + H2O
succinyl-Phe-Leu-Phe + 4-nitroaniline
-
chromogenic substrate
-
-
?
succinyl-Phe-Leu-Phe-4-nitroanilide + H2O
succinyl-Phe-Leu-Phe + 4-nitroaniline
-
low activity
-
-
?
succinyl-Val-Pro-Phe-4-nitroanilide + H2O
succinyl-Val-Pro-Phe + 4-nitroaniline
-
chromogenic substrate
-
-
?
succinyl-Val-Pro-Phe-4-nitroanilide + H2O
succinyl-Val-Pro-Phe + 4-nitroaniline
-
low activity
-
-
?
additional information
?
-
-
the enzyme causes canine atopic dermatitis
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
recombinant enzyme proform is activated by digestion with trypsin
-
-
?
additional information
?
-
-
recombinant enzyme proform is activated by digestion with trypsin
-
-
?
additional information
?
-
enzyme is regulated by steroid hormones
-
-
?
additional information
?
-
-
enzyme is regulated by steroid hormones
-
-
?
additional information
?
-
-
enzyme may contribute to tumor cell growth, tumor spread, and the metastatic potential of ovarian tumor cells
-
-
?
additional information
?
-
AACC insertion in the stratum corneum chymotryptic enzyme gene may result in a change to activity of stratum corneum chymotryptic enzyme within the skin barrier. Stratum corneum chymotryptic enzyme could have an important role in the development of atopic dermatitis
-
-
?
additional information
?
-
-
AACC insertion in the stratum corneum chymotryptic enzyme gene may result in a change to activity of stratum corneum chymotryptic enzyme within the skin barrier. Stratum corneum chymotryptic enzyme could have an important role in the development of atopic dermatitis
-
-
?
additional information
?
-
-
epidermal hyperproliferation and decreased skin barrier function in mice overexpressing stratum corneum chymotryptic enzyme
-
-
?
additional information
?
-
-
gene expression might be involved in lung tumorigenesis
-
-
?
additional information
?
-
-
increased expression of kallikrein 7 and decreased expression of its inhibitor antileukoprotease might play an important role in cervical adenocarcinoma development
-
-
?
additional information
?
-
kallikrein 7 is involved in desquamation
-
-
?
additional information
?
-
no cleavage of desmoglein 1
-
-
?
additional information
?
-
succinyl-Ala-Ala-Pro-Phe-tripeptidyl-p-nitroanilide is no substrate
-
-
?
additional information
?
-
the most favored P1 residue of hK7 is Tyr followed by Ala, Met, and Nle, whereas Phe is ranked rather low, and Trp seems to be totally excluded, at S2, the most preferred residue is again Tyr, well ahead of the medium-sized hydrophobic residues Leu, Nle, Thr, Met, and Phe, whereas Gly is almost not tolerated, at S3 and S4, nearly all residues are accepted with a slight preference for hydrophobic side chains
-
-
?
additional information
?
-
high enzyme activity shows a significantly better prognosis in breast cancer
-
-
?
additional information
?
-
-
high enzyme activity shows a significantly better prognosis in breast cancer
-
-
?
additional information
?
-
-
kallikrein 7 is involved in pathological keratinization, psoriasis and ovarian cancer
-
-
?
additional information
?
-
-
kallikrein 7 participates in normal desquamation by facilitating cell shedding at the skin surface, and it degrades components of the extracellular matrix, the aberrant expression and secretion of kallikrein 7 in human tumors may facilitate metastasis by directly degrading components of the extracellular matrix and may thus play an important role in tumorigenesis, overview, the enzyme is implicated in the degradation of intercellular cohesive structures in the stratum corneum preceding desquamation
-
-
?
additional information
?
-
the enzyme participates in skin desquamation but is also implicated in diverse skin diseases and is a potential biomarker of ovarian cancer
-
-
?
additional information
?
-
-
the enzyme participates in skin desquamation but is also implicated in diverse skin diseases and is a potential biomarker of ovarian cancer
-
-
?
additional information
?
-
active site structure and substrate specificity, overview, kallikrein 7 exhibits large positively charged surface patches, representing putative exosites for prime side substrate recognition, overview
-
-
?
additional information
?
-
-
active site structure and substrate specificity, overview, kallikrein 7 exhibits large positively charged surface patches, representing putative exosites for prime side substrate recognition, overview
-
-
?
additional information
?
-
-
no activity with laminin
-
-
?
additional information
?
-
-
similar to KLK5, KLK7 degrades proteins of corneodesmosomes, which are most likely physiological substrates of KLKs expressed in the stratum corneum of skin
-
-
?
additional information
?
-
the P3-P'3' sequence NLYRVR is identified as a preferred substrate for the enzyme, glutamate at position P3' is also well accepted, substrate specificity, overview. No activity with Abz-KVYFFFRENAI-Q-N-[2,4-dinitrophenyl]-ethylenediamine. Kininogenase activity of the enzyme using as substrate a synthetic peptide derived from human kininogen (Abz-MISLMKRPPGFSPFRSSRI-NH2) containing the amino acids F and M as two possible cleavage site
-
-
?
additional information
?
-
-
the P3-P'3' sequence NLYRVR is identified as a preferred substrate for the enzyme, glutamate at position P3' is also well accepted, substrate specificity, overview. No activity with Abz-KVYFFFRENAI-Q-N-[2,4-dinitrophenyl]-ethylenediamine. Kininogenase activity of the enzyme using as substrate a synthetic peptide derived from human kininogen (Abz-MISLMKRPPGFSPFRSSRI-NH2) containing the amino acids F and M as two possible cleavage site
-
-
?
additional information
?
-
recombinant KLK7 clearly shows Tyr over Phe preference at the P1 site. No activity is detected against substrates with Lys or Ala in P1 sites, and minimum activity (about 10% activity compared with trypsin-like KLKs) is observed against substrates with Arg in the P1 site
-
-
?
additional information
?
-
-
recombinant KLK7 clearly shows Tyr over Phe preference at the P1 site. No activity is detected against substrates with Lys or Ala in P1 sites, and minimum activity (about 10% activity compared with trypsin-like KLKs) is observed against substrates with Arg in the P1 site
-
-
?
additional information
?
