%D8%A8%D9%84%D8%A7%D8%B2%D9%85%D9%8A%D9%86PlasminaPlazminPLGPlasminPlasminPlasmin%C3%B3geno%D9%BE%D9%84%D8%A7%D8%B3%D9%85%DB%8C%D9%86PlasmiiniPlasminePlasmin%C3%B3xeno%D7%A4%D7%9C%D7%A1%D7%9E%D7%99%D7%9FPlasminogenPlasmina%E3%83%97%E3%83%A9%E3%82%B9%E3%83%9F%E3%83%B3%D0%9F%D0%BB%D0%B0%D0%B7%D0%BC%D0%B8%D0%BDPlasminePlazminaPlasmina%D0%9F%D0%BB%D0%B0%D0%B7%D0%BC%D0%B8%D0%BDPlazminPlazminPlasmin%D0%9F%D0%BB%D0%B0%D0%B7%D0%BC%D1%96%D0%BD%D0%BE%D0%B3%D0%B5%D0%BDQ21173374%E7%BA%A4%E6%BA%B6%E9%85%B6
about
PlasminPlatelet alpha granule contentsPlatelet alpha granule contents [extracellular region]histidine-rich glycoprotein:plasminogenfibrin multimer; crosslinked:tissue plasminogen activator (one-chain):plasminogenfibrin multimer; crosslinked:tissue plasminogen activator (two-chain):plasminogenplasminogen:histidine-rich glycoproteinhistidine-rich glycoprotein + plasminogen <-> histidine-rich glycoprotein:plasminogenhistidine-rich glycoprotein:plasminogen <-> histidine-rich glycoprotein + plasminogencrosslinked fibrin multimer:tissue plasminogen activator (one-chain) + plasminogen -> crosslinked fibrin multimer:tissue plasminogen activator (one-chain):plasminogencrosslinked fibrin multimer:tissue plasminogen activator (two-chain) + plasminogen -> crosslinked fibrin multimer:tissue plasminogen activator (two-chain):plasminogenplasminogen + histidine-rich glycoprotein -> plasminogen:histidine-rich glycoprotein
P527
P688
The plasminogen binding site of the C-type lectin tetranectin is located in the carbohydrate recognition domain, and binding is sensitive to both calcium and lysineResidues essential for plasminogen binding by the cation-independent mannose 6-phosphate receptorPlasminogen Tochigi: inactive plasmin resulting from replacement of alanine-600 by threonine in the active siteComplex formation of platelet thrombospondin with plasminogen. Modulation of activation by tissue activatorProteolytic cleavage and inactivation of alpha 2-plasmin inhibitor and C1 inactivator by human polymorphonuclear leukocyte elastaseProtease nexin-1 inhibits plasminogen activation-induced apoptosis of adherent cellsThe role of beta2-glycoprotein I (beta2GPI) in the activation of plasminogenNicked beta2-glycoprotein I: a marker of cerebral infarct and a novel role in the negative feedback pathway of extrinsic fibrinolysisHCV NS3 protease enhances liver fibrosis via binding to and activating TGF-β type I receptorTwo types of abnormal genes for plasminogen in families with a predisposition for thrombosisKringle domains of human angiostatin. Characterization of the anti-proliferative activity on endothelial cellsInduction of alpha2-antiplasmin inhibits E-cadherin processing mediated by the plasminogen activator/plasmin system, leading to suppression of progression of oral squamous cell carcinoma via upregulation of cell-cell adhesionPneumococcal phosphoglycerate kinase interacts with plasminogen and its tissue activatorNetwork of Surface-Displayed Glycolytic Enzymes in Mycoplasma pneumoniae and Their Interactions with Human PlasminogenA surface enolase participates in Borrelia burgdorferi-plasminogen interaction and contributes to pathogen survival within feeding ticksBorrelia burgdorferi enolase is a surface-exposed plasminogen binding proteinCytosolic proteins contribute to surface plasminogen recruitment of Neisseria meningitidisCloning and characterization of an alpha-enolase of the oral pathogen Streptococcus mutans that binds human plasminogenEnolases from Gram-positive bacterial pathogens and commensal lactobacilli share functional similarity in virulence-associated traitsIdentification of novel bacterial plasminogen-binding proteins in the human pathogen Mycobacterium tuberculosisCathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase and impairs survival and neuritogenesis of neuronal cellsInhibition of cell surface mediated plasminogen activation by a monoclonal antibody against alpha-EnolaseAcquisition of host