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References from Structural Biology and Protein Engineering of Thrombolytics. Local targets link to admitted publications; unresolved targets remain external evidence.
Unresolved reference
External reference
Thrombolytic therapy in the current ERA: myocardial infarction and beyond
10.2174/1381612824666171227211623 · 2018 · External reference
10.1182/blood-2011-07-369512
10.1182/blood-2011-07-369512 · External reference
10.1038/cddis.2016.279
10.1038/cddis.2016.279 · External reference
The plasminogen activation system in neuroinflammation
1862 · External reference
10.1016/j.neurobiolaging.2013.09.020
10.1016/j.neurobiolaging.2013.09.020 · External reference
10.3233/jad-180241
10.3233/jad-180241 · External reference
10.18632/oncotarget.19935
10.18632/oncotarget.19935 · External reference
Proteolysis is the most fundamental property of malignancy and its inhibition may be used therapeutically (Review)
2019 · External reference
Kinetics of the activation of plasminogen by human tissue plasminogen activator
10.1016/s0021-9258(19)81051-7 · 1982 · External reference
Isolation and characterization of urokinase from human plasma
10.1016/s0021-9258(19)81106-7 · 1982 · External reference
The evolution of recombinant thrombolytics: current status and future directions
2016 · External reference
10.1016/0014-5793(87)81501-6
10.1016/0014-5793(87)81501-6 · External reference
A mutant streptokinase lacking the C-terminal 42 amino acids is less immunogenic
10.1016/s0165-2478(99)00151-0 · 2000 · External reference
10.1160/th04-12-0842
10.1160/th04-12-0842 · External reference
Serine-578 is a major phosphorylation locus in human plasma plasminogen †
10.1021/bi970328d · 1997 · External reference
Structural studies of plasmin inhibition
10.1042/bst20180211 · 2019 · External reference
The peptide chains of human plasmin. mechanism of activation of human plasminogen to plasmin
10.1016/s0021-9258(18)95967-3 · 1967 · External reference
Secondary-site binding of Glu-plasmin, Lys-plasmin and miniplasmin to fibrin
10.1042/bj1970619 · 1981 · External reference
10.1016/s0021-9258(18)37875-x
10.1016/s0021-9258(18)37875-x · External reference
10.1111/j.1538-7836.2012.04765.x
10.1111/j.1538-7836.2012.04765.x · External reference
Lys-plasminogen is a significant intermediate in the activation of Glu-plasminogen during fibrinolysis in vitro
10.1016/s0021-9258(18)35729-6 · 1992 · External reference
10.1016/j.celrep.2012.02.012
10.1016/j.celrep.2012.02.012 · External reference
The role of plasminogen in angiogenesis in vivo
10.1046/j.1538-7836.2003.00182.x · 2003 · External reference
The mechanism of action of angiostatin: can you teach an old dog new tricks?