-
KLK7 exerts chymotryptic-like cleavage preferences. KLK7 subsite preferences are also characterised in the P2-P2 region, demonstrating a preference for hydrophobic residues in the non-prime and hydrophilic residues in the prime subsites
-
-
?
additional information
?
-
-
KLK7 exerts chymotryptic-like cleavage preferences. KLK7 subsite preferences are also characterised in the P2-P2 region, demonstrating a preference for hydrophobic residues in the non-prime and hydrophilic residues in the prime subsites
-
-
?
additional information
?
-
-
no kininogenase activity
-
-
?
additional information
?
-
-
enzyme exhibits a marked preference for cleavage downstream of Arg residues
-
-
?
additional information
?
-
-
the enzyme shows a unique extended chymotrypsin-like specificity and beta-amyloid peptide-degrading capacity
-
-
?
additional information
?
-
-
the enzyme's consensus motif is RX0(Y/F)-/-(Y/F)-/-(S/A/G/T) or RX0(Y/F)-/-(S/T/A) (0 = hydrophobic)
-
-
?
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(4R)-4-benzyl-2-(2-methylphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-(1-naphthyl)methyl-2-(2-methylphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2] imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-(4-benzyloxy)benzyl-2-(3,4-dimethoxyphenyl)-3,4-dihydro-5H-pyrido [10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-(4-hydroxyphenyl)-2-(3,4-dimethoxyphenyl)-3,4-dihydro-5H-pyrido [10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(2,4-dimethylphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2]imidazo [4,5-d][1,3]diazepin-5-one
-
cytotoxic effect
(4S)-4-benzyl-2-(2,5-dihydroxyphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2]imidazo-[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(2,5-dimethoxyphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2]imidazo [4,5-d][1,3]diazepin-5-one
-
cytotoxic effect
(4S)-4-benzyl-2-(2-hydroxyphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2]imidazo-[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(2-methoxyphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(2-methylphenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(2-methylpropyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(3,4,5-trimethoxyphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2] imidazo[4,5-d][1,3]diazepin-5-one
-
cytotoxic effect
(4S)-4-benzyl-2-(3,4-dimethoxyphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2]imidazo [4,5-d][1,3]diazepin-5-one
-
mechanism of inhibition, modeling, overview. Cytotoxic effect
(4S)-4-benzyl-2-(3,4-dimethoxyphenyl)-4,5-dihydro-3H-pyrido [10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-ol
-
-
(4S)-4-benzyl-2-(3-hydroxyphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2]imidazo-[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(3-methoxyphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(3-methylphenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(4-bromophenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(4-methoxyphenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(4-methylphenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(4-nitrophenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(pyridin-3-yl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-phenyl-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-3,4-dihydro-1H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepine-2,5-dione
-
-
(4S)-4-benzyloxymethyl-2-(2-methylphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2] imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyloxymethyl-2-(3,4-dimethoxyphenyl)-3,4-dihydro-5H-pyrido [10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-hydroxymethyl-2-(3,4-dimethoxyphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2] imi-dazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-methyl-2-(2-methylphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2]-imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-methyl-2-(3,4-dimethoxyphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2] imidazo[4,5-d][1,3]diazepin-5-one
-
-
(S)-4-benzyl-2-(3,4-dimethoxyphenyl)-3-methyl-3H-pyrido[10,20:1,2]imidazo [4,5-d][1,3]diazepin-5(4H)-one
-
-
(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)-1H-pyrrole-2-carboxamide
-
-
(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)-2-methylbenzamide
-
-
(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)-2-phenylacetamide
-
-
(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)-3,4-dimethoxybenzamide
-
-
(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)-3-phenylpropanamide
-
-
(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)benzamide
-
-
(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)cinnamamide
-
-
(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)isonicotinamide
-
-
(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)picolinamide
-
-
1-(2-bromobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole
1-(2-chlorobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole
2-(2-fluoro-phenyl)-5,6,7,8-tertrahydro-benzol[4,5]thieno[2,3-d][1,3]oxazin-4-one
-
Abz-KLASSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
Abz-KLDSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
Abz-KLESSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
Abz-KLGSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
Abz-KLHSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
Abz-KLISSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
Abz-KLKSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
Abz-KLLSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
Abz-KLMSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
Abz-KLNSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
Abz-KLPSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
Abz-KLQSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
Abz-KLRSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
Abz-KLSSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
Abz-KLTSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
Abz-KLVSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
Abz-KLWSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
Ala-Ala-Phe-chloromethyl ketone
-
Ala-Ala-Phe-chloromethylketone
alpha1-Aantichymotrypsin
-
99.6% inhibition at 0.00015 mM
-
alpha1-Macroglobulin
-
44.2% inhibition at 0.00015 mM
-
Alpha1-proteinase inhibitor
-
89.6% inhibition at 0.00015 mM
-
Cu2+
inhibition at low micromolar concentrations, structural basis for inhibition, overview; strong inhibitory effect
DMSO
catalytic activity of the protease decreases with increasing DMSO concentration
Eglin c
-
