α2-antiplasmin's carboxy-terminal lysine residue is a major site of interaction with plasmin
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference14 articles.
1. Identification and Some Properties of a New Fast-Reacting Plasmin Inhibitor in Human Plasma
2. Isolation and characterization of alpha2-plasmin inhibitor from human plasma. A novel proteinase inhibitor which inhibits activator-induced clot lysis.
3. The primary inhibitor of plasmin in human plasma
4. On the specific interaction between the lysine-binding sites in plasmin and complementary sites in α2-antiplasmin and in fibrinogen
5. On the Kinetics of the Reaction between Human Antiplasmin and Plasmin
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1. A High-Throughput Small-Angle X-ray Scattering Assay to Determine the Conformational Change of Plasminogen;International Journal of Molecular Sciences;2023-09-19
2. α2-Antiplasmin as a potential regulator of the spatial memory process and age-related cognitive decline;Molecular Brain;2020-10-15
3. On the localization of the cleavage site in human alpha‐2‐antiplasmin, involved in the generation of the non‐plasminogen binding form;Journal of Thrombosis and Haemostasis;2020-03-05
4. Conformationally organized lysine isosteres in Streptococcus pyogenes M protein mediate direct high-affinity binding to human plasminogen;Journal of Biological Chemistry;2017-09
5. Natural heterogeneity of α2-antiplasmin: functional and clinical consequences;Blood;2016-02-04
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