Amino acid residues Arg659, Arg660, and Tyr661 in the spacer domain of ADAMTS13 are critical for cleavage of von Willebrand factor

Leukocyte proteases cleave von Willebrand factor at or near the ADAMTS13 cleavage site

(2009) T. J. Raife et al.   BLOOD

A novel binding site for ADAMTS13 constitutively exposed on the surface of globular VWF

(2009) S. Zanardelli et al.   BLOOD

von Willebrand factor cleaved from endothelial cells by ADAMTS13 remains ultralarge in size

(2009) S.-Y. JIN et al.   JOURNAL OF THROMBOSIS AND HAEMOSTASIS

Multi-step binding of ADAMTS-13 to von Willebrand factor

(2009) H. B. FEYS et al.   JOURNAL OF THROMBOSIS AND HAEMOSTASIS

Crystal structures of the noncatalytic domains of ADAMTS13 reveal multiple discontinuous exosites for von Willebrand factor

(2009) M. Akiyama et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Pathogenesis of Thrombotic Microangiopathies

(2008) X. Long Zheng et al.   Annual Review of Pathology-Mechanisms of Disease

Extensive contacts between ADAMTS13 exosites and von Willebrand factor domain A2 contribute to substrate specificity

(2008) W. Gao et al.   BLOOD

The first deletion mutation in the TSP1-6 repeat domain of ADAMTS13 in a family with inherited thrombotic thrombocytopenic purpura

(2008) R. Palla et al.   HAEMATOLOGICA

ADAMTS-13 cleaves long von Willebrand factor multimeric strings anchored to endothelial cells in the absence of flow, platelets or conformation-altering chemicals

(2008) N. TURNER et al.   JOURNAL OF THROMBOSIS AND HAEMOSTASIS