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1. Full Text Functional differences between Streptococcus pyogenes cluster 1 and cluster 2b streptokinases are determined by their [beta]-domains
by Zhang, Yueling and Liang, Zhong and Glinton, Kristofor and Ploplis, Victoria A and Castellino, Francis J
FEBS Letters, ISSN 0014-5793, 05/2013, Volume 587, Issue 9, p. 1304
a* Two types of streptokinases (SK) have been found in different Streptococcus pyogenes strains, SK1 and SK2b. a* SK2b activity requires cell surface... 
Streptokinase
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2. INDIGENOUS RECOMBINANT STREPTOKINASE VS NATURAL STREPTOKINASE IN ACUTE MYOCARDIAL INFARCTION PATIENTS: PHASE III MULTICENTRIC RANDOMIZED DOUBLE BLIND TRIAL
by Diwedi, S. K and Hiremath, J. S and Kerkar, P. G and Reddy, Krishna N and Manjunath, C. N and Ramesh, S. S and Prabhavati, S and Dhobe, M and Singh, Kavita and Bhusari, P and Rao, Raman
INDIGENOUS RECOMBINANT STREPTOKINASE VS NATURAL STREPTOKINASE IN ACUTE MYOCARDIAL INFARCTION PATIENTS: PHASE III MULTICENTRIC RANDOMIZED DOUBLE BLIND TRIAL, 12/2005
Background : Streptokinase is the most widely used thrombolytic agent and can now be made using recombinant DNA technology. The present trial was initiated to... 
Streptokinase, Recombinant streptokinase, Myocardial infarction, Thrombolysis
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3. Activation of the human plasma fibrinolytic system by streptokinase
: therapeutic application in thrombo-embolic occlusions of the limb arteries and in myocardial infarction
by Amery, A
1969, 258
Streptokinase | Fibrinolysis | Blood plasma
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4. Site-specific thiol-mediated pegylation of streptokinase leads to improved properties with clinical potential
by Sawhney, Pooja and Kumar, Shekhar and Maheshwari, Neeraj and Guleria, Sumeet Singh and Dhar, Neelam and Kashyap, Radhika and Sahni, Girish
Current Pharmaceutical Design, ISSN 1381-6128, 10/2016, Volume 22, Issue 38, pp. 5868 - 5878
Streptokinase (SK) is an efficient thrombolytic agent that dissolves fibrin blood clots with clinical efficiency comparable to the high priced drug, tissue... 
PEGylation | Streptokinase | Immune-reactivity | Improved thrombolytic with clinical potential | Half-life | Clot lysis | Proteolytic stability | COMPLEX | MUTAGENESIS | DOMAIN | PROTEIN | MYOCARDIAL-INFARCTION | SYNTHETIC PEPTIDES | Improved thrombolytic with Clinical Potential | RECOMBINANT STREPTOKINASE | TISSUE-PLASMINOGEN-ACTIVATOR | PHARMACOLOGY & PHARMACY | BINDING | Proteolytic Stability | MACROMOLECULAR SUBSTRATE | Polyethylene Glycols - metabolism | Streptokinase - chemistry | Streptococcus - enzymology | Streptokinase - genetics | Sulfhydryl Compounds - metabolism | Humans | Models, Molecular | Crystallography, X-Ray | Polyethylene Glycols - chemistry | Sulfhydryl Compounds - chemistry | Protein Stability | Streptokinase - metabolism
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5. Fibrinolytic bacterial enzymes with thrombolytic activity
by Kotb, Essam
2012, SpringerBriefs in microbiology, ISBN 3642249795
Streptokinase | Fibrinolytic agents | Bacteria | enzymology
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6. Full Text Assessing Role of Higher dose of Streptokinase for Improving the Efficacy of Percutaneous Drainage in Pancreatic Necrosis
by Vaswani, Prateek and Gupta, Rajesh and Kang, Mandeep and Rana, Surinder S and Krishnamurthy, Gautham and Bhasin, Deepak K and Khullar, Madhu and Singh, Rajinder
Gastroenterology, ISSN 0016-5085, 2017, Volume 152, Issue 5, pp. S289 - S289
Gastroenterology and Hepatology | Streptokinase
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7. Full Text Cell‐free production of a therapeutic protein: Expression, purification, and characterization of recombinant streptokinase using a CHO lysate
by Tran, Kevin and Gurramkonda, Chandrasekhar and Cooper, Merideth A and Pilli, Manohar and Taris, Joseph E and Selock, Nicholas and Han, Tzu‐Chiang and Tolosa, Michael and Zuber, Adil and Peñalber‐Johnstone, Chariz and Dinkins, Christina and Pezeshk, Niloufar and Kostov, Yordan and Frey, Douglas D and Tolosa, Leah and Wood, David W and Rao, Govind
Biotechnology and Bioengineering, ISSN 0006-3592, 01/2018, Volume 115, Issue 1, pp. 92 - 102
The use of cell‐free systems to produce recombinant proteins has grown rapidly over the past decade. In particular, cell‐free protein synthesis (CFPS) systems... 
