Page last updated: 2024-08-07 15:32:29
Plasminogen
A plasminogen that is encoded in the genome of human. [PRO:DNx, UniProtKB:P00747]
Synonyms
EC 3.4.21.7
Research
Bioassay Publications (43)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 1 (2.33) | 18.7374 |
| 1990's | 6 (13.95) | 18.2507 |
| 2000's | 22 (51.16) | 29.6817 |
| 2010's | 13 (30.23) | 24.3611 |
| 2020's | 1 (2.33) | 2.80 |
Compounds (41)
Drugs with Inhibition Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| aminocaproic acid | Homo sapiens (human) | IC50 | 105.0000 | 1 | 1 |
| aminocaproic acid | Homo sapiens (human) | Ki | 53,000.0000 | 1 | 1 |
| 5-(n,n-hexamethylene)amiloride | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| bis(5-amidino-2-benzimidazolyl)methane | Homo sapiens (human) | IC50 | 26.0000 | 1 | 1 |
| bis(5-amidino-2-benzimidazolyl)methane | Homo sapiens (human) | Ki | 2.4750 | 2 | 2 |
| gabexate | Homo sapiens (human) | IC50 | 0.4310 | 1 | 1 |
| gabexate | Homo sapiens (human) | Ki | 1.9000 | 1 | 1 |
| nafamostat | Homo sapiens (human) | IC50 | 2.9000 | 1 | 1 |
| nafamostat | Homo sapiens (human) | Ki | 0.4100 | 1 | 1 |
| netropsin | Homo sapiens (human) | IC50 | 35.0000 | 1 | 2 |
| pentamidine | Homo sapiens (human) | IC50 | 28.4000 | 3 | 5 |
| tranexamic acid | Homo sapiens (human) | IC50 | 2,414.7000 | 5 | 5 |
| tranexamic acid | Homo sapiens (human) | Ki | 32,500.0000 | 2 | 2 |
| phenylguanidine | Homo sapiens (human) | Ki | 2,610.0000 | 1 | 1 |
| amiloride | Homo sapiens (human) | IC50 | 93.9933 | 3 | 3 |
| leupeptin | Homo sapiens (human) | IC50 | 1.2000 | 1 | 1 |
| mci 9038 | Homo sapiens (human) | Ki | 257.0000 | 1 | 1 |
| dx 9065 | Homo sapiens (human) | Ki | 23.0000 | 1 | 1 |
| efegatran | Homo sapiens (human) | IC50 | 0.3083 | 3 | 3 |
| 5-amidinoindole | Homo sapiens (human) | Ki | 112.0000 | 1 | 1 |
| 5-(4-piperidyl)isoxazol-3-ol | Homo sapiens (human) | IC50 | 2.8000 | 2 | 2 |
| ono 3307 | Homo sapiens (human) | Ki | 0.3100 | 1 | 1 |
| 4-guanidinobenzoate | Homo sapiens (human) | Ki | 10,000.0000 | 1 | 1 |
| melagatran | Homo sapiens (human) | IC50 | 3.0600 | 1 | 2 |
| melagatran | Homo sapiens (human) | Ki | 1.2500 | 2 | 2 |
| pefabloc | Homo sapiens (human) | IC50 | 240.0000 | 1 | 1 |
| beta-naphthamidine | Homo sapiens (human) | Ki | 51.1500 | 2 | 2 |
| razaxaban | Homo sapiens (human) | Ki | 8.6500 | 4 | 4 |
| dabigatran | Homo sapiens (human) | Ki | 1.6950 | 1 | 1 |
| benzamidine | Homo sapiens (human) | Ki | 237.5000 | 1 | 2 |
| 2-(4-chlorophenyl)guanidine | Homo sapiens (human) | Ki | 5,025.0000 | 2 | 2 |
| telaprevir | Homo sapiens (human) | IC50 | 8.7000 | 1 | 1 |
| 3,7-dimethoxy-5,3',4'-trihydroxyflavone | Homo sapiens (human) | IC50 | 1.5000 | 1 | 1 |
| hydroxygenkwanin | Homo sapiens (human) | IC50 | 2.3000 | 1 | 1 |
| bms 740808 | Homo sapiens (human) | Ki | 2.8000 | 1 | 1 |
| uk-356,202 | Homo sapiens (human) | Ki | 0.0170 | 1 | 1 |
| n-alpha-(2,4,6-triisopropyl-phenylsulfonyl)-3-amidino-(l)-phenyl-alanine-4-ethoxycarbonyl-piperazide hydrochloride | Homo sapiens (human) | Ki | 0.5600 | 4 | 8 |
| gw 813893 | Homo sapiens (human) | IC50 | 158.0000 | 1 | 1 |
| lb 30057 | Homo sapiens (human) | Ki | 47.9000 | 1 | 1 |
| a-317567 | Homo sapiens (human) | Ki | 1.3020 | 1 | 1 |
| betrixaban | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| rpr 120844 | Homo sapiens (human) | Ki | 4.4000 | 1 | 1 |
| n-(3-amino-1-(cyclobutylmethyl)-2,3-dioxopropyl)-3-(2-((((1,1-dimethylethyl)amino)carbonyl)amino)-3,3-dimethyl-1-oxobutyl)-6,6-dimethyl-3-azabicyclo(3.1.0)hexan-2-carboxamide | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
| m-chlorophenylguanidine | Homo sapiens (human) | Ki | 10,000.0000 | 1 | 1 |
| mk-7009 | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
| grassystatin a | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| rpx7009 | Homo sapiens (human) | IC50 | 1,000.0000 | 1 | 1 |
Drugs with Activation Measurements
Drugs with Other Measurements
