BRENDA - Enzyme Database
show all sequences of 3.4.22.43

DNA accelerates the inhibition of human cathepsin V by serpins

Ong, P.C.; McGowan, S.; Pearce, M.C.; Irving, J.A.; Kan, W.T.; Grigoryev, S.A.; Turk, B.; Silverman, G.A.; Brix, K.; Bottomley, S.P.; Whisstock, J.C.; Pike, R.N.; J. Biol. Chem. 282, 36980-36986 (2007)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
human cathepsins V expressed in Pichia pastoris
Homo sapiens
Inhibitors
Inhibitors
Commentary
Organism
Structure
cystatin
cystatin inhibition relies on occlusion of the active site rather than the substrate-like behavior of serpins, unaltered by addition of DNA
Homo sapiens
serpin
cofactors fine tuning serpin activity in the extracellular milieu analyzed, DNA accelerate the rate at which the model serpin MENT inhibit cathepsin V up to 50-fold, primarily effected via the protease and secondarily by the recruitment of the DNA as a template onto which cathepsin V and MENT are bound, altered substrate turnover and conformational change within the protease observed, enzyme concentration constant at 0.1 nM, serpin concentration varying between 0.5 and 60 nM with a maximum of 5 nM serpin in the presence of DNA
Homo sapiens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
presence of ds65-mer DNA causes a nonsignificant decrease in the Km value for the interaction between cathepsin V and the substrate, values from about 33.1 microM to 27.5 microM measured
Homo sapiens
Organism
Organism
UniProt
Commentary
Textmining
Homo sapiens
O60911
-
-
Purification (Commentary)
Purification (Commentary)
Organism
gel filtration, pre-activated before use
Homo sapiens
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
interaction between cathepsin V with the model serpins MENT and SCCA-1 and with cystatin A analyzed, association rate constant (ka) for cathepsin V interaction in the presence and absence of cofactors determined, stoichiometry of inhibition (SI) in the absence and presence of cofactors determined, kinetic parameters of MENT and cystatin A in the presence of various DNA constructs ranging between 18mers and 65mers measured, binding of serpins and cathepsin V to DNA indicated by gel mobility shift analysis, electrostatic potential of human cathepsins V and effect of dsDNA on cathepsin V fluorescence indicated
Homo sapiens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
N-benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarin 7-amide + H2O
mechanisms of interaction between serpins, human cathepsin V and DNA analyzed, kinetic constants for substrate cleavage in the presence and absence of cofactors determined, final concentrations of cathepsin V and ds65mer DNA at 0.1 and 10 nM, final substrate concentrations ranging from 5 to 200 microM in cathepsin V buffer
683662
Homo sapiens
N-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
presence of DNA reduces the turnover rate up to 50% indicating that the binding of DNA changes the active site of cathepsin V such that the enzyme interacts with peptide substrates differently
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
human cathepsins V expressed in Pichia pastoris
Homo sapiens
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
cystatin
cystatin inhibition relies on occlusion of the active site rather than the substrate-like behavior of serpins, unaltered by addition of DNA
Homo sapiens
serpin
cofactors fine tuning serpin activity in the extracellular milieu analyzed, DNA accelerate the rate at which the model serpin MENT inhibit cathepsin V up to 50-fold, primarily effected via the protease and secondarily by the recruitment of the DNA as a template onto which cathepsin V and MENT are bound, altered substrate turnover and conformational change within the protease observed, enzyme concentration constant at 0.1 nM, serpin concentration varying between 0.5 and 60 nM with a maximum of 5 nM serpin in the presence of DNA
Homo sapiens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
presence of ds65-mer DNA causes a nonsignificant decrease in the Km value for the interaction between cathepsin V and the substrate, values from about 33.1 microM to 27.5 microM measured
Homo sapiens
Purification (Commentary) (protein specific)
Commentary
Organism
gel filtration, pre-activated before use
Homo sapiens
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
interaction between cathepsin V with the model serpins MENT and SCCA-1 and with cystatin A analyzed, association rate constant (ka) for cathepsin V interaction in the presence and absence of cofactors determined, stoichiometry of inhibition (SI) in the absence and presence of cofactors determined, kinetic parameters of MENT and cystatin A in the presence of various DNA constructs ranging between 18mers and 65mers measured, binding of serpins and cathepsin V to DNA indicated by gel mobility shift analysis, electrostatic potential of human cathepsins V and effect of dsDNA on cathepsin V fluorescence indicated
Homo sapiens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
N-benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarin 7-amide + H2O
mechanisms of interaction between serpins, human cathepsin V and DNA analyzed, kinetic constants for substrate cleavage in the presence and absence of cofactors determined, final concentrations of cathepsin V and ds65mer DNA at 0.1 and 10 nM, final substrate concentrations ranging from 5 to 200 microM in cathepsin V buffer
683662
Homo sapiens
N-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
presence of DNA reduces the turnover rate up to 50% indicating that the binding of DNA changes the active site of cathepsin V such that the enzyme interacts with peptide substrates differently
Homo sapiens
Other publictions for EC 3.4.22.43
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
753977
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The Alkyne moiety as a latent ...