cell‐free in vitro translation | green fluorescent protein | mini‐bioreactors | intein technology | mini-bioreactors | cell-free in vitro translation | GENE | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | GLUCOSE | SYSTEMS | INTEINS | Green Fluorescent Proteins - isolation & purification | Streptokinase - biosynthesis | Streptokinase - genetics | Cricetulus | Green Fluorescent Proteins - genetics | Recombinant Proteins - genetics | Recombinant Proteins - biosynthesis | Recombinant Proteins - isolation & purification | Animals | Complex Mixtures | Cell-Free System | Green Fluorescent Proteins - biosynthesis | Streptokinase - isolation & purification | CHO Cells | Usage | Fluorescence | Monoclonal antibodies | Protein biosynthesis | Health aspects | Recombinant proteins | Cells | Biopharmaceutics | Disulfide bonds | Purification | Protein purification | Cell-free system | Glycosylation | Mammalian cells | Proteins | Streptokinase | Protein synthesis | Bioreactors | Technology | Production methods | Green fluorescent protein | Recombinant
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8. Streptokinase treatment for femoral artery thrombosis after cardiac catheterization in children
by Noori, NM and Rozati, A
01/2007
Background: Cardiac catheterization like other invasive procedures is afflicted with complications, one of the most important complications is vessel... 
Streptokinase | Catheterization | Children | Thrombosis
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9. Full Text High level production of active streptokinase in Pichia pastoris fed-batch culture
by Adivitiya and Dagar, Vikas Kumar and Devi, Nirmala and Khasa, Yogender Pal
International Journal of Biological Macromolecules, ISSN 0141-8130, 02/2016, Volume 83, pp. 50 - 60
Streptokinase is a biological macromolecule involved in dissolution of fibrin blood clot and favourably used in various clinical applications. This protein is... 
Glycosylation | Streptokinase | AOX1 promoter | Pichia pastoris | Secretory expression | Fed-batch fermentation | POLYMER SCIENCE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | STREPTOCOCCUS-EQUISIMILIS | RECOMBINANT STREPTOKINASE | CIRCULAR-DICHROISM | GENE | CONFORMATIONAL PROPERTIES | PROTEIN EXPRESSION | SEQUENCE | SECONDARY STRUCTURE | SECRETION | CHEMISTRY, APPLIED | Recombinant Proteins - metabolism | Streptokinase - genetics | Gene Expression - genetics | Peptides - genetics | Recombinant Proteins - genetics | Promoter Regions, Genetic - genetics | Pichia - metabolism | Peptides - metabolism | Protein Sorting Signals - genetics | Fermentation - genetics | Cloning, Molecular - methods | Mating Factor | Pichia - genetics | Batch Cell Culture Techniques - methods | Streptokinase - metabolism | Tryptophan | Fibrin | Fermentation | Index Medicus
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10. Full Text Streptokinase variants from Streptococcus pyogenes isolates display altered plasminogen activation characteristics – implications for pathogenesis
by Cook, Simon M and Skora, Amanda and Gillen, Christine M and Walker, Mark J and McArthur, Jason D
Molecular Microbiology, ISSN 0950-382X, 12/2012, Volume 86, Issue 5, pp. 1052 - 1062
Summary Streptococcus pyogenes (group A streptococcus, GAS) secretes streptokinase, a potent plasminogen activating protein. Among GAS isolates, streptokinase... 