10.1055/s-0037-1613016 · 2002 · External reference
10.1111/j.1538-7836.2004.00544.x
10.1111/j.1538-7836.2004.00544.x · External reference
10.1002/jcb.20480
10.1002/jcb.20480 · External reference
The X-ray crystallographic structure of the angiogenesis inhibitor angiostatin
10.1016/s0022-2836(02)00211-5 · 2002 · External reference
10.1016/s1474-4422(18)30323-5
10.1016/s1474-4422(18)30323-5 · External reference
10.1146/annurev.bioeng.1.1.427
10.1146/annurev.bioeng.1.1.427 · External reference
Clot penetration and retention by plasminogen activators promote fibrinolysis
10.1016/j.bcp.2012.10.011 · 2013 · External reference
Molecular and physical mechanisms of fibrinolysis and thrombolysis from mathematical modeling and experiments
10.1038/s41598-017-06383-w · 2017 · External reference
TAFIa, PAI-1 and α2-antiplasmin: complementary roles in regulating lysis of thrombi and plasma clots
10.1111/j.1538-7836.2007.02430.x · 2007 · External reference
PAI-1-resistant t-PA: low doses prevent fibrin deposition in rabbits with increased PAI-1 activity
10.1182/blood.v87.1.14.14 · 1996 · External reference
Tenecteplase versus alteplase for management of acute ischemic stroke: a pairwise and network meta-analysis of randomized clinical trials
10.1007/s11239-018-1721-3 · 2018 · External reference
Randomized comparison of coronary thrombolysis achieved with double-bolus reteplase (recombinant plasminogen activator) and front-loaded, accelerated alteplase (recombinant tissue plasminogen activator) in patients with acute myocardial infarction
10.1161/01.cir.94.5.891 · 1996 · External reference
More rapid, Complete, and stable coronary thrombolysis with bolus administration of reteplase compared with alteplase infusion in acute myocardial infarction
10.1161/01.cir.91.11.2725 · 1995 · External reference
Tenecteplase versus alteplase before thrombectomy for ischemic stroke
2018 · External reference
Different doses of tenecteplase vs alteplase in thrombolysis therapy of acute ischemic stroke: evidence from randomized controlled trials
10.2147/dddt.s170803 · 2018 · External reference
Efficacy and safety of desmoteplase in acute ischemic stroke patients a systematic review and meta-analysis
10.1097/md.0000000000006667 · 2017 · External reference
Reocclusion: the flip side of coronary thrombolysis
10.1016/0735-1097(95)00492-0 · 1996 · External reference
Unresolved reference
2003 · External reference
10.1038/cdd.2012.86
10.1038/cdd.2012.86 · External reference
PAI1 blocks effects of tissue-type plasminogen activator on cell-signaling and physiology mediated by the NMDA receptor
2018 · External reference
tPA modulation of the blood–brain barrier: a unifying explanation for the pleiotropic effects of tPA in the CNS
2017 · External reference
Expansion of the time window for treatment of acute ischemic stroke with intravenous tissue plasminogen activator a science advisory from the american heart association/american stroke association
10.1161/strokeaha.109.192535 · 2009 · External reference
Plasminogen activators: a comparison
10.1016/j.vph.2005.09.003 · 2006 · External reference
Therapeutic fibrinolysis: how efficacy and safety can be improved
10.1016/j.jacc.2016.07.780 · 2016 · External reference
Fibrinolysis: from blood to the brain
10.1111/jth.13849 · 2017 · External reference
Oxygen glucose deprivation switches the transport of tPA across the blood–brain barrier from an LRP-dependent to an increased LRP-independent process
10.1161/01.str.0000163050.39122.4f · 2005 · External reference
10.3389/fncel.2016.00002
10.3389/fncel.2016.00002 · External reference
10.1515/revneuro-2015-0069
10.1515/revneuro-2015-0069 · External reference
A Rho kinase (ROCK) inhibitor, fasudil, prevents matrix metalloproteinase-9-related hemorrhagic transformation in mice treated with tissue plasminogen activator
10.1016/j.neuroscience.2012.06.015 · 2012 · External reference
In vitro and in vivo effects of tPA and PAI-1 on blood vessel tone
10.1182/blood-2003-05-1685 · 2003 · External reference
In vivo clearance of tissue plasminogen activator: the complex role of sites of glycosylation and level of sialylation
10.1016/0268-9499(93)90050-6 · 1993 · External reference
The structure of the human tissue-type plasminogen activator gene: correlation of intron and exon structures to functional and structural domains
10.1073/pnas.81.17.5355 · 1984 · External reference
Involvement of finger domain and kringle 2 domain of tissue-type plasminogen activator in fibrin binding and stimulation of activity by fibrin
