Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
benzoyl-Phe-Val-Arg-4-methylcoumarinyl-7-amide + H2O
benzoyl-Phe-Val-Arg + 7-amino-4-methylcoumarin
cathepsin L2
-
-
?
benzyloxycarbonyl-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-Arg + 7-amino-4-methylcoumarin
cathepsin L2
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
cathepsin L2
-
-
?
benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
FhCL2
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
FhCL2
-
-
?
benzyloxycarbonyl-L-Pro-L-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-L-Pro-L-Arg + 7-amino-4-methylcoumarin
FhCL2
-
-
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methyl coumarin
-
cathepsin L2
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Boc-AGPR-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Boc-VLK-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Boc-VPR-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Collagen type I + H2O
?
-
cathepsin L2 cleaves collagen type I at 43 sites within the alpha1 chain and 26 sites within the alpha2 chain
-
-
?
collagen type II + H2O
?
-
cathepsin L2 exhibits collagenase activity by cleaving at multiple sites within the alpha1 and alpha2 triple helix regions (Col domains)
-
-
?
Fibrinogen + H2O
?
FhCL2 demonstrates only minor cleavage of the gamma-chain and slower cleavage of the alpha-chain and beta-chain
-
-
?
human IgG + H2O
?
-
both cathepsins L produce similar degradation patterns and cleave all human IgG subclasses at the hinge region, yielding at pH 7.3 and 37°C Fab and Fc fragments in the case of IgG1 and IgG3 or Fab(2) and Fc in IgG2 and IgG4. Both liver fluke cathepsins L cleave the peptide bonds 237His-Thr, 237Glu-Cys, 233Gly-Asp, and 241Ser-Cys of the gamma1, gamma2, gamma3, and gamma4 H chains, respectively. Therefore, the enzymes are interacting with the following P3-P'3 sequences, Lys-Thr-His-Thr-Cys-Pro, Cys-Val-Glu-Asp-Pro-Pro, Pro-Leu-Gly-Asp-Thr-Thr, and Cys-Pro-Ser-Cys-Pro-Ala. The specificity of the liver fluke cathepsins L for peptide bonds in proteins is less defined. The P1 position, for instance, can be occupied by hydrophobic, hydrophilic, acidic, or basic residues. The P3 and P2 positions are occupied by hydrophobic amino acids with the exception of the gamma1 sequence which contains a basic lysine and a hydrophilic threonine, respectively. In addition the specificity between the enzyme and its substrate would depend on which of the amino acids of the substrate can be really exposed to the active site
-
-
?
Leu-Val-Tyr-4-methylcoumarinyl-7-amide + H2O
Leu-Val-Tyr + 7-amino-4-methylcoumarin
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
procathepsin L2 + H2O
?
-
procathepsin L2 autocatalytically processes and activates to its mature enzyme (FheCL2). FheCL2, which, unlike FheCL1, can readily accept proline in the S2 subsite of its active site, can trans-process the double variant FheproCL1Pro-12/Gly26 by cleavage at the Pro-12-Ser-11-/-His-10 sequence
-
-
?
succinyl-Ala-Phe-Lys-4-methylcoumarinyl-7-amide + H2O
succinyl-Ala-Phe-Lys + 7-amino-4-methylcoumarin
cathepsin L2
-
-
?
succinyl-Leu-Leu-Val-Tyr-4-methylcoumarinyl-7-amide + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
cathepsin L2
-
-
?
tert-butoxycarbonyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tert-butoxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
FhCL2
-
-
?
tert-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumarinyl-7-amide + H2O
tert-butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
cathepsin L2
-
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
tosyl-Ala-Phe-Lys-4-methylcoumarinyl-7-amide + H2O
tosyl-Ala-Phe-Lys + 7-amino-4-methylcoumarin
cathepsin L2
-
-
?
tosyl-Gly-Phe-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-Phe-Arg + 7-amino-4-methylcoumarin
-
cathepsin L2
-
-
?
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methyl coumarin
-
cathepsin L2
-
-
?
tosyl-Gly-Pro-Lys-4-methylcoumarinyl-7-amide + H2O
tosyl-Gly-Pro-Lys + 7-amino-4-methylcoumarin
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
tosyl-GPK-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
tosyl-GPR-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Z-Gly-Pro-Gly-Gly-Pro-Ala + H2O
Z-Gly-Pro + Gly-Gly + L-Pro-L-Ala
-
-
-
-
?
Z-Gly-Pro-Leu-Gly-Pro + H2O
Z-Gly-Pro + L-Leu + Gly + L-Pro
-
-
-
-
?
Z-Leu-Arg-NHMe + H2O
?
-
-
-
-
?
