BRENDA - Enzyme Database show
show all sequences of 3.4.21.7

The plasmin-antiplasmin system: structural and functional aspects

Schaller, J.; Gerber, S.S.; Cell. Mol. Life Sci. 68, 785-801 (2011)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
the main physiological activators of plasminogen are tissue-type plasminogen activator, which is mainly involved in the dissolution of the fibrin polymers by plasmin, and urokinase-type plasminogen activator, which is primarily responsible for the generation of plasmin activity in the intercellular space. Both activators are multidomain serine proteases
Homo sapiens
Inhibitors
Inhibitors
Commentary
Organism
Structure
alpha2-antiplasmin
the main physiological inhibitor and a serpin
Homo sapiens
alpha2-Macroglobulin
general protease inhibitor
Homo sapiens
histidine-rich glycoprotein
binds at sites of tissue injury and seems to act as a high-affinity receptor to immobilize plasminogen on cell surfaces
Homo sapiens
additional information
features and mode of action of plasmin inhibitors, detailed overview
Homo sapiens
neuroserpin
mainly expressed in the brain, a serpin and single-chain glycoprotein of 55 kDa containing three potential N-glycosylation sites at Asn141, Asn305, and Asn385
Homo sapiens
plasminogen activator inhibitors 1
-
Homo sapiens
plasminogen activator inhibitors 2
-
Homo sapiens
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
extracellular
-
Homo sapiens
-
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
88432
-
x * 90000, plasminogen, SDS-PAGE, x * 88432, plasminogen, sequence determination
Homo sapiens
90000
-
x * 90000, plasminogen, SDS-PAGE, x * 88432, plasminogen, sequence determination
Homo sapiens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
fibrin + H2O
Homo sapiens
-
soluble fibrin fragments
-
-
?
additional information
Homo sapiens
rather broad specificity of plasmin in vivo catalyzing the inactivation and degradation of matrix proteins such as collagens, fibronectin, and laminins, and components of the blood coagulation cascade such as coagulation factor FVa, von Willebrand factor, and thrombospondin
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
P00747
plasminogen; gene PLG
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
glycoprotein
the human plasminogen is partially N-glycosylated at Asn289 and O-glycosylated at Ser249 and Thr346 giving rise to plasminogen variants I (Asn289, Thr346) and II (only Thr346)
Homo sapiens
phosphoprotein
plasminogen is partially phosphorylated at Ser578
Homo sapiens
proteolytic modification
the main physiological activators of plasminogen are tissue-type plasminogen activator, which is mainly involved in the dissolution of the fibrin polymers by plasmin, and urokinase-type plasminogen activator, which is primarily responsible for the generation of plasmin activity in the intercellular space. Both activators are multidomain serine proteases. Pgn is activated by the two main physiological plasminogen activators to the active, two-chain plasmin molecule held together by two interchain disulfide bridges, Cys548-Cys666, Cys558-Cys566, by cleavage of the Arg561-Val562 peptide bond and the release of the 77-residue N-terminal peptide. Two N-terminally different forms of plasminogen exist, Glu-Pgn and Lys-Pgn. Lys-Pgn is formed by cleavage of the Lys77-Lys78 peptide bond in Glu-Pgn, releasing the N-terminal peptide
Homo sapiens
Source Tissue
Source Tissue
Commentary
Organism
Textmining
commercial preparation
-
Homo sapiens
-
plasma
in blood as zymogen plasminogen
Homo sapiens
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
fibrin + H2O
-
717469
Homo sapiens
soluble fibrin fragments
-
-
-
?
fibrin + H2O
cleavage of the Lys583-Met584 peptide bond in the Aalpha chain, followed by the cleavage of the peptide bonds Lys206-Met207 and Lys230-Ala231, also in the Aalpha chain, thus releasing a C-terminal 40-kDa fragment and generating fragment X possessing 260 kDa. Cleavage of fragment X in all three chains results in one fragment Y (160 kDa) and one fragment D (100 kDa), and further cleavage of fragment Y produces a second fragment D and fragment E (60 kDa)
717469
Homo sapiens
soluble fibrin fragments
-
-
-
?