99.8% inhibition at 0.00015 mM
elafin
-
33.4% inhibition at 0.0015 mM
-
GKCLFSEPPICFPN
peptide inhibitor based on sunflower trypsin inhibitor-1
GKCLFSNPPICFPN
peptide inhibitor based on sunflower trypsin inhibitor-1, displays at least 1000fold selectivity over several proteases that are related by function (KLK5 and KLK14) or specificity (chymotrypsin)
GKCLFSSPPICFPN
peptide inhibitor based on sunflower trypsin inhibitor-1
LEKTI domain 6
i.e. lympho-epithelial Kazaltype-related inhibitor domain 6, specific inhibition, interaction and binding structure analysis, overview
-
LEKTI fragments
-
i.e. lympho-epithelial Kazaltype-related inhibitor fragments, furin-derived and secreted in cultured keratinocytes and in the epidermis, specifically inhibit KLK5, KLK7, and KLK14 and control desquamation through a pH-dependent interaction, overview
-
pepstatin A
-
weak inhibition, 23.6% inhibition at 0.1 mM
Soybean trypsin inhibitor
-
Suc-Ala-Ala-Pro-Phe-chloromethylketone
-
-
succinyl-Ala-Ala-Pro-Phe-chloromethyl ketone
-
1-(2-bromobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole
-
1-(2-bromobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole
-
1-(2-chlorobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole
-
1-(2-chlorobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole
-
Ala-Ala-Phe-chloromethylketone
-
Ala-Ala-Phe-chloromethylketone
-
-
antileukoprotease
-
88.8% inhibition at 0.0022 mM
-
Aprotinin
-
-
Aprotinin
-
90.3% inhibition at 0.0027 mM
chymostatin
-
-
chymostatin
-
proteolysis of both the desmosomal proteins by kallikrein 7 is effectively inhibited in the presence of chymostatin
LEKTI
-
i.e. lympho-epithelial Kazaltype-related inhibitor, a 15-domain serine proteinase inhibitor
LEKTI
-
LEKTI is expressed in stratum corneum and in stratum granulosum and is a reversible inhibitor encoded by the SPINK5 (serine protease inhibitor Kazal type 5) gene. LEKTI is a weak inhibitor toward KLK 7 but a much stronger inhibitor toward KLK5
Soybean trypsin inhibitor
-
99.6% inhibition at 0.00015 mM
-
Soybean trypsin inhibitor
-
strong inhibition
-
Zn2+
-
-
Zn2+
-
92.6% inhibition at 0.1 mM
Zn2+
inhibition at low micromolar concentrations, noncompetitive inhibition type, structural basis for inhibition involving His99, overview; strong inhibitory effect
additional information
-
no inhibition by leupeptin
-
additional information
-
inhibition assay: 15 min preincubation of the enzyme with inhibitor at 21°C; no inhibition by Mg2+, E-64, 1,10-phenanthrolin, EDTA
-
additional information
-
phosphoramidon inhibits thermolysin and thus activation of pro-kallikrein 7
-
additional information
-
phosphoramidon inhibits thermolysin and thus activation of pro-kallikrein 7
-
additional information
-
usage of the pyridoimidazodiazepinone core as a potential scaffold to develop selective and competitive reversible inhibitors, analysis of structure-activity relationships, inhibition mechanisms, and selectivity as well as cytotoxicity against selected three human cancer cell lines, i.e. the HeLa cells, prostatic PC-3 cell line, and colorectal adenocarcinoma SW-620 cells, structure-based molecular docking, overview. No inhibition by 1b, 1f, 1g, 1h, 1i, 1j, 1l, 1m, 1q, 1r, 1s, 1t, 1u, 1v, 1w, 1x, 1z, 1aa, 1ab, 1ac, 1ad, 2a, 2b, 2c, 2d, 2f, 2h, and 2i
-
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Adenocarcinoma
Expression of human kallikrein 7 (hK7/SCCE) and its inhibitor antileukoprotease (ALP/SLPI) in uterine endocervical glands and in cervical adenocarcinomas.
Adenocarcinoma
Expression of kallikrein-related peptidase 7 predicts poor prognosis in patients with unresectable pancreatic ductal adenocarcinoma.
Adenocarcinoma
Kallikrein 7 enhances pancreatic cancer cell invasion by shedding E-cadherin.
Adenocarcinoma
The extracellular matrix protein fibronectin is a substrate for kallikrein 7.
Alzheimer Disease
Altered kallikrein 7 and 10 concentrations in cerebrospinal fluid of patients with Alzheimer's disease and frontotemporal dementia.
Alzheimer Disease
Loss of kallikrein-related peptidase 7 exacerbates amyloid pathology in Alzheimer's disease model mice.
Breast Neoplasms
Evaluation of Kallikrein-related Peptidase 5 Expression and its Significance for Breast Cancer Patients: Association with Kallikrein-related Peptidase 7 Expression.
Breast Neoplasms
Expression analysis of the human kallikrein 7 (KLK7) in breast tumors: a new potential biomarker for prognosis of breast carcinoma.
Breast Neoplasms
Expression of the serine protease kallikrein 7 and its inhibitor antileukoprotease is decreased in prostate cancer.
Breast Neoplasms
Quantitative reverse transcription-PCR assay for detection of mRNA encoding full-length human tissue kallikrein 7: prognostic relevance of KLK7 mRNA expression in breast cancer.
Carcinogenesis
Analysis of human kallikrein 7 expression as a potential biomarker in cervical neoplasia.
Carcinogenesis
Kallikrein-related peptidase 7 (KLK7) is a proliferative factor that is aberrantly expressed in human colon cancer.
Carcinogenesis
The Role of Kallikrein 7 in Tumorigenesis.
Carcinoma
Expression of the protease inhibitor antileukoprotease and the serine protease stratum corneum chymotryptic enzyme (SCCE) is coordinated in ovarian tumors.
Carcinoma
Human kallikrein 7 induces epithelial-mesenchymal transition-like changes in prostate carcinoma cells: a role in prostate cancer invasion and progression.
Carcinoma
Human tissue kallikrein 7, a novel biomarker for advanced ovarian carcinoma using a novel in situ quantitative method of protein expression.
Carcinoma
Immunohistochemical expression of kallikrein 7 in oral squamous cell carcinoma.
Carcinoma
Kallikrein-related peptidase 7 promotes multicellular aggregation via the alpha(5)beta(1) integrin pathway and paclitaxel chemoresistance in serous epithelial ovarian carcinoma.
Carcinoma
The Co-Expression of Kallikrein 5 and Kallikrein 7 Associates with Poor Survival in Non-HPV Oral Squamous-Cell Carcinoma.
Carcinoma, Ovarian Epithelial
Kallikrein-related peptidase 7 promotes multicellular aggregation via the alpha(5)beta(1) integrin pathway and paclitaxel chemoresistance in serous epithelial ovarian carcinoma.
cathepsin l deficiency
Epidermal differentiation: the role of proteases and their inhibitors.
Colonic Neoplasms
Kallikrein-related peptidase 7 (KLK7) is a proliferative factor that is aberrantly expressed in human colon cancer.
Colorectal Neoplasms
Clinical significance of kallikrein-related peptidase 7 (KLK7) in colorectal cancer.
Dermatitis
Epidermal overexpression of stratum corneum chymotryptic enzyme in mice: a model for chronic itchy dermatitis.
