Plasminogen Substrate Recognition by the Streptokinase-Plasminogen Catalytic Complex Is Facilitated by Arg253, Lys256, and Lys257 in the Streptokinase β-Domain and Kringle 5 of the Substrate
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference68 articles.
1. Plasminogen Is a Critical Host Pathogenicity Factor for Group A Streptococcal Infection
2. Basic and clinical aspects of fibrinolysis and thrombolysis
3. Crystal Structure of the Catalytic Domain of Human Plasmin Complexed with Streptokinase
4. Streptokinase is a flexible multi-domain protein
5. Streptokinase Binds to Human Plasmin with High Affinity, Perturbs the Plasmin Active Site, and Induces Expression of a Substrate Recognition Exosite for Plasminogen
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1. Targeted drug delivery to the thrombus by fusing streptokinase with a fibrin-binding peptide (CREKA): an in silico study;Therapeutic Delivery;2024-04-30
2. Investigation of binding mechanism for human plasminogen Kringle 5 with its potential receptor vWA1 domain in Cochlin by bio-specific technologies and molecular dynamic simulation;Bioorganic Chemistry;2022-10
3. Thrombolytic Enzymes of Microbial Origin: A Review;International Journal of Molecular Sciences;2021-09-28
4. Role of Fibrinolytic Enzymes in Anti-Thrombosis Therapy;Frontiers in Molecular Biosciences;2021-05-28
5. Kringles of substrate plasminogen provide a ‘catalytic switch' in plasminogen to plasmin turnover by Streptokinase;Biochemical Journal;2020-03-06
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