additional information
rather broad specificity of plasmin in vivo catalyzing the inactivation and degradation of matrix proteins such as collagens, fibronectin, and laminins, and components of the blood coagulation cascade such as coagulation factor FVa, von Willebrand factor, and thrombospondin
717469
Homo sapiens
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 90000, plasminogen, SDS-PAGE, x * 88432, plasminogen, sequence determination
Homo sapiens
More
plasminogen is a single-chain, multidomain glycoprotein, and is composed of an N-terminal peptide, five triple-loop structures stabilized by three intrachain disulfide bridges called kringles, and the trypsin-like serine protease part carrying the catalytic triad His603, Asp646, and Ser741. Primary structure of human plasminogen, overview. The three-dimensional structural model of human plasminogen based on known and overlapping 3-D structures of plasminogen fragments exhibits a spiral shape
Homo sapiens
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
the main physiological activators of plasminogen are tissue-type plasminogen activator, which is mainly involved in the dissolution of the fibrin polymers by plasmin, and urokinase-type plasminogen activator, which is primarily responsible for the generation of plasmin activity in the intercellular space. Both activators are multidomain serine proteases
Homo sapiens
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
alpha2-antiplasmin
the main physiological inhibitor and a serpin
Homo sapiens
alpha2-Macroglobulin
general protease inhibitor
Homo sapiens
histidine-rich glycoprotein
binds at sites of tissue injury and seems to act as a high-affinity receptor to immobilize plasminogen on cell surfaces
Homo sapiens
additional information
features and mode of action of plasmin inhibitors, detailed overview
Homo sapiens
neuroserpin
mainly expressed in the brain, a serpin and single-chain glycoprotein of 55 kDa containing three potential N-glycosylation sites at Asn141, Asn305, and Asn385
Homo sapiens
plasminogen activator inhibitors 1
-
Homo sapiens
plasminogen activator inhibitors 2
-
Homo sapiens
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
extracellular
-
Homo sapiens
-
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
88432
-
x * 90000, plasminogen, SDS-PAGE, x * 88432, plasminogen, sequence determination
Homo sapiens
90000
-
x * 90000, plasminogen, SDS-PAGE, x * 88432, plasminogen, sequence determination
Homo sapiens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
fibrin + H2O
Homo sapiens
-
soluble fibrin fragments
-
-
?
additional information
Homo sapiens
rather broad specificity of plasmin in vivo catalyzing the inactivation and degradation of matrix proteins such as collagens, fibronectin, and laminins, and components of the blood coagulation cascade such as coagulation factor FVa, von Willebrand factor, and thrombospondin
?
-
-
-
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
glycoprotein
the human plasminogen is partially N-glycosylated at Asn289 and O-glycosylated at Ser249 and Thr346 giving rise to plasminogen variants I (Asn289, Thr346) and II (only Thr346)
Homo sapiens
phosphoprotein
plasminogen is partially phosphorylated at Ser578
Homo sapiens
proteolytic modification
the main physiological activators of plasminogen are tissue-type plasminogen activator, which is mainly involved in the dissolution of the fibrin polymers by plasmin, and urokinase-type plasminogen activator, which is primarily responsible for the generation of plasmin activity in the intercellular space. Both activators are multidomain serine proteases. Pgn is activated by the two main physiological plasminogen activators to the active, two-chain plasmin molecule held together by two interchain disulfide bridges, Cys548-Cys666, Cys558-Cys566, by cleavage of the Arg561-Val562 peptide bond and the release of the 77-residue N-terminal peptide. Two N-terminally different forms of plasminogen exist, Glu-Pgn and Lys-Pgn. Lys-Pgn is formed by cleavage of the Lys77-Lys78 peptide bond in Glu-Pgn, releasing the N-terminal peptide
Homo sapiens
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
commercial preparation
-
Homo sapiens
-
plasma
in blood as zymogen plasminogen
Homo sapiens
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
fibrin + H2O
-
717469
Homo sapiens
soluble fibrin fragments
-
-
-
?