10.1002/j.1460-2075.1986.tb04678.x · 1986 · External reference
A linear amino acid sequence involved in the interaction of t-PA with its endothelial cell receptor
10.1182/blood.v74.6.2034.2034 · 1989 · External reference
The role of the finger and growth factor domains in the clearance of tissue-type plasminogen activator by hepatocytes
10.1074/jbc.270.44.26053 · 1995 · External reference
10.1084/jem.20101880
10.1084/jem.20101880 · External reference
Tissue plasminogen activator has an O-linked fucose attached to threonine-61 in the epidermal growth factor domain
10.1021/bi00223a004 · 1991 · External reference
Two receptor systems are involved in the plasma clearance of tissue-type plasminogen activator (t-PA) in vivo
10.1172/jci118105 · 1995 · External reference
Variants of human tissue-type plasminogen activator that lack specific structural domains of the heavy chain
10.1002/j.1460-2075.1988.tb03127.x · 1988 · External reference
Penta-l-lysine potentiates fibrin-independent activity of human tissue plasminogen activator
10.1021/acs.jpcb.5b07735 · 2015 · External reference
Binding of tissue-type plasminogen activator to lysine, lysine analogs, and fibrin fragments
10.1021/bi00444a026 · 1989 · External reference
Tissue-type plasminogen activator is a multiligand cross-β structure receptor
10.1016/s0960-9822(02)01224-1 · 2002 · External reference
Molecular requirements for safer generation of thrombolytics by bioengineering the tissue-type plasminogen activator A chain
10.1111/jth.12128 · 2013 · External reference
10.1134/s1068162014060028
10.1134/s1068162014060028 · External reference
The 2.3 Å crystal structure of the catalytic domain of recombinant two-chain human tissue-type plasminogen activator
10.1006/jmbi.1996.0238 · 1996 · External reference
Converting tissue type plasminogen activator into a zymogen. important role of Lys156
10.1074/jbc.272.1.28 · 1997 · External reference
10.1038/nbt1085-923
10.1038/nbt1085-923 · External reference
10.1016/s0959-440x(97)80159-5
10.1016/s0959-440x(97)80159-5 · External reference
10.1074/jbc.m115.675538
10.1074/jbc.m115.675538 · External reference
Interplay between conformational selection and zymogen activation
10.1038/s41598-018-21728-9 · 2018 · External reference
Distinct mechanisms contribute to stringent substrate specificity of tissue-type plasminogen activator
10.1074/jbc.271.8.4461 · 1996 · External reference
10.1074/jbc.272.3.1811
10.1074/jbc.272.3.1811 · External reference
10.1074/jbc.270.31.18319
10.1074/jbc.270.31.18319 · External reference
First structural model of full-length human tissue-plasminogen activator: a SAXS data-based modeling study
10.1021/jp207243n · 2012 · External reference
The role of the lysyl binding site of tissue-type plasminogen activator in the interaction with a forming fibrin clot
10.1074/jbc.270.21.12355 · 1995 · External reference
On the interaction of the finger and the kringle-2 domain of tissue-type plasminogen activator with fibrin. inhibition of kringle-2 binding to fibrin by epsilon-amino caproic acid
10.1016/s0021-9258(18)67006-1 · 1986 · External reference
Making tissue-type plasminogen activator more fibrin specific
10.1093/protein/6.5.529 · 1993 · External reference
Unresolved reference
2001 · External reference
Molecular mechanisms of initiation of fibrinolysis by fibrin
10.1055/s-0037-1613368 · 2003 · External reference
Identification and characterization of novel tPA- and plasminogen-binding sites within fibrin(ogen) αC-domains †
10.1021/bi001789t · 2001 · External reference
The sequence gamma-(312-324) is a fibrin-specific epitope
10.1182/blood.v77.10.2169.2169 · 1991 · External reference
10.1016/s0021-9258(18)45518-4
10.1016/s0021-9258(18)45518-4 · External reference
Conversion of fibrinogen to fibrin: mechanism of exposure of tPA- and plasminogen-binding sites
10.1021/bi001847a · 2000 · External reference
Binding of synthetic B knobs to fibrinogen changes the character of fibrin and inhibits its ability to activate tissue plasminogen activator and its destruction by plasmin
10.1021/bi0524767 · 2006 · External reference
Unresolved reference
2002 · External reference
Interaction of one-chain and two-chain tissue plasminogen activator with intact and plasmin-degraded fibrin
10.1021/bi00398a038 · 1987 · External reference
10.1016/s0021-9258(18)88883-4
10.1016/s0021-9258(18)88883-4 · External reference
Is plasminogen activator inhibitor type 2 really a plasminogen activator inhibitor after all?