DOMAIN | ALPHA-2-ANTIPLASMIN | GROUP-A STREPTOCOCCUS | GENE | BIOCHEMISTRY & MOLECULAR BIOLOGY | VIRULENCE FACTOR | MICROBIOLOGY | INFECTION | MECHANISMS | INHIBITOR | EXPRESSION | FIBRINOGEN | Amino Acid Sequence | Streptococcal Infections - microbiology | Catalytic Domain | Streptokinase - genetics | Plasminogen Activators | Humans | Virulence | Molecular Sequence Data | Mice, Transgenic | Plasminogen - metabolism | Sequence Analysis, DNA | Streptococcal Infections - mortality | Genetic Variation | Streptococcus pyogenes - genetics | Streptokinase - chemistry | Streptococcus pyogenes - pathogenicity | Animals | Plasminogen - chemistry | Streptococcus pyogenes - enzymology | Mice | Mutation | Streptokinase - metabolism | Analysis | Streptokinase
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11. Full Text Comparative study of the reactivity of natural and mutated streptokinase with total antistreptokinase antibodies in human sera
by Bandehpour, Mojgan and Sharifnia, Zarrin and Mohajeri, Nasrin and Taherkhani, Maryam and Koochaki, Ameneh and Yarian, Fatemeh and Seyyed, Negar and Shirvani, Ramin and Pakzad, Parviz and Saadat, Habibollah and Kazemi, Bahram
Blood Coagulation & Fibrinolysis, ISSN 0957-5235, 12/2012, Volume 23, Issue 8, pp. 734 - 738
Streptokinase is widely used as an anticoagulant drug for the treatment of heart attacks. Because of antibody production against injected drug in individuals... 
natural streptokinase | mutant streptokinase | ELISA | EFFICACY | INTRAVENOUS STREPTOKINASE | REPERFUSION | PLASMINOGEN | 42 AMINO-ACIDS | ANISTREPLASE | CARE-UNIT | ACUTE MYOCARDIAL-INFARCTION | ANTIGENIC REGIONS | HEMATOLOGY | THROMBOLYTIC THERAPY | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Recombinant Proteins - therapeutic use | Amino Acid Sequence | Myocardial Infarction - blood | Sequence Deletion | Streptokinase - genetics | Enzyme-Linked Immunosorbent Assay | Anticoagulants - metabolism | Humans | Molecular Sequence Data | Anticoagulants - therapeutic use | Recombinant Proteins - genetics | Streptokinase - therapeutic use | Myocardial Infarction - immunology | Streptokinase - immunology | Anticoagulants - immunology | Myocardial Infarction - drug therapy | Antibodies, Bacterial - biosynthesis | Recombinant Proteins - immunology | Thrombolytic Therapy | Antibodies, Bacterial - immunology | Antibodies, Bacterial - blood | Streptokinase - metabolism
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12. Full Text Engineering, expression and purification of a chimeric fibrin-specific streptokinase
by Taheri, Mohammad Naser and Behzad-Behbahani, Abbas and Rafiei Dehbidi, Gholamreza and Salehi, Saeede and Sharifzadeh, Sedigheh
Protein Expression and Purification, ISSN 1046-5928, 12/2016, Volume 128, pp. 14 - 21
Streptokinase is a valuable fibrinolytic agent used to cope with myocardial infarction and brain stroke. Despite its high efficiency in dissolving blood clots,... 