plasmin activity by the Swine pathogen Streptococcus suis serotype 2Surface-expressed enolase contributes to the pathogenesis of clinical isolate SSU of Aeromonas hydrophilaalpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococciSurface localized and extracellular Glyceraldehyde-3-phosphate dehydrogenase of Bacillus anthracis is a plasminogen binding proteinMolecular cloning of an alpha-enolase from the human filarial parasite Onchocerca volvulus that binds human plasminogenBinding of Candida albicans enolase to plasmin(ogen) results in enhanced invasion of human brain microvascular endothelial cellsImmunogenic and plasminogen-binding surface-associated alpha-enolase of Trichomonas vaginalisBifidobacterial enolase, a cell surface receptor for human plasminogen involved in the interaction with the hostPlasminogen binding proteins and plasmin generation on the surface of Leptospira spp.: the contribution to the bacteria-host interactionsPlasminogen acquisition and activation at the surface of leptospira species lead to fibronectin degradation
P921
Q50257634-56C4BD98-1555-428C-A0C9-5BEACE1AFF89Q50259202-54F936C2-443A-49BF-839F-39F0D6EDBBAFQ50259219-574139AE-4B71-4A69-8156-1B288BA76729Q50259363-E59B26E5-623B-4DD4-B09D-2765B64A46FCQ50259367-F1AC856A-D96E-428A-BDBB-BB734D624B41Q50259374-59EB1D6D-C1BC-4839-BB7B-DB4F3A83FED4Q50259384-FEFEA625-D838-4C2D-859F-E4A0B52F4A5BQ50291237-0D4C4C8D-0501-4C92-98A5-746A9D1711FFQ50291238-4ACF36E7-16CC-4913-8875-232C7A8E9B3BQ50291240-84D7D658-68F0-49DB-9C2A-C701C0EA8B3CQ50291246-90C1A4F0-B3E5-4216-852A-155B144A1626Q50291252-83316576-F72D-4F56-9490-E4714DA155D2
P527
Q22004001-BBB7518C-59E8-4DF1-ACBB-65337AA7E18FQ24293140-1E5DBC91-7C61-48BF-B0D8-3578D01A74B4Q24301025-8117A232-7DA0-4E6D-90E0-1DEAFD403B46Q24301570-747CCC37-2E1A-4B3B-81E8-BCE5E9C0A699Q24302265-E270FB2D-D783-407B-B42F-9710FBFC1956Q24303595-B2EC7532-0411-4797-BD03-78FE124C6218Q24304748-7848B076-9A29-429B-A8C8-75B099E26095Q24305033-72EF9119-87FD-4337-8D56-CE3B57237A64Q24308693-CF6354DD-435E-4826-A6B3-BC5D0802226DQ24311560-43063DC3-1922-456A-91B9-E0A91D988A0DQ24319640-7C067632-5848-4F3A-9920-9523863F6A59Q24338762-D70E3AF1-734A-41A1-99A4-8548D89CC0A5Q27687448-D2A92D10-12FE-4694-8F26-35433BB19263Q28118121-1642ACEC-3F75-431C-B40C-AC4700CFA760Q28902809-42050AE6-0F64-4AE1-8CDD-FBCC5B14A09DQ28902816-30A450EC-639B-4A3F-A56B-2BF8AACD04E4Q28903782-7B399C2F-BE5A-42B0-88A0-A2D8B5871330Q28903906-71959919-5D9A-410D-BFEA-B39C4BD0987DQ28904962-8F66FD64-C51D-4B05-A08F-BDC47CE4EF8EQ28909146-5FD1F1AD-BF56-4B72-ADD8-F00752B3BE32Q28909727-F65F7F57-1C5E-419F-B72F-2063D372BC4FQ28910334-66F76DF7-6D65-4014-9FA7-54EFF058D34FQ28910343-64DE7ACB-26E2-45E2-82EE-0C9E1DEB92F6Q28910346-3B7497B0-417A-44E7-BCA1-0E9117D5B7D9Q28910377-6B972DF9-A7E4-4427-8916-70A29A0E4699Q28910401-BA4EA289-81CF-4275-9722-5058433C6F7CQ28910410-641DB14A-A144-4CCC-8763-CF0F6D98B09FQ28910414-130F723D-3E1A-4CFD-AAD4-07BDCFB1A311Q28910454-EB78E330-409B-4244-93BE-29C9FF86C9C0Q28910467-8DFFF89B-7420-40AF-9EBA-F1FBB664BD9EQ34464277-bd6df801-443b-eb6e-e6a0-5a3bb7315b52Q41853863-16b1590d-4b12-a014-217d-7a2bea95d678
P921
description
Protein in Homo sapiens
@de
mammalian protein found in Homo sapiens
@en
protein
@id
proteinë
@sq
proteïne in Plasminogen
@nl
protèin
@ace
بروتين في الإنسان العاقل
@ar
name
PLG
@cy
Plasmiini
@fi
Plasmin
@de
Plasmin
@sv
Plasmina
@ca
Plasmina
@it
Plasmina
@pt
Plasmine
@nl
Plasminogen
@en
Plasminogen
@id
type
label
PLG
@cy
Plasmiini
@fi
Plasmin
@de
Plasmin
@sv
Plasmina
@ca
Plasmina
@it
Plasmina
@pt
Plasmine
@nl
Plasminogen
@en
Plasminogen
@id
altLabel
PLG
@en
plasmin
@en
plasminogen
@en
prefLabel
PLG
@cy
Plasmiini
@fi
Plasmin
@de
Plasmin
@sv
Plasmina
@ca
Plasmina
@it
Plasmina
@pt
Plasmine
@nl
Plasminogen
@en
Plasminogen
@id
P361
P527
P638
P680
P681
P682
P705
P352
P486
P6366
P1417
science/plasminogen
P2868
P31
P352
P486
P527
P6366
2781071845
2911011648
P637
NP_001161810
P638
P680
P681
P682
P702
P703
P705
ENSP00000308938
ENSP00000355891
ENSP00000389424