10.1111/jth.12704 · 2014 · External reference
Neuroserpin: a selective inhibitor of tissue-type plasminogen activator in the central nervous system
10.1160/th03-12-0766 · 2004 · External reference
10.1111/j.1538-7836.2007.02516.x
10.1111/j.1538-7836.2007.02516.x · External reference
Amino acid residues that affect interaction of tissue-type plasminogen activator with plasminogen activator inhibitor 1
10.1073/pnas.87.9.3530 · 1990 · External reference
10.1074/jbc.m115.677567
10.1074/jbc.m115.677567 · External reference
A faster-acting and more potent form of tissue plasminogen activator
10.1073/pnas.91.9.3670 · 1994 · External reference
10.1074/jbc.272.23.14580
10.1074/jbc.272.23.14580 · External reference
Role of residue Y99 in tissue plasminogen activator
10.1110/ps.9.3.619 · 2000 · External reference
tPA point mutation at autolysis loop enhances resistance to PAI-1 inhibition and catalytic activity
2018 · External reference
Plasminogen activator inhibitor 1 contains a cryptic high affinity receptor binding site that is exposed upon complex formation with tissue-type plasminogen activator
10.1055/s-0037-1615365 · 1998 · External reference
Participation of a galectin-dependent mechanism in the hepatic clearance of tissue-type plasminogen activator and plasma kallikrein
10.1016/s0049-3848(02)00393-6 · 2002 · External reference
10.1016/s0021-9258(18)35732-6
10.1016/s0021-9258(18)35732-6 · External reference
Molecular analysis of ligand binding to the second cluster of complement-type repeats of the low density lipoprotein receptor-related protein. evidence for an allosteric component in receptor-associated protein-mediated inhibition of ligand binding
10.1074/jbc.272.21.13608 · 1997 · External reference
10.1016/s0021-9258(17)40755-1
10.1016/s0021-9258(17)40755-1 · External reference
The second and fourth cluster of class A cysteine-rich repeats of the low density lipoprotein receptor-related protein share ligand-binding properties
10.1074/jbc.274.44.31305 · 1999 · External reference
10.1016/j.molcel.2006.02.021
10.1016/j.molcel.2006.02.021 · External reference
10.1016/j.jmb.2010.03.022
10.1016/j.jmb.2010.03.022 · External reference
10.1074/jbc.m115.688820
10.1074/jbc.m115.688820 · External reference
10.1074/jbc.m113.473728
10.1074/jbc.m113.473728 · External reference
Tissue-type plasminogen activator crosses the intact blood-brain barrier by low-density lipoprotein receptor-related protein-mediated transcytosis
10.1161/01.cir.0000163542.48611.a2 · 2005 · External reference
Thrombolytic activity of YM866, a novel modified tissue-type plasminogen activator, in a photochemically induced platelet-rich thrombosis model
10.1097/00005344-199406000-00005 · 1994 · External reference
10.1016/s0021-9258(19)50142-9
10.1016/s0021-9258(19)50142-9 · External reference
Optimized tPA: a non-neurotoxic fibrinolytic agent for the drainage of intracerebral hemorrhages
10.1177/0271678x17719180 · 2018 · External reference
10.1161/strokeaha.116.012678
10.1161/strokeaha.116.012678 · External reference
Recombinant desmodus rotundus salivary plasminogen activator crosses the blood–brain barrier through a low-density lipoprotein receptor-related protein-dependent mechanism without exerting neurotoxic effects
10.1161/01.str.0000258100.04923.84 · 2007 · External reference
10.1155/2012/353687
10.1155/2012/353687 · External reference
10.1016/j.pep.2006.06.002
10.1016/j.pep.2006.06.002 · External reference
10.1016/j.bbrc.2004.12.126
10.1016/j.bbrc.2004.12.126 · External reference
10.1016/s0006-291x(03)00656-9
10.1016/s0006-291x(03)00656-9 · External reference
