Identification and Characterization of Prolylcarboxypeptidase as an Endothelial Cell Prekallikrein Activator
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference37 articles.
1. High Molecular Weight Kininogen Peptides Inhibit the Formation of Kallikrein on Endothelial Cell Surfaces and Subsequent Urokinase-Dependent Plasmin Formation
2. High Molecular Weight Kininogen Regulates Prekallikrein Assembly and Activation on Endothelial Cells: A Novel Mechanism for Contact Activation
3. Isolation and Characterization of the Kininogen-binding Protein p33 from Endothelial Cells
4. Identification of the zinc-dependent endothelial cell binding protein for high molecular weight kininogen and factor XII: identity with the receptor that binds to the globular "heads" of C1q (gC1q-R).
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3. Pathophysiology of bradykinin and histamine mediated angioedema;Frontiers in Allergy;2023-10-18
4. C1 inhibitor and prolylcarboxypeptidase modulate prekallikrein activation on endothelial cells;Journal of Allergy and Clinical Immunology;2023-10
5. Human plasma kallikrein: roles in coagulation, fibrinolysis, inflammation pathways, and beyond;Frontiers in Physiology;2023-08-30
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