Fibrinolysis Inhibitors: Potential Drugs for the Treatment and Prevention of Bleeding.Journal of medicinal chemistry, , 02-27, Volume: 63, Issue:4, 2020
Discovery of the Fibrinolysis Inhibitor AZD6564, Acting via Interference of a Protein-Protein Interaction.ACS medicinal chemistry letters, , May-08, Volume: 5, Issue:5, 2014
Selective urokinase-type plasminogen activator inhibitors. 4. 1-(7-sulfonamidoisoquinolinyl)guanidines.Journal of medicinal chemistry, , May-17, Volume: 50, Issue:10, 2007
Synthesis and evaluation of 4-substituted benzylamine derivatives as beta-tryptase inhibitors.Bioorganic & medicinal chemistry letters, , Jun-01, Volume: 16, Issue:11, 2006
Aromatic amidines: comparison of their ability to block respiratory syncytial virus induced cell fusion and to inhibit plasmin, urokinase, thrombin, and trypsin.Journal of medicinal chemistry, , Volume: 26, Issue:2, 1983
Fibrinolysis Inhibitors: Potential Drugs for the Treatment and Prevention of Bleeding.Journal of medicinal chemistry, , 02-27, Volume: 63, Issue:4, 2020
Discovery and SAR of Novel and Selective Inhibitors of Urokinase Plasminogen Activator (uPA) with an Imidazo[1,2-a]pyridine Scaffold.Journal of medicinal chemistry, , Dec-10, Volume: 58, Issue:23, 2015
Fibrinolysis Inhibitors: Potential Drugs for the Treatment and Prevention of Bleeding.Journal of medicinal chemistry, , 02-27, Volume: 63, Issue:4, 2020
Protease inhibitors: current status and future prospects.Journal of medicinal chemistry, , Feb-10, Volume: 43, Issue:3, 2000
Fibrinolysis Inhibitors: Potential Drugs for the Treatment and Prevention of Bleeding.Journal of medicinal chemistry, , 02-27, Volume: 63, Issue:4, 2020
Active site-directed plasmin inhibitors: Extension on the P2 residue.Bioorganic & medicinal chemistry, , Feb-15, Volume: 24, Issue:4, 2016
Inhibitors of melanogenesis in B16 melanoma 4A5 cells from flower buds of Lawsonia inermis (Henna).Bioorganic & medicinal chemistry letters, , Jul-01, Volume: 25, Issue:13, 2015
Discovery of the Fibrinolysis Inhibitor AZD6564, Acting via Interference of a Protein-Protein Interaction.ACS medicinal chemistry letters, , May-08, Volume: 5, Issue:5, 2014
Potent fibrinolysis inhibitor discovered by shape and electrostatic complementarity to the drug tranexamic acid.Journal of medicinal chemistry, , Apr-25, Volume: 56, Issue:8, 2013
6-Substituted amiloride derivatives as inhibitors of the urokinase-type plasminogen activator for use in metastatic disease.Bioorganic & medicinal chemistry letters, , 12-15, Volume: 29, Issue:24, 2019
Discovery and SAR of Novel and Selective Inhibitors of Urokinase Plasminogen Activator (uPA) with an Imidazo[1,2-a]pyridine Scaffold.Journal of medicinal chemistry, , Dec-10, Volume: 58, Issue:23, 2015
2-Amidino analogs of glycine-amiloride conjugates: inhibitors of urokinase-type plasminogen activator.Bioorganic & medicinal chemistry letters, , Apr-01, Volume: 22, Issue:7, 2012
Discovery of N-[(1R,2S,5S)-2-{[(5-chloroindol-2-yl)carbonyl]amino}-5-(dimethylcarbamoyl)cyclohexyl]-5-methyl-4,5,6,7-tetrahydrothiazolo[5,4-c]pyridine-2-carboxamide hydrochloride: a novel, potent and orally active direct inhibitor of factor Xa.Bioorganic & medicinal chemistry, , Feb-01, Volume: 17, Issue:3, 2009
Retro-binding thrombin active site inhibitors: identification of an orally active inhibitor of thrombin catalytic activity.Bioorganic & medicinal chemistry letters, , Nov-04, Volume: 12, Issue:21, 2002
Structure-activity study of tripeptide thrombin inhibitors using alpha-alkyl amino acids and other conformationally constrained amino acid substitutions.Journal of medicinal chemistry, , Oct-27, Volume: 38, Issue:22, 1995
Retro-binding tripeptide thrombin active-site inhibitors: discovery, synthesis, and molecular modeling.Journal of medicinal chemistry, , Jul-08, Volume: 37, Issue:14, 1994
Discovery of the Fibrinolysis Inhibitor AZD6564, Acting via Interference of a Protein-Protein Interaction.ACS medicinal chemistry letters, , May-08, Volume: 5, Issue:5, 2014