10.3390/ijms14036259
10.3390/ijms14036259 · External reference
Annexin II: a plasminogen-plasminogen activator co-receptor
10.2741/kim · 2002 · External reference
10.1681/asn.2011111123
10.1681/asn.2011111123 · External reference
Biochemical-properties of the kringle 2 and protease domains are maintained in the refolded T-Pa deletion variant Bm 06.022
10.1093/protein/5.1.93 · 1992 · External reference
a long-half-life and fibrin-specific form of tissue-plasminogen activator in rabbit models of embolic stroke and peripheral bleeding
10.1161/01.str.25.10.2072 · 1994 · External reference
A region of tissue plasminogen activator that affects plasminogen activation differentially with various fibrin(ogen)-related stimulators
10.1021/bi00117a016 · 1992 · External reference
ESPRIT: a European study of the prevention of reocclusion after initial thrombolysis with duteplase in acute myocardial infarction
10.1093/oxfordjournals.eurheartj.a014716 · 1996 · External reference
Intravenous NPA for the treatment of infarcting myocardium early; inTIME-II, a double-blind comparison of single-bolus lanoteplase vs accelerated alteplase for the treatment of patients with acute myocardial infarction
10.1053/euhj.2000.2498 · 2000 · External reference
Functional effects of asparagine-linked oligosaccharide on natural and variant human tissue-type plasminogen activator
10.1016/s0021-9258(19)37646-x · 1988 · External reference
Comparison of drug disposition between wild-type and novel tissue-type plasminogen activator pamiteplase in rats
10.1016/s0090-9556(24)15191-4 · 2000 · External reference
Serine-proteases as plasminogen activators in terms of fibrinolysis
10.1111/j.2042-7158.2012.01457.x · 2012 · External reference
Design of a novel chimeric tissue plasminogen activator with favorable Vampire bat plasminogen activator properties
10.1016/j.enzmictec.2014.09.005 · 2014 · External reference
Experiences with pro-urokinase and potentiation of its fibrinolytic effect by urokinase and by tissue plasminogen activator
10.1016/s0735-1097(87)80423-0 · 1987 · External reference
Complementary modes of action of tissue-type plasminogen activator and pro-urokinase by which their synergistic effect on clot lysis may be explained
10.1172/jci113394 · 1988 · External reference
Why so little progress in therapeutic thrombolysis? The current state of the art and prospects for improvement
10.1007/s11239-015-1217-3 · 2015 · External reference
Fibrin-specific and effective clot lysis requires both plasminogen activators and for them to be in a sequential rather than simultaneous combination
10.1007/s11239-017-1514-0 · 2017 · External reference
Discovery and SAR of novel and selective inhibitors of urokinase plasminogen activator (uPA) with an imidazo[1,2-a]pyridine scaffold
10.1021/acs.jmedchem.5b01171 · 2015 · External reference
An anti-urokinase plasminogen activator receptor antibody (ATN-658) blocks prostate cancer invasion, migration, growth, and experimental skeletal metastasis in vitro and in vivo
10.1593/neo.10296 · 2010 · External reference
10.1371/journal.pone.0085349
10.1371/journal.pone.0085349 · External reference
The soluble form of urokinase receptor promotes angiogenesis through its Ser88-Arg-Ser-Arg-Tyr92 chemotactic sequence: new vessel formation by SRSRY sequence of u-PAR
10.1111/j.1538-7836.2010.04075.x · 2010 · External reference
10.1016/j.addr.2015.11.010
10.1016/j.addr.2015.11.010 · External reference
Urokinase directly activates matrix metalloproteinases-9: a potential role in glioblastoma invasion
10.1016/j.bbrc.2008.03.038 · 2008 · External reference
