Chimerism Reveals a Role for the Streptokinase β-Domain in Nonproteolytic Active Site Formation, Substrate, and Inhibitor Interactions
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference45 articles.
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2. 1 Mechanisms of physiological fibrinolysis
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4. Direct evidence for the generation of an active site in the plasminogen moiety of the streptokinase-human plasminogen activator complex
5. Interaction of staphylokinase with different molecular forms of plasminogen
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2. The β‐domain of streptokinase affects several functionalities, including specific/proteolytic activity kinetics;FEBS Open Bio;2019-05-30
3. Site-specific PEGylation of micro-plasmin for improved thrombolytic therapy through engineering enhanced resistance against serpin mediated inhibition;PLOS ONE;2019-05-29
4. Mechanical Stability and Fibrinolytic Resistance of Clots Containing Fibrin, DNA, and Histones;Journal of Biological Chemistry;2013-03
5. Streptococcus uberis Plasminogen Activator (SUPA) Activates Human Plasminogen through Novel Species-specific and Fibrin-targeted Mechanisms;Journal of Biological Chemistry;2012-06
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