fibrin + H2O
cleavage of the Lys583-Met584 peptide bond in the Aalpha chain, followed by the cleavage of the peptide bonds Lys206-Met207 and Lys230-Ala231, also in the Aalpha chain, thus releasing a C-terminal 40-kDa fragment and generating fragment X possessing 260 kDa. Cleavage of fragment X in all three chains results in one fragment Y (160 kDa) and one fragment D (100 kDa), and further cleavage of fragment Y produces a second fragment D and fragment E (60 kDa)
717469
Homo sapiens
soluble fibrin fragments
-
-
-
?
additional information
rather broad specificity of plasmin in vivo catalyzing the inactivation and degradation of matrix proteins such as collagens, fibronectin, and laminins, and components of the blood coagulation cascade such as coagulation factor FVa, von Willebrand factor, and thrombospondin
717469
Homo sapiens
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 90000, plasminogen, SDS-PAGE, x * 88432, plasminogen, sequence determination
Homo sapiens
More
plasminogen is a single-chain, multidomain glycoprotein, and is composed of an N-terminal peptide, five triple-loop structures stabilized by three intrachain disulfide bridges called kringles, and the trypsin-like serine protease part carrying the catalytic triad His603, Asp646, and Ser741. Primary structure of human plasminogen, overview. The three-dimensional structural model of human plasminogen based on known and overlapping 3-D structures of plasminogen fragments exhibits a spiral shape
Homo sapiens
General Information
General Information
Commentary
Organism
malfunction
Defects or mutations in the PLG gene are the cause of thrombophilia, a form of recurrent thrombosis, and type I plasminogen deficiency. Ligneous conjunctivitis is usually the most common and initial form of type I plasminogen deficiency and is a rare form of chronic conjunctivitis characterized by chronic tearing and redness of the conjunctivae
Homo sapiens
metabolism
besides the main physiological inhibitor alpha2-antiplasmin, the plasmin-antiplasmin system is also regulated by the general protease inhibitor alpha2-macroglobulin, a member of the protease inhibitor I39 family. The activity of the plasminogen activators is primarily regulated by the plasminogen activator inhibitors 1 and 2, members of the serine protease inhibitor superfamily
Homo sapiens
additional information
the catalytic triad is formed by His603, Asp646, and Ser741
Homo sapiens
physiological function
primary function of plasmin is the cleavage of insoluble fibrin polymers at specific sites resulting in soluble fragments. In addition, plasmin acts as a proteolytic factor in many other physiological processes such as mediation of cell migration by degrading the extracellular matrix, wound healing, tissue remodelling, angiogenesis, embryogenesis, and pathogen and tumour cell invasion. The plasmin-antiplasmin system plays a key role in blood coagulation and fibrinolysis. Plasmin and alpha2-antiplasmin are primarily responsible for a controlled and regulated dissolution of the fibrin polymers into soluble fragments
Homo sapiens
General Information (protein specific)
General Information
Commentary
Organism
malfunction
Defects or mutations in the PLG gene are the cause of thrombophilia, a form of recurrent thrombosis, and type I plasminogen deficiency. Ligneous conjunctivitis is usually the most common and initial form of type I plasminogen deficiency and is a rare form of chronic conjunctivitis characterized by chronic tearing and redness of the conjunctivae
Homo sapiens
metabolism
besides the main physiological inhibitor alpha2-antiplasmin, the plasmin-antiplasmin system is also regulated by the general protease inhibitor alpha2-macroglobulin, a member of the protease inhibitor I39 family. The activity of the plasminogen activators is primarily regulated by the plasminogen activator inhibitors 1 and 2, members of the serine protease inhibitor superfamily
Homo sapiens
additional information
the catalytic triad is formed by His603, Asp646, and Ser741
Homo sapiens
physiological function
primary function of plasmin is the cleavage of insoluble fibrin polymers at specific sites resulting in soluble fragments. In addition, plasmin acts as a proteolytic factor in many other physiological processes such as mediation of cell migration by degrading the extracellular matrix, wound healing, tissue remodelling, angiogenesis, embryogenesis, and pathogen and tumour cell invasion. The plasmin-antiplasmin system plays a key role in blood coagulation and fibrinolysis. Plasmin and alpha2-antiplasmin are primarily responsible for a controlled and regulated dissolution of the fibrin polymers into soluble fragments
Homo sapiens
Other publictions for EC 3.4.21.7
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
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)
731263
Alves
Comparative study on the inhib ...