Z-Phe-Arg-NHMe + H2O
?
-
-
-
-
?
Z-VVR-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
additional information
?
-
Collagen + H2O
?
FhCL2 cleaves substrates with a bulky proline in the P2 position as the native collagen, which contains a repeat motif of Gly-Pro-Xaa (in which Xaa is any amino acid). By contrast these substrates are poorly cleaved by FhCL1 and not at all by human cathepsin L
-
-
?
Collagen + H2O
?
whereas FheCL1 produces clear degradation fragments, FheCL2 degrades the collagen completely, particularly at pH 4.0, indicating that only the latter cleaves efficiently within the helical structures
-
-
?
Fibrin + H2O
?
-
-
-
?
Fibrin + H2O
?
-
cathepsin L proteinase cleaves fibrinogen and produces a novel type of fibrin clot
-
-
?
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
FhCL2
-
-
?
additional information
?
-
cathepsin L1 and cathepsin L2 proteinases may be the prime mechanism by which the parasite penetrates tissue
-
-
?
additional information
?
-
FheCL1 and FheCL2 exhibit similar preferences for amino acids at P1. Both enzymes have a clear preference for Arg at P1 position, but other residues accommodate in this position include Lys, Glu, Thr, and Met. These are all cleaved at similar relative rates to that observed for human cathepsin L and cathepsin K. FheCL1 and FheCL2 are similar to cathepsin K with regard to their preference for a P2 position Leu over Phe (human cathepsin L has a preference for P2 position Phe over Leu). Both enzymes can accommodate Pro in the P2 position, but this is more readily accepted by FheCL2 compared with FheCL1. Neither enzyme, however, cleaves substrates with this residue in the P2 position as readily as human cathepsin K
-
-
?
additional information
?
-
-
FheCL1 and FheCL2 exhibit similar preferences for amino acids at P1. Both enzymes have a clear preference for Arg at P1 position, but other residues accommodate in this position include Lys, Glu, Thr, and Met. These are all cleaved at similar relative rates to that observed for human cathepsin L and cathepsin K. FheCL1 and FheCL2 are similar to cathepsin K with regard to their preference for a P2 position Leu over Phe (human cathepsin L has a preference for P2 position Phe over Leu). Both enzymes can accommodate Pro in the P2 position, but this is more readily accepted by FheCL2 compared with FheCL1. Neither enzyme, however, cleaves substrates with this residue in the P2 position as readily as human cathepsin K
-
-
?
additional information
?
-
-
cathepsin L2 readily cleaves substrates with Pro in the P2 position and peptide substrates mimicking the repeating Gly-Pro-Xaa motifs
-
-
?
additional information
?
-
-
the cathepsin L zymogen is autocatalytically activated and processed to mature enzyme by incubation for 2 h at 37°C in 0.1 M sodium citrate buffer (pH 5.0) containing 2 mM dithiothreitol and 2.5 mM EDTA
-
-
?
additional information
?
-
S2 subsite preferences are aliphatic over aromatic, L-proline. The enzyme has a preference for leucine over phenylalanine at the P2 position
-
-
?
additional information
?
-
-
S2 subsite preferences are aliphatic over aromatic, L-proline. The enzyme has a preference for leucine over phenylalanine at the P2 position
-
-
?
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.
Alopecia
Cell type-specific functions of the lysosomal protease cathepsin L in the heart.
Alopecia
Evaluation of the CTSL2 Gene as a Candidate Gene For Alopecia X in Pomeranians and Keeshonden.
Breast Neoplasms
Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas.
Carcinoma, Renal Cell
Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas.
Colorectal Neoplasms
Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas.
Diabetes Mellitus, Type 1
Polymorphisms in the cathepsin L2 (CTSL2) gene show association with type 1 diabetes and early-onset myasthenia gravis.
Endometrial Neoplasms
Expression of cysteine protease cathepsin L is increased in endometrial cancer and correlates with expression of growth regulatory genes.
Infections
Fasciola hepatica serine protease inhibitor family (serpins): Purposely crafted for regulating host proteases.
Infections
Immune responses of cattle to experimental anti-Fasciola hepatica vaccines.
Myasthenia Gravis
Polymorphisms in the cathepsin L2 (CTSL2) gene show association with type 1 diabetes and early-onset myasthenia gravis.
Neoplasms
Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas.