Chromogenic substrate assay | Kringle 2 | Fibrin-binding streptokinase | Fibrinolytic agent | H-1-NMR | ACTIVATOR KRINGLE-2 DOMAIN | STIMULATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | INVOLVEMENT | BIOCHEMICAL RESEARCH METHODS | STRUCTURAL-CHARACTERIZATION | PLASMINOGEN-ACTIVATOR | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | THROMBOLYTIC THERAPY | BINDING | Recombinant Fusion Proteins - isolation & purification | Tissue Plasminogen Activator - isolation & purification | Humans | Bacterial Proteins - chemistry | Tissue Plasminogen Activator - chemistry | Tissue Plasminogen Activator - genetics | Streptokinase - chemistry | Fibrin - chemistry | Escherichia coli - metabolism | Protein Engineering | Recombinant Fusion Proteins - biosynthesis | Streptokinase - biosynthesis | Streptokinase - genetics | Bacterial Proteins - genetics | Recombinant Fusion Proteins - chemistry | Fibrinolysis | Streptococcus - enzymology | Tissue Plasminogen Activator - biosynthesis | Streptococcus - genetics | Escherichia coli - genetics | Recombinant Fusion Proteins - genetics | Streptokinase - isolation & purification | Bacterial Proteins - biosynthesis | Fibrin - metabolism | Bacterial Proteins - isolation & purification | Stroke (Disease) | Fibrin | Tissue plasminogen activator | Analysis | Escherichia coli | Recombinant proteins | Protein binding
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13. Full Text U.K. Controlled Trial of Intrapleural Streptokinase for Pleural Infection
by Maskell, Nicholas A and Davies, Robert J.O and Davies, Christopher W.H and Nunn, Andrew J and Hedley, Emma L and Gleeson, Fergus V and Miller, Robert and Gabe, Rhian and Rees, Glyn L and Peto, Timothy E.A and Woodhead, Mark A and Lane, Donald J and Darbyshire, Janet H and MIST1 Grp and First Multicenter Intrapleural Sepsis Trial (MIST1) Group
The New England Journal of Medicine, ISSN 0028-4793, 03/2005, Volume 352, Issue 9, pp. 865 - 874
In this randomized trial involving 454 patients with pleural infections that required antibiotic therapy and chest-tube drainage, there was no benefit from the... 
COMPLICATED PARAPNEUMONIC EFFUSIONS | MEDICINE, GENERAL & INTERNAL | COMMUNITY-ACQUIRED PNEUMONIA | MANAGEMENT | EMPYEMA | DEOXYRIBONUCLEASE | UROKINASE | Instillation, Drug | Humans | Middle Aged | Male | Lung - diagnostic imaging | Empyema, Pleural - mortality | Anti-Bacterial Agents - therapeutic use | Fibrinolytic Agents - adverse effects | Community-Acquired Infections - drug therapy | Fibrinolytic Agents - therapeutic use | Pleural Diseases - diagnostic imaging | Female | Length of Stay | Pleural Diseases - drug therapy | Pleural Diseases - surgery | Streptokinase - adverse effects | Empyema, Pleural - surgery | Double-Blind Method | Bacterial Infections - diagnostic imaging | Bacterial Infections - drug therapy | United Kingdom | Combined Modality Therapy | Pleural Diseases - mortality | Streptokinase - therapeutic use | Bacterial Infections - surgery | Cross Infection - drug therapy | Empyema, Pleural - drug therapy | Drainage | Radiography | Pneumonia - complications | Bacterial Infections - mortality | Dosage and administration | Streptokinase | Research | Drug therapy | Pleural diseases | Clinical trials | Infections | Respiratory diseases | Surgery | Clinical outcomes
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14. Full Text Rapid binding of plasminogen to streptokinase in a catalytic complex reveals a three-step mechanism
by Verhamme, Ingrid M and Bock, Paul E
Journal of Biological Chemistry, ISSN 0021-9258, 10/2014, Volume 289, Issue 40, pp. 28006 - 28018
Rapid kinetics demonstrate a three-step pathway of streptokinase (SK) binding to plasminogen (Pg), the zymogen of plasmin (Pm). Formation of a fluorescently... 