Homo sapiens
Biochem. Biophys. Res. Commun.
457
358-362
2015
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5
2
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2
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732222
Farhat
TGF-beta1 suppresses plasmin a ...
Mus musculus
J. Cell. Physiol.
230
318-326
2015
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2
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732405
Foley
Interplay between fibrinolysis ...
Homo sapiens
J. Thromb. Haemost.
13
610-618
2015
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1
1
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731322
Varju
Fractal kinetic behavior of pl ...
Homo sapiens
Biochemistry
53
6348-6356
2014
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732904
Briassouli
A central role of plasmin in c ...
Homo sapiens
Rheumatology
52
1448-1453
2013
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1
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1
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731653
Swedberg
Natural and engineered plasmin ...
Homo sapiens
ChemBioChem
13
336-348
2012
1
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25
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7
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9
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25
22
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9
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731900
Buhl
Urinary plasmin activates coll ...
Homo sapiens
Hypertension
60
1346-1351
2012
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732241
Gohda
Predicting subsite interaction ...
Homo sapiens
J. Enzyme Inhib. Med. Chem.
27
571-577
2012
2
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732706
Koch
Staphylococcus aureus proteins ...
Homo sapiens
PLoS ONE
7
e47638
2012
3
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717069
Sulniute
Plasmin is essential in preven ...
Mus musculus
Am. J. Pathol.
179
819-828
2011
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717259
Swedberg
Plasmin substrate binding site ...
Homo sapiens
Biochemistry
50
8454-8462
2011
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1
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3
1
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13
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13
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1
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717355
Teno
Identification of novel plasmi ...
Homo sapiens
Bioorg. Med. Chem. Lett.
21
6305-6309
2011
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10
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717386
Venkatraman
Steady states and dynamics of ...
Homo sapiens
Biophys. J.
101
1825-1834
2011
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717417
Arkebauer
Carbon monoxide and nitric oxi ...
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Blood Coagul. Fibrinolysis
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712-719
2011
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Schaller
The plasmin-antiplasmin system ...
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Cell. Mol. Life Sci.
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2011
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717604
Dahiya
Intermolecular interactions in ...
Homo sapiens
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717666
Aaltonen
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Effect of microfiltration of m ...
Bos taurus
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2011
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717845
Okunishi
Plasmin overcomes resistance t ...
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2011
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717866
Kanno
Plasminogen/plasmin modulates ...
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2011
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Gohda
Predicting subsite interaction ...
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2011
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718272
Li
Plasmin plays an essential rol ...
Homo sapiens, Mus musculus
PLoS ONE
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2011
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2
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718277
Chung
Bacillus anthracis interacts w ...
Homo sapiens
PLoS ONE
6
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2011
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708063
Gerber
The human alpha(2)-plasmin inh ...
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2010
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708672
Koizumi
Inhibition of proteases involv ...
Homo sapiens
Hum. Reprod.
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2010
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Christensen
Osteopontin is cleaved at mult ...
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717165
Li
Plasmin triggers chemotaxis of ...
Homo sapiens
Arterioscler. Thromb. Vasc. Biol.
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2010
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717216
Doeuvre
Plasmin on adherent cells: fro ...
Homo sapiens
Biochem. J.
432
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2010
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718043
Feys
Inactivation of ADAMTS13 by pl ...
Homo sapiens
J. Thromb. Haemost.
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2010
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718070
Martinez-Rizo
Plasmin plays a key role in th ...
Homo sapiens
Liver Int.
30
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2010
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695548
Ohtsuka
Electrochemical assay of plasm ...
Homo sapiens
Anal. Biochem.
385
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2009
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697026
Flight
Textilinin-1, an alternative a ...
Mus musculus
Br. J. Haematol.
145
207-211
2009
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697405
Potier
Cutaneous manifestations in Hy ...
Homo sapiens
Clin. Exp. Allergy
39
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2009
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698137
Hermel
Effect of intravitreal plasmin ...
Homo sapiens
Graefes Arch. Clin. Exp. Ophthalmol.
247
331-334
2009
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698446
Bonadonna
Clonal mast cell disorders in ...
Homo sapiens
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2009
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698888
Yuan
The serine protease plasmin cl ...
