The β‐domain of streptokinase affects several functionalities, including specific/proteolytic activity kinetics
Author:
Affiliation:
1. Virology Department Pasteur Institute of Iran Tehran Iran
2. Microbiology Department Pasteur Institute of Iran Tehran Iran
3. NanoBiotechnology Department Pasteur Institute of Iran Tehran Iran
Funder
Pasteur Institute of Iran
Publisher
Wiley
Subject
General Biochemistry, Genetics and Molecular Biology
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/2211-5463.12657
Reference19 articles.
1. Streptokinase variants fromStreptococcus pyogenesisolates display altered plasminogen activation characteristics - implications for pathogenesis
2. Towards A Superior Streptokinase for Fibrinolytic Therapy of Vascular Thrombosis
3. Reprogrammed streptokinases develop fibrin-targeting and dissolve blood clots with more potency than tissue plasminogen activator
4. Function of the central domain of streptokinase in substrate plasminogen docking and processing revealed by site-directed mutagenesis
5. Computational simulations assessment of mutations impact on streptokinase (SK) from a group G streptococci with enhanced activity–insights into the functional roles of structural dynamics flexibility of SK and stabilization of SK–μplasmin catalytic complex;Kazemi F;J Biomol Struct Dyn,2018
Cited by 2 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. C-terminal lysine residues enhance plasminogen activation by inducing conformational flexibility and stabilization of activator complex of staphylokinase with plasmin;Archives of Biochemistry and Biophysics;2023-07
2. Lysine Residues in the MK-Rich Region Are Not Required for Binding of the PbsP Protein From Group B Streptococci to Plasminogen;Frontiers in Cellular and Infection Microbiology;2021-09-08
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