DYSGALACTIAE SUBSP EQUISIMILIS | PEPTIDE CHLOROMETHYL KETONES | ACTIVE-SITE | BLOOD-COAGULATION PROTEINASES | BIOCHEMISTRY & MOLECULAR BIOLOGY | Fluorescence | HIGH-AFFINITY | Fibrinolysis | Plasmin | CONFORMATIONAL ACTIVATION | GROUP-A STREPTOCOCCI | Streptokinase | EQUIMOLAR COMPLEXES | GLOBAL KINETIC EXPLORER | Bacterial Pathogenesis | Kinetics | FLUORESCENCE PROBES | Streptococcal Infections - microbiology | Streptokinase - genetics | Biocatalysis | Humans | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Plasminogen - genetics | Substrate Specificity | Plasminogen - metabolism | Streptococcal Infections - enzymology | Streptococcus - chemistry | Amino Acid Motifs | Streptokinase - chemistry | Fibrinolysin - chemistry | Streptococcus - enzymology | Streptococcus - genetics | Plasminogen - chemistry | Protein Binding | Bacterial Proteins - metabolism | Protein Conformation | Binding Sites | Fibrinolysin - metabolism | Streptokinase - metabolism | Enzymology
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15. Full Text Intra-pleural fibrinolytic therapy versus conservative management in the treatment of adult parapneumonic effusions and empyema
by Cameron, R and Davies, H.R
Cochrane database of systematic reviews (Online), ISSN 1469-493X, 2008, Issue 2, p. CD002312
Background Pleural effusions and empyema may complicate lower respiratory tract infections. Treatment of these collections of pus includes surgical drainage... 
Pleural effusion [drug therapy] | Streptokinase [administration & dosage] | Empyema, pleural [drug therapy] | Pneumonia [complications] | Randomized controlled trials as topic | Fibrinolytic agents [administration & dosage] | RANDOMIZED CONTROLLED TRIAL | MEDICINE, GENERAL & INTERNAL | TISSUE-PLASMINOGEN ACTIVATOR | INSTILLATION | HUMAN RECOMBINANT DEOXYRIBONUCLEASE | INFECTION | INTRAPLEURAL STREPTOKINASE | CATHETER DRAINAGE | THORACIC EMPYEMA | HEMOTHORAX | UROKINASE | Streptokinase - administration & dosage | Humans | Thrombolytic Therapy - methods | Pneumonia - complications | Adult | Pleural Effusion - drug therapy | Fibrinolytic Agents - administration & dosage | Urokinase-Type Plasminogen Activator - administration & dosage | Empyema, Pleural - drug therapy | Randomized Controlled Trials as Topic
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16. Full Text PEGylation of truncated streptokinase leads to formulation of a useful drug with ameliorated attributes
by Sawhney, Pooja and Katare, Keya and Sahni, Girish
PLoS ONE, ISSN 1932-6203, 05/2016, Volume 11, Issue 5, p. e0155831
Streptokinase (SK) remains a favored thrombolytic agent in the developing world as compared to the nearly 10-fold more expensive human tissue-plasminogen... 
SITE | DOMAIN | PROTEIN | MYOCARDIAL-INFARCTION | MECHANISM | PLASMINOGEN-ACTIVATOR COMPLEX | MULTIDISCIPLINARY SCIENCES | THROMBOLYSIS | BINDING | FIBRINOGEN | MACROMOLECULAR SUBSTRATE | Streptokinase - chemistry | Fibrinolytic Agents - chemistry | Streptokinase - immunology | Streptococcus - enzymology | Streptokinase - genetics | Animals | Antibodies, Bacterial - immunology | Polyethylene Glycols - chemistry | Mice | Fibrinolytic Agents - immunology | Amino Acid Substitution | Cysteine - genetics | Care and treatment | Dosage and administration | Immune response | Streptokinase | Analysis | Heart attack | Myocardial infarction | Enzymes | Heart attacks | Hematology | Amino acids | Radioactive half-life | Hemorrhage | Thrombosis | Thrombolysis | Plasmin | Biological activity | t-Plasminogen activator | Proteins | Fibrin | Infarction | Scientific imaging | Molecular biology | Mass spectrometry | Pharmaceutical sciences | Half life
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17. Full Text Fibrinolytic agents for peripheral arterial occlusion
by Robertson, Iain and Robertson, Iain and Kessel, David O and Kessel, David O and Berridge, David C and Berridge, David C
The Cochrane database of systematic reviews, ISSN 1469-493X, 2013, Volume 12, Issue 12, p. CD001099
Background Peripheral arterial thrombolysis is used in the management of peripheral arterial ischaemia. Streptokinase was originally used but safety concerns... 