Homo sapiens
J. Biol. Chem.
284
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2009
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699867
Kothari
Plasmin enhances cell surface ...
Homo sapiens
J. Thromb. Haemost.
7
121-131
2009
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Miah
Functional analysis of mutant ...
Homo sapiens
J. Thromb. Haemost.
7
665-672
2009
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700313
Zhang
Estrogen-induced uterine abnor ...
Mus musculus
Mol. Reprod. Dev.
76
160-172
2009
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701187
Zhi-Liang
Pharmacologic vitreolysis with ...
Rattus norvegicus
Retina (Philadelphia, Pa.)
29
269-274
2009
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707135
Head
Inhibition of p75 neurotrophin ...
Mus musculus
Anesthesiology
110
813-825
2009
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707847
Nakagawa
Nicked beta2-glycoprotein I bi ...
Homo sapiens
Blood
114
2553-2559
2009
-
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707930
Maeda
Characteristic response of ast ...
Rattus norvegicus
Brain Res.
1305
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2009
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708474
Millers
Crystal structure of textilini ...
Homo sapiens
FEBS J.
276
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2009
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709033
Pedroja
Plasminogen activator inhibito ...
Mus musculus
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284
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2009
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Expression, purification and c ...
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65
238-243
2009
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1
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685399
Nogami
Identification of a plasmin-in ...
Homo sapiens
Biochim. Biophys. Acta
1784
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2008
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685923
Erbas
Breast cyst fluid plasmin acti ...
Homo sapiens
Cancer Invest.
26
22-27
2008
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1
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686420
Biswas
Proteolytic cleavage of human ...
Homo sapiens
Endocrinology
149
749-757
2008
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686689
Tanka-Salamon
Suppressed catalytic efficienc ...
synthetic construct
FEBS J.
275
1274-1282
2008
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1
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686775
Gray
Activation of pro-BDNF by the ...
Homo sapiens
FEBS Lett.
582
907-910
2008
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687206
Lei
Plasmin is the major protease ...
Homo sapiens, Oryctolagus cuniculus
Invest. Ophthalmol. Vis. Sci.
49
42-48
2008
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695428
Paczek
Trypsin, elastase, plasmin and ...
Homo sapiens
Age Ageing
37
318-323
2008
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695935
Brazon
Discreplasminin, a plasmin inh ...
Homo sapiens
Arch. Toxicol.
83
669-678
2008
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1
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4
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695957
Guo
Protective effects of plasmin( ...
Homo sapiens
Arthritis Rheum.
58
764-772
2008
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1
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6
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-
696130
Kamio
Plasmin is involved in inflamm ...
Homo sapiens
Biochem. Pharmacol.
75
1974-1980
2008
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-
696940
Tjwa
Plasmin therapy enhances mobil ...
Mus musculus
Blood
112
4048-4050
2008
-
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1
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1
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-
697079
Hou
Annexin A2 regulates the level ...
Mus musculus
Cancer Invest.
26
809-815
2008
-
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1
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-
-
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-
-
-
697407
Heide
Serum tryptase and SCORMA (SCO ...
Homo sapiens
Clin. Exp. Dermatol.
34
462-468
2008
-
1
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1
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-
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-
698139
Marcinkiewicz
A role for plasmin in platelet ...
Homo sapiens
Growth Horm. IGF Res.
18
325-334
2008
-
-
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1
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1
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1
-
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-
-
-
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-
-
-
-
-
-
-
-
-
698248
Attali
The interaction of Streptococc ...
Homo sapiens
Infect. Immun.
76
5350-5356
2008
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1
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3
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2
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2
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-
-
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-
-
-
-
-
-
-
-
-
698291
Kucharewicz
Plasmin system regulation in a ...
Rattus norvegicus
Int. Arch. Allergy Immunol.
147
190-196
2008
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1
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-
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4
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-
-
-
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-
-
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-
698776
Mannaioni
Plasmin potentiates synaptic N ...
Mus musculus
J. Biol. Chem.
283
20600-20611
2008
-
-
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1
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2
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3
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1
-
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-
-
-
-
-
-
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-
698862
Passero
Plasmin activates epithelial N ...
