3.4.24.87	additional information	antibodies that recognize domains T67, T8, and CUB domains have additive effects. Binding activates ADAMTS13 up to 4.2fold at pH 7.4, but antibodies have markedly decreased effects on ADAMTS13 activity at pH 6	735184	
3.4.24.87	additional information	CCl4 at concentration of 6.5 mM does not directly enhance the activity of ADAMTS-13	670063	
3.4.24.87	additional information	cleavage of von Willebrand factor A2 requires the force-induced A2 unfolding	711576	
3.4.24.87	additional information	coagulation factor VIII, platelet glycoprotein 1balpha, and heparin sulfate accelerate the cleavage of von Willebrand factor	720833	
3.4.24.87	additional information	in the absence of factor VIII, lyophilized platelets increase the formation of cleavage product by 2-3fold under fluid shear stresses. However, in the presence of physiological concentration of factor VIII (1 nM), the formation of von Willebrand factor cleavage product increases dramatically as a function of increasing platelets (150000 per microliter) with the maximal rate enhancement of about 8fold	719881	
3.4.24.87	additional information	inhibition of ADAMTS13 by auto-antibodies is reversed by rituximab, overview	713531	
3.4.24.87	additional information	low salt concentrations activate the proteolytic activity	650717	
3.4.24.87	additional information	mild denaturation of fluid shear stress increase the hydrolysis of von Willebrand factor	711809	
3.4.24.87	additional information	removal of the C-terminal domain of the enzyme by activated coagulation factor XI or alpha-thrombin causes an increase in enzyme activity	753666	
3.4.24.87	additional information	substrate modified by alpha2-3,6,8,9-neuraminidase from Arthrobacter ureafaciens removing alpha2-3- and alpha2-6-linked sialic acid results in reduced ADAMTS13 activity	711575	
3.4.24.87	plasmin	truncation of the enzyme by plasmin enhances its activity in blood plasma	755582	
3.4.24.87	Ristocetin	activates	650715	
3.4.24.87	Rituximab	a monoclonal anti-CD 20 antibody, Rituximab leads to a prompt reduction in IgG antibody levels, followed by an increase in ADAMTS 13 activity increases. However, in patients receiving Rituximab electively, normalisation of ADAMTS 13 enzyme activity may be delayed for up to 3 months	711559	
3.4.24.87	Urea	activates at 1 M	652481	
3.4.24.87	Urea	activation, substrate is degraded at 1 M	650717, 650725	
3.4.24.87	Urea	required	650714	
3.4.24.87	von Willebrand factor	binding to substrate von Willebrand factor D4 allosterically activates ADAMTS13, increasing its catalytic activity. Binding also positions ADAMTS13 on the substrate where it can act rapidly when shear stress exposes the scissile bond in the adjacent A2 domain	735184	
3.4.24.87	von Willebrand factor	the enzyme is conformationally activated by von Willebrand factor which engages the TSP8-CUB2 domains, inducing the conformational change that disrupts the CUB1-spacer domain interaction and thereby activates the enzyme	754157