10.1007/s11064-010-0141-3
10.1007/s11064-010-0141-3 · External reference
10.2174/138945011797635777
10.2174/138945011797635777 · External reference
Evolving role of uPA/uPAR system in human cancers
10.1016/j.ctrv.2007.10.005 · 2008 · External reference
Urokinase links plasminogen activation and cell adhesion by cleavage of the RGD motif in vitronectin
2016 · External reference
10.3892/ijo.28.6.1463
10.3892/ijo.28.6.1463 · External reference
Involvement of urokinase-type plasminogen activator system in cancer: an overview: uPA system in cancer
10.1002/med.21308 · 2014 · External reference
10.1016/s0021-9258(19)62711-0
10.1016/s0021-9258(19)62711-0 · External reference
Heparin binding to the urokinase kringle domain
10.1021/bi00148a019 · 1992 · External reference
10.1083/jcb.137.3.779
10.1083/jcb.137.3.779 · External reference
Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator
10.1073/pnas.88.9.3992 · 1991 · External reference
10.1038/nbt1291-1347
10.1038/nbt1291-1347 · External reference
Proteolytic cleavage of single-chain pro-urokinase induces conformational change which follows activation of the zymogen and reduction of its high affinity for fibrin
10.1016/s0021-9258(17)39035-x · 1985 · External reference
10.1016/j.jmb.2011.05.026
10.1016/j.jmb.2011.05.026 · External reference
10.1016/s0021-9258(17)46663-4
10.1016/s0021-9258(17)46663-4 · External reference
Discovery of a novel conformational equilibrium in urokinase-type plasminogen activator
10.1038/s41598-017-03457-7 · 2017 · External reference
Interconversion of active and inactive conformations of urokinase-type plasminogen activator
10.1021/bi3005957 · 2012 · External reference
10.1371/journal.pone.0192661
10.1371/journal.pone.0192661 · External reference
Pro-urokinase: a study of its stability in plasma and of a mechanism for its selective fibrinolytic effect
10.1182/blood.v67.5.1215.1215 · 1986 · External reference
10.1002/prot.20686
10.1002/prot.20686 · External reference
Urokinase-type plasminogen activator: proenzyme, receptor, and inhibitors
10.1083/jcb.104.4.801 · 1987 · External reference
Inactivation of single-chain urokinase (pro-urokinase) by thrombin and thrombin-like enzymes: relevance of the findings to the interpretation of fibrin-binding experiments
10.1182/blood.v69.3.769.769 · 1987 · External reference
Structural basis for recognition of urokinase-type plasminogen activator by plasminogen activator inhibitor-1
10.1074/jbc.m110.204537 · 2011 · External reference
10.1074/jbc.275.10.7239
10.1074/jbc.275.10.7239 · External reference
10.1016/j.jmb.2004.09.032
10.1016/j.jmb.2004.09.032 · External reference
Characterising the subsite specificity of urokinase-type plasminogen activator and tissue-type plasminogen activator using a sequence-defined peptide aldehyde library
2019 · External reference
Plasma clearance of urokinase-type plasminogen activator
10.1016/s0268-9499(98)80018-0 · 1998 · External reference
The urokinase/PAI-2 complex - A new high affinity ligand for the endocytosis receptor low density lipoprotein receptor-related protein
2006 · External reference
Low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor mediates cellular uptake of pro-urokinase
10.1016/s0021-9258(20)80620-6 · 1993 · External reference
Regions involved in binding of urokinase-type-1 inhibitor complex and pro-urokinase to the endocytic alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein. evidence that the urokinase receptor protects pro-urokinase against binding to the endocytic receptor
10.1016/s0021-9258(18)47301-2 · 1994 · External reference