Dermatitis, Atopic
Epidermal overexpression of stratum corneum chymotryptic enzyme in mice: a model for chronic itchy dermatitis.
Dermatitis, Atopic
Evaluation of kallikrein 7 as a disease-causing gene for canine atopic dermatitis using microsatellite-based association mapping.
Dermatitis, Atopic
Generation of a quenched phosphonate activity-based probe for labelling the active KLK7 protease.
Dermatitis, Atopic
Genetic association between an AACC insertion in the 3'UTR of the stratum corneum chymotryptic enzyme gene and atopic dermatitis.
Dermatitis, Atopic
TH2 cytokines increase kallikrein 7 expression and function in patients with atopic dermatitis.
Dermatitis, Atopic
The 3'-UTR AACCins5874 in the stratum corneum chymotryptic enzyme gene (SCCE/KLK7), associated with atopic dermatitis; causes an increased mRNA expression without altering its stability.
Eczema
Analysis of the individual and aggregate genetic contributions of previously identified serine peptidase inhibitor Kazal type 5 (SPINK5), kallikrein-related peptidase 7 (KLK7), and filaggrin (FLG) polymorphisms to eczema risk.
Eczema
Transcriptional gene silencing of kallikrein 5 and kallikrein 7 using siRNA prevents epithelial cell detachment induced by alkaline shock in an in vitro model of eczema.
Frontotemporal Dementia
Altered kallikrein 7 and 10 concentrations in cerebrospinal fluid of patients with Alzheimer's disease and frontotemporal dementia.
Ichthyosis
Expression of stratum corneum chymotryptic enzyme in ichthyoses and squamoproliferative processes.
Ichthyosis
Skin Barrier Function Is Not Impaired and Kallikrein 7 Gene Polymorphism Is Frequently Observed in Korean X-linked Ichthyosis Patients Diagnosed by Fluorescence in Situ Hybridization and Array Comparative Genomic Hybridization.
Insulin Resistance
Role of Kallikrein 7 in Body Weight and Fat Mass Regulation.
Melanoma
Aberrant expression of kallikrein-related peptidase 7 is correlated with human melanoma aggressiveness by stimulating cell migration and invasion.
Melanoma
Cell adhesion and communication proteins are differentially expressed in melanoma progression model.
Melanoma
Kallikrein-related peptidase 7 overexpression in melanoma cells modulates cell adhesion leading to a malignant phenotype.
Neoplasm Metastasis
Analysis of human kallikrein 7 expression as a potential biomarker in cervical neoplasia.
Neoplasms
3D-quantitative structure-activity relationship and docking studies of coumarin derivatives as tissue kallikrein 7 inhibitors.
Neoplasms
An unexpected switch in peptide binding mode: from simulation to substrate specificity.
Neoplasms
Analysis of human kallikrein 7 expression as a potential biomarker in cervical neoplasia.
Neoplasms
Definition of an immunogenic region within the ovarian tumor antigen stratum corneum chymotryptic enzyme.
Neoplasms
Discovery, Synthesis, Pharmacological Profiling, and Biological Characterization of Brintonamides A-E, Novel Dual Protease and GPCR Modulators from a Marine Cyanobacterium.
Neoplasms
Experiment research of cisplatin implants inhibiting transplantation tumor growth and regulating the expression of KLK7 and E-cad of tumor-bearing mice with gastric cancer.
Neoplasms
Expression of kallikrein 7 diminishes pancreatic cancer cell adhesion to vitronectin and enhances urokinase-type plasminogen activator receptor shedding.
Neoplasms
Expression of kallikrein-related peptidase 7 is decreased in prostate cancer.
Neoplasms
Expression of the protease inhibitor antileukoprotease and the serine protease stratum corneum chymotryptic enzyme (SCCE) is coordinated in ovarian tumors.
Neoplasms
Immunohistochemical localization and analysis of kallikrein-related peptidase 7 and 11 expression in paired cancer and benign foci in prostate cancer patients.
Neoplasms
Isomannide derivatives as new class of inhibitors for human kallikrein 7.
Neoplasms
Kallikrein 7 enhances pancreatic cancer cell invasion by shedding E-cadherin.
Neoplasms
Kallikrein-related peptidase 7 (KLK7) is a proliferative factor that is aberrantly expressed in human colon cancer.
Neoplasms
Parallel underexpression of kallikrein 5 and kallikrein 7 mRNA in breast malignancies.
Neoplasms
The extracellular matrix protein fibronectin is a substrate for kallikrein 7.
Neoplasms
The serine protease stratum corneum chymotryptic enzyme (kallikrein 7) is highly overexpressed in squamous cervical cancer cells.
Neoplasms
The stratum corneum chymotryptic enzyme that mediates shedding and desquamation of skin cells is highly overexpressed in ovarian tumor cells.
Netherton Syndrome
Epidermal differentiation: the role of proteases and their inhibitors.
Netherton Syndrome
Generation of a quenched phosphonate activity-based probe for labelling the active KLK7 protease.
Netherton Syndrome
SPINK5 knockdown in organotypic human skin culture as a model system for Netherton syndrome: effect of genetic inhibition of serine proteases kallikrein 5 and kallikrein 7.
Nevus
Cell adhesion and communication proteins are differentially expressed in melanoma progression model.
Obesity
Ablation of kallikrein 7 (KLK7) in adipose tissue ameliorates metabolic consequences of high fat diet-induced obesity by counteracting adipose tissue inflammation in vivo.
Ovarian Neoplasms
Clinical value of protein expression of kallikrein-related peptidase 7 (KLK7) in ovarian cancer.
Ovarian Neoplasms
Crystallization and preliminary crystallographic studies of human kallikrein 7, a serine protease of the multigene kallikrein family.
Ovarian Neoplasms
Expression of the protease inhibitor antileukoprotease and the serine protease stratum corneum chymotryptic enzyme (SCCE) is coordinated in ovarian tumors.
Ovarian Neoplasms
Human tissue kallikrein 7, a novel biomarker for advanced ovarian carcinoma using a novel in situ quantitative method of protein expression.
Ovarian Neoplasms
Integration of two in-depth quantitative proteomics approaches determines the kallikrein-related peptidase 7 (KLK7) degradome in ovarian cancer cell secretome.