Bos taurus
J. Biol. Chem.
283
36586-36591
2008
-
-
-
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-
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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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1
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1
-
-
-
-
-
-
-
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-
-
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699204
Dalsgaard
Plasmin digestion of photooxid ...
Bos taurus
J. Dairy Sci.
91
2175-2183
2008
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1
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1
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1
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6
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1
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1
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-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
701162
Papanikolaou
Effect of plasmin, plasminogen ...
Bos taurus
Reprod. Fertil. Dev.
20
320-327
2008
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1
-
-
-
-
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2
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2
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1
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2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
701279
Hunt
Simplified recombinant plasmin ...
Homo sapiens
Thromb. Haemost.
100
413-419
2008
-
1
1
-
1
-
2
2
-
-
-
-
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3
-
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-
-
-
-
1
-
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2
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1
1
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1
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2
-
2
-
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-
-
-
-
-
1
-
-
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-
2
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-
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701290
Novokhatny
Structure and activity of plas ...
Homo sapiens
Thromb. Res.
122
S3-S8
2008
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1
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-
-
-
-
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4
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-
-
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-
1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
684328
Cosgrove
A complex, tissue-specific rol ...
Mus musculus
Am. J. Physiol.
293
F10-F11
2007
-
1
-
-
-
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1
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-
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1
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1
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4
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1
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1
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1
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
684778
Li
Plasmin triggers cytokine indu ...
Homo sapiens
Arterioscler. Thromb. Vasc. Biol.
27
1383-1389
2007
-
1
-
-
-
-
4
-
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-
-
-
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2
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-
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2
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9
-
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-
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-
-
-
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-
1
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4
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2
-
-
9
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
684784
Fujiyoshi
Plasmin Induces Endothelium-De ...
Homo sapiens, Sus scrofa
Arterioscler. Thromb. Vasc. Biol.
27
949-954
2007
-
1
-
-
-
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5
-
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4
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3
-
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1
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5
-
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3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
685347
Kawao
Plasmin decreases the BH3-only ...
Homo sapiens
Biochim. Biophys. Acta
1773
718-727
2007
1
1
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5
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2
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1
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1
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1
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
685797
Nielsen
Hydroxyethyl starch enhances f ...
Homo sapiens
Blood Coagul. Fibrinolysis
18
647-656
2007
-
-
-
-
-
-
2
-
-
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1
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1
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
687666
Nogami
Mechanisms of plasmin-catalyze ...
Homo sapiens
J. Biol. Chem.
282
5287-5295
2007
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1
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1
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1
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1
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1
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-
-
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-
-
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-
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-
688153
Zhang
Urokinase-type plasminogen act ...
Homo sapiens
J. Immunol.
179
3297-3304
2007
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1
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1
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2
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668502
Diaz
Requirement of the enzymatic a ...
Homo sapiens
Exp. Cell Res.
312
2203-2213
2006
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668957
Huppertz
-
Inhibition of the proteolytic ...
Bos taurus
Int. dairy J.
16
691-696
2006
1
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670064
Drinane
Plasminogen and plasmin activi ...
Homo sapiens
J. Thromb. Haemost.
4
1288-1295
2006
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1
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684824
Ward
Potentiation of TLR4 signallin ...
synthetic construct
Biochem. Biophys. Res. Commun.
341
299-303
2006
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1
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2
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685071
Doolittle
Binding of synthetic B knobs t ...
Homo sapiens
Biochemistry
45
2657-2667
2006
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2
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2
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685074
Schaefer
Incorporation of fragment X in ...
Homo sapiens
Biochemistry
45
4257-4265
2006
1
1
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4
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685510
Xue
Structure-activity studies of ...
synthetic construct
Bioorg. Med. Chem.
14
8467-8487
2006
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18
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688737
Huang
Noninhibitory PAI-1 enhances p ...
Rattus norvegicus
Kidney Int.
70
515-522
2006
-
1
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5
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688780
Ishida
Matrix metalloproteinase-1 act ...
Homo sapiens
Lung
184
15-19
2006
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1
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667503
Quagraine
Plasmin alters the activity an ...
Homo sapiens
Biochem. J.
388
81-91
2005
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1
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668067
Crawley
Proteolytic inactivation of AD ...