Potent fibrinolysis inhibitor discovered by shape and electrostatic complementarity to the drug tranexamic acid.Journal of medicinal chemistry, , Apr-25, Volume: 56, Issue:8, 2013
Fibrinolysis Inhibitors: Potential Drugs for the Treatment and Prevention of Bleeding.Journal of medicinal chemistry, , 02-27, Volume: 63, Issue:4, 2020
Antithrombotic effects of LB30870, a potent, orally active, selective and direct thrombin inhibitor, and pharmacokinetics of its prodrug.Bioorganic & medicinal chemistry letters, , Sep-01, Volume: 23, Issue:17, 2013
Orally active thrombin inhibitors. Part 1: optimization of the P1-moiety.Bioorganic & medicinal chemistry letters, , May-15, Volume: 16, Issue:10, 2006
Orally active thrombin inhibitors. Part 2: optimization of the P2-moiety.Bioorganic & medicinal chemistry letters, , May-15, Volume: 16, Issue:10, 2006
Interaction with the S1 beta-pocket of urokinase: 8-heterocycle substituted and 6,8-disubstituted 2-naphthamidine urokinase inhibitors.Bioorganic & medicinal chemistry letters, , Jun-21, Volume: 14, Issue:12, 2004
Identification of novel binding interactions in the development of potent, selective 2-naphthamidine inhibitors of urokinase. Synthesis, structural analysis, and SAR of N-phenyl amide 6-substitution.Journal of medicinal chemistry, , Jan-15, Volume: 47, Issue:2, 2004
Structure-activity relationship and pharmacokinetic profile of 5-ketopyrazole factor Xa inhibitors.Bioorganic & medicinal chemistry letters, , Jan-15, Volume: 18, Issue:2, 2008
Aminobenzisoxazoles with biaryl P4 moieties as potent, selective, and orally bioavailable factor Xa inhibitors.Bioorganic & medicinal chemistry letters, , Apr-01, Volume: 16, Issue:7, 2006
1-[3-Aminobenzisoxazol-5'-yl]-3-trifluoromethyl-6-[2'-(3-(R)-hydroxy-N-pyrrolidinyl)methyl-[1,1']-biphen-4-yl]-1,4,5,6-tetrahydropyrazolo-[3,4-c]-pyridin-7-one (BMS-740808) a highly potent, selective, efficacious, and orally bioavailable inhibitor of blooBioorganic & medicinal chemistry letters, , Aug-01, Volume: 16, Issue:15, 2006
Discovery of potent, efficacious, and orally bioavailable inhibitors of blood coagulation factor Xa with neutral P1 moieties.Bioorganic & medicinal chemistry letters, , Nov-01, Volume: 16, Issue:21, 2006
1-[3-Aminobenzisoxazol-5'-yl]-3-trifluoromethyl-6-[2'-(3-(R)-hydroxy-N-pyrrolidinyl)methyl-[1,1']-biphen-4-yl]-1,4,5,6-tetrahydropyrazolo-[3,4-c]-pyridin-7-one (BMS-740808) a highly potent, selective, efficacious, and orally bioavailable inhibitor of blooBioorganic & medicinal chemistry letters, , Aug-01, Volume: 16, Issue:15, 2006
Fibrinolysis Inhibitors: Potential Drugs for the Treatment and Prevention of Bleeding.Journal of medicinal chemistry, , 02-27, Volume: 63, Issue:4, 2020
Secondary amides of sulfonylated 3-amidinophenylalanine. New potent and selective inhibitors of matriptase.Journal of medicinal chemistry, , Jul-13, Volume: 49, Issue:14, 2006
3-Amidinophenylalanine-based inhibitors of urokinase.Bioorganic & medicinal chemistry letters, , Nov-01, Volume: 9, Issue:21, 1999
Discovery of betrixaban (PRT054021), N-(5-chloropyridin-2-yl)-2-(4-(N,N-dimethylcarbamimidoyl)benzamido)-5-methoxybenzamide, a highly potent, selective, and orally efficacious factor Xa inhibitor.Bioorganic & medicinal chemistry letters, , Apr-15, Volume: 19, Issue:8, 2009
Enables
This protein enables 12 target(s):
| Target | Category | Definition |
|---|
| protease binding | molecular function | Binding to a protease or a peptidase. [GOC:hjd] |
| endopeptidase activity | molecular function | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain. [http://merops.sanger.ac.uk/about/glossary.htm#ENDOPEPTIDASE] |
| serine-type endopeptidase activity | molecular function | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE] |