Ovarian Neoplasms
Prognostic value of kallikrein-related peptidase 7 (KLK7) mRNA expression in advanced high-grade serous ovarian cancer.
Ovarian Neoplasms
Unfavorable prognostic value of human kallikrein 7 quantified by ELISA in ovarian cancer cytosols.
Pancreatic Neoplasms
Desmoglein 2 is a substrate of kallikrein 7 in pancreatic cancer.
Pancreatic Neoplasms
Expression of kallikrein 7 diminishes pancreatic cancer cell adhesion to vitronectin and enhances urokinase-type plasminogen activator receptor shedding.
Pancreatic Neoplasms
Kallikrein 7 enhances pancreatic cancer cell invasion by shedding E-cadherin.
Pancreatic Neoplasms
Kallikrein-related peptidase 7 is a potential target for the treatment of pancreatic cancer.
Papillon-Lefevre Disease
Epidermal differentiation: the role of proteases and their inhibitors.
Prostatic Neoplasms
Expression of kallikrein-related peptidase 7 is decreased in prostate cancer.
Prostatic Neoplasms
Expression of the serine protease kallikrein 7 and its inhibitor antileukoprotease is decreased in prostate cancer.
Prostatic Neoplasms
Human kallikrein 7 induces epithelial-mesenchymal transition-like changes in prostate carcinoma cells: a role in prostate cancer invasion and progression.
Prostatic Neoplasms
Immunohistochemical localization and analysis of kallikrein-related peptidase 7 and 11 expression in paired cancer and benign foci in prostate cancer patients.
Pruritus
Epidermal overexpression of stratum corneum chymotryptic enzyme in mice: a model for chronic itchy dermatitis.
Psoriasis
Crystallization and preliminary crystallographic studies of human kallikrein 7, a serine protease of the multigene kallikrein family.
Psoriasis
Epidermal overexpression of stratum corneum chymotryptic enzyme in mice: a model for chronic itchy dermatitis.
Psoriasis
Stratum corneum chymotryptic enzyme in psoriasis.
Skin Diseases
A fluorescence lifetime-based assay for protease inhibitor profiling on human kallikrein 7.
Skin Diseases
A novel theranostic activity-based probe targeting kallikrein 7 for the diagnosis and treatment of skin diseases.
Skin Diseases
An unexpected switch in peptide binding mode: from simulation to substrate specificity.
Skin Diseases
Epidermal overexpression of stratum corneum chymotryptic enzyme in mice: a model for chronic itchy dermatitis.
Skin Diseases
Generation of a quenched phosphonate activity-based probe for labelling the active KLK7 protease.
Skin Diseases
Generation of recombinant antibodies against human tissue kallikrein 7 to treat skin diseases.
Skin Diseases
Pyrido-imidazodiazepinones as a new class of reversible inhibitors of human kallikrein 7.
Sleep Deprivation
Sleep loss and cytokines levels in an experimental model of psoriasis.
Squamous Cell Carcinoma of Head and Neck
Immunohistochemical expression of kallikrein 7 in oral squamous cell carcinoma.
Stomach Neoplasms
Experiment research of cisplatin implants inhibiting transplantation tumor growth and regulating the expression of KLK7 and E-cad of tumor-bearing mice with gastric cancer.
Uterine Cervical Neoplasms
Serum human kallikrein 7 represents a new marker for cervical cancer.
Uterine Cervical Neoplasms
The serine protease stratum corneum chymotryptic enzyme (kallikrein 7) is highly overexpressed in squamous cervical cancer cells.
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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
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31
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2003
Homo sapiens (P49862)
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El Moujahed, A.; Gutman, N.; Brillard, M.; Gauthier, F.
Substrate specificity of two kallikrein family gene products isolated from the rat submandibular gland
FEBS Lett.
265
137-140
1990
Rattus norvegicus
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Yousef, G.M.; Diamandis, E.P.
The new human tissue kallikrein gene family: structure, function, and association to disease
Endocr. Rev.
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2001
Homo sapiens (P49862)
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Lundstrom, A.; Egelrud, T.
Stratum corneum chymotryptic enzyme: a proteinase which may be generally present in the stratum corneum and with a possible involvement in desquamation
Acta Derm. Venereol.
71
471-474
1991
Homo sapiens
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Egelrud, T.
Purification and preliminary characterization of stratum corneum chymotryptic enzyme: a proteinase that may be involved in desquamation
J. Invest. Dermatol.
101
200-204
1993
Homo sapiens
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Hansson, L.; Stromqvist, M.; Backman, A.; Wallbrandt, P.; Carlstein, A.; Egelrud, T.
Cloning, expression, and characterization of stratum corneum chymotryptic enzyme. A skin-specific human serine proteinase
J. Biol. Chem.
269
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1994
Homo sapiens (P49862), Homo sapiens
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Skytt, A.; Stromqvist, M.; Egelrud, T.
Primary substrate specificity of recombinant human stratum corneum chymotryptic enzyme
Biochem. Biophys. Res. Commun.
211
586-589
1995
Homo sapiens
brenda
Franzke, C.W.; Baici, A.; Bartels, J.; Christophers, E.; Wiedow, O.
Antileukoprotease inhibits stratum corneum chymotryptic enzyme. Evidence for a regulative function in desquamation
J. Biol. Chem.
271
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1996
Homo sapiens
brenda
Tanimoto, H.; Underwood, L.J.; Shigemasa, K.; Yan Yan, M.S.; Clarke, J.; Parmley, T.H.; O'Brien, T.J.
The stratum corneum chymotryptic enzyme that mediates shedding and desquamation of skin cells is highly overexpressed in ovarian tumor cells
Cancer
86
2074-2082
1999
Homo sapiens
brenda
Nylander-Lundqvist, E.; Egelrud, T.
Formation of active IL-1 beta from pro-IL-1 beta catalyzed by stratum corneum chymotryptic enzyme in vitro
Acta Derm. Venereol.
77
203-206
1997
Homo sapiens
brenda
Yousef, G.M.; Scorilas, A.; Magklara, A.; Soosaipillai, A.; Diamandis, E.P.