LOWER-EXTREMITY | PROSPECTIVE RANDOMIZED-TRIAL | Humans | LIMB ISCHEMIA | LOCAL THROMBOLYSIS | Arterial Occlusive Diseases [drug therapy] | Peripheral Vascular Diseases [drug therapy] | Urokinase-Type Plasminogen Activator [adverse effects; therapeutic use] | Fibrinolytic Agents [adverse effects; therapeutic use] | Randomized Controlled Trials as Topic | Thrombosis [drug therapy] | Thrombolytic Therapy [adverse effects; methods] | MEDICINE, GENERAL & INTERNAL | STREPTOKINASE | Streptokinase [adverse effects; therapeutic use] | Tissue Plasminogen Activator [adverse effects; therapeutic use] | TISSUE-PLASMINOGEN-ACTIVATOR | Recombinant Proteins [adverse effects; therapeutic use] | THROMBOLYTIC THERAPY | UROKINASE | Recombinant Proteins - therapeutic use | Streptokinase - adverse effects | Urokinase-Type Plasminogen Activator - adverse effects | Urokinase-Type Plasminogen Activator - therapeutic use | Peripheral Vascular Diseases - drug therapy | Tissue Plasminogen Activator - therapeutic use | Recombinant Proteins - adverse effects | Streptokinase - therapeutic use | Tissue Plasminogen Activator - adverse effects | Fibrinolytic Agents - adverse effects | Arterial Occlusive Diseases - drug therapy | Fibrinolytic Agents - therapeutic use | Thrombolytic Therapy - methods | Thrombosis - drug therapy | Thrombolytic Therapy - adverse effects
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18. Full Text Mo1342 Use of Streptokinase for Enhancement of Percutaneous Drainage of Pancreatic Necrosis: A Double Blinded Randomized Controlled Trial
by Gupta, Rahul and Gupta, Rajesh and Kang, Mandeep and Bhasin, Deepak K and Khullar, Madhu and Singh, Rajinder
Gastroenterology, ISSN 0016-5085, 2015, Volume 148, Issue 4, pp. S-677 - S-677
Gastroenterology and Hepatology | Usage | Streptokinase
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19. Full Text Thrombolytic and fibrinogenolytic properties of bioconjugate streptokinase-polyamidoamine dendrimers in vitro
by Mukhametova, L.I and Aisina, R.B and Zakharyan, E.M and Karakhanov, E.A and Gershkovich, K.B and Varfolomeyev, S.D
Thrombosis Research, ISSN 0049-3848, 2017, Volume 154, pp. 50 - 52
Highlights • Thrombolytic activity of SK-PAMAM dendrimer conjugates depends on the dendrimer generation and the modification degree of SK amino groups. •... 
Hematology, Oncology and Palliative Medicine | Conjugates | Dendrimers | Streptokinase | Fibrinogenolysis | Thrombolytic activity | PERIPHERAL VASCULAR DISEASE | STAPHYLOKINASE | ACTIVATION | MECHANISM | HEMATOLOGY | HUMAN PLASMINOGEN | Fibrinolytic Agents - pharmacology | Streptokinase - pharmacology | Fibrinolytic Agents - therapeutic use | Humans | Thrombolytic Therapy - methods | Streptokinase - therapeutic use | Analysis
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