Neoplasms
Electrophoretic analysis of the cleaved form of serpin, squamous cell carcinoma antigen-1 in normal and malignant squamous epithelial tissues.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0012
benzoyl-Phe-Val-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.0141
benzyloxycarbonyl-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.0091
benzyloxycarbonyl-Arg-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.0014
benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide
FheCL2
0.04
benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarinyl-7-amide
FheCL2
0.084
benzyloxycarbonyl-L-Pro-L-Arg-4-methylcoumarinyl-7-amide
FheCL2
0.0036 - 0.0044
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
0.004
benzyloxycarbonyl-Phe-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.0155 - 0.0399
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
0.0752 - 0.084
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin
0.0094
Boc-AGPR-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.0022
Boc-VLK-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.01139
Boc-VPR-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.0038
Leu-Val-Tyr-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.0412
succinyl-Ala-Phe-Lys-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.0232
succinyl-Leu-Leu-Val-Tyr-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.0337
tert-butoxycarbonyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
FheCL2
0.0073
tert-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.0248
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.0327
tosyl-Gly-Phe-Arg-7-amido-4-methylcoumarin
-
FhCatL2
0.0153 - 0.0171
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
0.0483
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
-
FhCatL2
0.0355
tosyl-Gly-Pro-Lys-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.0129
tosyl-GPK-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.0139
tosyl-GPR-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.00213
Z-Leu-Arg-NHMe
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.0078
Z-Phe-Arg-NHMe
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.00153
Z-VVR-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.0036
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
37°C, pH 7.3
0.0044
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
37°C, pH 5.5
0.0155
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
FhCatL2
0.016
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
37°C, pH 7.3
0.0399
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
37°C, pH 5.5
0.0752
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin
37°C, pH 7.3
0.084
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin
37°C, pH 5.5
0.0153
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
FheCL2
0.0171
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.06
benzoyl-Phe-Val-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.09
benzyloxycarbonyl-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.02
benzyloxycarbonyl-Arg-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
1.62
benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide
FheCL2
1.7
benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarinyl-7-amide
FheCL2
2.64
benzyloxycarbonyl-L-Pro-L-Arg-4-methylcoumarinyl-7-amide
FheCL2
1.6 - 3.2
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
0.56
benzyloxycarbonyl-Phe-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.4 - 50
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
1.9 - 2.6
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin
0.55
Boc-AGPR-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.07
Boc-VLK-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.23
Boc-VPR-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.21
Leu-Val-Tyr-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.14
succinyl-Ala-Phe-Lys-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.08
succinyl-Leu-Leu-Val-Tyr-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
2.48
tert-butoxycarbonyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
FheCL2
3.75
tert-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
1.19
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
26.3
tosyl-Gly-Phe-Arg-7-amido-4-methylcoumarin
-
FhCatL2
1.17 - 1.93
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
440
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
-
FhCatL2
1.37
tosyl-Gly-Pro-Lys-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.18
tosyl-GPK-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.26
tosyl-GPR-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.95
Z-Leu-Arg-NHMe
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.09
Z-Phe-Arg-NHMe
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.014
Z-VVR-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
1.6
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
37°C, pH 5.5
3.2
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
37°C, pH 7.3
0.4
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
37°C, pH 7.3
1.7
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
37°C, pH 5.5
50
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
FhCatL2
1.9
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin
37°C, pH 7.3
2.6
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin
37°C, pH 5.5
1.17
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
FheCL2
1.93
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
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.
Dowd, A.J.; Smith, A.M.; McGonigle, S.; Dalton, J.P.
Purification and characterization of a second cathepsin L proteinase secreted by parasitic trematode Fasciola hepatica
Eur. J. Biochem.
223
91-98
1994
Fasciola hepatica (P80342)
brenda
Stack, C.M.; Donnelly, S.; Lowther, J.; Xu, W.; Collins, P.R.; Brinen, L.S.; Dalton, J.P.
The major secreted cathepsin L1 protease of the liver fluke, Fasciola hepatica: a Leu-12 to Pro-12 replacement in the nonconserved C-terminal region of the prosegment prevents complete enzyme autoactivation and allows definition of the molecular events in
J. Biol. Chem.
282
16532-16543
2007
Fasciola hepatica
brenda
Stack, C.M.; Caffrey, C.R.; Donnelly, S.M.; Seshaadri, A.; Lowther, J.; Tort, J.F.; Collins, P.R.; Robinson, M.W.; Xu, W.; McKerrow, J.H.; Craik, C.S.; Geiger, S.R.; Marion, R.; Brinen, L.S.; Dalton, J.P.
Structural and functional relationships in the virulence-associated cathepsin L proteases of the parasitic liver fluke, Fasciola hepatica
J. Biol. Chem.
283
9896-9908
2008
Fasciola hepatica (Q24940), Fasciola hepatica
brenda
Dowd, A.J.; McGonigle, S.; Dalton, J.P.
Fasciola hepatica cathepsin L proteinase cleaves fibrinogen and produces a novel type of fibrin clot
Eur. J. Biochem.