The KLK7 (PRSS6) gene, encoding for the stratum corneum chymotryptic enzyme is a new member of the human kallikrein gene family - genomic characterization, mapping, tissue expression and hormonal regulation
Gene
254
119-128
2000
Homo sapiens (P49862), Homo sapiens
brenda
Ny, A.; Egelrud, T.
Epidermal hyperproliferation and decreased skin barrier function in mice overexpressing stratum corneum chymotryptic enzyme
Acta Derm. Venereol.
84
18-22
2004
Homo sapiens
brenda
Planque, C.; de Monte, M.; Guyetant, S.; Rollin, J.; Desmazes, C.; Panel, V.; Lemarie, E.; Courty, Y.
KLK5 and KLK7, two members of the human tissue kallikrein family, are differentially expressed in lung cancer
Biochem. Biophys. Res. Commun.
329
1260-1266
2005
Homo sapiens
brenda
Tan, O.L.; Whitbread, A.K.; Clements, J.A.; Dong, Y.
Kallikrein-related peptidase (KLK) family mRNA variants and protein isoforms in hormone-related cancers: do they have a function?
Biol. Chem.
387
697-705
2006
Homo sapiens
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Prezas, P.; Arlt, M.J.; Viktorov, P.; Soosaipillai, A.; Holzscheiter, L.; Schmitt, M.; Talieri, M.; Diamandis, E.P.; Krueger, A.; Magdolen, V.
Overexpression of the human tissue kallikrein genes KLK4, 5, 6, and 7 increases the malignant phenotype of ovarian cancer cells
Biol. Chem.
387
807-811
2006
Homo sapiens
brenda
Diamandis, E.P.; Scorilas, A.; Kishi, T.; Blennow, K.; Luo, L.Y.; Soosaipillai, A.; Rademaker, A.W.; Sjogren, M.
Altered kallikrein 7 and 10 concentrations in cerebrospinal fluid of patients with Alzheimers disease and frontotemporal dementia
Clin. Biochem.
37
230-237
2004
Homo sapiens
brenda
Kishi, T.; Soosaipillai, A.; Grass, L.; Little, S.P.; Johnstone, E.M.; Diamandis, E.P.
Development of an immunofluorometric assay and quantification of human kallikrein 7 in tissue extracts and biological fluids
Clin. Chem.
50
709-716
2004
Homo sapiens (P49862), Homo sapiens
brenda
Baretton, G.; Luther, T.; Tjan-Heijnen, V.C.; Talieri, M.; Schmitt, M.; Sweep, F.C.; Span, P.N.; Magdolen, V.
Quantitative reverse transcription-PCR assay for detection of mRNA encoding full-length human tissue kallikrein 7: prognostic relevance of KLK7 mRNA expression in breast cancer
Clin. Chem.
52
1070-1079
2006
Homo sapiens (P49862), Homo sapiens
brenda
Santin, A.D.; Cane, S.; Bellone, S.; Bignotti, E.; Palmieri, M.; De Las Casas, L.E.; Roman, J.J.; Anfossi, S.; OBrien, T.; Pecorelli, S.
The serine protease stratum corneum chymotryptic enzyme (kallikrein 7) is highly overexpressed in squamous cervical cancer cells
Gynecol. Oncol.
94
283-288
2004
Homo sapiens
brenda
Caubet, C.; Jonca, N.; Brattsand, M.; Guerrin, M.; Bernard, D.; Schmidt, R.; Egelrud, T.; Simon, M.; Serre, G.
Degradation of corneodesmosome proteins by two serine proteases of the kallikrein family, SCTE/KLK5/hK5 and SCCE/KLK7/hK7
J. Invest. Dermatol.
122
1235-1244
2004
Homo sapiens (P49862)
brenda
Vasilopoulos, Y.; Cork, M.J.; Murphy, R.; Williams, H.C.; Robinson, D.A.; Duff, G.W.; Ward, S.J.; Tazi-Ahnini, R.
Genetic association between an AACC insertion in the 3UTR of the stratum corneum chymotryptic enzyme gene and atopic dermatitis
J. Invest. Dermatol.
123
62-66
2004
Homo sapiens (P49862), Homo sapiens
brenda
Tian, X.; Shigemasa, K.; Hirata, E.; Gu, L.; Uebaba, Y.; Nagai, N.; OBrien, T.J.; Ohama, K.
Expression of human kallikrein 7 (hK7/SCCE) and its inhibitor antileukoprotease (ALP/SLPI) in uterine endocervical glands and in cervical adenocarcinomas
Oncol. Rep.
12
1001-1006
2004
Homo sapiens
brenda
Talieri, M.; Diamandis, E.P.; Gourgiotis, D.; Mathioudaki, K.; Scorilas, A.
Expression analysis of the human kallikrein 7 (KLK7) in breast tumors: A new potential biomarker for prognosis of breast carcinoma
Thromb. Haemost.
91
180-186
2004
Homo sapiens
brenda
Psyrri, A.; Kountourakis, P.; Scorilas, A.; Markakis, S.; Camp, R.; Kowalski, D.; Diamandis, E.P.; Dimopoulos, M.A.
Human tissue kallikrein 7, a novel biomarker for advanced ovarian carcinoma using a novel in situ quantitative method of protein expression
Ann. Oncol.
19
1271-1277
2008
Homo sapiens
brenda
Prezas, P.; Scorilas, A.; Yfanti, C.; Viktorov, P.; Agnanti, N.; Diamandis, E.; Talieri, M.
The role of human tissue kallikreins 7 and 8 in intracranial malignancies
Biol. Chem.
387
1607-1612
2006
Homo sapiens
brenda
Singh, J.; Naran, A.; Misso, N.L.; Rigby, P.J.; Thompson, P.J.; Bhoola, K.D.
Expression of kallikrein-related peptidases (KRP/hK5, 7, 6, 8) in subtypes of human lung carcinoma
Int. Immunopharmacol.
8
300-306
2008
Homo sapiens
brenda
Debela, M.; Magdolen, V.; Schechter, N.; Valachova, M.; Lottspeich, F.; Craik, C.S.; Choe, Y.; Bode, W.; Goettig, P.