Homo sapiens
Blood
105
1085-1093
2005
-
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2
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668955
Crudden
-
Kinetic studies of the thermal ...
Bos taurus
Int. Dairy J.
15
1245-1253
2005
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669641
Crudden
Kinetics of changes in plasmin ...
Bos taurus
J. Dairy Res.
72
493-504
2005
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1
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1
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669645
Frohbieter
Effects of Pseudomonas fluores ...
Bos taurus
J. Dairy Sci.
88
3392-3401
2005
-
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4
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1
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1
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1
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-
-
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-
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-
650808
Syrovets
Novel aspects and new roles fo ...
Homo sapiens
Cell. Mol. Life Sci.
61
873-885
2004
-
-
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3
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1
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1
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-
667544
Huet
Inhibition of plasmin-mediated ...
Homo sapiens
Biochem. Pharmacol.
67
643-654
2004
-
-
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5
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1
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668903
Bergmann
Characterization of plasmin(og ...
Homo sapiens
Indian J. Med. Res.
119 Suppl
29-32
2004
-
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2
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6
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669210
Schneider
Activated thrombin-activatable ...
Homo sapiens
J. Biol. Chem.
279
13340-13345
2004
-
-
-
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1
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1
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1
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1
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-
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669643
Borda
High pressure thermal inactiva ...
Bos taurus
J. Dairy Sci.
87
2351-2358
2004
-
-
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1
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1
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1
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1
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1
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-
-
-
-
-
-
-
-
670233
Nowak
Peroxynitrite and fibrinolytic ...
Homo sapiens
Mol. Cell. Biochem.
267
141-146
2004
-
-
-
-
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1
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1
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1
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2
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1
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1
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-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
650209
Mitsudo
Inhibition of serine proteinas ...
Homo sapiens
Biochemistry
42
3874-3881
2003
-
-
-
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-
-
1
-
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-
-
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2
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1
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1
1
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-
-
-
-
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-
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-
-
-
-
-
-
-
-
650728
Ries
Influence of soluble fibrin on ...
Homo sapiens
Blood Coagul. Fibrinolysis
14
203-209
2003
-
-
-
-
-
-
1
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1
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1
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1
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-
-
-
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-
-
-
-
-
-
-
-
-
653426
Midura-Nowaczek
Synthesis of benzylamides of d ...
Homo sapiens
Pharmazie
58
687-689
2003
-
-
-
-
-
-
4
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1
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2
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2
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-
-
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-
-
-
-
-
650727
Brown
The reaction between plasmin a ...
Homo sapiens
Blood Coagul. Fibrinolysis
13
711-714
2002
-
-
-
-
-
-
1
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-
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1
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2
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1
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-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
651314
Lauer
Generation of a novel proteoly ...
Homo sapiens
FEBS Lett.
531
309-313
2002
-
-
-
-
-
-
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1
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2
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2
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-
652995
Abato
Inhibitors of plasmin that ext ...
Homo sapiens
J. Org. Chem.
67
1184-1191
2002
-
-
-
-
-
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2
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1
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2
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2
2
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
652141
Jiang
Proteolytic cleavage of chromo ...
Homo sapiens
J. Biol. Chem.
276
25022-25029
2001
-
-
-
-
-
-
-
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1
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1
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2
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1
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-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
652679
Vakili
Urokinase plasminogen activato ...
Homo sapiens
J. Immunol.
167
3406-3413
2001
-
-
-
-
-
-
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1
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1
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2
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-
-
-
-
-
3
-
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-
-
1
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-
-
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-
1
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-
1
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-
-
-
-
-
3
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
653359
Exley
Plasmin cleaves Abeta42 in vit ...
Homo sapiens
Neuroreport
12
2967-2970
2001
-
-
-
-
-
-
-
-
-
-
-
-
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1
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1
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-
-
1
-
-
-
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-
-
-
-
-
-
-
-
653880
Hseu
Inhibition of human plasmin ac ...
Homo sapiens
Sci. Total Environ.
273
93-99
2001
-
-
-
-
-
-
2
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4
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2
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
649912
Fitzpatrick
Regulation of plasmin activity ...
Homo sapiens
Biochemistry
39
1021-1028
2000
-
-
-
-
-
-
1
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2
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