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752678
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500
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2
2
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753117
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Homo sapiens
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175
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1
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1
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2
3
3
2
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753828
Huang
Exogenous cathepsin V protein ...
Homo sapiens
Int. J. Biochem. Cell Biol.
89
6-15
2017
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1
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4
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1
1
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752418
Naumnik
Endostatin and cathepsin-V in ...
Homo sapiens
Adv. Exp. Med. Biol.
833
55-61
2015
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4
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4
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2
2
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754753
Pribis
The HIV protease inhibitor sa ...
Homo sapiens
Mol. Med.
21
749-757
2015
-
1
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1
-
5
-
1
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1
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4
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2
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2
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1
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5
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1
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1
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2
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2
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1
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1
1
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732591
Wong
CTSL2 is a pro-apoptotic targe ...
Homo sapiens
Oncogene
33
1249-1257
2014
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1
2
2
1
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-
731213
McCarthy
-
Cathepsin L proteases of the p ...
Lepeophtheirus salmonis
Aquaculture
356-357
264-271
2012
-
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1
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1
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1
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-
731573
Skrzypczak
Expression of cysteine proteas ...
Homo sapiens
Cancer Invest.
30
398-403
2012
-
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-
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-
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2
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2
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2
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2
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1
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1
-
-
732049
Funkelstein
Human cathepsin V protease par ...
Homo sapiens
J. Biol. Chem.
287
15232-15241
2012
-
-
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1
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1
2
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3
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4
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5
1
2
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1
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1
2
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4
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5
1
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-
-
-
-
-
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1
1
-
-
-
732502
Keegan
Tumor necrosis factor alpha st ...
Homo sapiens
Mol. Cell. Biochem.
367
65-72
2012
-
-
-
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1
1
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2
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3
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1
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3
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1
1
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1
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1
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732867
Novinec
A simple and efficient protoco ...
Homo sapiens
Protein Expr. Purif.
82
1-5
2012
1
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1
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1
2
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1
1
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2
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1
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1
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1
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4
1
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2
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2
2
717159
Wilder
Manipulating substrate and pH ...
Homo sapiens
Arch. Biochem. Biophys.
516
52-57
2011
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1
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1
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2
1
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2
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1
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1
1
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1
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1
1
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1
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717374
Severino
Acridone alkaloids as potent i ...
Homo sapiens
Bioorg. Med. Chem.
19
1477-1481
2011
-
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1
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-
11
-
1
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2
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1
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1
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9
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11
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1
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11
11
9
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1
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1
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717375
Piovan
Structure-activity relationshi ...
Homo sapiens
Bioorg. Med. Chem.
19
2009-2014
2011
-
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6
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707590
Elie
Identification and pre-clinica ...
Homo sapiens
Biochimie
92
1618-1624
2010
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1
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1
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707591
Sevenich
Expression of human cathepsin ...
Homo sapiens
Biochimie
92
1674-1680
2010
-
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1
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1
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4
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4
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4
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1
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1
1
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707626
Coppini
Plasminogen hydrolysis by cath ...
Homo sapiens
Biol. Chem.
391
561-570
2010
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1
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1
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1
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1
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7
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1
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1
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1
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7
-
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-
6
6
709133
Renko
Versatile loops in mycocypins ...
Homo sapiens
J. Biol. Chem.
285
308-316
2010
-
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1
1
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2
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3
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2
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1
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1
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2
2
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707906
Cheng
The cystatin M/E-controlled pa ...
Homo sapiens
Br. J. Dermatol.
161
253-264
2009
-
-
-
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1
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3
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18
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2
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1
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18
-
-
-
-
-
-
-
-
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-
-
1
-
-
1
-
-
709405
Zeeuwen
The biology of cystatin M/E an ...
Homo sapiens
J. Invest. Dermatol.
129
1327-1338
2009
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1
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3
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3
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