Specificity profiling of seven human tissue kallikreins reveals individual subsite preferences
J. Biol. Chem.
281
25678-25688
2006
Homo sapiens (P49862)
brenda
Deraison, C.; Bonnart, C.; Lopez, F.; Besson, C.; Robinson, R.; Jayakumar, A.; Wagberg, F.; Brattsand, M.; Hachem, J.P.; Leonardsson, G.; Hovnanian, A.
LEKTI fragments specifically inhibit KLK5, KLK7, and KLK14 and control desquamation through a pH-dependent interaction
Mol. Biol. Cell
18
3607-3619
2007
Homo sapiens
brenda
Debela, M.; Hess, P.; Magdolen, V.; Schechter, N.M.; Steiner, T.; Huber, R.; Bode, W.; Goettig, P.
Chymotryptic specificity determinants in the 1.0 A structure of the zinc-inhibited human tissue kallikrein 7
Proc. Natl. Acad. Sci. USA
104
16086-16091
2007
Homo sapiens (P49862), Homo sapiens
brenda
Fernandez, I.S.; Staendker, L.; Forssmann, W.G.; Gimenez-Gallego, G.; Romero, A.
Crystallization and preliminary crystallographic studies of human kallikrein 7, a serine protease of the multigene kallikrein family
Acta Crystallogr. Sect. F
F63
669-672
2007
Homo sapiens
brenda
Stenshamn, K.; Bongcam-Rudloff, E.; Hillbertz, N.S.; Nodtvedt, A.; Bergvall, K.; Hedhammar, A.; Andersson, G.
Evaluation of kallikrein 7 as a disease-causing gene for canine atopic dermatitis using microsatellite-based association mapping
Anim. Genet.
37
601-603
2006
Canis lupus familiaris
brenda
Ramani, V.C.; Haun, R.S.
The extracellular matrix protein fibronectin is a substrate for kallikrein 7
Biochem. Biophys. Res. Commun.
369
1169-1173
2008
Homo sapiens
brenda
Johnson, S.K.; Ramani, V.C.; Hennings, L.; Haun, R.S.
Kallikrein 7 enhances pancreatic cancer cell invasion by shedding E-cadherin
Cancer
109
1811-1820
2007
Homo sapiens
brenda
Shan, S.J.; Scorilas, A.; Katsaros, D.; Rigault de la Longrais, I.; Massobrio, M.; Diamandis, E.P.
Unfavorable prognostic value of human kallikrein 7 quantified by ELISA in ovarian cancer cytosols
Clin. Chem.
52
1879-1886
2006
Homo sapiens
brenda
Fernandez, I.S.; Staendker, L.; Maegert, H.J.; Forssmann, W.G.; Gimenez-Gallego, G.; Romero, A.
Crystal structure of human epidermal kallikrein 7 (hK7) synthesized directly in its native state in E. coli: insights into the atomic basis of its inhibition by LEKTI domain 6 (LD6)
J. Mol. Biol.
377
1488-1497
2008
Homo sapiens (P49862), Homo sapiens
brenda
Debela, M.; Beaufort, N.; Magdolen, V.; Schechter, N.M.; Craik, C.S.; Schmitt, M.; Bode, W.; Goettig, P.
Structures and specificity of the human kallikrein-related peptidases KLK 4, 5, 6, and 7
Biol. Chem.
389
623-632
2008
Homo sapiens
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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
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Buraczewska, I.; Berne, B.; Lindberg, M.; Loden, M.; Toermae, H.
Long-term treatment with moisturizers affects the mRNA levels of genes involved in keratinocyte differentiation and desquamation
Arch. Dermatol. Res.
301
175-181
2009
Homo sapiens
brenda
Xuan, Q.; Yang, X.; Mo, L.; Huang, F.; Pang, Y.; Qin, M.; Chen, Z.; He, M.; Wang, Q.; Mo, Z.N.
Expression of the serine protease kallikrein 7 and its inhibitor antileukoprotease is decreased in prostate cancer
Arch. Pathol. Lab. Med.
132
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2008
Homo sapiens
brenda
Eissa, A.; Diamandis, E.P.
Human tissue kallikreins as promiscuous modulators of homeostatic skin barrier functions
Biol. Chem.
389
669-680
2008
Homo sapiens
brenda
Dong, Y.; Matigian, N.; Harvey, T.J.; Samaratunga, H.; Hooper, J.D.; Clements, J.A.
Tissue-specific promoter utilisation of the kallikrein-related peptidase genes, KLK5 and KLK7, and cellular localisation of the encoded proteins suggest roles in exocrine pancreatic function
Biol. Chem.
389
99-109
2008
Homo sapiens
brenda
Ramani, V.C.; Hennings, L.; Haun, R.S.
Desmoglein 2 is a substrate of kallikrein 7 in pancreatic cancer
BMC Cancer
8
373
2008
Homo sapiens
brenda
Termini, L.; Boccardo, E.; Esteves, G.H.; Hirata, R.; Martins, W.K.; Colo, A.E.; Neves, E.J.; Villa, L.L.; Reis, L.F.
Characterization of global transcription profile of normal and HPV-immortalized keratinocytes and their response to TNF treatment
BMC Med. Genomics
1
29
2008
Homo sapiens
brenda
Weidinger, S.; Baurecht, H.; Wagenpfeil, S.; Henderson, J.; Novak, N.; Sandilands, A.; Chen, H.; Rodriguez, E.; ORegan, G.M.; Watson, R.; Liao, H.; Zhao, Y.; Barker, J.N.; Allen, M.; Reynolds, N.; Meggitt, S.; Northstone, K.; Smith, G.D.; Strobl, C.; Stahl, C.; Kneib, T.; Klopp, N.; Bieber, T.; Behren, B.e.h.r.e.n.d.
Analysis of the individual and aggregate genetic contributions of previously identified serine peptidase inhibitor Kazal type 5 (SPINK5), kallikrein-related peptidase 7 (KLK7), and filaggrin (FLG) polymorphisms to eczema risk
J. Allergy Clin. Immunol.
122
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2008
Homo sapiens
brenda
Doering, K.; Meder, G.; Hinnenberger, M.; Woelcke, J.; Mayr, L.M.; Hassiepen, U.