10.1111/j.1742-4658.2006.05511.x
10.1111/j.1742-4658.2006.05511.x · External reference
Assembly of urokinase receptor-mediated plasminogen activation complexes involves direct, non-active-site interactions between urokinase and plasminogen
10.1021/bi981714d · 1999 · External reference
10.1126/science.1121143
10.1126/science.1121143 · External reference
Structural analysis of the interaction between urokinase-type plasminogen activator and its receptor: a potential target for anti-invasive cancer therapy
10.1042/bst0300177 · 2002 · External reference
Unresolved reference
1986 · External reference
In silico docking of urokinase plasminogen activator and integrins
10.1186/1471-2105-9-s2-s8 · 2008 · External reference
opposite modulation of cell migration by distinct subregions of urokinase connecting peptide
10.1002/cbic.201200774 · 2013 · External reference
Tissue-type plasminogen activator (tPA) interacts with urokinase-type plasminogen activator (uPA) via tPA’s lysine binding site: an explanation of the poor fibrin affinity of recombinant tPA/uPA chimeric molecules
10.1074/jbc.270.15.8680 · 1995 · External reference
10.1074/jbc.272.38.23818
10.1074/jbc.272.38.23818 · External reference
Thrombolysis vs. bleeding from hemostatic sites by a prourokinase mutant compared with tissue plasminogen activator
10.1111/j.1538-7836.2006.01993.x · 2006 · External reference
The fibrinolytic activity of hemolytic streptococci
10.1084/jem.58.4.485 · 1933 · External reference
10.1016/s0021-9258(19)67737-9
10.1016/s0021-9258(19)67737-9 · External reference
10.1126/science.1101245
10.1126/science.1101245 · External reference
10.1371/journal.pone.0170936
10.1371/journal.pone.0170936 · External reference
10.1073/pnas.96.16.8879
10.1073/pnas.96.16.8879 · External reference
10.1016/j.biotechadv.2003.09.004
10.1016/j.biotechadv.2003.09.004 · External reference
How safe is the readministration of streptokinase?
10.2165/00002018-199513020-00002 · 1995 · External reference
Antibodies to streptokinase
10.1136/bmj.312.7028.393 · 1996 · External reference
Nucleotide sequence of the streptokinase gene from Streptococcus equisimilis H46A
10.1016/0378-1119(85)90145-3 · 1985 · External reference
Preparation and certain properties of highly purified streptokinase
10.1016/s0021-9258(18)96306-4 · 1967 · External reference
Characterization of structural and folding properties of streptokinase by n.m.r. spectroscopy
10.1042/bj2900313 · 1993 · External reference
10.1126/science.281.5383.1662
10.1126/science.281.5383.1662 · External reference
10.1074/jbc.m400253200
10.1074/jbc.m400253200 · External reference
10.1021/bi981915h
10.1021/bi981915h · External reference
Zymogen activation in the streptokinase-plasminogen complex - Ile1 is required for the formation of a functional active site
10.1046/j.1432-1327.2000.01434.x · 2000 · External reference
10.1021/bi011309d
10.1021/bi011309d · External reference
10.1074/jbc.m003963200
10.1074/jbc.m003963200 · External reference
10.1074/jbc.m101966200
10.1074/jbc.m101966200 · External reference
10.1074/jbc.m301825200
10.1074/jbc.m301825200 · External reference
10.1074/jbc.273.5.3110
10.1074/jbc.273.5.3110 · External reference
Effects of deletion of streptokinase residues 48-59 on plasminogen activation
10.1093/protein/15.9.753 · 2002 · External reference
10.1016/s0049-3848(00)00225-5
10.1016/s0049-3848(00)00225-5 · External reference
The domain organization of streptokinase: nuclear magnetic resonance, circular dichroism, and functional characterization of proteolytic fragments
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