232
241-246
1995
Fasciola hepatica
brenda
Berasain, P.; Carmona, C.; Frangione, B.; Dalton, J.P.; Goni, F.
Fasciola hepatica: parasite-secreted proteinases degrade all human IgG subclasses: determination of the specific cleavage sites and identification of the immunoglobulin fragments produced
Exp. Parasitol.
94
99-110
2000
Fasciola hepatica
brenda
Smooker, P.M.; Whisstock, J.C.; Irving, J.A.
Siyaguna, S.; Spithill, T.W.: Pike, R.N.: A single amino acid substitution affects substrate specificity in cysteine proteinases from Fasciola hepatica
Protein Sci.
9
2567-2572
2000
Fasciola hepatica
brenda
Robinson, M.W.; Dalton, J.P.; Donnelly, S.
Helminth pathogen cathepsin proteases
Trends Biochem. Sci.
33
601-608
2008
Fasciola hepatica (Q24940)
brenda
Robinson, M.W.; Tort, J.F.; Lowther, J.; Donnelly, S.M.; Wong, E.; Xu, W.; Stack, C.M.; Padula, M.; Herbert, B.; Dalton, J.P.
Proteomics and phylogenetic analysis of the cathepsin L protease family of the helminth pathogen Fasciola hepatica: expansion of a repertoire of virulence-associated factors
Mol. Cell. Proteomics
7
1111-1123
2008
Fasciola hepatica (Q7JNQ8)
brenda
Villa-Mancera, A.; Quiroz-Romero, H.; Correa, D.; Ibarra, F.; Reyes-Perez, M.; Reyes-Vivas, H.; Lopez-Velazquez, G.; Gazarian, K.; Gazarian, T.; Alonso, R.A.
Induction of immunity in sheep to Fasciola hepatica with mimotopes of cathepsin L selected from a phage display library
Parasitology
135
1437-1445
2008
Fasciola hepatica
brenda
Sukuru, S.C.; Nigsch, F.; Quancard, J.; Renatus, M.; Chopra, R.; Brooijmans, N.; Mikhailov, D.; Deng, Z.; Cornett, A.; Jenkins, J.L.; Hommel, U.; Davies, J.W.; Glick, M.
A lead discovery strategy driven by a comprehensive analysis of proteases in the peptide substrate space
Protein Sci.
19
2096-2109
2010
Homo sapiens
brenda
Norbury, L.J.; Beckham, S.; Pike, R.N.; Grams, R.; Spithill, T.W.; Fecondo, J.V.; Smooker, P.M.
Adult and juvenile Fasciola cathepsin L proteases: different enzymes for different roles
Biochimie
93
604-611
2011
Fasciola hepatica (Q7JNQ8), Fasciola hepatica
brenda
Robinson, M.W.; Corvo, I.; Jones, P.M.; George, A.M.; Padula, M.P.; To, J.; Cancela, M.; Rinaldi, G.; Tort, J.F.; Roche, L.; Dalton, J.P.
Collagenolytic activities of the major secreted cathepsin L peptidases involved in the virulence of the helminth pathogen, Fasciola hepatica
PLoS Negl. Trop. Dis.
5
e1012
2011
Fasciola hepatica
brenda
Leng, Y.P.; Ma, Y.S.; Li, X.G.; Chen, R.F.; Zeng, P.Y.; Li, X.H.; Qiu, C.F.; Li, Y.P.; Zhang, Z.; Chen, A.F.
L-Homocysteine-induced cathepsin V mediates the vascular endothelial inflammation in hyperhomocysteinaemia
Br. J. Pharmacol.
175
1157-1172
2018
Mus musculus, Mus musculus C57BL/6
brenda
Mebius, M.M.; Op Heij, J.M.J.; Tielens, A.G.M.; de Groot, P.G.; Urbanus, R.T.; van Hellemond, J.J.
Fibrinogen and fibrin are novel substrates for Fasciola hepatica cathepsin L peptidases
Mol. Biochem. Parasitol.
221
10-13
2018
Fasciola hepatica (A0A220T1Z2), Fasciola hepatica
brenda
Martinez-Sernandez, V.; Perteguer, M.J.; Hernandez-Gonzalez, A.; Mezo, M.; Gonzalez-Warleta, M.; Orbegozo-Medina, R.A.; Romaris, F.; Paniagua, E.; Garate, T.; Ubeira, F.M.
Comparison of recombinant cathepsins L1, L2, and L5 as ELISA targets for serodiagnosis of bovine and ovine fascioliasis
Parasitol. Res.
117
1521-1534
2018
Fasciola hepatica (A0A220T1Z2), Fasciola hepatica
brenda