A fluorescence lifetime-based assay for protease inhibitor profiling on human kallikrein 7
J. Biomol. Screen.
14
1-9
2009
Homo sapiens (P49862), Homo sapiens
brenda
Ramani, V.C.; Haun, R.S.
Expression of kallikrein 7 diminishes pancreatic cancer cell adhesion to vitronectin and enhances urokinase-type plasminogen activator receptor shedding
Pancreas
37
399-404
2008
Homo sapiens
brenda
Gabril, M.; White, N.M.; Moussa, M.; Chow, T.F.; Metias, S.M.; Fatoohi, E.; Yousef, G.M.
Immunohistochemical analysis of kallikrein-related peptidases in the normal kidney and renal tumors: potential clinical implications
Biol. Chem.
391
403-409
2010
Homo sapiens
brenda
Ohler, A.; Debela, M.; Wagner, S.; Magdolen, V.; Becker-Pauly, C.
Analyzing the protease web in skin: meprin metalloproteases are activated specifically by KLK4, 5 and 8 vice versa leading to processing of proKLK7 thereby triggering its activation
Biol. Chem.
391
455-460
2010
Homo sapiens
brenda
Dong, Y.; Tan, O.L.; Loessner, D.; Stephens, C.; Walpole, C.; Boyle, G.M.; Parsons, P.G.; Clements, J.A.
Kallikrein-related peptidase 7 promotes multicellular aggregation via the alpha(5)beta(1) integrin pathway and paclitaxel chemoresistance in serous epithelial ovarian carcinoma
Cancer Res.
70
2624-2633
2010
Homo sapiens
brenda
Li, X.; Liu, J.; Wang, Y.; Zhang, L.; Ning, L.; Feng, Y.
Parallel underexpression of kallikrein 5 and kallikrein 7 mRNA in breast malignancies
Cancer Sci.
100
601-607
2009
Homo sapiens
brenda
Termini, L.; Maciag, P.C.; Soares, F.A.; Nonogaki, S.; Pereira, S.M.; Alves, V.A.; Longatto-Filho, A.; Villa, L.L.
Analysis of human kallikrein 7 expression as a potential biomarker in cervical neoplasia
Int. J. Cancer
127
485-490
2010
Homo sapiens
brenda
Morizane, S.; Yamasaki, K.; Kabigting, F.D.; Gallo, R.L.
Kallikrein expression and cathelicidin processing are independently controlled in keratinocytes by calcium, vitamin D3, and retinoic acid
J. Invest. Dermatol.
130
1297-1306
2010
Homo sapiens
brenda
Talieri, M.; Mathioudaki, K.; Prezas, P.; Alexopoulou, D.K.; Diamandis, E.P.; Xynopoulos, D.; Ardavanis, A.; Arnogiannaki, N.; Scorilas, A.
Clinical significance of kallikrein-related peptidase 7 (KLK7) in colorectal cancer
Thromb. Haemost.
101
741-747
2009
Homo sapiens
brenda
Ramani, V.C.; Kaushal, G.P.; Haun, R.S.
Proteolytic action of kallikrein-related peptidase 7 produces unique active matrix metalloproteinase-9 lacking the C-terminal hemopexin domains
Biochim. Biophys. Acta
1813
1525-1531
2011
Homo sapiens
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Jamaspishvili, T.; Scorilas, A.; Kral, M.; Khomeriki, I.; Kurfurstova, D.; Kolar, Z.; Bouchal, J.
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Homo sapiens
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Oliveira, J.R.; Bertolin, T.C.; Andrade, D.; Oliveira, L.C.; Kondo, M.Y.; Santos, J.A.; Blaber, M.; Juliano, L.; Severino, B.; Caliendo, G.; Santagada, V.; Juliano, M.A.
Specificity studies on Kallikrein-related peptidase 7 (KLK7) and effects of osmolytes and glycosaminoglycans on its peptidase activity
Biochim. Biophys. Acta
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Homo sapiens (P49862), Homo sapiens
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Walker, F.; Nicole, P.; Jallane, A.; Soosaipillai, A.; Mosbach, V.; Oikonomopoulou, K.; Diamandis, E.P.; Magdolen, V.; Darmoul, D.
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Homo sapiens
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Shropshire, T.D.; Reifert, J.; Rajagopalan, S.; Baker, D.; Feinstein, S.C.; Daugherty, P.S.
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Rattus norvegicus
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Arama, D.; Soualmia, F.; Lisowski, V.; Longevial, J.; Bosc, E.; Maillard, L.; Martinez, J.; Masurier, N.; El Amri, C.
Pyrido-imidazodiazepinones as a new class of reversible inhibitors of human kallikrein 7
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Homo sapiens
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Li, W.; Zhao, Y.; Ren, L.; Wu, X.
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Homo sapiens
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Homo sapiens (P49862), Homo sapiens
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Haddada, M.; Draoui, H.; Deschamps, L.; Walker, F.; Delaunay, T.; Brattsand, M.; Magdolen, V.; Darmoul, D.
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Homo sapiens (P49862), Homo sapiens
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Murafuji, H.; Muto, T.; Goto, M.; Imajo, S.; Sugawara, H.; Oyama, Y.; Minamitsuji, Y.; Miyazaki, S.; Murai, K.; Fujioka, H.
Discovery and structure-activity relationship of imidazolinylindole derivatives as kallikrein 7 inhibitors
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Homo sapiens (P49862), Homo sapiens, Mus musculus (Q91VE3), Mus musculus
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Yu, Y.; Prassas, I.; Dimitromanolakis, A.; Diamandis, E.P.
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Homo sapiens (P49862), Homo sapiens
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de Veer, S.J.; Furio, L.; Swedberg, J.E.; Munro, C.A.; Brattsand, M.; Clements, J.A.; Hovnanian, A.; Harris, J.M.
Selective substrates and inhibitors for kallikrein-related peptidase 7 (KLK7) shed light on KLK proteolytic activity in the stratum corneum
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Homo sapiens (P49862)
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Silva, L.M.; Stoll, T.; Kryza, T.; Stephens, C.R.; Hastie, M.L.; Irving-Rodgers, H.F.; Dong, Y.; Gorman, J.J.; Clements, J.A.
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Homo sapiens (P49862), Homo sapiens
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