Mechanism of Na+/K+-ATPase activation by trypsin and kallikrein
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference29 articles.
1. Stimulation of high-affinity GTPase by trypsin and trypsin-like proteinases in membranes of human platelets
2. The activation of phosphatase activity of the Ca2+-ATPase from human red cell membranes by calmodulin, ATP and partial proteolysis
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4. Activation of the Ca2+-ATPase of human erythrocyte membrane by an endogenous Ca2+-dependent neutral protease
5. [27] Proteolytic cleavage as a tool for studying structure and conformation of pure membrane-bound Na+,K+-ATPase
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1. Tissue Kallikrein–Kinin System;Comprehensive Physiology;2000-12
2. Separation by heparin-affinity chromatography of catalytically active and inactive forms of trypsin which retain the (NaK)ATPase stimulating property;Clinica Chimica Acta;1996-12
3. Inactivation precedes overall molecular conformation changes during enzyme denaturation;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1995-12
4. Effects of herpes simplex virus type 1 infection on the plasma membrane and related functions of HeLa S3 cells;Journal of General Virology;1994-12-01
5. Alteration of plasma proteinase-antiproteinase system in type 1 diabetic patients. Influence of sex and relationship with metabolic control;Diabetes Research and Clinical Practice;1992-10
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