| signaling receptor binding | molecular function | Binding to one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function. [GOC:bf, GOC:ceb, ISBN:0198506732] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| serine-type peptidase activity | molecular function | Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). [https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE] |
| enzyme binding | molecular function | Binding to an enzyme, a protein with catalytic activity. [GOC:jl] |
| kinase binding | molecular function | Binding to a kinase, any enzyme that catalyzes the transfer of a phosphate group. [GOC:jl] |
| protein domain specific binding | molecular function | Binding to a specific domain of a protein. [GOC:go_curators] |
| apolipoprotein binding | molecular function | Binding to an apolipoprotein, the protein component of a lipoprotein complex. [GOC:BHF, GOC:rl] |
| protein-folding chaperone binding | molecular function | Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport. [PMID:10585443] |
| protein antigen binding | molecular function | Binding to a protein antigen. [PMID:9360996] |
Located In
This protein is located in 11 target(s):
| Target | Category | Definition |
|---|
| extracellular region | cellular component | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. [GOC:go_curators] |
| extracellular space | cellular component | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. [ISBN:0198547684] |
| plasma membrane | cellular component | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. [ISBN:0716731363] |
| external side of plasma membrane | cellular component | The leaflet of the plasma membrane that faces away from the cytoplasm and any proteins embedded or anchored in it or attached to its surface. [GOC:dos, GOC:tb] |
| cell surface | cellular component | The external part of the cell wall and/or plasma membrane. [GOC:jl, GOC:mtg_sensu, GOC:sm] |
| platelet alpha granule lumen | cellular component | The volume enclosed by the membrane of the platelet alpha granule. [GOC:mah, PMID:8467233] |
| collagen-containing extracellular matrix | cellular component | An extracellular matrix consisting mainly of proteins (especially collagen) and glycosaminoglycans (mostly as proteoglycans) that provides not only essential physical scaffolding for the cellular constituents but can also initiate crucial biochemical and biomechanical cues required for tissue morphogenesis, differentiation and homeostasis. The components are secreted by cells in the vicinity and form a sheet underlying or overlying cells such as endothelial and epithelial cells. [GOC:BHF, GOC:rph, PMID:21123617] |
| extracellular exosome | cellular component | A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894] |
| blood microparticle | cellular component | A phospholipid microvesicle that is derived from any of several cell types, such as platelets, blood cells, endothelial cells, or others, and contains membrane receptors as well as other proteins characteristic of the parental cell. Microparticles are heterogeneous in size, and are characterized as microvesicles free of nucleic acids. [GOC:BHF, GOC:mah, PMID:16373184] |
| Schaffer collateral - CA1 synapse | cellular component | A synapse between the Schaffer collateral axon of a CA3 pyramidal cell and a CA1 pyramidal cell. [PMID:16399689] |
| glutamatergic synapse | cellular component | A synapse that uses glutamate as a neurotransmitter. [GOC:dos] |
Active In
This protein is active in 1 target(s):
| Target | Category | Definition |
|---|
| extracellular space | cellular component | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. [ISBN:0198547684] |
Involved In
This protein is involved in 19 target(s):
| Target | Category | Definition |
|---|
| proteolysis | biological process | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. [GOC:bf, GOC:mah] |
| blood coagulation | biological process | The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers. [PMID:30700128] |
| negative regulation of cell population proliferation | biological process | Any process that stops, prevents or reduces the rate or extent of cell proliferation. [GOC:go_curators] |
| negative regulation of cell-substrate adhesion | biological process | Any process that decreases the frequency, rate or extent of cell-substrate adhesion. Cell-substrate adhesion is the attachment of a cell to the underlying substrate via adhesion molecules. [GOC:dph, GOC:pf, GOC:tb] |
| extracellular matrix disassembly | biological process | A process that results in the breakdown of the extracellular matrix. [GOC:jid] |
| tissue regeneration | biological process | The regrowth of lost or destroyed tissues. [GOC:curators] |
| fibrinolysis | biological process | A process that solubilizes fibrin in the bloodstream of a multicellular organism, chiefly by the proteolytic action of plasmin. [GOC:jl, PMID:15842654] |
| positive regulation of blood vessel endothelial cell migration | biological process | Any process that activates or increases the frequency, rate or extent of the migration of the endothelial cells of blood vessels. [GOC:go_curators] |
| myoblast differentiation | biological process | The process in which a relatively unspecialized cell acquires specialized features of a myoblast. A myoblast is a mononucleate cell type that, by fusion with other myoblasts, gives rise to the myotubes that eventually develop into striated muscle fibers. [CL:0000056, GOC:go_curators, GOC:mtg_muscle] |
| muscle cell cellular homeostasis | biological process | The cellular homeostatic process that preserves a muscle cell in a stable functional or structural state. [GOC:mah, PMID:3091429, PMID:7781901] |
| tissue remodeling | biological process | The reorganization or renovation of existing tissues. This process can either change the characteristics of a tissue such as in blood vessel remodeling, or result in the dynamic equilibrium of a tissue such as in bone remodeling. [GOC:ebc] |
| biological process involved in interaction with symbiont | biological process | An interaction between two organisms living together in more or less intimate association. The term symbiont is used for the smaller (macro) of the two members of a symbiosis; the various forms of symbiosis include parasitism, commensalism and mutualism. [GOC:cc] |
| negative regulation of fibrinolysis | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of fibrinolysis, an ongoing process that solubilizes fibrin, resulting in the removal of small blood clots. [GOC:ai] |
| positive regulation of fibrinolysis | biological process | Any process that activates, maintains or increases the frequency, rate or extent of fibrinolysis, an ongoing process that solubilizes fibrin, resulting in the removal of small blood clots. [GOC:ai] |
| trophoblast giant cell differentiation | biological process | The process in which a relatively unspecialized cell acquires specialized features of a trophoblast giant cell of the placenta. Trophoblast giant cells are the cell of the placenta that line the maternal decidua. [GOC:dph, PMID:16269175] |
| labyrinthine layer blood vessel development | biological process | The process whose specific outcome is the progression of a blood vessel of the labyrinthine layer of the placenta over time, from its formation to the mature structure. The embryonic vessels grow through the layer to come in close contact with the maternal blood supply. [GOC:dph] |
| mononuclear cell migration | biological process | The movement of a mononuclear cell within or between different tissues and organs of the body. [GOC:mah] |
| trans-synaptic signaling by BDNF, modulating synaptic transmission | biological process | Cell-cell signaling between presynapse and postsynapse, via the vesicular release and reception of brain derived neurotrophic factor (BDNF), that modulates the synaptic transmission properties of the synapse. [GOC:dos] |
| negative regulation of cell-cell adhesion mediated by cadherin | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of cell-cell adhesion mediated by cadherin. [GOC:obol] |